PPR
{

RETE|ID 1 FBpp0001256	SYM 1 shi<up>+</up>P-exon	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 4 Feb 1998	RESZ 259
ID|FBpp0001256
SYM|shi<up>+</up>P-exon
ASAL|<fbsym>FBal0071044==shi<up>+</up></fbsym>
DT|4 Feb 1998
|4 Feb 1998
ASGN|<fbsym>FBgn0003392==shi</fbsym>

REFDSR
{
RDID|FBrf0105495
|FlyBase
|1992-
CC|alternative 3' exon
}

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001540	SYM 1 gsb<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 5 Nov 1999	RESZ 470
ID|FBpp0001540
SYM|gsb<up>+</up>PA
SYN|gsb-d<up>+</up>PA
ASAL|<fbsym>FBal0100470==gsb<up>+</up></fbsym>
DT|5 Nov 1999
|10 Mar 1998
ASGN|<fbsym>FBgn0001148==gsb</fbsym>

REFDSR
{
RDID|FBrf0064406
|Chu-LaGraff and Doe
|1993
BODP|<fbsym>gsb-d</fbsym> protein was used as a neuroblast marker.  It is expressed in rows 5
| and 6/7 neuroblasts.
CVBODP|<t> E <a> neuroblast | row 5 <p>
|<t> E <a> neuroblast | row 6/7 <p>
}

REF
{
REFM|FBrf0064406
|Chu-LaGraff and Doe
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001553	SYM 1 Aldh<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 450
ID|FBpp0001553
SYM|Aldh<up>+</up>PA
ASAL|<fbsym>FBal0066370==Aldh<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0012036==Aldh</fbsym>

REFDSR
{
RDID|FBrf0058677
|Leal and Barbancho
|1993
PCL|Acetaldeyhde dehyrogenase activity from the <fbsym>FBgn0012036==Aldh</fbsym> gene is mainly cytosolic
| in adults though some is located in the mitochondria.
CVCEL|cytoplasm
|mitochondrion
}

REF
{
REFM|FBrf0058677
|Leal and Barbancho
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001554	SYM 1 PC-Pld<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 435
ID|FBpp0001554
SYM|PC-Pld<up>+</up>PA
ASAL|<fbsym>FBal0068143==PC-Pld<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0013310==PC-Pld</fbsym>

REFDSR
{
RDID|FBrf0058680
|Miller et al.
|1993
CC|Dietary alcohols at low to moderate levels increase
| phosphatidylcholine-specific phospholipase D in larvae. PC-PLD activity was
| enhanced by Ca[2+] and by GTP-&ggr;S in vitro.
}

REF
{
REFM|FBrf0058680
|Miller et al.
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001619	SYM 1 pnt<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 20 Mar 1998	RESZ 459
ID|FBpp0001619
SYM|pnt<up>+</up>PA
ASAL|<fbsym>FBal0070902==pnt<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003118==pnt</fbsym>

REFDSR
{
RDID|FBrf0057432
|Lautenberger et al.
|1992
CC|The amino acid sequences of various <fbsym>Ets</fbsym> gene family members were studied
| to determine evolutionary relatedness. Phylogenetic trees were derived.
}

REF
{
REFM|FBrf0047835
|Pribyl et al.
|1988
REFM|FBrf0057432
|Lautenberger et al.
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001628	SYM 1 Mhc<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 385
ID|FBpp0001628
SYM|Mhc<up>+</up>PB
ASAL|<fbsym>FBal0068063==Mhc<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002741==Mhc</fbsym>

REFDSR
{
RDID|FBrf0046579
|Wassenberg et al.
|1987
ASTR|<fbsym>FBtr0000111==Mhc<up>+</up>RA</fbsym>
CC|Predicted from sequence data (J02788). Encoded by transcript containing exon 3a.
}

REF
{
REFM|FBrf0046579
|Wassenberg et al.
|1987
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001629	SYM 1 Mhc<up>+</up>PC	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 385
ID|FBpp0001629
SYM|Mhc<up>+</up>PC
ASAL|<fbsym>FBal0068063==Mhc<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002741==Mhc</fbsym>

REFDSR
{
RDID|FBrf0046579
|Wassenberg et al.
|1987
ASTR|<fbsym>FBtr0000112==Mhc<up>+</up>RB</fbsym>
CC|Predicted from sequence data (J02788). Encoded by transcript containing exon 3b.
}

REF
{
REFM|FBrf0046579
|Wassenberg et al.
|1987
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001632	SYM 1 ct<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 5	DT 1 23 Apr 2001	RESZ 6274
ID|FBpp0001632
SYM|ct<up>+</up>P
ASAL|<fbsym>FBal0068792==ct<up>+</up></fbsym>
DT|23 Apr 2001
|10 Mar 1998
ABODURL|2b10.html 2B10
ASGN|<fbsym>FBgn0004198==ct</fbsym>

REFDSR
{
RDID|FBrf0048770
|Blochlinger et al.
|1988
ABOD|polyclonal
PCL|Within a simple external sensory organ, the nuclei of the tormogen and
| trichogen cells express <fbsym>FBgn0004198==ct</fbsym> protein strongly, while the thecogen cells and
| neurons are not consistently labeled.
BODP|All external sensory organs of the embryo, including the antenno-maxillary
| complex and the external sensory organs in the spiracles, express <fbsym>FBgn0004198==ct</fbsym>
| protein. Staining is visible before morphological differentiation of cells
| of the external sensory organs at stage 11-12 of embryogenesis. Additional
| tissues which express the <fbsym>FBgn0004198==ct</fbsym> protein include some neurons with multiple
| dendritic arborizations, and cells lining the Malpighian tubules.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E  <a> external sensory organ <p>
CVCEL|nucleus
}

REFDSR
{
RDID|FBrf0051828
|Blochlinger et al.
|1990
ABOD|polyclonal
BODP|In the 5-6 hour embryo, <fbsym>FBgn0004198==ct</fbsym> protein is expressed in sensory precursor
| cells, which will give rise to the external sensory organs. <fbsym>FBgn0004198==ct</fbsym> protein
| appears in many putative external sensory organ precursors in 5-10 hour
| embryos, starting with the position of the double innervated sensillum
|  trichoideum and sensillum campaniformium (des2 and v'es2) in abdominal
| segments, and the basiconical sensilla (les3, v'es3) in the thoracic
| segments. In most external sensory organs at late embryogenesis, the
| trichogen and tormogen label more intensely for <fbsym>FBgn0004198==ct</fbsym> protein than the
| neuron and thecogen. Some CNS cells, the Malpighian tubules, and cells
| surrounding the anterior and posterior spiracles express <fbsym>FBgn0004198==ct</fbsym> protein
| starting at 5-7 hours of embryogen sis.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | >5-6 hr <a> external sensory organ <p><t> E | 5-6 hr <a> des2 neuron <p>
|<t> E | 5-6 hr <a> v'es2 neuron <p>
|<t> E | 5-6 hr <a> les3 neuron <p>
|<t> E | 5-6 hr <a> v'es3 neuron <p>
|<t> E | 6-7 hr <a> desC neuron <p>
|<t> E | 6-7hr <a> desD neuron <p>
|<t> E | 8 hr <a> desB neuron <p>
|<t> E | 8 hr <a> lesC neuron <p>
|<t> E | 8 hr <a> lesB neuron <p>
|<t> E | 8 hr <a> lesA neuron <p>
|<t> E | 8 hr <a> v'esA neuron <p>
|<t> E | 8 hr <a> vesC neuron <p>
|<t> E | 10 hr <a> v'esB neuron <p>
|<t> E | 10 hr <a> v'esC neuron <p>
|<t> E | 10 hr <a> vesB neuron <p><t> E | >5-6 hr <a> embryonic/larval posterior spiracle | surrounding <p>
|<t> E | >5-6 hr <a> embryonic/larval anterior spiracle | surrounding <p>
|<t> E | >5-6 hr <a> Malpighian tubule <p>
|<t> E | >6-7 hr <a> embryonic central nervous system | presumptive | restricted <p>
CVCEL|nucleus
CC|When the complete <fbsym>FBgn0004198==ct</fbsym> coding sequence is expressed under the control of a
| heat shock promoter, 320 kD and 280 kD bands are observed on a Western
| blot. The same two protein sizes are detected in Western blots of wild type embryos.
}

REFDSR
{
RDID|FBrf0058084
|Blochlinger et al.
|1993
BODP|<fbsym>FBgn0004198==ct</fbsym> protein accumulation from larval through adult stages was studied by
| immunolocalization. <fbsym>FBgn0004198==ct</fbsym> protein is found in diverse tissues, including the
| wing and leg discs, muscle, ovarian follicle cells, and the central nervous
| system. In many tissues, <fbsym>FBgn0004198==ct</fbsym> protein is expressed in a subset of cells. In
| many cases, it is found in precursors, and persists in differentiated
| cells. In the third instar larval wing disc, <fbsym>FBgn0004198==ct</fbsym> protein is first detected
| in regions corresponding to the prospective notum, wing blade, and wing
| hinge. In the first 2 hours of puparium formation, <fbsym>FBgn0004198==ct</fbsym> protein expression
| is detected in the distal anterior wing margin where, by 6 hours, <fbsym>FBgn0004198==ct</fbsym>
| protein is detected in the chemosensory organ cells. At 24 hours of
| pupariat on, expression is also detected in macrochaetae and microchaetae
| of the notum. The prospective wing margin stains from third larval instar
| through 24 hours of pupa formation. Regions of the leg disc which will give
| rise to the tarsus and to pioneer neurons express <fbsym>FBgn0004198==ct</fbsym> protein from third
| larval instar through 3 hour pupae. Malpighian tubules, ovarian follicle
| cells from stage S2 to S14, larval adepithelial cells and adult muscles of
| the thorax, head and abdomen are among tissues which express <fbsym>FBgn0004198==ct</fbsym> protein.
| Structures of the adult head which express <fbsym>FBgn0004198==ct</fbsym> protein include the cortex
| of medulla and lobulla, and the neuropil. The interommatidial bristle
| precursors and cone cell precursors of 24 hour pupal eye discs, and adult
| cone cells also contain <fbsym>FBgn0004198==ct</fbsym> protein.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> dorsal mesothoracic disc | restricted <p>
|<t> L | third instar <a> ventral thoracic disc | restricted <p>
|<t> PP | 0-2 hr <a> chemosensory sensory organ | precursor <of> dorsal mesothoracic disc <p>
|<t> P | 6 hr<a> chemosensory sensory organ <of> dorsal mesothoracic disc <p>
|<t> P | 24 hr <a> microchaetae <p>
|<t> P | 24 hr <a> macrochaetae <p>
|<t> P | 24 hr <a> interommatidial bristle | precursor <p>
|<t> L | third instar <a> tarsus | precursor <p>
|<t> L | third instar <a> pioneer neuron | precursor <p>
|<t> PP | 3 hr <a> tarsus | precursor <p>
|<t> PP | 3 hr <a> pioneer neuron | precursor <p>
|<t> A <a> Malpighian tubule <p>
|<t> O,A | stage S2-S14 <a> follicle cell <p>
|<t> L | third instar <a> adepithelial cell <p>
|<t> A <a> adult muscle system <p>
|<t> A <a> medulla cortex <p>
|<t> A <a> lobula plate cortex <p>
|<t> L-A <a> cone cell <p>
}

REFDSR
{
RDID|FBrf0129996
|Nolo et al.
|2000
MRK|thecogen cell
}

REF
{
REFM|FBrf0048770
|Blochlinger et al.
|1988
REFM|FBrf0051828
|Blochlinger et al.
|1990
REFM|FBrf0057354
|Neufeld et al.
|1992
REFM|FBrf0058084
|Blochlinger et al.
|1993
REFM|FBrf0129996
|Nolo et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001638	SYM 1 Mhc<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 1341
ID|FBpp0001638
SYM|Mhc<up>+</up>P
ASAL|<fbsym>FBal0068063==Mhc<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002741==Mhc</fbsym>

REFDSR
{
RDID|FBrf0050538
|George et al.
|1989
CC|At least 480 <fbsym>FBgn0002741==Mhc</fbsym> isoforms are theoretically encoded by the gene when all
| the different possible combinations of alternate exons are considered. The
| alternative exons encode sequences close to or within regions thought to
| have important structural or enzymatic functions. Putative functional
| domains and regions of exceptional sequence conservation, however, are most
| often distributed in both alternative and common exons. Some of the
| characterized domains map to exons as follows: a conserved hydrophobic
| pocket sequence in exons 3-4, the highly conserved ATP-binding domain in
| exon 4, the highly divergent proteolytic cleavage site that defines the
| 25-50kD junction in exon 4, two highly conserved regions of unidentified
| function in exons 4-6 and 8-9, the 50-20kD junction in exon 10, the primary
| actin-binding site in exon 10, a secondary actin-binding site in exon 11,
| the sites of myosin light chain binding in exon 12, the head-tail junction
| in exon 12, the hinge region in exons 14-16, and the non-coiled tailpiece
| in exons 17-19.
}

REF
{
REFM|FBrf0050538
|George et al.
|1989
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001639	SYM 1 Pc<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 794
ID|FBpp0001639
SYM|Pc<up>+</up>PA
ASAL|<fbsym>FBal0068148==Pc<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003042==Pc</fbsym>

REFDSR
{
RDID|FBrf0050645
|Zink and Paro
|1989
ABOD|polyclonal
CC|<fbsym>FBgn0003042==Pc</fbsym> protein is associated with ~60 sites on the polytene chromosomes. It is
| associated with loci shown to interact with <fbsym>FBgn0003042==Pc</fbsym> by genetic methods. It is
| abundant at the ANT-C and the BX-C and is found at several locations of
| <fbsym>FBgn0003042==Pc</fbsym>-group genes. The <fbsym>FBgn0003042==Pc</fbsym> protein expressed in salivary glands is encoded
| by a 1.0kb <fbsym>FBgn0003042==Pc</fbsym> transcript and is smaller than the 390aa <fbsym>FBgn0003042==Pc</fbsym> protein.
}

REF
{
REFM|FBrf0050645
|Zink and Paro
|1989
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001640	SYM 1 Gpdh<up>+</up>P	AAL 1 866	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 5	DT 1 31 Dec 1998	RESZ 1997
ID|FBpp0001640
SYM|Gpdh<up>+</up>P
ASAL|<fbsym>FBal0067849==Gpdh<up>+</up></fbsym>
DT|31 Dec 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0001128==Gpdh</fbsym>

REFDSR
{
RDID|FBrf0051226
|Lissemore et al.
|1990
BODP|<fbsym>FBgn0001128==Gpdh</fbsym> activity increases nearly fourfold when dietary sucrose is increase
| from 0.1% to 10%. Glucose, fructose, or starch at a 5% concentration also
| lead to a 2-3-fold increase in <fbsym>FBgn0001128==Gpdh</fbsym> activity. <fbsym>FBgn0001128==Gpdh</fbsym> activity increases
| with increasing ethanol. Sucrose and ethanol together have an additive
| effect on <fbsym>FBgn0001128==Gpdh</fbsym> activity.
ASM|enzyme assay or biochemical detection
}

REFDSR
{
RDID|FBrf0057573
|Li
|1992
AAL|866
CC|The quantities of six out of seven enzymes tested were higher in <fbsym>FBal0000314==Adh[F]</fbsym>
| homozygotes than in <fbsym>FBal0000321==Adh[S]</fbsym> homozygotes. Levels were significantly higher
| at the 0.001 level for <fbsym>FBgn0000055==Adh</fbsym>, <fbsym>FBgn0001091==Gapdh1</fbsym>, and <fbsym>FBgn0003076==Pgm</fbsym> and higher at the 0.05
| level for <fbsym>FBgn0001128==Gpdh</fbsym>. <fbsym>FBgn0001248==Idh</fbsym> levels were not increased in <fbsym>FBal0000314==Adh[F]</fbsym> flies.
}

REFDSR
{
RDID|FBrf0059165
|Hoshino et al.
|1993
CC|The quantities of six out of seven enzymes tested were higher in <fbsym>FBal0000314==Adh[F]</fbsym>
| homozygotes than in <fbsym>FBal0000321==Adh[S]</fbsym> homozygotes. Levels were significantly higher
| at the 0.001 level for <fbsym>FBgn0000055==Adh</fbsym>, <fbsym>FBgn0001091==Gapdh1</fbsym>, and <fbsym>FBgn0003076==Pgm</fbsym> and higher at the 0.05
| level for <fbsym>FBgn0001128==Gpdh</fbsym>. <fbsym>FBgn0001248==Idh</fbsym> levels were not increased in <fbsym>FBal0000314==Adh[F]</fbsym> flies.
}

REF
{
REFM|FBrf0044670
|Cook et al.
|1986
REFM|FBrf0049550
|Sanchez-Herrero and Akam
|1989
REFM|FBrf0051226
|Lissemore et al.
|1990
REFM|FBrf0057573
|Li
|1992
REFM|FBrf0059165
|Hoshino et al.
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001651	SYM 1 Nrg<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 879
ID|FBpp0001651
SYM|Nrg<up>+</up>P
ASAL|<fbsym>FBal0068125==Nrg<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002968==Nrg</fbsym>

REFDSR
{
RDID|FBrf0052686
|Hortsch et al.
|1990
ABOD|monoclonal
BODP|A monoclonal antibody which recognizes both forms of the <fbsym>FBgn0002968==Nrg</fbsym> protein
| detects <fbsym>FBgn0002968==Nrg</fbsym> protein in neurons of the central nervous system and
| peripheral nervous system of the embryo, as well as in epidermal cells and
| neurons of thirdinstar larval imaginal discs.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | >6 hr <a> central nervous system | restricted <p>
|<t> E | >=7 hr <a> embryonic peripheral nervous system | restricted <p>
|<t> L | third instar <a> neuron <of> imaginal disc <p>
|<t> L | third instar <a> epidermis <of> imaginal disc <p>
}

REF
{
REFM|FBrf0052686
|Hortsch et al.
|1990
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001662	SYM 1 ovo<up>+</up>PA	AAL 1 -	PSZ 1 131 	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 528
ID|FBpp0001662
SYM|ovo<up>+</up>PA
ASAL|<fbsym>FBal0070857==ovo<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003028==ovo</fbsym>

REFDSR
{
RDID|FBrf0053878
|Mevel-Ninio et al.
|1991
PSZ|131 | predicted
CC|The <fbsym>FBgn0003028==ovo</fbsym> protein is at least 1209 amino acids long. In addition to four
| zinc finger repeats, the protein contains homopolymeric runs of several
| different amino acids, and has an extremely hydrophilic amino acid profile.
}

REF
{
REFM|FBrf0053878
|Mevel-Ninio et al.
|1991
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001667	SYM 1 Psc<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 200
ID|FBpp0001667
SYM|Psc<up>+</up>PA
ASAL|<fbsym>FBal0068204==Psc<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0005624==Psc</fbsym>

REF
{
REFM|FBrf0054776
|van Lohuizen et al.
|1991
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001670	SYM 1 Shal<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 833
ID|FBpp0001670
SYM|Shal<up>+</up>P
ASAL|<fbsym>FBal0074236==Shal<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0005564==Shal</fbsym>

