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ARF GTPase-activating protein Git (ARF GAP GIT) (dGIT protein) (G protein-coupled receptor kinase interacting ArfGAP)

 GIT_DROME               Reviewed;         731 AA.
Q95RG8; Q9V5N5;
02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
02-JUN-2021, entry version 186.
RecName: Full=ARF GTPase-activating protein Git;
Short=ARF GAP GIT;
Short=dGIT protein {ECO:0000303|PubMed:18996366};
AltName: Full=G protein-coupled receptor kinase interacting ArfGAP;
Name=Git; Synonyms=arfgap2;
ORFNames=CG16728 {ECO:0000312|FlyBase:FBgn0033539};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic
review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
FUNCTION, INTERACTION WITH PIX AND PAK, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=18996366; DOI=10.1016/j.ydbio.2008.09.001;
Bahri S.M., Choy J.M., Manser E., Lim L., Yang X.;
"The Drosophila homologue of Arf-GAP GIT1, dGIT, is required for proper
muscle morphogenesis and guidance during embryogenesis.";
Dev. Biol. 325:15-23(2009).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25792865; DOI=10.5607/en.2015.24.1.8;
Hong S.T., Mah W.;
"A critical role of GIT1 in vertebrate and invertebrate brain
development.";
Exp. Neurobiol. 24:8-16(2015).
-!- FUNCTION: GTPase-activating protein for ADP ribosylation factor family
members, including ARF1. Multidomain scaffold protein that interacts
with numerous proteins and therefore participates in many cellular
functions, including receptor internalization, focal adhesion
remodeling, and signaling by both G protein-coupled receptors and
tyrosine kinase receptors (By similarity). Through Pak activation, may
positively regulate microtubule nucleation during interphase. May play
a role in the regulation of cytokinesis (By similarity). During
embryogenesis, promotes proper muscle morphogenesis and proper guidance
and targeting of subsets of myotubes (PubMed:18996366). Required for
the recruitment of Pak to muscle attachments in the embryo, probably
indirectly through pix/dPIX (PubMed:18996366). May be important for
brain development (PubMed:25792865). {ECO:0000250|UniProtKB:Q9Y2X7,
ECO:0000250|UniProtKB:Q9Z272, ECO:0000269|PubMed:18996366,
ECO:0000269|PubMed:25792865}.
-!- SUBUNIT: May form homodimers (via coiled coil) (By similarity). Forms a
complex with pix and Pak; the interaction with Pak may be indirect and
mediated by pix/dPIX (PubMed:18996366). {ECO:0000250|UniProtKB:Q9Z272,
ECO:0000269|PubMed:18996366}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18996366}. Cell
junction, synapse {ECO:0000250|UniProtKB:Q9Y2X7}. Cell junction, focal
adhesion {ECO:0000250|UniProtKB:Q9Y2X7}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:Q9Y2X7}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2X7}.
Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y2X7}.
Note=Localizes to the leading edge of growing myotubes.
{ECO:0000269|PubMed:18996366}.
-!- TISSUE SPECIFICITY: Expressed in embryonic muscle syncytia (at protein
level). {ECO:0000269|PubMed:18996366}.
-!- DEVELOPMENTAL STAGE: Detected muscle syncytia in embryonic stage 14 and
early stage 15. At mid stage 15, localizes at the leading edge of
growing myotubes. In the ventral ends of VO5 and VO6 muscles enriched
at the base of membrane protrusions at the leading edge of growing
myotubes, while it is less expressed in filopodia. In the late stage
embryo, concentrated at all muscle attachment sites, although subtle
variation in expression and/or localization may be observed in
different muscles subsets. Remains enriched in myotubes until the end
of embryogenesis (at protein level). {ECO:0000269|PubMed:18996366}.
-!- DOMAIN: The coiled coil region may mediate dimerization.
{ECO:0000250|UniProtKB:Q9Z272}.