REFDSR
{
RDID|FBrf0054816
|Covarrubias et al.
|1991
CC|Co-injection experiments in Xenopus oocytes were used to test for formation
| of functional heterodimers between <fbsym>FBgn0003380==Sh</fbsym> subfamily members. In fact, no
| functional heterodimers (as shown by novel current kinetics) were detected
| when all pairwise combinations of the four different channel subfamilies
| (<fbsym>FBgn0003380==Sh</fbsym>, <fbsym>FBgn0003383==Shab</fbsym>, <fbsym>FBgn0005564==Shal</fbsym>, and <fbsym>FBgn0003386==Shaw</fbsym>) were tested. The
| independence of each channel system was retained even when all four were co-expressed.
}

REF
{
REFM|FBrf0054816
|Covarrubias et al.
|1991
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001687	SYM 1 Psc<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 1683
ID|FBpp0001687
SYM|Psc<up>+</up>P
ASAL|<fbsym>FBal0068204==Psc<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ABODURL|6e8.html 6E8
ASGN|<fbsym>FBgn0005624==Psc</fbsym>

REFDSR
{
RDID|FBrf0058093
|Martin and Adler
|1993
ABOD|mc, pc
PCL|The <fbsym>FBgn0005624==Psc</fbsym> protein localizes to the nucleus.
BODP|<fbsym>FBgn0005624==Psc</fbsym> protein is detected  associated with condensed chromosomes in the
| nuclei of the 16-nucleus embryo, and remains at high levels until
| cellularization. The levels of <fbsym>FBgn0005624==Psc</fbsym> protein are low until late
| embryogenesis, when intensestaining in the brain and ventral ganglia become
| apparent. Pole cell nuclei also contain <fbsym>FBgn0005624==Psc</fbsym> protein from the time they
| bud to their migration to the gonad during mid-embryogenesis. First instar
| larval brain and ventral ganglion contain <fbsym>FBgn0005624==Psc</fbsym> protein, and third instar
| larval imaginal discs express <fbsym>FBgn0005624==Psc</fbsym> protein. Larval polytene cell nuclei
| stain for <fbsym>FBgn0005624==Psc</fbsym> protein. <fbsym>FBgn0005624==Psc</fbsym> protein binds to about 45 sites on salivary
| gland polytene chromosomes, most of which are also binding sites for <fbsym>FBgn0003042==Pc</fbsym>
| and polyhomeotic proteins.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E <a>  <p>
|<t> E <a> pole cell <p>
|<t> E <a> central nervous system <p>
|<t> L | first instar <a> larval brain <p>
|<t> L | first instar <a> larval ventral ganglion <p>
|<t> L | third instar <a> imaginal disc <p>
|<t> L | third instar <a> embryonic/larval salivary gland <p>
CVCEL|nucleus
}

REF
{
REFM|FBrf0058093
|Martin and Adler
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001697	SYM 1 Ubx<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 13	DT 1 13 Apr 2000	RESZ 7273
ID|FBpp0001697
SYM|Ubx<up>+</up>P
ASAL|<fbsym>FBal0068484==Ubx<up>+</up></fbsym>
DT|13 Apr 2000
|10 Mar 1998
ASGN|<fbsym>FBgn0003944==Ubx</fbsym>

REFDSR
{
RDID|FBrf0042035
|Struhl and White
|1985
ASM|immunolocalization
CVBODP|<t> E | stage 15-16 <a> ventral nervous system <of> parasegment 5-13 <p>
}

REFDSR
{
RDID|FBrf0048766
|Thali et al.
|1988
HG|mammalian OTF-2
CC|<fbsym>FBgn0003944==Ubx</fbsym> protein binds to a heterologous homeotic binding site refered to as
| Octa, which is a target for mammalian OTF-2.
}

REFDSR
{
RDID|FBrf0049619
|Tremml and Bienz
|1989
BODP|<fbsym>FBgn0000095==Antp</fbsym> protein is first detected at germ band retraction stage in a 6-7 cell
| width stripe in the midgut visceral mesoderm and the ectoderm of
| parasegment 7.
ASM|immunolocalization
CVBODP|<t> E | stage 13-14 <a> visceral mesoderm <of> embryonic/larval midgut <of>
}

REFDSR
{
RDID|FBrf0049620
|Tremml and Bienz
|1989
AGT|<fbsym>FBal0003885==eve<up>3</up></fbsym>
|<fbsym>FBal0003886==eve<up>4</up></fbsym>
|<fbsym>FBal0003774==en<up>59</up></fbsym>
|<fbsym>FBal0003769==en<up>54</up></fbsym>
|<fbsym>FBal0003770==en<up>55</up></fbsym>
|<fbsym>FBal0018509==wg<up>l-17</up></fbsym>
|<fbsym>FBal0013265==opa<up>1</up></fbsym>
|<fbsym>FBal0005358==h<up>41</up></fbsym>
|<fbsym>FBal0013225==odd<up>5</up></fbsym>
|<fbsym>FBal0013967==prd<up>4</up></fbsym>
|<fbsym>FBal0032617==run<up>B102</up></fbsym>
|<fbsym>FBal0044874==Kr<up>B206</up></fbsym>
BODP|The <fbsym>UBX</fbsym> expression domain is twice as wide in homozygous <fbsym>FBgn0001077==ftz</fbsym> mutant
| embryos as in wild type. Embryos homozygous for <fbsym>FBal0003885==eve[3]</fbsym> showed no <fbsym>UBX</fbsym>
| staining but there is some staining in embryos homozygousfor <fbsym>FBal0003886==eve[4]</fbsym>.
| Normal homeotic gene function is seen in embryos homozygous for <fbsym>FBal0003774==en[59]</fbsym>,
| <fbsym>FBal0003769==en[54]</fbsym>, <fbsym>FBal0003770==en[55]</fbsym>, <fbsym>FBal0018509==wg[l-17]</fbsym>, <fbsym>FBal0013265==opa[1]</fbsym>, <fbsym>FBal0005358==h[41]</fbsym>, <fbsym>FBal0013225==odd[5]</fbsym>, <fbsym>FBal0013967==prd[4]</fbsym> and
| <fbsym>FBal0032617==run[B102]</fbsym>. No <fbsym>FBgn0003944==Ubx</fbsym> gene expression is seen in <fbsym>FBgn0001077==ftz</fbsym>,<fbsym>FBgn0003145==prd</fbsym>
| double mutant embryos, some staining is seen in <fbsym>FBgn0003002==opa</fbsym>,<fbsym>FBgn0003145==prd</fbsym>
| double mutant embryos and there is normal staining in <fbsym>FBgn0002985==odd</fbsym>
|,<fbsym>FBgn0000606==eve</fbsym> double mutant embryos. The <fbsym>UBX</fbsym> domain is in the right
| position in <fbsym>FBal0044874==Kr[B206]</fbsym> mutants, shifted posteriorly in <fbsym>FBgn0001320==kni</fbsym> mutants and
| shifted anteriorly in <fbsym>FBgn0001180==hb</fbsym> mutants.
ASM|immunolocalization
CVBODP|<t> E <a> parasegment 7 <of> visceral mesoderm <p>
}

REFDSR
{
RDID|FBrf0051363
|Immergluck et al.
|1990
BODP|The posterior <fbsym>FBgn0000490==dpp</fbsym> stripe coincides with <fbsym>FBgn0003944==Ubx</fbsym> expression in parasegment 7.
| <fbsym>FBgn0003944==Ubx</fbsym> expression is unaffected in <fbsym>FBal0003074==dpp[s4]</fbsym> embryos.
CC|<fbsym>FBgn0000490==dpp</fbsym> expression is dependent on <fbsym>FBgn0003944==Ubx</fbsym> in parasegment 7 of the visceral mesoderm.
}

REFDSR
{
RDID|FBrf0051545
|Panganiban et al.
|1990
BODP|Mutations in the shv region of <fbsym>FBgn0000490==dpp</fbsym> cause a range of effects on <fbsym>FBgn0003944==Ubx</fbsym>
| expression. Generally, the <fbsym>FBgn0003944==Ubx</fbsym> expression domain is narrowed or the <fbsym>FBgn0003944==Ubx</fbsym>
| protein level is reduced. <fbsym>FBgn0000014==abd-A</fbsym> mutationscause expansion of the domain of
| <fbsym>FBgn0003944==Ubx</fbsym> expression in the visceral mesoderm to include the entire posterior midgut.
ASM|immunolocalization
}

REFDSR
{
RDID|FBrf0051550
|Macias et al.
|1990
BODP|In <fbsym>FBgn0000014==abd-A</fbsym>[-] embryos, <fbsym>FBgn0003944==Ubx</fbsym> protein levels are higher than in wild type
| embryos in posterior compartments of metameres of the <fbsym>FBgn0000014==abd-A</fbsym> domain
| suggesting that <fbsym>FBgn0000014==abd-A</fbsym> downregulates <fbsym>FBgn0003944==Ubx</fbsym> in these domains.
CVBODP|<t> E <a>  <p>
}

REFDSR
{
RDID|FBrf0055887
|Noordermeer et al.
|1992
AGT|<fbsym>FBal0013024==nkd<up>2</up></fbsym>
BODP|In <fbsym>wg[hs.P]</fbsym> embryos, after heat shock, <fbsym>FBgn0003944==Ubx</fbsym> protein is only seen in those
| cells that do not express <fbsym>FBgn0000577==en</fbsym>. This is a similar expression pattern to
| that found in <fbsym>FBgn0002945==nkd</fbsym> mutant embryos.
ASM|immunolocalization
}

REFDSR
{
RDID|FBrf0056121
|Johnson and Krasnow
|1992
CC|In vitro studies showed that <fbsym>FBgn0003944==Ubx</fbsym> and <fbsym>FBgn0000606==eve</fbsym> proteins exert active and
| opposite effects on in vitro transcription when bound to a common site
| upstream of a target (<fbsym>FBgn0000055==Adh</fbsym>) core promoter: <fbsym>UBX</fbsym> acts as an
| activator and EVE acts as a repressor, and both affect the extent of
| preinitiation complex formation. A subsequent step renders mature complexes
| transiently refractory to activation and repression.
}

REFDSR
{
RDID|FBrf0058983
|Paro and Zink
|1992
CC|Gel-shift analysis shows specific binding of <fbsym>FBgn0003944==Ubx</fbsym> protein to fragments from
| the <fbsym>FBgn0003042==Pc</fbsym> gene region.
}

REFDSR
{
RDID|FBrf0059253
|Thuringer and Bienz
|1993
AGT|<fbsym>FBal0036008==wg<up>hs.PN</up></fbsym>
|<fbsym>FBal0031073==dpp<up>hs.PT</up></fbsym>
BODP|Ubiquitously expressed <fbsym>FBgn0004009==wg</fbsym> leads to the anterior expansion of the domain of
| <fbsym>FBgn0003944==Ubx</fbsym> expression in the visceral mesoderm to encompass parasegments 6 and
| 7. Ubiquitous <fbsym>FBgn0000490==dpp</fbsym> has no effect on the domain of <fbsym>FBgn0003944==Ubx</fbsym> expression.
ASM|immunolocalization
}

REFDSR
{
RDID|FBrf0063844
|Rowe and Akam
|1988
ASTR|<fbsym>FBtr0005414==Ubx<up>+</up>R3.2</fbsym>
|<fbsym>FBtr0005415==Ubx<up>+</up>R4.3</fbsym>
}

REFDSR
{
RDID|FBrf0076031
|Chan et al.
|1994
CC|Utilizing a short probe from the <fbsym>FBgn0000490==dpp</fbsym> visceral mesoderm midgut enhancer
| element, the authors showed through electromobility shift assays that both
| <fbsym>FBgn0003944==Ubx</fbsym> and <fbsym>FBgn0000611==exd</fbsym> proteins bound <fbsym>FBgn0000490==dpp</fbsym> DNA.  The binding of either of these
| proteins is synergistically enhanced in the presence of the other.
|  Furhtermore, wildtype function of <fbsym>FBgn0003944==Ubx</fbsym> is required and sufficient to
| activate <fbsym>FBgn0000490==dpp</fbsym> expression in the visceral mesoderm.
}

REF
{
REFM|FBrf0042035
|Struhl and White
|1985
REFM|FBrf0048766
|Thali et al.
|1988
REFM|FBrf0049619
|Tremml and Bienz
|1989
REFM|FBrf0049620
|Tremml and Bienz
|1989
REFM|FBrf0051363
|Immergluck et al.
|1990
REFM|FBrf0051545
|Panganiban et al.
|1990
REFM|FBrf0051550
|Macias et al.
|1990
REFM|FBrf0055887
|Noordermeer et al.
|1992
REFM|FBrf0056121
|Johnson and Krasnow
|1992
REFM|FBrf0058983
|Paro and Zink
|1992
REFM|FBrf0059253
|Thuringer and Bienz
|1993
REFM|FBrf0063844
|Rowe and Akam
|1988
REFM|FBrf0076031
|Chan et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001725	SYM 1 mle<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 578
ID|FBpp0001725
SYM|mle<up>+</up>PA
ASAL|<fbsym>FBal0070649==mle<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002774==mle</fbsym>

REFDSR
{
RDID|FBrf0068422
|Bone et al.
|1994
ABOD|polyclonal
PCL|<fbsym>FBgn0002774==mle</fbsym> protein binds to the same sites on the male X chromosome as <fbsym>FBgn0005617==msl-1</fbsym>
| protein. The pattern of binding of H4Ac16 along the X chromosome is largely
| coincident with that of <fbsym>FBgn0002774==mle</fbsym> and <fbsym>FBgn0005617==msl-1</fbsym>.
CVCEL|chromosome
}

REF
{
REFM|FBrf0068422
|Bone et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001728	SYM 1 CycE<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 4	DT 1 20 Mar 1998	RESZ 3235
ID|FBpp0001728
SYM|CycE<up>+</up>P
ASAL|<fbsym>FBal0066527==CycE<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0010382==CycE</fbsym>

REFDSR
{
RDID|FBrf0068557
|Knoblich et al.
|1994
CC|Coimmunoprecipitation experiments show that <fbsym>FBgn0010382==CycE</fbsym> protein specifically
| associates with <fbsym>FBgn0004106==cdc2</fbsym> kinase.
}

REFDSR
{
RDID|FBrf0082560
|Sauer et al.
|1995
PCL|<fbsym>FBgn0010382==CycE</fbsym> protein is present throughout the early embryonic cycles. It is
| predominantly nuclear during interphase and becomes dispersed in the
| cytoplasm during mitosis. Two types of <fbsym>FBgn0010382==CycE</fbsym> protein are observed by
| immunoblotting. Theform with the lower mobility is maximal during mitosis.
| The higher mobility form is abundant in G[[2]] and is nearly absent during
| M and early S phases.
ASM|immunolocalization
|western blot
CC|<fbsym>FBgn0010382==CycE</fbsym> protein is the major partner of <fbsym>FBgn0004107==cdc2c</fbsym> protein. <fbsym>FBgn0010382==CycE</fbsym> and <fbsym>FBgn0004107==cdc2c</fbsym>
| kinase activity are present throughout the cell cycle.
}

REFDSR
{
RDID|FBrf0084309
|Richardson et al.
|1995
ABOD|mc,pc
BODP|<fbsym>FBgn0010382==CycE</fbsym> protein is present in embryos in mitotically proliferating and
| endoreplicating cells. In larval optic lobes, the pattern of <fbsym>FBgn0010382==CycE</fbsym> protein
| expression is similar to the pattern of S phases. It is present in the
| outer opticanlage, the inner optic anlage, and in a band corresponding to
| the S phase lamina precursor cells. It is absent in G[[1]] phase lamina
| precursor cells. It is also present in a region of the lamina where only a
| portion of the cells are in S phase. In the eye imaginal disc, <fbsym>FBgn0010382==CycE</fbsym>
| protein is present in a subset of the asynchronously proliferating cells
| and in a band of cells just posterior to the morphogenetic furrow that are
| in S phase but not in G[[1]] cells within and anterior to the furrow. In
| summary, <fbsym>FBgn0010382==CycE</fbsym> protein is absent in G[[1]] phase cells but appears at the
| onset of S phase in proliferating cells of the larval optic lobe and eye
| imaginal disc.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L <a> outer optic anlagen <p>
|<t> L <a> inner optic anlagen <p>
|<t> L <a> lamina anlagen <p>
|<t> L <a> eye-antennal disc | restricted <p>
|<t> L <a> morphogenetic furrow | posterior to <p>
}

REFDSR
{
RDID|FBrf0090669
|Lilly and Spradling
|1996
BODP|<fbsym>FBgn0010382==CycE</fbsym> protein is expressed at varying levels (suggesting cycling) in both
| nurse cells and follicle cells. Within individual egg chambers, nurse cell
| nuclei with high, intermediate or low (to undetectable) levels of <fbsym>FBgn0010382==CycE</fbsym>
| protein are observed. Levels are always high in the germinal vesicle and
| increase as egg chambers develop.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> O,A <a> nurse cell <p>
|<t> O,A <a> follicle cell <p>
|<t> O,A <a> germinal vesicle <p>
}

REF
{
REFM|FBrf0068557
|Knoblich et al.
|1994
REFM|FBrf0082560
|Sauer et al.
|1995
REFM|FBrf0084309
|Richardson et al.
|1995
REFM|FBrf0090669
|Lilly and Spradling
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001733	SYM 1 Csp<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 1080
ID|FBpp0001733
SYM|Csp<up>+</up>P
ASAL|<fbsym>FBal0066519==Csp<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0004179==Csp</fbsym>

REFDSR
{
RDID|FBrf0068753
|Zinsmaier et al.
|1994
ABOD|monoclonal
BODP|<fbsym>FBgn0004179==Csp</fbsym> protein is detected presynaptically at larval and adult neuromuscular
| junctions. Synaptic boutons are strongly stained. In the CNS, Synapse rich
| regions of the neuropil are stained, but the surrounding cell bodies are
| not. One isoform is detected predominantly in photoreceptor terminals but
| not at motor nerve terminals. <fbsym>FBgn0004179==Csp</fbsym> protein is thought to be associated
| with synaptic vesicles.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L <a> neuromuscular junction <p>
|<t> A <a> neuromuscular junction <of> adult thorax <p>
|<t> A <a> bouton <p>
|<t> A <a> neuropil <p>
|<t> A <a> lamina neuropil <p>
|<t> A <a> medulla neuropil <p>
|<t> A <a> lobula plate neuropil <p>
|<t>A <a> synaptic vesicle <p>
|<t> A <a> photoreceptor cell <p>
}

REF
{
REFM|FBrf0068753
|Zinsmaier et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001751	SYM 1 cact<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 4	DT 1 21 Nov 2000	RESZ 3844
ID|FBpp0001751
SYM|cact<up>+</up>P
ASAL|<fbsym>FBal0068728==cact<up>+</up></fbsym>
DT|21 Nov 2000
|10 Mar 1998
ASGN|<fbsym>FBgn0000250==cact</fbsym>

REFDSR
{
RDID|FBrf0073424
|Isoda and Nusslein-Volhard
|1994
CC|Disulfide crosslinking studies were used to show that <fbsym>FBgn0000462==dl</fbsym> and <fbsym>FBgn0000250==cact</fbsym>
| proteins exist as three different complexes in the embyro. Complex 1
| (190kD) is a <fbsym>FBgn0000462==dl</fbsym> homodimer (dl[[2]]). Complex 2 (270kD) consists of a
| complex 1 and a <fbsym>FBgn0000250==cact</fbsym> molecule (dl[[2]]cact). Complex 3 is a <fbsym>FBgn0000250==cact</fbsym>
| protein complex.
}

REFDSR
{
RDID|FBrf0079887
|Belvin et al.
|1995
CC|<fbsym>FBgn0000250==cact</fbsym> protein is rapidly degraded in response to the dorsal-ventral
| signalling pathway. The degradation does not require the presence of <fbsym>FBgn0000462==dl</fbsym>
| protein. More stable mutant forms of the protein block signalling. Protein
| stability is regulated by two independent processes. Ankyrin repeats at the
| amino-terminal end of the protein are required for signal-dependent
| degradation while the carboxy-terminal end of the protein (which includes a
| PEST sequence) is required for signal-independent degradation of free
| <fbsym>FBgn0000250==cact</fbsym> protein.
}

REFDSR
{
RDID|FBrf0090754
|Reach et al.
|1996
ABOD|polyclonal
BODP|The level of <fbsym>FBgn0000250==cact</fbsym> protein in 0-3hr embyros of three genetic backgrounds
| was studied. One is dorsalventral signal constitutive
| (<fbsym>FBal0016833==Tl[8]</fbsym>), one wild type, and one signal deficient
| (<fbsym>FBal0005010==gd[2]</fbsym>). <fbsym>FBgn0000250==cact</fbsym> levelsare lowest in the signal constitutive
| mutant, intermediate in wild type, and highest in signal deficient embryos.
| These differences are apparent as early as stage 2. Furthermore, <fbsym>FBgn0000250==cact</fbsym>
| protein is present in a dorsoventral gradient. High levels of protein are
| present in the dorsal cytoplasm where no intracellular signal transduction
| occurs and little protein is found in the ventral cytoplasm where
| signalling is strongest. In <fbsym>FBal0016833==Tl[8]</fbsym> and <fbsym>FBal0005010==gd[2]</fbsym> embryos, <fbsym>FBgn0000250==cact</fbsym> protein
| levels are uniformly low or high respectively.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | early <a>  <p> dorsal ventral gradient
CC|<fbsym>FBgn0000250==cact</fbsym> regulation was reconstituted in SL2 cells. Immunoblot and
| immunoprecipitation experiments indicate that <fbsym>FBgn0010441==pll</fbsym> protein induces the
| spatially graded degradation of <fbsym>FBgn0000250==cact</fbsym> protein. This response is dependent
| on the presence of a motif in <fbsym>FBgn0000250==cact</fbsym> protein which resembles sites of
| signal-dependent phosphorylation in vertebrate homologs. Substitution of
| the four serines in this motif at positions 74, 78, 82, and 83 with
| nonphosphorylatable alanine results in a form of <fbsym>FBgn0000250==cact</fbsym> protein that is
| resistant to <fbsym>FBgn0010441==pll</fbsym>-protein-induced degradation. Mutation of individual
| sites indicates that no single site is absolutely required and that all
| sites are not equal. Mutation of the four potential phosphorylation sites
| renders <fbsym>FBgn0000250==cact</fbsym> resistant to signal-dependent degredation in embryos as well.
}

REFDSR
{
RDID|FBrf0125338
|Bhaskar et al.
|2000
CC|<fbsym>FBgn0010602==lwr</fbsym> protein releives the inhibition of <fbsym>FBgn0000462==dl</fbsym> protein nuclear uptake by
| <fbsym>FBgn0000250==cact</fbsym> protein in cultured cells.
}

REF
{
REFM|FBrf0073424
|Isoda and Nusslein-Volhard
|1994
REFM|FBrf0079887
|Belvin et al.
|1995
REFM|FBrf0090754
|Reach et al.
|1996
REFM|FBrf0125338
|Bhaskar et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001770	SYM 1 trx<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 1848
ID|FBpp0001770
SYM|trx<up>+</up>P
ASAL|<fbsym>FBal0071404==trx<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003862==trx</fbsym>

REFDSR
{
RDID|FBrf0076508
|Kuzin et al.
|1994
PCL|<fbsym>FBgn0003862==trx</fbsym> protein strongly binds to 16 specific sites along the polytene
| chromosomes. Among these is the <fbsym>FBgn0000659==fkh</fbsym> gene region.
BODP|<fbsym>FBgn0003862==trx</fbsym> protein is present at high levels in the embryonic CNS. It is also
| observed in a variety of tissues in larvae including imaginal discs,
| salivary glands, and gut tissues. Staining is weak in the brain and ventral
| ganglia. <fbsym>FBgn0003862==trx</fbsym> protein is expressed in most nuclei in the eye-antennal disc
| but is expressed predominantly in the posterior regions of the wing,
| haltere, and mesothoracic leg discs.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> dorsal mesothoracic disc | posterior <p>
|<t> L | third instar <a> dorsal metathoracic disc | posterior <p>
|<t> L | third instar <a> eye-antennal disc <p>
|<t> L | third instar <a> ventral mesothoracic disc | posterior <p>
|<t> L | third instar <a> imaginal disc <p>
|<t> L | third instar <a> embryonic/larval digestive system <p>
|<t> L | third instar <a> Malpighian tubule <p>
|<t> L | third instar <a> gastric caecum <p>
|<t> L | third instar <a> embryonic/larval midgut <p>
|<t> L | third instar <a> embryonic/larval proventriculus <p>
|<t> L | third instar <a> embryonic/larval salivary gland <p>
CVCEL|nucleus
|polytene chromosome
CC|<fbsym>FBgn0003862==trx</fbsym> gene product binds within an 8.4kb regulatory region of the <fbsym>FBgn0000659==fkh</fbsym> gene
| that directs embryonic expression. It also binds to ectopic sites carrying
| these sequences in transformed lines.
}

REF
{
REFM|FBrf0076508
|Kuzin et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001771	SYM 1 Pu<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 787
ID|FBpp0001771
SYM|Pu<up>+</up>P
ASAL|<fbsym>FBal0068211==Pu<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003162==Pu</fbsym>

REFDSR
{
RDID|FBrf0076754
|Chen et al.
|1994
ABOD|polyclonal
BODP|The <fbsym>FBgn0003162==Pu</fbsym> protein is detected in the nurse cell cytoplasm in stage S10B of
| oogenesis, and has been transferred to granules in the oocyte cytoplasm at
| stage S14 of oogenesis. The level of <fbsym>FBgn0003162==Pu</fbsym> protein is high in the
| unfertilized egg, declines through early embryogenesis, and is not detected
| after cellularization.
ASM|immunolocalization
CVBODP|il<t> E | early <a> yolk granule <p>
CC|The <fbsym>FBgn0003162==Pu</fbsym> antibody detects a 52 kD protein in 0-2 hr embryos.
}

REF
{
REFM|FBrf0076754
|Chen et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001777	SYM 1 &agr;-Spec<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 573
ID|FBpp0001777
SYM|&agr;-Spec<up>+</up>PA
ASAL|<fbsym>FBal0066293==&agr;-Spec<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003470==&agr;-Spec</fbsym>

REFDSR
{
RDID|FBrf0077251
|Viel and Branton
|1994
CC|The regions of the tail ends of the <fbsym>&agr;-Spec</fbsym> and &bgr;-Spec@ chains that
| are necessary for interchain binding were mapped in vitro. Segments 20 and
| 21 and part of 22 of the &agr; chain and segments 2 and 3 and part of 1 of
| the &bgr; chain are required for interchain binding.
}

REF
{
REFM|FBrf0077251
|Viel and Branton
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001786	SYM 1 tkv<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 20 Mar 1998	RESZ 554
ID|FBpp0001786
SYM|tkv<up>+</up>P
ASAL|<fbsym>FBal0071387==tkv<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003716==tkv</fbsym>

REFDSR
{
RDID|FBrf0080209
|Letsou et al.
|1995
CC|<fbsym>FBgn0003169==put</fbsym> protein binds BMP2 in concert with <fbsym>FBgn0003716==tkv</fbsym>, forming heteromeric receptor
| complexes in COS1 cell transient assays.
}

REFDSR
{
RDID|FBrf0104902
|Haerry et al.
|1998
ASTR|<fbsym>FBtr0000825==tkv<up>+</up>R</fbsym>
}

REF
{
REFM|FBrf0080209
|Letsou et al.
|1995
REFM|FBrf0104902
|Haerry et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001787	SYM 1 ovo<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 2457
ID|FBpp0001787
SYM|ovo<up>+</up>P
ASAL|<fbsym>FBal0070857==ovo<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003028==ovo</fbsym>

REFDSR
{
RDID|FBrf0080251
|Mevel-Ninio et al.
|1995
PCL|The <fbsym>FBgn0003028==ovo</fbsym> protein is detected in germ cell nuclei, and may be associated
| with chromatin.
BODP|An <fbsym>FBgn0003028==ovo</fbsym>-<fbsym>lacZ</fbsym> fusion protein (hereafter referred to as <fbsym>FBgn0003028==ovo</fbsym>
| protein) is detected in female germ cell nuclei early in oogenesis. The
| protein accumulates in nurse cell nuclei until stage 10, after which time
| it is seen in the oocyte nucleus. During embryogenesis, the <fbsym>FBgn0003028==ovo</fbsym> protein
| is at first expressed at high levels throughout the embryo, and this
| general expression, decreases greatly by stage 8, when the specific
| expression of <fbsym>FBgn0003028==ovo</fbsym> protein in pole cell nuclei becomes apparent. <fbsym>FBgn0003028==ovo</fbsym>
| protein expression persists in pole cell nuclei through embryonic
| development, and continues until the incorporation of the pole cells into
| the developing gonads at stage 14. From this stage onwards, <fbsym>FBgn0003028==ovo</fbsym> protein
| is detected in the developing gonads, and at stage 17, <fbsym>FBgn0003028==ovo</fbsym> protein
| staining is seen in the nuclei of the germ cells in the gonads. The <fbsym>FBgn0003028==ovo</fbsym>
| protein is detected in the nuclei of germ cells in female first instar
| larvae, but its expression becomes limited to a subpopulation of these
| cells in female second and third instar larvae. In male second and third
| instar larvae, <fbsym>FBgn0003028==ovo</fbsym> protein staining is seen in the anterior of the gonad,
| and in the adult male, staining is seen at the tip of the testis, in the
| nuclei of presumptive stem cells and cysts.
CVBODP|<t> O,A <a> female germline stem cell <p>
|<t> O,A | stage 8 <a> nurse cell <p>
|<t> O,A | stage 10 <a> oocyte  <p>
|<t> E | blastoderm <a>  <p> ubiquitous
|<t> E | stage 8-14 <a> pole cell <p>
|<t> E | stage 17 <a> germ cell | nucleus <p>
|<t> O,L | first instar <a> female germline stem cell <p>
|<t> L | first instar <a> gonad  <p>
|<t> O,L | second instar <a> female germline stem cell | restricted <p>
|<t> O,L | third instar <a> female germline stem cell | restricted <p>
|<t> A,S <a> male germline stem cell <p>
CVCEL|nucleus
}

REF
{
REFM|FBrf0080251
|Mevel-Ninio et al.
|1995
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001793	SYM 1 mnb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 988
ID|FBpp0001793
SYM|mnb<up>+</up>P
ASAL|<fbsym>FBal0070653==mnb<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002777==mnb</fbsym>

REFDSR
{
RDID|FBrf0080444
|Tejedor et al.
|1995
BODP|<fbsym>FBgn0002777==mnb</fbsym> protein is most prominent in the mushroom body neuropil and the outer
| proliferation centers of the optic lobes in the larval brain. In adult
| brains, the level of <fbsym>FBgn0002777==mnb</fbsym> protein is low in the optic lobes and central
| brain hemispheres but is high in retinal pigment cells as well as in the
| &agr;, &bgr;, and &ggr; cells and the peduncle of the mushroom bodies.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L <a> corpora pedunculata <p>
|<t> L <a> outer optic anlagen <p>
|<t> L <a> larval optic lobe <p>
|<t> A <a> &agr;-lobe <p>
|<t> A <a> &bgr;-lobe <p>
|<t> A <a> &ggr;-lobe <p>
|<t> A <a> corpora pedunculata <p>
|<t> A <a> retina <p>
|<t> A<a> pigment cell <p>
}

REF
{
REFM|FBrf0080444
|Tejedor et al.
|1995
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001812	SYM 1 sr<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 187
ID|FBpp0001812
SYM|sr<up>+</up>P
ASAL|<fbsym>FBal0071143==sr<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003499==sr</fbsym>

REF
{
REFM|FBrf0084118
|Lee et al.
|1995
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001825	SYM 1 psq<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 1017
ID|FBpp0001825
SYM|psq<up>+</up>P
ASAL|<fbsym>FBal0070921==psq<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0004399==psq</fbsym>

REFDSR
{
RDID|FBrf0086124
|Weber et al.
|1995
ABOD|polyclonal
PCL|<fbsym>FBgn0004399==psq</fbsym> protein localizes to the nucleus.
BODP|In the eye-antennal disc <fbsym>FBgn0004399==psq</fbsym> protein localizes to ommatidial precluster
| cells, with highest levels in R3 and R4. In the larval wing disc, in
| addition to the overall low expression, there is a region of high <fbsym>FBgn0004399==psq</fbsym>
| protein expression in the wing blade primordium.
CVBODP|<t> L <a> eye-antennal disc | restricted <p>
|<t> L <a> dorsal mesothoracic disc <p>
CVCEL|nucleus
CC|The BTB-domain is predicted for the products of the class A transcripts
| (<fbsym>FBtr0001424==psq[+]R7.0A1</fbsym> and <fbsym>FBtr0001425==psq[+]R7.0A2</fbsym>) only, <fbsym>FBpp0001060==psq[+]P1085</fbsym> and
| <fbsym>FBpp0001061==psq[+]P535</fbsym>.
}

REF
{
REFM|FBrf0086124
|Weber et al.
|1995
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001876	SYM 1 fru<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 771
ID|FBpp0001876
SYM|fru<up>+</up>P
ASAL|<fbsym>FBal0068967==fru<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0004652==fru</fbsym>

REFDSR
{
RDID|FBrf0091159
|Ryner et al.
|1996
CC|Multiple <fbsym>FBgn0004652==fru</fbsym> proteins are produced from alternatively spliced <fbsym>FBgn0004652==fru</fbsym>
| transcripts. A female-specific form of <fbsym>FBgn0004652==fru</fbsym> protein lacks 101 N-terminal
| amino acids present in a male-specific <fbsym>FBgn0004652==fru</fbsym> protein. Differences are also
| found in the zinc finger pairs present at the carboxy terminus. In related
| proteins, these zinc finger pairs confer distinct DNA-binding specificity
| and are expressed in cell-specific patterns.
}

REF
{
REFM|FBrf0091159
|Ryner et al.
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001942	SYM 1 DNA-ligI<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 20 Mar 1998	RESZ 1220
ID|FBpp0001942
SYM|DNA-ligI<up>+</up>PA
ASAL|<fbsym>FBal0066545==DNA-ligI<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0013774==DNA-ligI</fbsym>

REFDSR
{
RDID|FBrf0046241
|Takahashi and Senshu
|1987
PCL|DNA-LIGI is found in the cytoplasmic fraction of embryonic extracts.
BODP|Activity was high in 0-4hr embryos, lower in 8hr embryos and undetectable in
| 16hr embryos.
ASM|enzyme assay or biochemical detection
CVBODP|<t> E | early-mid <a>  <p>
CVCEL|cytoplasm
CC|The properties of two DNA ligases purified from embryos were compared. The
| enzymes differ in size, thermostability, affinity for ATP, Km, and optimal
| reaction conditions (salt optima, requirement for DTT, and reaction to
| PVA). They are similar in requirement for ATP as cofactor and Mg[2+] as
| divalent cation, inhibition by N-ethylmaleimide, optimal ligation temp, and
| substrate specificity. The AMP-adducts have molecular weights of 86kD and 75kD.
}

REFDSR
{
RDID|FBrf0046586
|Rabin and Chase
|1987
CC|The substrate specificity and mechanism of action of DNA-lig are described.
| The joining reactions is shown to be reversible.
}

REF
{
REFM|FBrf0046241
|Takahashi and Senshu
|1987
REFM|FBrf0046586
|Rabin and Chase
|1987
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001943	SYM 1 DNA-ligII<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 889
ID|FBpp0001943
SYM|DNA-ligII<up>+</up>PA
ASAL|<fbsym>FBal0066546==DNA-ligII<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0013775==DNA-ligII</fbsym>

REFDSR
{
RDID|FBrf0046241
|Takahashi and Senshu
|1987
PCL|DNA-ligII is concentrated in the nucleus.
BODP|Activity was detected throughout embryogenesis.
ASM|enzyme assay or biochemical detection
CVCEL|nucleus
CC|The properties of two DNA ligases purified from embryos were compared. The
| enzymes differ in size, thermostability, affinity for ATP, Km, and optimal
| reaction conditions (salt optima, requirement for DTT, and reaction to
| PVA). They are similar in requirement for ATP as cofactor and Mg[2+] as
| divalent cation, inhibition by N-ethylmaleimide, optimal ligation temp, and
| substrate specificity. The major AMP-adduct has a molecular weight of 70kD.
}

REF
{
REFM|FBrf0046241
|Takahashi and Senshu
|1987
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001951	SYM 1 Sxl<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 3	DT 1 22 Aug 2000	RESZ 1429
ID|FBpp0001951
SYM|Sxl<up>+</up>P
ASAL|<fbsym>FBal0068426==Sxl<up>+</up></fbsym>
DT|22 Aug 2000
|10 Mar 1998
ABODURL|m114.html M114
|m182a.html M18
ASGN|<fbsym>FBgn0003659==Sxl</fbsym>

REFDSR
{
RDID|FBrf0051358
|Parkhurst et al.
|1990
BODP|<fbsym>FBgn0003659==Sxl</fbsym> is normally expressed uniformly in female embryos starting from early
| blastoderm stages and is not expressed in male embryos. In <fbsym>h[hb.P]</fbsym>
| embryos, the ectopic <fbsym>FBgn0001168==h</fbsym> protein suppresses <fbsym>FBgn0003659==Sxl</fbsym> in the anterior of the
| embryo resulting in its expression only at the posterior end in female
| embryos. In <fbsym>sc[hb.P]</fbsym> embryos, ectopic <fbsym>FBgn0004170==sc</fbsym> protein causes ectopic <fbsym>FBgn0003659==Sxl</fbsym>
| expression in the anterior end of male embryos.
ASM|immunolocalization
CVBODP|<t> E | female <a>  <p> 0-100% egg length
}

REFDSR
{
RDID|FBrf0055582
|Younger-Shepherd et al.
|1992
CC|<fbsym>FBgn0003659==Sxl</fbsym> expression is derepressed in <fbsym>FBgn0010109==dpn</fbsym> null male embryos while the female
| embryo expression pattern is unchanged. <fbsym>FBgn0003659==Sxl</fbsym> was also misexpressed in
| embryos with altered dosage of the <fbsym>FBgn0010109==dpn</fbsym> and <fbsym>FBgn0004170==sc</fbsym> genes.
}

REF
{
REFM|FBrf0051358
|Parkhurst et al.
|1990
REFM|FBrf0055582
|Younger-Shepherd et al.
|1992
REFM|FBrf0111851
|Dong and Bell
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001956	SYM 1 Ddc<up>+</up>P	AAL 1 -	PSZ 1 56 	HG 1 -	DBA 1 -	REF 1 7	DT 1 22 Aug 2000	RESZ 3604
ID|FBpp0001956
SYM|Ddc<up>+</up>P
ASAL|<fbsym>FBal0066711==Ddc<up>+</up></fbsym>
DT|22 Aug 2000
|10 Mar 1998
ASGN|<fbsym>FBgn0000422==Ddc</fbsym>

REFDSR
{
RDID|FBrf0037051
|Hirsh and Davidson
|1981
PSZ|60 | observed
BODP|<fbsym>FBgn0000422==Ddc</fbsym> protein enzymatic activity levels rise during late larval stages, are
| highest during the pre-pupal stage of development, and rise again prior to
| ecolsion after a decrease in activity.
ASM|enzyme assay or biochemical detection
CVBODP|enzyme assay or biochemical detection
|<t> L | third instar-A <a> <p>
ASTR|<fbsym>FBtr0001949==Ddc<up>+</up>R2.1</fbsym>
}

REFDSR
{
RDID|FBrf0042353
|Gietz and Hodgetts
|1985
BODP|<fbsym>FBgn0000422==Ddc</fbsym> activity reaches a maximum late in embryogenesis and persists into
| first instar larvae. It does not parallel ecdysone activity which is at a
| maximum at midembryogenesis.
}

REFDSR
{
RDID|FBrf0046010
|Konrad and Marsh
|1987
PSZ|56 | observed
ABOD|polyclonal
BODP|Immunolocalization experiments using an anti-<fbsym>FBgn0000422==Ddc</fbsym> antibody
| indicate that <fbsym>FBgn0000422==Ddc</fbsym> protein is expressed in the epidermis and the nervous
| system of the third instar larva and adult. A segmentally repeated pattern
| of staining is seenin the larval ventral ganglion and brain.  A subset of
| the <fbsym>FBgn0000422==Ddc</fbsym>-positive cells match the pattern of serotonin-containing cells.
| The staining in the adult hindgut and oviduct is likely to be due neurons
| associated with these structures.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L <a> ring gland <p>
|<t> L | third instar stage 2 <a> epidermis <p>
|<t> L | third instar <a> larval brain | restricted <p>
|<t> L | third instar <a> larval stomatogastric nervous system <p>
|<t> L | third instar <a> frontal ganglion <p>
|<t> L | third instar <a> recurrent nerve <p>
|<t> L | third instar <a> larval ventricular ganglion <p>
|<t> L | third instar <a> larval ventral ganglion <p>
|<t> L | third instar <a> larval maxillary nerve  <p>
|<t> A <a> thoracic ganglion | restricted <p>
|<t> A <a> adult brain | restricted <p>
|<t> A <a> adult hindgut <p>
|<t> A | female <a> oviduct <p>
}

REFDSR
{
RDID|FBrf0046284
|Beall and Hirsh
|1987
ABOD|polyclonal
BODP|In third instar larvae, <fbsym>FBgn0000422==Ddc</fbsym> protein localizes to approximately 125
| neurons, and a subset of glial cells. About 80 of the 125 neurons also
| stain for serotonin.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> larval central nervous system <p>
|<t> L | third instar <a> neuron | subset <p>
|<t> L | third instar <a> glial cell | subset <p>
}

REFDSR
{
RDID|FBrf0053728
|Walter et al.
|1991
BODP|<fbsym>FBgn0000422==Ddc</fbsym> activity was investigated in whole imagos and in developing wings. In
| the whole imago, activity increases steadily between 64 hours after
| pupariation and eclosion. In wings, there is a peak of activity at 76 hrs
| which correlates with the time when the wing microchaetae and hairs have
| become fully melanized.
ASM|enzyme assay or biochemical detection
}

REFDSR
{
RDID|FBrf0082387
|Mukhopadhyay and Campos
|1995
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> larval brain | restricted <p>
|<t> L | third instar <a> LP1 neuron <p>
}

REF
{
REFM|FBrf0037051
|Hirsh and Davidson
|1981
REFM|FBrf0042353
|Gietz and Hodgetts
|1985
REFM|FBrf0046010
|Konrad and Marsh
|1987
REFM|FBrf0046284
|Beall and Hirsh
|1987
REFM|FBrf0053728
|Walter et al.
|1991
REFM|FBrf0082387
|Mukhopadhyay and Campos
|1995
REFM|FBrf0108469
|Tatarenkov et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0001974	SYM 1 Gal<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 453
ID|FBpp0001974
SYM|Gal<up>+</up>PA
ASAL|<fbsym>FBal0067828==Gal<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0001089==Gal</fbsym>

REFDSR
{
RDID|FBrf0054708
|Knipple et al.
|1991
BODP|GAL activity was detected in pupal and adult stages but not in larvae.
ASM|enzyme assay or biochemical detection
CVBODP|<t> P <a>  <p>
|<t> A <a>  <p>
ASTR|<fbsym>FBtr0002010==Gal<up>+</up>R2.3</fbsym>
}

REF
{
REFM|FBrf0054708
|Knipple et al.
|1991
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002004	SYM 1 qrt<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 394
ID|FBpp0002004
SYM|qrt<up>+</up>PA
ASAL|<fbsym>FBal0070940==qrt<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003185==qrt</fbsym>

REFDSR
{
RDID|FBrf0047839
|Cheney and Lang
|1988
CC|The <fbsym>FBgn0003185==qrt</fbsym> protein is thought to encode a protein modifying enzyme since
| mutants show protein modification defects.
}

REF
{
REFM|FBrf0047839
|Cheney and Lang
|1988
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002027	SYM 1 sli<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 3	DT 1 6 Jan 2000	RESZ 1415
ID|FBpp0002027
SYM|sli<up>+</up>P
ASAL|<fbsym>FBal0071062==sli<up>+</up></fbsym>
DT|6 Jan 2000
|10 Mar 1998
ABODURL|c555.6d.html C555.6D
ASGN|<fbsym>FBgn0003425==sli</fbsym>

REFDSR
{
RDID|FBrf0047629
|Rothberg et al.
|1988
ABOD|polyclonal
BODP|<fbsym>FBgn0003425==sli</fbsym> protein is first detected in the midline neurepithelium after germ
| band extension. During germ band shortening, expression becomes restricted
| to median ectodermal cells (MECs). After germ band contraction is complete,
| <fbsym>FBgn0003425==sli</fbsym>protein is detected in MECs, the axon commissures they surround, and
| longitudinal connectives. In supraesophageal segments, strong axon
| labelling is detected, and this labelling seems to be on the cell surface.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | extended germ band stage <a> ventral midline <p>
|<t> E | contracted germ band stage <a> longitudinal connectives | restricted <p>
|<t> E | contracted germ band stage <a> axon <of> embryonic central nervous system <p>
CVCEL|plasma membrane
}

REFDSR
{
RDID|FBrf0107628
|Brose et al.
|1999
CC|Like its mammalian counterparts, the full-length <fbsym>FBgn0003425==sli</fbsym> protein may be
| proteolytically processed to give a 55-60 kD C-terminal fragment and a 140
| kD N-terminal fragment.
}

REF
{
REFM|FBrf0047629
|Rothberg et al.
|1988
REFM|FBrf0056064
|Patthy
|1992
REFM|FBrf0107628
|Brose et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002029	SYM 1 nonA<up>+</up>P	AAL 1 -	PSZ 1 80	HG 1 -	DBA 1 -	REF 1 2	DT 1 12 Feb 2001	RESZ 944
ID|FBpp0002029
SYM|nonA<up>+</up>P
ASAL|<fbsym>FBal0070828==nonA<up>+</up></fbsym>
DT|12 Feb 2001
|10 Mar 1998
ASGN|<fbsym>FBgn0004227==nonA</fbsym>

REFDSR
{
RDID|FBrf0056578
|Rendahl et al.
|1992
PSZ|80
ABOD|polyclonal
PCL|NONA@ is nuclear except in early embryos prior to cellular blastoderm stage
| where it is cytoplasmic.
BODP|<fbsym>FBgn0004227==nonA</fbsym> protein is distributed ubiquitously in oocytes, embryos, larvae,
| pupae, and adults.
ASM|immunolocalization
CVBODP|<t> O,A <a> oocyte | ubiquitous <p>
|<t> E <a>  <p> ubiquitous
|<t> L <a>  <p> ubiquitous
|<t> P <a>  <p> ubiquitous
|<t> A <a>  <p> ubiquitous
CVCEL|nucleus
CC|The RNA-binding motif of <fbsym>FBgn0004227==nonA</fbsym> protein is most similar to those of <fbsym>FBgn0003659==Sxl</fbsym>
| protein, the polyA-binding proteins, and <fbsym>FBgn0003742==tra2</fbsym> protein.
}

REF
{
REFM|FBrf0056578
|Rendahl et al.
|1992
REFM|FBrf0126775
|Hovemann et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002038	SYM 1 Dip-A<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 812
ID|FBpp0002038
SYM|Dip-A<up>+</up>PA
SYN|Dip A
ASAL|<fbsym>FBal0066899==Dip-A<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0000453==Dip-A</fbsym>

REFDSR
{
RDID|FBrf0000000Flybase Curation
BODP|<fbsym>FBgn0000453==Dip-A</fbsym> specific activity is highest in embryos and young larvae and is
| present at fairly uniform levels thereafter. <fbsym>FBgn0000453==Dip-A</fbsym> specific activity was
| found to be fairly uniform in all tissues studied except in gut and
| Malphigian tubules where it is higher than average and adult thorax where
| it is low.
CVBODP|<t> L <a> embryonic/larval digestive system <p>
|<t> L <a> Malpighian tubule <p>
|<t> A <a> pupal/adult digestive system <p>
|<t> A <a> Malpighian tubule <p>
|<t> O,A | female <a> ovary <p>
}

REF
{
REFM|FBrf0000000Flybase Curation
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002040	SYM 1 Lap-D<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 5 Nov 1999	RESZ 1002
ID|FBpp0002040
SYM|Lap-D<up>+</up>PB
SYN|LapP<up>+</up>PA
ASAL|<fbsym>FBal0067982==Lap-D<up>+</up></fbsym>
DT|5 Nov 1999
|10 Mar 1998
ASGN|<fbsym>FBgn0002530==Lap-D</fbsym>

REFDSR
{
RDID|FBrf0000000Flybase Curation
ASM|enzyme assay or biochemical detection
PCL|The <fbsym>LapP</fbsym> protein in early embryos is present in an insoluble form and is
| thought to be membrane or vesicle associated.
BODP|The level of <fbsym>LapP</fbsym> protein in embryos does not change significantly but a
| change from an insoluble to a soluble form occurs. It's likely location in
| early embryos is in the yolk. The rise in <fbsym>LapP</fbsym> activity that occurs just
| before pupariation is dependent on ecdysone.
CVBODP|<t> O,A | female <a> ovary <p>
|<t> P <a> puparium <p>
|<t> P <a> exuvial fluid <p>
CC|No specific assays are available for "LapG" activity. Estimates of LapG
| activity are therefore based on the total Lap activity less the "LapP" contribution.
}

REF
{
REFM|FBrf0000000Flybase Curation
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002041	SYM 1 Lap-D<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 5 Nov 1999	RESZ 939
ID|FBpp0002041
SYM|Lap-D<up>+</up>PA
SYN|LapG<up>+</up>PA
ASAL|<fbsym>FBal0067982==Lap-D<up>+</up></fbsym>
DT|5 Nov 1999
|10 Mar 1998
ASGN|<fbsym>FBgn0002530==Lap-D</fbsym>

REFDSR
{
RDID|FBrf0000000Flybase Curation
BODP|Activity is highest in larvae and adults. It is found mainly in the gut but
| is also found in the Malpighian tubules.
|<fbsym>LapG</fbsym> activity is low in early embryos and rises from 15 hours through
| hatching. A rise in <fbsym>LapG</fbsym> activity after eclosion appears to be dependent
| upon ingestion of dietary protein.
CVBODP|<t> L <a> embryonic/larval digestive system <p>
|<t> L <a> Malpighian tubule <p>
|<t> A <a> pupal/adult digestive system <p>
|<t> A <a> Malpighian tubule <p>
CC|No specific assays are available for "LapG" activity. Estimates of <fbsym>LapG</fbsym>
| activity are therefore based on the total Lap activity less the "LapP" contribution.
}

REF
{
REFM|FBrf0000000Flybase Curation
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002058	SYM 1 bcd<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 6	DT 1 22 Aug 2000	RESZ 1918
ID|FBpp0002058
SYM|bcd<up>+</up>P
ASAL|<fbsym>FBal0068679==bcd<up>+</up></fbsym>
DT|22 Aug 2000
|10 Mar 1998
ASGN|<fbsym>FBgn0000166==bcd</fbsym>

REFDSR
{
RDID|FBrf0055557
|Gavis and Lehmann
|1992
AGT|<fbsym>FBal0035302==nos<up>bcd.3UTR</up></fbsym>
BODP|<fbsym>FBgn0000166==bcd</fbsym> protein is not detected in <fbsym>FBal0035302==nos[bcd.3UTR]</fbsym> embryos.
ASM|immunolocalization
}

REFDSR
{
RDID|FBrf0086609
|Sauer et al.
|1995
CC|In vitro constructs containing <fbsym>FBgn0000166==bcd</fbsym> sequences were attributed with wild
| type <fbsym>FBgn0000166==bcd</fbsym> function.  Affinity chromatography and gel shift assays were
| used to demonstrate that two separate activation domains of <fbsym>FBgn0000166==bcd</fbsym> protein
|  interact with components of the TFIID complex.  Specifically, the
| glutamine rich domian interacts with <fbsym>Taf110</fbsym>, and the alanine rich domain
| interacts with <fbsym>Taf60</fbsym>.  Transcription activation assays demonstrate that
| these two domains act in synergism.
}

REFDSR
{
RDID|FBrf0105200
|Burz et al.
|1998
CC|<fbsym>FBgn0000166==bcd</fbsym> protein is expressed in yeast under the control of &bgr;estradiol in
| order to control the amount of <fbsym>FBgn0000166==bcd</fbsym> protein produced.  Cooperative binding
| to <fbsym>FBgn0000166==bcd</fbsym> response regions on various lacZ reporter constructs was studied
| with transcription assays, in vitro gel shift assays and foot print
| analysis.  The <fbsym>FBgn0000166==bcd</fbsym> responsive region of <fbsym>FBgn0001320==kni</fbsym> was used both in vitro and
| in vivo to ascertain the strength of <fbsym>FBgn0000166==bcd</fbsym> binding sites.
}

REF
{
REFM|FBrf0043921
|Frigerio et al.
|1986
REFM|FBrf0051645
|Seeger and Kaufman
|1990
REFM|FBrf0055557
|Gavis and Lehmann
|1992
REFM|FBrf0086609
|Sauer et al.
|1995
REFM|FBrf0105200
|Burz et al.
|1998
REFM|FBrf0126798
|Zhu and Hanes
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002072	SYM 1 Ars<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 557
ID|FBpp0002072
SYM|Ars<up>+</up>PA
ASAL|<fbsym>FBal0066403==Ars<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0000122==Ars</fbsym>

REFDSR
{
RDID|FBrf0045645
|Pelliccia et al.
|1987
BODP|The peak of <fbsym>FBgn0000122==Ars</fbsym> enzyme activity coincides with the time of hatching from
| embryo to larva.
ASM|enzyme assay or biochemical detection
CC|Two independently regulated aryl sulfatase activities are shown to be
| present in Drosophila and are referred to as Type I and Type II.
}

REF
{
REFM|FBrf0045645
|Pelliccia et al.
|1987
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002199	SYM 1 Me<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 727
ID|FBpp0002199
SYM|Me<up>+</up>PA
ASAL|<fbsym>FBal0068058==Me<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0002704==Me</fbsym>

REFDSR
{
RDID|FBrf0057573
|Li
|1992
CC|The quantities of six out of seven enzymes tested were higher in <fbsym>FBal0000314==Adh[F]</fbsym>
| homozygotes than in <fbsym>FBal0000321==Adh[S]</fbsym> homozygotes. Levels were significantly higher
| at the 0.001 level for <fbsym>FBgn0000055==Adh</fbsym>, <fbsym>FBgn0001091==Gapdh1</fbsym>, and <fbsym>FBgn0003076==Pgm</fbsym> and higher at the 0.05
| level for <fbsym>FBgn0001128==Gpdh</fbsym>. <fbsym>FBgn0001248==Idh</fbsym> levels were not increased in <fbsym>FBal0000314==Adh[F]</fbsym> flies.
}

REF
{
REFM|FBrf0057573
|Li
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002213	SYM 1 shi<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 579
ID|FBpp0002213
SYM|shi<up>+</up>PA
ASAL|<fbsym>FBal0071044==shi<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003392==shi</fbsym>

REFDSR
{
RDID|FBrf0056470
|Chen et al.
|1992
ABOD|polyclonal
ASTR|<fbsym>FBtr0000493==shi<up>+</up>R5.1</fbsym>
|<fbsym>FBtr0000494==shi<up>+</up>R4.3</fbsym>
CC|A form of <fbsym>FBgn0003392==shi</fbsym> protein which localizes predominantly to the head. This form
| includes 6aa inserted at the first alternate splice site (Alt1) that are
| absent in the "body" form of the protein.
}

REF
{
REFM|FBrf0056470
|Chen et al.
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002214	SYM 1 shi<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 880
ID|FBpp0002214
SYM|shi<up>+</up>PB
ASAL|<fbsym>FBal0071044==shi<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003392==shi</fbsym>

REFDSR
{
RDID|FBrf0056470
|Chen et al.
|1992
ABOD|polyclonal
ASTR|<fbsym>FBtr0000495==shi<up>+</up>R3.6</fbsym>
CC|A form of <fbsym>FBgn0003392==shi</fbsym> protein which localizes predominantly to the body. This form
| lacks 6aa inserted at the first alternate splice site (Alt1) that are
| present in the "head" form of the protein. An antibody to <fbsym>FBgn0003392==shi</fbsym> was
| generated in mouse that reacts primarily with the body form of <fbsym>FBgn0003392==shi</fbsym>
| protein. This difference supports the existence of different brain and body
| forms but the differential immunoreactivity could not be completely
| explained by the splicing variants identified here.
}

REF
{
REFM|FBrf0056470
|Chen et al.
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002216	SYM 1 Ssb<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 2359
ID|FBpp0002216
SYM|Ssb<up>+</up>PA
ASAL|<fbsym>FBal0068340==Ssb<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0010085==Ssb</fbsym>

REFDSR
{
RDID|FBrf0056550
|Budnik and Gorczyca
|1992
AGT|<fbsym>FBal0015610==shi<up>1</up></fbsym>
PCL|Electron microscopical analysis shows that <fbsym>FBgn0010085==Ssb</fbsym> protein is concentrated at
| the presynaptic terminal in close proximity to synaptic vesicles and in the
| postsynaptic subsynaptic reticulum. It is nuclear in testis and ovary.
BODP|<fbsym>FBgn0010085==Ssb</fbsym> protein localizes to a specific subset of neuromuscular junction
| terminals in the larval body wall. Expression is exclusive to the synaptic
| boutons of type II terminals and is seen from 18hr of embryonic development
| through to 8hr afterpuparium formation. Expression is also seen in a small
| segmentally repeated set of neurons in the larval ventral ganglion and in a
| number of cell clusters and in the neuropil in the brain. Larval testis and
| ovary cells are also stained.
ASM|immunolocalization
CVBODP|<t> L <a> somatic muscle <p>
|<t> L <a> synapse <p>
|<t> L <a> central nervous system <p>
|<t> L <a> neuropil <p>
|<t> L <a> larval brain | restricted  <p>
|<t> L <a> larval ventral ganglion <p>
|<t> L,S <a> testis <p>
|<t> O,L <a> ovary <p>
|<t> L <a> abdominal2..7 dorsal acute muscle 1 <p>
|<t> L <a> abdominal 2..7 dorsal acute muscle 2 <p>
|<t> L <a> abdominal 2..7 dorsal acute muscle 3 <p>
|<t> L <a> abdominal 2..7 segment border muscle <p>
|<t> L <a> abdominal 2..7 dorsal oblique muscle 1 <p>
|<t> L <a> abdominal 2..7 dorsal oblique muscle 2 <p>
|<t> L <a> abdominal 2..7 ventral longitudinal muscle 1 <p>
|<t> L <a> abdominal 2..7 ventral longitudinal muscle 2 <p>
|<t> L <a> abdominal 2..7 ventral oblique muscle 1 <p>
|<t> L <a> abdominal 2..7 ventral oblique muscle 2 <p>
|<t> L <a> abdominal 2..7 ventral oblique muscle 4 <p>
|<t> L <a> abdominal 2..7 ventral oblique muscle 5 <p>
|<t> L <a> abdominal 2..7 ventral oblique muscle 6 <p>
|<t> L <a> abdominal 2..7 lateral transverse muscle 2 <p>
|<t> L <a> abdominal 2..7 ventral acute muscle 1 <p>
|<t> L <a> abdominal 2..7 ventral acute muscle 2 <p>
|<t> L <a> abdominal 2..7 ventral acute muscle 3 <p>
CVCEL|nucleus
|synapse
CC|Ultrastructural studies done by electron microscopy.
}

REF
{
REFM|FBrf0056550
|Budnik and Gorczyca
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002220	SYM 1 fz<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 211
ID|FBpp0002220
SYM|fz<up>+</up>P
ASAL|<fbsym>FBal0069190==fz<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ABODURL|1c11.html 1C11
ASGN|<fbsym>FBgn0001085==fz</fbsym>

REF
{
REFM|FBrf0056423
|Chan et al.
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002231	SYM 1 tra<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 20 Mar 1998	RESZ 654
ID|FBpp0002231
SYM|tra<up>+</up>P
ASAL|<fbsym>FBal0071393==tra<up>+</up></fbsym>
DT|20 Mar 1998
|10 Mar 1998
ASGN|<fbsym>FBgn0003741==tra</fbsym>

REFDSR
{
RDID|FBrf0057906
|Tian and Maniatis
|1993
CC|<fbsym>FBgn0003741==tra</fbsym> and <fbsym>FBgn0003742==tra2</fbsym> proteins as well as a set of SR proteins isolated from HeLa
| cells were shown to be necessary for the formation of a complex which
| commits the <fbsym>FBgn0000504==dsx</fbsym> pre-mRNA to the female-specific splicing pathway. The
| factors bind to a regulatory element located downstream of the 3'
| female-specific splice site.
}

REF
{
REFM|FBrf0057906
|Tian and Maniatis
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002232	SYM 1 Abd-B<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 6	DT 1 5 Jan 2000	RESZ 2421
ID|FBpp0002232
SYM|Abd-B<up>+</up>P
ASAL|<fbsym>FBal0066331==Abd-B<up>+</up></fbsym>
DT|5 Jan 2000
|10 Mar 1998
ASGN|<fbsym>FBgn0000015==Abd-B</fbsym>

REFDSR
{
RDID|FBrf0049619
|Tremml and Bienz
|1989
BODP|<fbsym>FBgn0000015==Abd-B</fbsym> protein is first detected at germ band retraction stage in the
| midgut and hindgut visceral mesoderm and the ectoderm of parasegments 11-15.
ASM|immunolocalization
CVBODP|<t> E | stage 13-14 <a> visceral mesoderm <of> embryonic/larval midgut <of>
|<t> E | stage 13-14 <a> visceral mesoderm <of> embryonic/larval hindgut <of>
}

REFDSR
{
RDID|FBrf0051569
|de Lorenzi and Bienz
|1990
ABOD|polyclonal
BODP|The <fbsym>FBgn0000015==Abd-B</fbsym> protein is first detected in stage 10 embryos in the anterior
| region of parasegment 15, parasegment 14 and the posterior region of
| parasegment 13. By stage 11, the anterior boundary of <fbsym>FBgn0000015==Abd-B</fbsym> expression is
| expanded into parasegment 11, and expression is detected mainly in the
| visceral mesoderm  of parasegments 11-13. By stage 13 of embryogenesis, the
| anterior boarder of expression is extended into parasegment 10 of the ectoderm.
ASM|immunolocalization
CVBODP|<t> E | stage 10 <a> parasegment 13-15 <p>
|<t> E | stage 11-13 <a> parasegment 11-15 <p>
|<t> E | stage 11 <a> visceral mesoderm <of> parasegment 11-14 <p>
|<t> E | stage 13 <a> ectoderm <of> parasegment 10-13 <p>
CVCEL|nucleus
CC|The antibody reported in this paper recognizes both the Abd-B-m and Abd-B-r proteins.
}

REFDSR
{
RDID|FBrf0068620
|Orlando and Paro
|1993
BODP|<fbsym>FBgn0000015==Abd-B</fbsym> protein is expressed in SL-2 cells.
ASM|western blot
|immunolocalization
}

REFDSR
{
RDID|FBrf0072541
|Bachiller et al.
|1994
ASM|immunolocalization
CVBODP|<t> E | stage 12 <a> parasegment 11-14 <p>
}

REFDSR
{
RDID|FBrf0080088
|Hendrickson and Sakonju
|1995
ASM|immunolocalization
CVBODP|<t> E | stage 12 <a> parasegment 10-14 <p>
}

REFDSR
{
RDID|FBrf0088118
|Freeland and Kuhn
|1996
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> female genital disc | restricted <p>
|<t> L | third instar <a> male genital disc | restricted <p>
}

REF
{
REFM|FBrf0049619
|Tremml and Bienz
|1989
REFM|FBrf0051569
|de Lorenzi and Bienz
|1990
REFM|FBrf0068620
|Orlando and Paro
|1993
REFM|FBrf0072541
|Bachiller et al.
|1994
REFM|FBrf0080088
|Hendrickson and Sakonju
|1995
REFM|FBrf0088118
|Freeland and Kuhn
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002312	SYM 1 scb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 28 Jul 1998	RESZ 761
ID|FBpp0002312
SYM|scb<up>+</up>P
ASAL|<fbsym>FBal0071018==scb<up>+</up></fbsym>
DT|28 Jul 1998
|28 Jul 1998
ASGN|<fbsym>FBgn0003328==scb</fbsym>

REFDSR
{
RDID|FBrf0100355
|Grotewiel et al.
|1998
BODP|<fbsym>FBgn0003328==scb</fbsym> protein is concentrated in the mushroom body (corpora pedunculata)
| perikarya, calyces, peduncles and &agr;, &bgr;, and &ggr; lobes in adults.
| It is also observed in the ellipsoid body.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> A <a> corpora pedunculata <p>
|<t> A <a> cell body <of> corpora pedunculata <p>
|<t> A <a> calyx of corpora pedunculata <p>
|<t> A <a> &agr;-lobe <p>
|<t> A <a> &bgr;-lobe <p>
|<t> A <a> &ggr;-lobe <p>
|<t> A <a> ellipsoid body <p>
}

REF
{
REFM|FBrf0100355
|Grotewiel et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002316	SYM 1 grh<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 4	DT 1 5 Nov 1999	RESZ 3039
ID|FBpp0002316
SYM|grh<up>+</up>P
SYN|grh<up>+</up>PA
ASAL|<fbsym>FBal0069210==grh<up>+</up></fbsym>
DT|5 Nov 1999
|28 Jul 1998
ID2|FBpp0001549
ASGN|<fbsym>FBgn0004586==grh</fbsym>

REFDSR
{
RDID|FBrf0049797
|Bray et al.
|1989
BODP|<fbsym>FBgn0004586==grh</fbsym> protein is first detected at stage 11 in the epidermis and CNS. <fbsym>FBgn0004586==grh</fbsym>
| protein expression remains fairly constant in the epidermis but changes
| with developmental time in the CNS. Early on, <fbsym>FBgn0004586==grh</fbsym> protein is detected in
| one or two medial nuclei per segmental neuromere. Later, it is detected in
| more lateral nuclei in a pattern that changes as development proceeds. At
| stage 15, expression is observed in around 30 cells per neuromere in a
| segmentally repeated pattern. By stage 17, the number of nuclei expressing
| the protein has decreased particularly in the abdominal regions of the
| ventral nerve cord. <fbsym>FBgn0004586==grh</fbsym> protein is also detected in small regions of the
| foregut and the hindgut. <fbsym>FBgn0004586==grh</fbsym> protein and <fbsym>FBgn0000422==Ddc</fbsym> protein are not
| co-expressed in the same cells in late embryos. Co-expression was observed
| in primary cultures of neuroblasts.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | stage >=11 <a> ventral nerve cord | segmentally repeated <p>
|<t> E | stage >=11 <a> epidermis <p>
|<t> E <a> embryonic/larval hindgut <p>
|<t> E <a> embryonic/larval foregut <p>
CVCEL|nucleus
}

REFDSR
{
RDID|FBrf0049808
|Dynlacht et al.
|1989
CC|<fbsym>FBgn0004586==grh</fbsym> protein was purified from embryonic extracts. Three prominent
| polypeptides of 140, 120, and 83kD were observed. All of these bind to
| promoter elements within the <fbsym>FBgn0000422==Ddc</fbsym>, <fbsym>FBgn0003944==Ubx</fbsym>, and <fbsym>FBgn0001077==ftz</fbsym> genes. The purified
| protein was shown to act as binding site-dependent transcription factor in vitro.
}

REFDSR
{
RDID|FBrf0058446
|Santaren et al.
|1993
CVBODP|<t> L | third instar <a> dorsal mesothoracic disc <p>
}

REFDSR
{
RDID|FBrf0098901
|Uv et al.
|1997
BODP|<fbsym>FBgn0004586==grh</fbsym> protein expression persists in epidermal cells and in parts of the
| foregut and hindgut in the larval period. It is also detected in the
| trachea, anterior spiracles, proventriculus, and in cells that secrete the
| head skeleton. <fbsym>FBgn0004586==grh</fbsym> protein is expressed uniformly in the imaginal discs
| and in the optic lobes.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L <a> epidermis <p>
|<t> L <a> embryonic/larval foregut <p>
|<t> L <a> embryonic/larval hindgut <p>
|<t> L <a> embryonic/larval trachea <p>
|<t> L <a> embryonic/larval anterior spiracle <p>
|<t> L <a> embryonic/larval proventriculus <p>
|<t> L <a> imaginal disc <p>
|<t> L <a> larval optic lobe <p>
|<t> L <a> neuroblast <p>
}

REF
{
REFM|FBrf0049797
|Bray et al.
|1989
REFM|FBrf0049808
|Dynlacht et al.
|1989
REFM|FBrf0058446
|Santaren et al.
|1993
REFM|FBrf0098901
|Uv et al.
|1997
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002322	SYM 1 norpA<up>+</up>P	AAL 1 -	PSZ 1 130 	HG 1 -	DBA 1 -	REF 1 1	DT 1 28 Jul 1998	RESZ 1624
ID|FBpp0002322
SYM|norpA<up>+</up>P
ASAL|<fbsym>FBal0070830==norpA<up>+</up></fbsym>
DT|28 Jul 1998
|28 Jul 1998
ASGN|<fbsym>FBgn0004625==norpA</fbsym>

REFDSR
{
RDID|FBrf0058783
|Zhu et al.
|1993
PSZ|130 | observed
ABOD|polyclonal
BODP|Western blots show that <fbsym>FBgn0004625==norpA</fbsym> protein is abundant in extracts from adult
| heads. Small amounts are detected in adult bodies. Protein is detected in
| homogenates of adult legs, male thorax, female thorax, and male abdomen,
| but not in female abdomen. Phospholipase C activity was measured in
| Drosophila tissues. A high level of activity was found in heads and a
| severeley reduced level was found in heads of <fbsym>FBgn0004625==norpA</fbsym> mutants. The majority
| of the activity is localized in the eye. In <fbsym>cli</fbsym> mutants (lacking eyes),
| the level is reduced by about 65% indicating that there is some activity in
| other tissues such as the ocelli. Low levels of activity could also be
| measured in the body. Immunonostaining of adult tissue sections with an
| antibody against <fbsym>FBgn0004625==norpA</fbsym> protein shows staining in the retina, ocelli,
| optic lobes, cerebrum, and thoracic ganglia.
ASM|western blot
CVBODP|western blot
|<t> A <a> adult head <p>
|<t> A <a> leg <p>
|<t> A | female <a> adult abdomen <p>
|<t> A <a> adult thorax <p>
|enzyme assay or biochemical detection
|<t> A <a> adult head <p>
|<t> A <a> eye <p>
|immunolocalization
|<t> A <a> retina <p>
|<t> A <a> ocellus <p>
|<t> A <a> thoracic ganglion <p>
|<t> A <a> adult brain <p>
|<t> A <a> optic lobe <p>
}

REF
{
REFM|FBrf0058783
|Zhu et al.
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002340	SYM 1 ifc<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 28 Jul 1998	RESZ 383
ID|FBpp0002340
SYM|ifc<up>+</up>PB
ASAL|<fbsym>FBal0069264==ifc<up>+</up></fbsym>
DT|28 Jul 1998
|28 Jul 1998
ASGN|<fbsym>FBgn0001941==ifc</fbsym>

REFDSR
{
RDID|FBrf0091054
|Endo et al.
|1996
CC|Predicted from an alternate <fbsym>FBgn0001941==ifc</fbsym> transcript. Significantly smaller than
| ifc<up>+</up>P321. Length unspecified.
}

REF
{
REFM|FBrf0091054
|Endo et al.
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002382	SYM 1 cad<up>+</up>PA	AAL 1 197	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 28 Jul 1998	RESZ 254
ID|FBpp0002382
SYM|cad<up>+</up>PA
ASAL|<fbsym>FBal0068729==cad<up>+</up></fbsym>
DT|28 Jul 1998
|28 Jul 1998
ASGN|<fbsym>FBgn0000251==cad</fbsym>

REFDSR
{
RDID|FBrf0042432
|Mlodzik et al.
|1985
AAL|197
}

REF
{
REFM|FBrf0042432
|Mlodzik et al.
|1985
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002399	SYM 1 Dhod<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 28 Jul 1998	RESZ 529
ID|FBpp0002399
SYM|Dhod<up>+</up>P
ASAL|<fbsym>FBal0066830==Dhod<up>+</up></fbsym>
DT|28 Jul 1998
|28 Jul 1998
ASGN|<fbsym>FBgn0000447==Dhod</fbsym>

REFDSR
{
RDID|FBrf0080501
|Yang et al.
|1995
BODP|Using an enzyme assay, <fbsym>FBgn0000447==Dhod</fbsym> protein activity is demonstrated in elongated
| spermatid bundles, but is absent from earlier and later stages.
ASM|enzyme assay or biochemical detection
CVBODP|enzyme assay or biochemical detection
|<t> S,A <a> spermatid <p>
}

REF
{
REFM|FBrf0080501
|Yang et al.
|1995
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002409	SYM 1 pan<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 1	DT 1 28 Jul 1998	RESZ 1117
ID|FBpp0002409
SYM|pan<up>+</up>P
ASAL|<fbsym>FBal0078829==pan<up>+</up></fbsym>
DT|28 Jul 1998
|28 Jul 1998
ASGN|<fbsym>FBgn0019664==pan</fbsym>

REFDSR
{
RDID|FBrf0093264
|van de Wetering et al.
|1997
HG|Caenorhabditis elegans | pop-1 (U37532)
|Homo sapiens | TCF-1E (Z47362)
CC|Repeats 3-8 of the <fbsym>FBgn0000117==arm</fbsym> protein interact with aa 1-90 of <fbsym>FBgn0019664==pan</fbsym> in a yeast
| two-hybrid assay. The DNA binding site of the <fbsym>FBgn0019664==pan</fbsym> HMG box was assayed,
| and revealed the consensus CCTTTGATCTT. Cotransfection of <fbsym>FBgn0000117==arm</fbsym> and <fbsym>FBgn0019664==pan</fbsym>
| vectors resulted in  transcriptional activation of a <fbsym>CAT</fbsym> or a <fbsym>LUC</fbsym>
|  reporter, and the C-terminus of <fbsym>FBgn0000117==arm</fbsym> protein was necessary for this
| activation. The transactivation capacity of the C-terminus of <fbsym>FBgn0000117==arm</fbsym> was
| further demonstrated by fusing it to a GAL4-DNA binding domain, and
| assaying expression of a <fbsym>CAT</fbsym> reporter.
}

REF
{
REFM|FBrf0093264
|van de Wetering et al.
|1997
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002438	SYM 1 gsb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 3	DT 1 5 Jan 2000	RESZ 2939
ID|FBpp0002438
SYM|gsb<up>+</up>P
SYN|gsb-d<up>+</up>P
ASAL|<fbsym>FBal0100470==gsb<up>+</up></fbsym>
DT|5 Jan 2000
|16 Sep 1998
ASGN|<fbsym>FBgn0001148==gsb</fbsym>

REFDSR
{
RDID|FBrf0058110
|Gutjahr et al.
|1993
ABOD|polyclonal
BODP|<fbsym>gsb-d</fbsym> protein is detected in a segmentally repeated pattern a the end of
| cellularization.  Odd-numbered stripes 1-13 plus an anterior stripe 0
| appear first, and are followed by the appearance of even stripes 2-12 at
| mid-gastrulation, and ofstripe 14 at the start of germ band extension.
| Towards the end of germ band extension, stripes 4-14 become restricted to
| neurectoderm. <fbsym>gsb-d</fbsym> protein expression is highest at this stage, with
| expression also detected in 4 anterior and 3 posterior regions. Expression
| is also detected in the most medial neuroblasts of row 5. Anterior and
| posterior accumulation decreases after this stage. At the end of germ band
| retraction, ectodermal expression increases once more, to disappear again
| by stage 14. During germ band extension, all neuroblasts of row 5 and 6
| express <fbsym>gsb-p</fbsym> protein, and those of row 7 express it transiently.
| Additional cells which may be the VUM precursors also express <fbsym>gsb-p</fbsym>
| protein transiently. Low levels of expression persist in a few neuroblasts
| and ganglion mother cells until germ band retraction. Mesodermal <fbsym>gsb-p</fbsym>
| protein expression is first detected at mid-germ-band extension, persists
| in three patches in thoracic segments that subsequently merge, and
| dissapears around head involution. Intercalary segment primordium
| expression is detected starting at mid germ band extension. Expression is
| detected in a dorsal patch of the labral segment and in additional patches
| in the presumptive head during the slow phase of germ band extension.
| Additional stripes (stripes 15-17) appear in the tail region during germ
| band extension. <fbsym>gsb-p</fbsym> protein is expressed transiently in the pharynx and
| anal pad during head involution.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | stage 4-13 <a>  <p> segmentally repeated
|<t> E | stage 10 <a> neurectoderm <p> segmentally repeated
|<t> E | stage 10-12 <a> mesoderm <p>
|<t> E | stage 10-12 <a> neuroblast <p>
|<t> E | stage 8-13 <a> embryonic intercalary segment<p>
|<t> E | stage 10-13 <a> labral segment | restricted <p>
|<t> E | stage 9-13 <a> abdominal segment 9..11 | restricted <p>
|<t> E | stage 14 <a> anal pad | restricted <p>
|<t> E | stage 14 <a> embryonic/larval pharynx | restricted <p>
}

REFDSR
{
RDID|FBrf0088118
|Freeland and Kuhn
|1996
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> female genital disc | restricted <p>
|<t> E | third instar <a> male genital disc | restricted <p>
}

REF
{
REFM|FBrf0043894
|Bopp et al.
|1986
REFM|FBrf0058110
|Gutjahr et al.
|1993
REFM|FBrf0088118
|Freeland and Kuhn
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002439	SYM 1 gsb-n<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 3	DT 1 5 Jan 2000	RESZ 2129
ID|FBpp0002439
SYM|gsb-n<up>+</up>P
SYN|gsb-p<up>+</up>P
ASAL|<fbsym>FBal0100471==gsb-n<up>+</up></fbsym>
DT|5 Jan 2000
|16 Sep 1998
ASGN|<fbsym>FBgn0001147==gsb-n</fbsym>

REFDSR
{
RDID|FBrf0058110
|Gutjahr et al.
|1993
ABOD|polyclonal
BODP|<fbsym>gsb-p</fbsym> protein is first detected at embryonic stage 10, in a subset of
| neuroblasts, ganglion mother cells, and neurons. By the end of stage 11
| neuronal expression has intensified and is segmentally repeated, from the
| mandibular to the abdominal neuromere. Expression is also detected in the
| terminal regions, like the neurons of the brain in the head, the neurons of
| abdominal segment 9, and the cells of the anal pad in the tail region.
| Subsequently expression continues to be detected in a subset of neurons
| until stage 17. Additional expression is detected after germ band
| retraction in a few lateral cells per hemisegment, in ventral ectodermal
| stripes in the posterior region of each segment, in patches of epidermal
| cells or their derivatives in the head region (such as the pharynx), and in
| the nuclei of one of the ventral superficial oblique muscles. Expression of
| <fbsym>FBgn0000577==en</fbsym> and <fbsym>gsb-p</fbsym> proteins overlap extensively in the central nervous system.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | stage 10 <a> neuroblast <p>
|<t> E | stage 10 <a> ganglion mother cell <p>
|<t> E | stage >10 <a> embryonic neuron <p>
|<t> E | stage >11 <a> embryonic neuron | segmentally repeated pattern <p>
|<t> E | stage >13 <a> neuron <of> abdominal segment 9 <p>
|<t> E | stage >13 <a> neuron <of> embryonic brain <p>
|<t> E | stage >13 <a> anal pad <p>
|<t> E | stage >13 <a> embryonic/larval pharynx <p>
|<t> E | stage >13 <a> ventral oblique muscle <p>
}

REFDSR
{
RDID|FBrf0088118
|Freeland and Kuhn
|1996
ASM|immunolocalization
CVBODP|immunolocalization
|<t> L | third instar <a> female genital disc | restricted <p>
|<t> L | third instar <a> male genital disc | restricted <p>
}

REF
{
REFM|FBrf0043894
|Bopp et al.
|1986
REFM|FBrf0058110
|Gutjahr et al.
|1993
REFM|FBrf0088118
|Freeland and Kuhn
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002442	SYM 1 vvl<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 215
ID|FBpp0002442
SYM|vvl<up>+</up>P
SYN|prd3<up>+</up>P
ASAL|<fbsym>FBal0071473==vvl<up>+</up></fbsym>
DT|21 Nov 2000
|16 Sep 1998
ASGN|<fbsym>FBgn0003995==vvl</fbsym>

REF
{
REFM|FBrf0043921
|Frigerio et al.
|1986
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002532	SYM 1 Lam<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 3	DT 1 31 Dec 1998	RESZ 1885
ID|FBpp0002532
SYM|Lam<up>+</up>P
ASAL|<fbsym>FBal0067976==Lam<up>+</up></fbsym>
DT|31 Dec 1998
|31 Dec 1998
ASGN|<fbsym>FBgn0002525==Lam</fbsym>

REFDSR
{
RDID|FBrf0050224
|Harel et al.
|1989
PCL|<fbsym>FBgn0002525==Lam</fbsym> protein is a nuclear envelope polypeptide which remains in an
| envelope-like structure enclosing the mitotic apparatus throughout mitosis.
BODP|<fbsym>FBgn0002525==Lam</fbsym> protein localizes to the nucleus during early embryogenesis.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | early <a>  <p>
CVCEL|nuclear envelope
}

REFDSR
{
RDID|FBrf0084310
|Riemer et al.
|1995
PCL|<fbsym>FBgn0002525==Lam</fbsym> protein is nuclear. There is some, but not complete, overlap in
| subcellular <fbsym>FBgn0002525==Lam</fbsym> and <fbsym>FBgn0010397==LamC</fbsym> protein expression.
BODP|Starting with 0-3 hr embryos, <fbsym>FBgn0002525==Lam</fbsym> protein is detected in all developmental
| stages. In embryo and larvae, expression is detected in all nuclei.
ASM|western blot
|immunolocalization
CVBODP|western blot
|<t> E-A <a>  <p>
|immunolocalization
|<t> E <a>  <p>
|<t> L <a>  <p>
CVCEL|nucleus
}

REFDSR
{
RDID|FBrf0094065
|Ashery-Padan et al.
|1997
PCL|Between stages S4 and S6-S7 of oogenesis, <fbsym>FBgn0002525==Lam</fbsym> protein localizes to the
| nuclear periphery in all cell types, but after stage S6-S7, nucleoplasmic
| and cytoplasmic accumulation is also observed. During larval, pupal and
| adult stages <fbsym>FBgn0002525==Lam</fbsym> protein localizes to the nucleus of most cells. No <fbsym>FBgn0002525==Lam</fbsym>
| protein is detected during stages 6-11 of spermiogenesis.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E-A <a>  <p>
|<t> O <a>  <p>
CVCEL|nucleus
|nucleoplasm
|cytoplasm
}

REF
{
REFM|FBrf0050224
|Harel et al.
|1989
REFM|FBrf0084310
|Riemer et al.
|1995
REFM|FBrf0094065
|Ashery-Padan et al.
|1997
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002546	SYM 1 Ecol\lacZ<up>ftz.PC</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 14 May 1999	RESZ 458
ID|FBpp0002546
SYM|Ecol\lacZ<up>ftz.PC</up>PA
SYN|lacZ<up>ftz.PC</up>PA
ASAL|<fbsym>FBal0041452==Ecol\lacZ<up>ftz.PC</up></fbsym>
DT|14 May 1999
|31 Dec 1998
ASGN|<fbsym>FBgn0014447==Ecol\lacZ</fbsym>

REFDSR
{
RDID|FBrf0042045
|Hiromi et al.
|1985
BODP|In embryos, peak accumulation is from 4.5-10.5 hours after egg-laying.
ASM|western blot
CVBODP|western blot
|<t> E <a>  <p>
|<t> L | first instar <a>  <p>
}

REF
{
REFM|FBrf0042045
|Hiromi et al.
|1985
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002547	SYM 1 Ecol\lacZ<up>P\T.T:Khc</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 14 May 1999	RESZ 401
ID|FBpp0002547
SYM|Ecol\lacZ<up>P\T.T:Khc</up>PA
SYN|lacZ<up>P\T.T:Khc</up>PA
ASAL|<fbsym>FBal0038885==Ecol\lacZ<up>P\T.T:Khc</up></fbsym>
DT|14 May 1999
|31 Dec 1998
ASGN|<fbsym>FBgn0014447==Ecol\lacZ</fbsym>

REFDSR
{
RDID|FBrf0073174
|Giniger et al.
|1993
CVCEL|microtubule
CC|Acts as a reporter of microtubule polarity, accumulating at plus ends.
}

REF
{
REFM|FBrf0073174
|Giniger et al.
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002574	SYM 1 activin-&bgr;<up>+</up>PA	AAL 1 373	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 1	DT 1 21 Apr 1999	RESZ 570
ID|FBpp0002574
SYM|activin-&bgr;<up>+</up>PA
ASAL|<fbsym>FBal0090895==activin-&bgr;<up>+</up></fbsym>
DT|21 Apr 1999
|21 Apr 1999
ASGN|<fbsym>FBgn0024913==activin-&bgr;</fbsym>

REFDSR
{
RDID|FBrf0102959
|Kutty et al.
|1998
AAL|373
HG|Xenopus laevis | Activin &bgr; (S61773)
|Danio rerio | Activin &bgr;B (X76051)
|Homo sapiens | Activin &bgr;A (PID g124279)
|Homo sapiens | Activin &bgr;B (PID g106726)
CC|The predicted polypeptide could be cleaved to give a 113 aa mature peptide
| with homology to vertebrate activins.
}

REF
{
REFM|FBrf0102959
|Kutty et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002576	SYM 1 how<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Apr 1999	RESZ 644
ID|FBpp0002576
SYM|how<up>+</up>P
ASAL|<fbsym>FBal0076686==how<up>+</up></fbsym>
DT|21 Apr 1999
|21 Apr 1999
ASGN|<fbsym>FBgn0017397==how</fbsym>

REFDSR
{
RDID|FBrf0105220
|Di Fruscio et al.
|1998
PCL|A <fbsym>GFP</fbsym>-<fbsym>FBgn0017397==how</fbsym> fusion protein localizes to the nucleus of mouse
| NIH 3T3 and Drosophila S2 cells.
CVCEL|nucleus
CC|<fbsym>FBgn0017397==how</fbsym> protein binds homopolymeric RNA (poly(A)) in vitro. A <fbsym>Myc</fbsym>
|-epitope-tagged <fbsym>FBgn0017397==how</fbsym> protein expressed in HeLa cells migrates with a
| molecular mass of about 55 kD.
}

REF
{
REFM|FBrf0105220
|Di Fruscio et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002605	SYM 1 Fmrf<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 21 Apr 1999	RESZ 1413
ID|FBpp0002605
SYM|Fmrf<up>+</up>P
ASAL|<fbsym>FBal0067802==Fmrf<up>+</up></fbsym>
DT|21 Apr 1999
|21 Apr 1999
ASGN|<fbsym>FBgn0000715==Fmrf</fbsym>

REFDSR
{
RDID|FBrf0054530
|Schneider et al.
|1991
BODP|<fbsym>FBgn0000715==Fmrf</fbsym> protein was detected starting at embryonic stage 15 in some medial
| protocerebral neurons, followed by some subesophageal neuromeres at stage
| 16, and in more superior and medial protocerebral neurons at stage 17.
| Expression levels increased in larval stages.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | stage >=15 <a> central nervous system | restricted <p>
|<t> E | stage >=15 <a> neuron | subset <p>
|<t> L <a> central nervous system | restricted <p>
|<t> L <a> neuron | subset <p>
}

REFDSR
{
RDID|FBrf0054531
|O'Brien et al.
|1991
BODP|<fbsym>FBgn0000715==Fmrf</fbsym> protein expression correlates with <fbsym>FBgn0000715==Fmrf</fbsym> transcript expression.
| <fbsym>FBgn0000715==Fmrf</fbsym> protein continues to be detected in prepupal through adult stages.
| Many larval neuronal signals continue to be detected in the adult.
| Inaddition, adult-specific signals are detected in the adult brain and
| ventral ganglion.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> PP-A <a> central nervous system | restricted <p>
|<t> PP-A <a> neuron | subset <p>
}

REF
{
REFM|FBrf0054530
|Schneider et al.
|1991
REFM|FBrf0054531
|O'Brien et al.
|1991
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002612	SYM 1 numb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 6	DT 1 21 Nov 2000	RESZ 2599
ID|FBpp0002612
SYM|numb<up>+</up>P
ASAL|<fbsym>FBal0070835==numb<up>+</up></fbsym>
DT|21 Nov 2000
|21 Apr 1999
ASGN|<fbsym>FBgn0002973==numb</fbsym>

REFDSR
{
RDID|FBrf0068654
|Rhyu et al.
|1994
PCL|<fbsym>FBgn0002973==numb</fbsym> protein associates with the plasma membrane of the sensory organ
| precursor cell and of the neuroblast, and is asymmetrically localized.
BODP|<fbsym>FBgn0002973==numb</fbsym> protein localizes in a ring along the plasma membrane of the sensory
| organ precursor cell, and is distributed asymmetrically to the daughter
| cell. During neuroblast division, <fbsym>FBgn0002973==numb</fbsym> protein is asymmetrically
| localized in the neuroblast, and segregates into the ganglion mother cell.
| Expression is also detected in epidermal cell membranes.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E <a> sensillum precursor <p>
|<t> E <a> neuroblast <p>
|<t> E <a> embryonic ganglion mother cell <p>
|<t> A <a> external sensory organ precursor cell <p>
|<t> A <a> peripheral nervous system | restricted <p>
CVCEL|plasma membrane
}

REFDSR
{
RDID|FBrf0084093
|Knoblich et al.
|1995
PCL|<fbsym>FBgn0002973==numb</fbsym> protein is homogenously distributed along the plasma membrane during
| interphase and early prophase in embryonic neuroblasts. Beginning in late
| prophase, <fbsym>FBgn0002973==numb</fbsym> forms a crescent overlying one of two centromeres and
| remainsin this crescent through later stages of mitosis. During telophase,
| it segregates into one of the two daughter cells where it is found evenly
| distributed along the plasma membrane. <fbsym>FBgn0002973==numb</fbsym> protein localization is
| microtubule and actin independent.
CVCEL|plasma membrane
}

REFDSR
{
RDID|FBrf0095577
|Li et al.
|1997
CC|The phosphotyrosine binding domains (PID) of most polypeptides studied
| preferentially bind peptides containing an NPXpY motif (X = any amino
| acid), whereas the the PID of <fbsym>FBgn0002973==numb</fbsym> protein binds peptides with a "YIGPY#"
| motif (# = a hydrophobic amino acid). The affinity of the PID domain for
| the peptide increases when the second tyrosine is phosphorylated. The
| GP(p)Y core motif is required for high-affinity binding. The same amino
| acids in the <fbsym>FBgn0002973==numb</fbsym> PID are likely to bind both the phosphorylated and
| non-phosphorylated forms of the peptide.
}

REF
{
REFM|FBrf0068654
|Rhyu et al.
|1994
REFM|FBrf0084093
|Knoblich et al.
|1995
REFM|FBrf0095577
|Li et al.
|1997
REFM|FBrf0098349
|Shen et al.
|1997
REFM|FBrf0099990
|Chien et al.
|1998
REFM|FBrf0103035
|Shen et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002623	SYM 1 CtBP<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 315
ID|FBpp0002623
SYM|CtBP<up>+</up>PA
SYN|CtBP-PA
ASAL|<fbsym>FBal0079492==CtBP<up>+</up></fbsym>
DT|21 Nov 2000
|22 Apr 1999
ASGN|<fbsym>FBgn0020496==CtBP</fbsym>

REFDSR
{
RDID|FBrf0102176
|Poortinga et al.
|1998
ASTR|<fbsym>FBtr0004231==CtBP<up>+</up>RD</fbsym>
}

REF
{
REFM|FBrf0102176
|Poortinga et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002630	SYM 1 sc-P*	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 5 Nov 1999	RESZ 581
ID|FBpp0002630
SYM|sc-P*
ASAL|<fbsym>FBal0071015==sc<up>+</up></fbsym>
DT|5 Nov 1999
|22 Apr 1999
ASGN|<fbsym>FBgn0004170==sc</fbsym>

REFDSR
{
RDID|FBrf0076492
|Singson et al.
|1994
CC|<fbsym>FBgn0000413==da</fbsym> protein alone or in combination with <fbsym>FBgn0000022==ac</fbsym> protein or <fbsym>FBgn0004170==sc</fbsym> protein binds
| in vitro to E-box sequences from the <fbsym>FBgn0000216==Brd</fbsym>, <fbsym>FBgn0000591==E(spl)</fbsym>, <fbsym>FBgn0002633==HLHm7</fbsym>, and <fbsym>FBgn0003326==sca</fbsym> promoters.
}

REF
{
REFM|FBrf0076492
|Singson et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002632	SYM 1 da-P*	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 5 Nov 1999	RESZ 581
ID|FBpp0002632
SYM|da-P*
ASAL|<fbsym>FBal0068807==da<up>+</up></fbsym>
DT|5 Nov 1999
|22 Apr 1999
ASGN|<fbsym>FBgn0000413==da</fbsym>

REFDSR
{
RDID|FBrf0076492
|Singson et al.
|1994
CC|<fbsym>FBgn0000413==da</fbsym> protein alone or in combination with <fbsym>FBgn0000022==ac</fbsym> protein or <fbsym>FBgn0004170==sc</fbsym> protein binds
| in vitro to E-box sequences from the <fbsym>FBgn0000216==Brd</fbsym>, <fbsym>FBgn0000591==E(spl)</fbsym>, <fbsym>FBgn0002633==HLHm7</fbsym>, and <fbsym>FBgn0003326==sca</fbsym> promoters.
}

REF
{
REFM|FBrf0076492
|Singson et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002643	SYM 1 Clk<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 27 Jun 1999	RESZ 376
ID|FBpp0002643
SYM|Clk<up>+</up>PB
ASAL|<fbsym>FBal0087184==Clk<up>+</up></fbsym>
DT|27 Jun 1999
|27 Jun 1999
ASGN|<fbsym>FBgn0023076==Clk</fbsym>

REFDSR
{
RDID|FBrf0102727
|Allada et al.
|1998
CC|The shorter form of <fbsym>FBgn0023076==Clk</fbsym> protein is missing the bHLH and PASA domains but
| contains the PASB domain.
}

REF
{
REFM|FBrf0102727
|Allada et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002673	SYM 1 Antp<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 30 May 2000	RESZ 3044
ID|FBpp0002673
SYM|Antp<up>+</up>P
ASAL|<fbsym>FBal0066388==Antp<up>+</up></fbsym>
DT|30 May 2000
|27 Jun 1999
ASGN|<fbsym>FBgn0000095==Antp</fbsym>

REFDSR
{
RDID|FBrf0043896
|Carroll et al.
|1986
ABOD|polyclonal
BODP|<fbsym>FBgn0000095==Antp</fbsym> protein is first detected in germ band extended embryos in the
| presumptive thoracic region. The region extends from the posterior
| compartment of the labial segment to the anterior compartment of A1. The
| heaviest staining is in parasegment 4. As the germ band shortens, <fbsym>FBgn0000095==Antp</fbsym>
| protein is observed in the ectoderm of posterior T1 and in T2 and T3. As
| the germ band shortens further, expression diminishes in posterior T3 and
| appears in the ventral nervous system. With germ band shortening,
| expression in the ectoderm continues to decrease. <fbsym>FBgn0000095==Antp</fbsym> protein first
| appears in the ventral nervous system in 10 pairs of patches in the
| neurogenic region. <fbsym>FBgn0000095==Antp</fbsym> protein is present in the ventral nervous system
| from the posterior part of T1 to the anterior part of A7. At early stages,
| protein levels are uniform between the thoracic and abdominal segments. As
| development proceeds protein levels increase in posterior T1, anterior T2
| and anterior T3 and diminish in the abdominal segments. <fbsym>FBgn0000095==Antp</fbsym> protein is
| also present in some cells of the PNS during germ band retraction. In the
| thorax, areas of strong <fbsym>FBgn0000095==Antp</fbsym> protein do not overlap areas of strong <fbsym>FBgn0003944==Ubx</fbsym>
| protein expression.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E <a> ectoderm <p>
|<t> E | stage >12 <a> embryonic central nervous system <p>
|<t> E | stage >12 <a> embryonic peripheral nervous system | restricted <p>
|<t> E <a> labial segment <p>
|<t> E <a> embryonic prothoracic segment <p>
|<t> E<a> embryonic mesothoracic segment <p>
|<t> E <a> embryonic metathoracic segment <p>
|<t> E <a> embryonic abdominal segment 1..7 <p>
CVCEL|nucleus
CC|The antibody is expected to recognize all forms of <fbsym>FBgn0000095==Antp</fbsym> protein.
}

REFDSR
{
RDID|FBrf0057495
|Ultsch et al.
|1992
CC|The secondary structure of an N-terminally elongated <fbsym>FBgn0000095==Antp</fbsym> protein
| fragment, including both the homeodomain and the YPWM motif, from amino
| acids -14 to +67 was determined by NMR in solution (this study).  Results
| strongly support the conclusion that the homeodomain is connected through a
| flexible linker to the main body in the <fbsym>FBgn0000095==Antp</fbsym> protein and that the minor
| groove contacts by residues 1-6 are intrinsic to the DNA binding
| interactions of the <fbsym>FBgn0000095==Antp</fbsym> protein (this study).  The stability and
| specificity of the DNA binding previously observed for the shorter <fbsym>FBgn0000095==Antp</fbsym>
| homeodomain polypeptide is preserved for the elongated polypeptide.
}

REF
{
REFM|FBrf0043896
|Carroll et al.
|1986
REFM|FBrf0057495
|Ultsch et al.
|1992
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002717	SYM 1 yin<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 13 Sep 1999	RESZ 2220
ID|FBpp0002717
SYM|yin<up>+</up>P
ASAL|<fbsym>FBal0075448==yin<up>+</up></fbsym>
DT|13 Sep 1999
|13 Sep 1999
ASGN|<fbsym>FBgn0015565==yin</fbsym>

REFDSR
{
RDID|FBrf0104507
|Roman et al.
|1998
ABOD|polyclonal
BODP|<fbsym>FBgn0015565==yin</fbsym> protein is detected in the apical membranes of the midgut and rectal
| epithelium, and in basal regions of the rectal papillae. In the female
| reproductive tract, expression is in the oviducts, seminal receptacles, and
| spermathecal ducts.During oogenesis, <fbsym>FBgn0015565==yin</fbsym> is detected in the oocyte, and
| is associated with &agr; yolk spheres in mature oocytes. In embryos, <fbsym>FBgn0015565==yin</fbsym>
| protein is detected associated with yolk spheres, and is detected in late
| stage embryos when the midgut has engulfed the central yolk mass. Low
| levels of expression are detected in the central nervous system neuropil,
| with slightly elevated levels in t e &agr; and &bgr; lobes of the mushroom
| body. Expression is high in the fat bodies surrounding the central nervous
| sytem. Some expression is seen in the antennal nerve. Expression is also
| detected in a small number of premeoitic germ cell cysts in testes.
ASM|western blot
|immunolocalization
CVBODP|western blot
|<t> E <a>  <p>
|<t> A <a>  <p>
|immunolocalization
|<t> E <a> yolk <p>
|<t> A <a> adult midgut | restricted <p>
|<t> A <a> posterior adult hindgut | restricted <p>
|<t> A <a> adult rectal papilla | basal <p>
|<t> A <a> oviduct <p>
|<t> A <a> seminalreceptacle <p>
|<t> A <a> spermathecal duct <p>
|<t> A <a> uterus <p>
|<t> A <a> neuropil <p>
|<t> A <a> adult antennal nerve <p>
|<t> A <a> &agr;-lobe <of> mushroom body <p>
|<t> A <a> &agr;-lobe<of> mushroom body <p>
|<t> A <a> adult fat body <p>
|<t> A,O | stage S9-S14 <a> oocyte <p>
|<t> A,S <a> primary spermatocyte cyst | restricted <p>
CC|<fbsym>FBgn0015565==yin</fbsym>-transfected HeLa cells exhibit proton-dependent high affinity
| alanylalanine transport. An 81.6 kD <fbsym>FBgn0015565==yin</fbsym> protein is detected in <fbsym>FBgn0015565==yin</fbsym>
| transfected HeLa cells, as well as in Western blots of Drosophila embryo
| and adult protein extracts.
}

REF
{
REFM|FBrf0104507
|Roman et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002840	SYM 1 sgg<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 22 Dec 2000	RESZ 231
ID|FBpp0002840
SYM|sgg<up>+</up>P
ASAL|<fbsym>FBal0071039==sgg<up>+</up></fbsym>
DT|22 Dec 2000
|4 Nov 1999
ASGN|<fbsym>FBgn0003371==sgg</fbsym>

REF
{
REFM|FBrf0108395
|Gallet et al.
|1999
REFM|FBrf0111519
|Willert et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002846	SYM 1 EcR<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 6 Jan 2000	RESZ 191
ID|FBpp0002846
SYM|EcR<up>+</up>P
ASAL|<fbsym>FBal0067745==EcR<up>+</up></fbsym>
DT|6 Jan 2000
|4 Nov 1999
ASGN|<fbsym>FBgn0000546==EcR</fbsym>

REF
{
REFM|FBrf0059134
|Thomas et al.
|1993
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002847	SYM 1 arm<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 6	DT 1 22 Dec 2000	RESZ 4187
ID|FBpp0002847
SYM|arm<up>+</up>P
ASAL|<fbsym>FBal0068658==arm<up>+</up></fbsym>
DT|22 Dec 2000
|4 Nov 1999
ABODURL|n27a1.html N2 7A1 ARMADILLO
ASGN|<fbsym>FBgn0000117==arm</fbsym>

REFDSR
{
RDID|FBrf0065529
|Peifer et al.
|1993
PCL|The localization of <fbsym>FBgn0000117==arm</fbsym> protein often parallels the location of adherens junctions.
BODP|<fbsym>FBgn0000117==arm</fbsym> protein expression was studied during oogenesis. <fbsym>FBgn0000117==arm</fbsym> protein is
| asymmetrically localized within follicle cells. Within each follicle cell,
| it accumulates heavily on the lateral cell surface near the apical end
| abutting the germ cells. It is less abundant on the rest of the follicle
| cell-follicle cell interface. Staining is the heaviest in a band around the
| follicle cell near the interface between the lateral and apical surfaces.
| The majority of <fbsym>FBgn0000117==arm</fbsym> protein in the ovary is found in the follicle cells
| but it is also observed in n rse cells and in the oocyte. Accumulation is
| germ cells is first seen at the anterior tip of the germarium. Similar
| intense staining is seen at the anterior tip of the testis. As with
| follicle cells, <fbsym>FBgn0000117==arm</fbsym> protein accumulates near or at the cell surface of
| germ cells but is not concentrated at any one position along the cell-cell
| interface. Protein accumulation appears to be heaviest where the nurse
| cell-nurse cell junction abuts the overlying follicle cells. It also
| accumulates in the cortical region of the oocyte. <fbsym>FBgn0000117==arm</fbsym> protein accumulates
| differentially in different follicle cells. Polar ollicle cells show more
| intense <fbsym>FBgn0000117==arm</fbsym> staining.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> O, A | female <a> follicle cell <p>
|<t> O, A | female <a> nurse cell <p>
|<t> O, A | female <a> oocyte <p>
CVCEL|cell-cell adherens junction
}

REFDSR
{
RDID|FBrf0079169
|Peifer et al.
|1994
CC|<fbsym>FBgn0000117==arm</fbsym> protein is phosphorylated on both serine or threonine and on tyrosine
| residues. The level of phosphorylation varies in different tissues and at
| different times of development. Phosphorylation of <fbsym>FBgn0000117==arm</fbsym> protein is
| negatively regulated by <fbsym>FBgn0004009==wg</fbsym> protein. <fbsym>FBgn0003371==sgg</fbsym> protein is required for <fbsym>FBgn0000117==arm</fbsym>
| protein phosphorylation.
}

REFDSR
{
RDID|FBrf0090729
|Orsulic and Peifer
|1996
CC|The binding sites on <fbsym>FBgn0000117==arm</fbsym> protein for <fbsym>FBgn0003391==shg</fbsym> protein and <fbsym>&agr:;Cat</fbsym> were
| mapped. The binding site for <fbsym>&agr:;Cat</fbsym> maps to the first 39 amino acids
| of <fbsym>FBgn0000117==arm</fbsym> protein. The region necessary for <fbsym>FBgn0003391==shg</fbsym> binding maps to the
| central repeats. The central repeat region also appears to be important for
| <fbsym>FBgn0000117==arm</fbsym> protein localization to adherens junctions.
}

REFDSR
{
RDID|FBrf0091133
|Pai et al.
|1996
CC|A 76 amino acid region of <fbsym>FBgn0000117==arm</fbsym> protein is necessary and sufficient for
| binding <fbsym>&agr;-Cat</fbsym> protein; point mutations in this region abolish
| <fbsym>&agr;-Cat</fbsym> binding in vitro. The N-terminal 258 amino acids of <fbsym>&agr;-Cat</fbsym>
| interact with <fbsym>FBgn0000117==arm</fbsym> protein. A large region of <fbsym>FBgn0000117==arm</fbsym> protein spanning six
| Armadillo repeats is required for <fbsym>FBgn0003391==shg</fbsym> protein binding; when mutations are
| introduced into repeats 3-8, binding is abolished. Forty one amino acids of
| the <fbsym>FBgn0003391==shg</fbsym> cytoplasmic tail are sufficient for <fbsym>FBgn0000117==arm</fbsym> protein binding.
}

REFDSR
{
RDID|FBrf0107755
|Hamada et al.
|1999
CC|<fbsym>FBgn0026597==Axn</fbsym> protein interacts with the Armadillo repeat domain of <fbsym>FBgn0000117==arm</fbsym> protein.
}

REF
{
REFM|FBrf0065529
|Peifer et al.
|1993
REFM|FBrf0079169
|Peifer et al.
|1994
REFM|FBrf0090729
|Orsulic and Peifer
|1996
REFM|FBrf0091133
|Pai et al.
|1996
REFM|FBrf0107755
|Hamada et al.
|1999
REFM|FBrf0111519
|Willert et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002893	SYM 1 Mhc<up>+</up>PD	AAL 1 -	PSZ 1 155 	HG 1 -	DBA 1 -	REF 1 1	DT 1 6 Jan 2000	RESZ 506
ID|FBpp0002893
SYM|Mhc<up>+</up>PD
SYN|minor-myosin
ASAL|<fbsym>FBal0068063==Mhc<up>+</up></fbsym>
DT|6 Jan 2000
|6 Jan 2000
ASGN|<fbsym>FBgn0002741==Mhc</fbsym>

REFDSR
{
RDID|FBrf0082353
|Miedema et al.
|1995
PSZ|155 | observed
BODP|The 155kD form of <fbsym>FBgn0002741==Mhc</fbsym> protein is mainly detected in testis.
CVBODP|<t> A | male <a> testis <p>
ASTR|<fbsym>FBtr0005450==Mhc<up>+</up>R4.5</fbsym>
|<fbsym>FBtr0005451==Mhc<up>+</up>R4.2</fbsym>
}

REF
{
REFM|FBrf0082353
|Miedema et al.
|1995
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0002896	SYM 1 aret<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 22 Dec 2000	RESZ 238
ID|FBpp0002896
SYM|aret<up>+</up>P
ASAL|<fbsym>FBal0068657==aret<up>+</up></fbsym>
DT|22 Dec 2000
|6 Jan 2000
ASGN|<fbsym>FBgn0000114==aret</fbsym>

REF
{
REFM|FBrf0098905
|Webster et al.
|1997
REFM|FBrf0107851
|Lie and Macdonald
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003022	SYM 1 &agr;Try-P	AAL 1 256	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 11 Apr 2000	RESZ 327
ID|FBpp0003022
SYM|&agr;Try-P
ASAL|<fbsym>FBal0074447==&agr;Try<up>+</up></fbsym>
DT|11 Apr 2000
|11 Apr 2000
ARGS|FBgn0003863
DARTS|FBtr0005397
ASGN|<fbsym>FBgn0003863==&agr;Try</fbsym>

REFDSR
{
RDID|FBrf0104946
|FlyBase
|1996-
AAL|256
ASTR|<fbsym>FBtr0005397==&agr;Try-RA</fbsym>
}

REF
{
REFM|FBrf0104946
|FlyBase
|1996-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003034	SYM 1 shi<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 13 Apr 2000	RESZ 194
ID|FBpp0003034
SYM|shi<up>+</up>P
ASAL|<fbsym>FBal0071044==shi<up>+</up></fbsym>
DT|13 Apr 2000
|13 Apr 2000
ASGN|<fbsym>FBgn0003392==shi</fbsym>

REF
{
REFM|FBrf0103356
|Roos and Kelly
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003059	SYM 1 Ecol\lacZ<up>P\T.W</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 13 Apr 2000	RESZ 472
ID|FBpp0003059
SYM|Ecol\lacZ<up>P\T.W</up>PA
ASAL|<fbsym>FBal0043887==Ecol\lacZ<up>P\T.W</up></fbsym>
DT|13 Apr 2000
|13 Apr 2000
ASGN|<fbsym>FBgn0014447==Ecol\lacZ</fbsym>

REFDSR
{
RDID|FBrf0049800
|Bier et al.
|1989
BODP|Observed expression always nuclear, independent of insertion site.
CVCEL|nucleus
CC|Nuclear expression ascribed to nuclear localization signal derived from
| <fbsym>FBgn0013311==P\T</fbsym> sequences.
}

REF
{
REFM|FBrf0049800
|Bier et al.
|1989
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003098	SYM 1 ttk<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 30 May 2000	RESZ 200
ID|FBpp0003098
SYM|ttk<up>+</up>P
ASAL|<fbsym>FBal0071410==ttk<up>+</up></fbsym>
DT|30 May 2000
|30 May 2000
ASGN|<fbsym>FBgn0003870==ttk</fbsym>

REF
{
REFM|FBrf0051631
|Harrison and Travers
|1990
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003143	SYM 1 &agr;-Cat<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 16 Aug 2000	RESZ 624
ID|FBpp0003143
SYM|&agr;-Cat<up>+</up>P
ASAL|<fbsym>FBal0066290==&agr;-Cat<up>+</up></fbsym>
DT|16 Aug 2000
|16 Aug 2000
ASGN|<fbsym>FBgn0010215==&agr;-Cat</fbsym>

REFDSR
{
RDID|FBrf0091133
|Pai et al.
|1996
CVCEL|adherens junction
CC|A 76 amino acid region of <fbsym>FBgn0000117==arm</fbsym> protein is necessary and sufficient for
| binding <fbsym>&agr;-Cat</fbsym> protein; point mutations in this region abolish
| <fbsym>&agr;-Cat</fbsym> binding in vitro. The N-terminal 258 amino acids of <fbsym>&agr;-Cat</fbsym>
| interact with <fbsym>FBgn0000117==arm</fbsym> protein.
}

REF
{
REFM|FBrf0091133
|Pai et al.
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003145	SYM 1 Dredd<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 2	DT 1 22 Dec 2000	RESZ 442
ID|FBpp0003145
SYM|Dredd<up>+</up>P
SYN|DCP2
ASAL|<fbsym>FBal0079409==Dredd<up>+</up></fbsym>
DT|22 Dec 2000
|16 Aug 2000
ASGN|<fbsym>FBgn0020381==Dredd</fbsym>

REFDSR
{
RDID|FBrf0099057
|Inohara et al.
|1997
HG|Homo sapiens | CASP8 (SWP:Q14790)
CC|<fbsym>FBgn0020381==Dredd</fbsym> protein has two death effector domains, and a caspase-like domain.
}

REF
{
REFM|FBrf0099057
|Inohara et al.
|1997
REFM|FBrf0112020
|Rodriguez et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003181	SYM 1 loco<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 22 Aug 2000	RESZ 200
ID|FBpp0003181
SYM|loco<up>+</up>P
ASAL|<fbsym>FBal0079315==loco<up>+</up></fbsym>
DT|22 Aug 2000
|22 Aug 2000
ASGN|<fbsym>FBgn0020278==loco</fbsym>

REF
{
REFM|FBrf0108191
|Granderath et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003258	SYM 1 Parp<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 443
ID|FBpp0003258
SYM|Parp<up>+</up>PA
ASAL|<fbsym>FBal0068145==Parp<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0010247==Parp</fbsym>

REFDSR
{
RDID|FBrf0102327
|Hanai et al.
|1998
ASTR|<fbsym>FBtr0006175==Parp<up>+</up>R2.6</fbsym>
CC|A smaller <fbsym>FBgn0010247==Parp</fbsym> protein which is generated from an alternatively spliced
| mRNA lacks the auto-modification domain.
}

REF
{
REFM|FBrf0102327
|Hanai et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003280	SYM 1 shot<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 1382
ID|FBpp0003280
SYM|shot<up>+</up>PA
SYN|isoform A
ASAL|<fbsym>FBal0071047==shot<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0013733==shot</fbsym>

REFDSR
{
RDID|FBrf0105832
|Gregory and Brown
|1998
ABOD|polyclonal
BODP|<fbsym>FBgn0013733==shot</fbsym> protein is expressed in specific epidermal cells that attach to
| muscles, linking the muscles to the exoskeleton. It is strongly expressed
| in the same cells that express high levels of PS integrins. Strong
| expression is also observed inthe proventriculus and the pharynx. Weak
| expression is observed in the PNS in the scolopale of the chordotonal organs.
CVBODP|immunolocalization
|<t> E | stage 16 <a> muscle attachment site <p>
|<t> E | stage 16 <a> embryonic/larval proventriculus <p>
|<t> E | stage 16 <a> embryonic/larval pharynx <p>
|<t> E | stage 16 <a> scolopidia <p>
ASTR|<fbsym>FBtr0006194==shot<up>+</up>RA</fbsym>
CC|The <fbsym>FBgn0013733==shot</fbsym> protein shows similarily to three distinct classes of proteins.
| The amino-terminal portion resembles the plakin class of cytoskeletal
| cross-linker proteins. The central portion of the protein consists of 22
| 109aa dystrophin-like repeats. The carboxy-terminal part of the protein has
| similarity to Gas2, an actin-associated protein expressed in
| growth-arrested cultured cells.
}

REF
{
REFM|FBrf0105832
|Gregory and Brown
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003281	SYM 1 shot<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 319
ID|FBpp0003281
SYM|shot<up>+</up>PB
SYN|isoform B
ASAL|<fbsym>FBal0071047==shot<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0013733==shot</fbsym>

REFDSR
{
RDID|FBrf0105832
|Gregory and Brown
|1998
ASTR|<fbsym>FBtr0006195==shot<up>+</up>RB</fbsym>
}

REF
{
REFM|FBrf0105832
|Gregory and Brown
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003282	SYM 1 shot<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 2	DT 1 21 Nov 2000	RESZ 2657
ID|FBpp0003282
SYM|shot<up>+</up>P
ASAL|<fbsym>FBal0071047==shot<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0013733==shot</fbsym>

REFDSR
{
RDID|FBrf0105940
|Strumpf and Volk
|1998
ABOD|polyclonal
BODP|<fbsym>FBgn0013733==shot</fbsym> protein is apparent from stage 14 of embryogenesis. In the last
| stages of muscle development, <fbsym>FBgn0013733==shot</fbsym> protein is found at high levels in
| muscle-bound tendon cells where it is concentrated at the surface,
| presumably along the membrane. Lower levels are observed in epidermal cells
| and chordotonal organs.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | stage >=14 <a> muscle attachment site <p>
|<t> E | stage 16 <a> tendon cell <p>
|<t> E | stage 16 <a> epidermis <p>
|<t> E | stage 16 <a> chordotonal organ <p>
CC|<fbsym>FBgn0013733==shot</fbsym> protein shows regions of similarity to three distinct vertebrate
| cytoskeletal-related protein families. The amino-terminal portion resembles
| the amino-terminal domain of plakin family members. The central portion has
| 22 repeats of 105-113 amino acids that are similar to the spectrin-like
| repeats found in dystrophin, &agr;-actinin, and spectrin. The carboxy
| terminal domain shows similarity to the Gar2/GAR22 family of
| cytoskeletal-related proteins.
}

REFDSR
{
RDID|FBrf0125142
|Lee et al.
|2000
BODP|<fbsym>FBgn0013733==shot</fbsym> protein is detected in developing axons starting in embryonic stage
| 12. It can be detected in the intersegmental nerve and in the cortical
| regions of the neuronal cell bodies of chordotonal and dorsal cluster
| sensory neurons. The antibody used for this analysis does not recognize the
| short isoforms of the protein.
CVBODP|immunolocalization
|<t> E | stage >=12 <a> axon <p>
|<t> E <a> chordotonal organ <p>
|<t> E <a> anterior fascicle <p>
|<t> E <a> sensory neuron <p>
CC|The longer <fbsym>FBgn0013733==shot</fbsym> proteins contain an N-terminal actin-binding domain, a
| long central triple helical coiled-coil domain, and a C-terminal domain
| that contains two EF-hand Ca<up>2+</up>-binding motifs and a region of
| homology to the growth arrest protein Gas2. At least 4 different promoters
| and alternative splicing occuring at a number of different sites throughout
| the gene lead to a number of different protein isoforms. Some isoforms lack
| some or all of the actin-binding domain at the N-terminal end. Some
| isoforms contain an extra 300aa within the central rod region and the
| various isoforms have different classes of globular C-terminal domains.
}

REF
{
REFM|FBrf0105940
|Strumpf and Volk
|1998
REFM|FBrf0125142
|Lee et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003325	SYM 1 shot<up>+</up>PC	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 291
ID|FBpp0003325
SYM|shot<up>+</up>PC
ASAL|<fbsym>FBal0071047==shot<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0013733==shot</fbsym>

REFDSR
{
RDID|FBrf0125142
|Lee et al.
|2000
ASTR|<fbsym>FBtr0006269==shot<up>+</up>RC</fbsym>
}

REF
{
REFM|FBrf0125142
|Lee et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003326	SYM 1 shot<up>+</up>PD	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 291
ID|FBpp0003326
SYM|shot<up>+</up>PD
ASAL|<fbsym>FBal0071047==shot<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0013733==shot</fbsym>

REFDSR
{
RDID|FBrf0125142
|Lee et al.
|2000
ASTR|<fbsym>FBtr0006270==shot<up>+</up>RD</fbsym>
}

REF
{
REFM|FBrf0125142
|Lee et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003328	SYM 1 shot<up>+</up>PF	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 291
ID|FBpp0003328
SYM|shot<up>+</up>PF
ASAL|<fbsym>FBal0071047==shot<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0013733==shot</fbsym>

REFDSR
{
RDID|FBrf0125142
|Lee et al.
|2000
ASTR|<fbsym>FBtr0006272==shot<up>+</up>RF</fbsym>
}

REF
{
REFM|FBrf0125142
|Lee et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003344	SYM 1 endos<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 1	DT 1 6 Jan 2005	RESZ 323
ID|FBpp0003344
SYM|endos<up>+</up>PA
SYN|l(3)S067006<up>+</up>PA
ASAL|<fbsym>FBal0134574==endos<up>+</up></fbsym>
DT|6 Jan 2005
|21 Nov 2000
ASGN|<fbsym>FBgn0061515==endos</fbsym>

REFDSR
{
RDID|FBrf0127030
|Burmester et al.
|2000
HG|C. elegans | C50D2.7 (Acc. AF040642)
}

REF
{
REFM|FBrf0127030
|Burmester et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003353	SYM 1 sbb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 392
ID|FBpp0003353
SYM|sbb<up>+</up>P
ASAL|<fbsym>FBal0095934==sbb<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0010575==sbb</fbsym>

REFDSR
{
RDID|FBrf0127316
|Senti et al.
|2000
BODP|<fbsym>FBgn0010575==sbb</fbsym> protein is widely expressed in eye-antennal discs.
CVBODP|immunolocalization
|<t> L <a> eye disc | ubiquitous <p>
}

REF
{
REFM|FBrf0127316
|Senti et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003377	SYM 1 babo<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 998
ID|FBpp0003377
SYM|babo<up>+</up>P
ASAL|<fbsym>FBal0066409==babo<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0011300==babo</fbsym>

REFDSR
{
RDID|FBrf0106271
|Brummel et al.
|1999
CC|<fbsym>FBgn0011300==babo</fbsym> protein activates TGF-&bgr;/Activin response elements, but not BMP
| response elements, in in vitro assays. Activated <fbsym>FBgn0011300==babo</fbsym> protein
| phosphorylates the C-terminal SSXS motif of <fbsym>FBgn0025800==Smox</fbsym> protein. <fbsym>FBgn0011655==Med</fbsym> and
| <fbsym>FBgn0025800==Smox</fbsym> proteins form some complexes in the absence of activated <fbsym>FBgn0011300==babo</fbsym>
| protein, but the level of complex formation increases significantly in the
| presence of the activated <fbsym>FBgn0011300==babo</fbsym> protein. <fbsym>FBgn0025800==Smox</fbsym> protein also interacts
| transiently with <fbsym>FBgn0003169==put</fbsym>-<fbsym>FBgn0011300==babo</fbsym> protein complexes.
}

REF
{
REFM|FBrf0106271
|Brummel et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003399	SYM 1 qtc<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 293
ID|FBpp0003399
SYM|qtc<up>+</up>PB
ASAL|<fbsym>FBal0101934==qtc<up>+</up></fbsym>
DT|21 Nov 2000
|21 Nov 2000
ASGN|<fbsym>FBgn0028572==qtc</fbsym>

REFDSR
{
RDID|FBrf0127087
|Gaines et al.
|2000
ASTR|<fbsym>FBtr0006373==qtc<up>+</up>RB</fbsym>
}

REF
{
REFM|FBrf0127087
|Gaines et al.
|2000
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003408	SYM 1 att<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 289
ID|FBpp0003408
SYM|att<up>+</up>PA
DT|21 Nov 2000
|21 Nov 2000

REFDSR
{
RDID|FBrf0089733
|Madigan et al.
|1996
HG|Bos taurus | GDC (X66035)
ASTR|<fbsym>FBtr0006390==att<up>+</up>R1.8</fbsym>
|<fbsym>FBtr0006391==att<up>+</up>R1.6</fbsym>
}

REF
{
REFM|FBrf0089733
|Madigan et al.
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003409	SYM 1 att<up>+</up>PB	AAL 1 -	PSZ 1 -	HG 1 +	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 742
ID|FBpp0003409
SYM|att<up>+</up>PB
DT|21 Nov 2000
|21 Nov 2000

REFDSR
{
RDID|FBrf0089733
|Madigan et al.
|1996
HG|Bos taurus | GDC (X66035)
ASTR|<fbsym>FBtr0006392==att<up>+</up>R1.4</fbsym>
CC|The testis-specific 1.4 kb <fbsym>FBgn0019839==att</fbsym> transcript has the potential to encode two
| distinct proteins. In vitro translation experiments demonstrate that both
| proteins can be produced. One protein, which may start at a non-consensus
| CUG, is a shorter version of the protein encoded by the soma-specific <fbsym>FBgn0019839==att</fbsym>
| transcript. The second putative ORF is in a different reading frame than
| the somatic transcript and has no homology to known proteins.
}

REF
{
REFM|FBrf0089733
|Madigan et al.
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003410	SYM 1 att<up>+</up>PC	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 21 Nov 2000	RESZ 734
ID|FBpp0003410
SYM|att<up>+</up>PC
DT|21 Nov 2000
|21 Nov 2000

REFDSR
{
RDID|FBrf0089733
|Madigan et al.
|1996
ASTR|<fbsym>FBtr0006392==att<up>+</up>R1.4</fbsym>
CC|The testis-specific 1.4 kb <fbsym>FBgn0019839==att</fbsym> transcript has the potential to encode two
| distinct proteins. In vitro translation experiments demonstrate that both
| proteins can be produced. One putative ORF, which may start at a
| non-consensus CUG, is a shorter version of the putative ORF encoded by the
| soma-specific <fbsym>FBgn0019839==att</fbsym> transcript. The second putative testis-specific ORF is
| in a different reading frame than the somatic ORF and has no homology to
| known proteins.
}

REF
{
REFM|FBrf0089733
|Madigan et al.
|1996
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003491	SYM 1 dl<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 12 Feb 2001	RESZ 185
ID|FBpp0003491
SYM|dl<up>+</up>P
ASAL|<fbsym>FBal0068833==dl<up>+</up></fbsym>
DT|12 Feb 2001
|12 Feb 2001
ASGN|<fbsym>FBgn0000462==dl</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003492	SYM 1 &agr;-Adaptin<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 2 May 2001	RESZ 236
ID|FBpp0003492
SYM|&agr;-Adaptin<up>+</up>P
SYN|dri<up>+</up>P
ASAL|<fbsym>FBal0075450==&agr;-Adaptin<up>+</up></fbsym>
DT|2 May 2001
|12 Feb 2001
ASGN|<fbsym>FBgn0015567==&agr;-Adaptin</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003497	SYM 1 cnc<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 12 Feb 2001	RESZ 873
ID|FBpp0003497
SYM|cnc<up>+</up>P
ASAL|<fbsym>FBal0068767==cnc<up>+</up></fbsym>
DT|12 Feb 2001
|12 Feb 2001
ASGN|<fbsym>FBgn0000338==cnc</fbsym>

REFDSR
{
RDID|FBrf0105883
|McGinnis et al.
|1998
BODP|<fbsym>FBgn0000338==cnc</fbsym> antiserum detects a low level ubiquitous staining in syncytial
| embryos. From stage 6-14, staining is localized to the mandibular and
| labral segments. After stage 14 a low level ubiquitous staining is observed
| in addition to the strong staining in the mandibular and labral cells. The
| antibody recognizes all <fbsym>FBgn0000338==cnc</fbsym> isoforms.
ASM|immunolocalization
CVBODP|immunolocalization
|<t> E | stage >=6 <a> embryonic mandibular segment <p>
|<t> E | stage >=6 <a> embryonic labral segment <p>
|<t> E | early <a>  <p> ubiquitous
|<t> E | stage >14 <a>  <p> ubiquitous
}

REF
{
REFM|FBrf0105883
|McGinnis et al.
|1998
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003502	SYM 1 ATPsyn-&ggr;<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 12 Feb 2001	RESZ 331
ID|FBpp0003502
SYM|ATPsyn-&ggr;<up>+</up>PA
ASAL|<fbsym>FBal0079279==ATPsyn-&ggr;<up>+</up></fbsym>
DT|12 Feb 2001
|12 Feb 2001
ASGN|<fbsym>FBgn0020235==ATPsyn-&ggr;</fbsym>

REFDSR
{
RDID|FBrf0106292
|Caggese et al.
|1999
ASTR|<fbsym>FBtr0006677==ATPsyn-&ggr;<up>+</up>RA</fbsym>
}

REF
{
REFM|FBrf0106292
|Caggese et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003505	SYM 1 Scs&agr;<up>+</up>PA	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 12 Feb 2001	RESZ 315
ID|FBpp0003505
SYM|Scs&agr;<up>+</up>PA
ASAL|<fbsym>FBal0074212==Scs&agr;<up>+</up></fbsym>
DT|12 Feb 2001
|12 Feb 2001
ASGN|<fbsym>FBgn0004888==Scs&agr;</fbsym>

REFDSR
{
RDID|FBrf0106292
|Caggese et al.
|1999
ASTR|<fbsym>FBtr0006681==Scs&agr;<up>+</up>RA</fbsym>
}

REF
{
REFM|FBrf0106292
|Caggese et al.
|1999
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003515	SYM 1 kel<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 12 Feb 2001	RESZ 587
ID|FBpp0003515
SYM|kel<up>+</up>P
ASAL|<fbsym>FBal0069287==kel<up>+</up></fbsym>
DT|12 Feb 2001
|12 Feb 2001
ASGN|<fbsym>FBgn0001301==kel</fbsym>

REFDSR
{
RDID|FBrf0074302
|Robinson et al.
|1994
BODP|<fbsym>FBgn0001301==kel</fbsym> protein is observed in ring canals starting in germarium region 3.
| Initially staining is seen in a subset of ring canals. All ring canals are
| stained by stage 3.
CVBODP|immunolocalization
|<t> O,A | stage >S1 <a> nurse cell ring canal <p>
|<t> O,A | germarium region 3 <a> nurse cell ring canal <p>
}

REF
{
REFM|FBrf0074302
|Robinson et al.
|1994
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003544	SYM 1 Dl<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 214
ID|FBpp0003544
SYM|Dl<up>+</up>P
ASAL|<fbsym>FBal0066914==Dl<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ABODURL|c594.9b.html C594.9B
ASGN|<fbsym>FBgn0000463==Dl</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003546	SYM 1 chp<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 213
ID|FBpp0003546
SYM|chp<up>+</up>P
ASAL|<fbsym>FBal0068756==chp<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ABODURL|24b10.html 24B10
ASGN|<fbsym>FBgn0000313==chp</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003547	SYM 1 eya<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 15 Oct 2001	RESZ 236
ID|FBpp0003547
SYM|eya<up>+</up>P
SYN|cli<up>+</up>P
ASAL|<fbsym>FBal0126664==eya<up>+</up></fbsym>
DT|15 Oct 2001
|23 Apr 2001
ABODURL|eya10h6.html eya10H6
ASGN|<fbsym>FBgn0000320==eya</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003549	SYM 1 crb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 209
ID|FBpp0003549
SYM|crb<up>+</up>P
ASAL|<fbsym>FBal0068782==crb<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ABODURL|cq4.html Cq4
ASGN|<fbsym>FBgn0000368==crb</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003550	SYM 1 orb<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 293
ID|FBpp0003550
SYM|orb<up>+</up>P
ASAL|<fbsym>FBal0070847==orb<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ABODURL|orb4h8.html <fbsym>FBgn0004882==orb</fbsym> 4H8
|orb6h4.html <fbsym>FBgn0004882==orb</fbsym> 6H4
ASGN|<fbsym>FBgn0004882==orb</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003554	SYM 1 &agr;-Spec<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 209
ID|FBpp0003554
SYM|&agr;-Spec<up>+</up>P
ASAL|<fbsym>FBal0066293==&agr;-Spec<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ASGN|<fbsym>FBgn0003470==&agr;-Spec</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003558	SYM 1 en<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 185
ID|FBpp0003558
SYM|en<up>+</up>P
ASAL|<fbsym>FBal0068909==en<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ASGN|<fbsym>FBgn0000577==en</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003560	SYM 1 Nrt<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 188
ID|FBpp0003560
SYM|Nrt<up>+</up>P
ASAL|<fbsym>FBal0068126==Nrt<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ASGN|<fbsym>FBgn0004108==Nrt</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003562	SYM 1 CycA<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 191
ID|FBpp0003562
SYM|CycA<up>+</up>P
ASAL|<fbsym>FBal0066524==CycA<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ASGN|<fbsym>FBgn0000404==CycA</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003564	SYM 1 pnut<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 191
ID|FBpp0003564
SYM|pnut<up>+</up>P
ASAL|<fbsym>FBal0070903==pnut<up>+</up></fbsym>
DT|23 Apr 2001
|23 Apr 2001
ASGN|<fbsym>FBgn0013726==pnut</fbsym>

REF
{
REFM|FBrf0105495
|FlyBase
|1992-
}

}

# EOR

PPR
{

RETE|ID 1 FBpp0003566	SYM 1 elav<up>+</up>P	AAL 1 -	PSZ 1 -	HG 1 -	DBA 1 -	REF 1 1	DT 1 23 Apr 2001	RESZ 191
ID|FBpp0003566
SYM|elav<up>+</up>P
ASAL|<fbsym>FBal00689