-!- DISRUPTION PHENOTYPE: Homozygous knockout flies show a semi-lethal
phenotype and exhibit defective wing morphology at 100% penetrance
(PubMed:18996366). Mutant embryos show striking guidance phenotypes in
ventral oblique muscle 5 (VO5) and ventral oblique muscle 6 (VO6),
characterized by bypass and mistargeting of the mutant muscles toward
the ventral midline. Defects in targeting of the growing ventral tips
of mutant muscles toward the ventral midline are already detectable at
late stage 14/early stage 15 embryos. Defects in other ventral muscles
are less obvious, although ventral acute muscle 3 (VA3) occasionally
show mistargeting toward the ventral midline (PubMed:18996366). Defects
in number and shape of subsets of muscles are also observed, but at low
frequency (PubMed:18996366). Adult knockout flies show decreased
central brain size and abnormal morphology of the mushroom body, the
most common pattern being early termination of one alpha-lobe. The
penetrance of the impaired mushroom body development is incomplete
(PubMed:25792865). {ECO:0000269|PubMed:18996366,
ECO:0000269|PubMed:25792865}.
---------------------------------------------------------------------------
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EMBL; AE013599; AAF58766.2; -; Genomic_DNA.
EMBL; AY061380; AAL28928.1; -; mRNA.
RefSeq; NP_610599.3; NM_136755.4.
SMR; Q95RG8; -.
IntAct; Q95RG8; 10.
STRING; 7227.FBpp0087353; -.
PRIDE; Q95RG8; -.
DNASU; 36122; -.
EnsemblMetazoa; FBtr0088258; FBpp0087353; FBgn0033539.
GeneID; 36122; -.
KEGG; dme:Dmel_CG16728; -.
UCSC; CG16728-RA; d. melanogaster.
CTD; 36122; -.
FlyBase; FBgn0033539; Git.
eggNOG; KOG0818; Eukaryota.
GeneTree; ENSGT00940000169561; -.
HOGENOM; CLU_009739_0_0_1; -.
OMA; PASMYER; -.
OrthoDB; 349344at2759; -.
Reactome; R-DME-3928664; Ephrin signaling.
BioGRID-ORCS; 36122; 0 hits in 3 CRISPR screens.
GenomeRNAi; 36122; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0033539; Expressed in embryo and 44 other tissues.
GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
GO; GO:0005096; F:GTPase activator activity; ISM:FlyBase.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0060090; F:molecular adaptor activity; IMP:FlyBase.
GO; GO:0007420; P:brain development; IMP:UniProtKB.
GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
GO; GO:0046621; P:negative regulation of organ growth; IGI:FlyBase.
GO; GO:0035332; P:positive regulation of hippo signaling; IGI:FlyBase.
GO; GO:1905383; P:protein localization to presynapse; IMP:FlyBase.
GO; GO:0043087; P:regulation of GTPase activity; ISM:FlyBase.
GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
GO; GO:0099504; P:synaptic vesicle cycle; IMP:FlyBase.
GO; GO:0036465; P:synaptic vesicle recycling; IMP:FlyBase.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 3.30.40.160; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR037278; ARFGAP/RecO.
InterPro; IPR001164; ArfGAP_dom.
InterPro; IPR038508; ArfGAP_dom_sf.
InterPro; IPR022018; GIT1_C.
InterPro; IPR013724; GIT_SHD.
Pfam; PF01412; ArfGap; 1.
Pfam; PF12205; GIT1_C; 1.
Pfam; PF08518; GIT_SHD; 2.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00248; ANK; 2.
SMART; SM00105; ArfGap; 1.
SMART; SM00555; GIT; 2.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57863; SSF57863; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
PROSITE; PS50115; ARFGAP; 1.
1: Evidence at protein level;
ANK repeat; Cell junction; Cell projection; Coiled coil; Cytoplasm;
Cytoskeleton; GTPase activation; Metal-binding; Reference proteome; Repeat;
Synapse; Zinc; Zinc-finger.
CHAIN 1..731
/note="ARF GTPase-activating protein Git"
/id="PRO_0000452578"
DOMAIN 32..168
/note="Arf-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
REPEAT 216..245
/note="ANK 1"
/evidence="ECO:0000255"
REPEAT 249..278
/note="ANK 2"
/evidence="ECO:0000255"
ZN_FING 49..72
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
COILED 477..518
/evidence="ECO:0000255"
SEQUENCE 731 AA; 80773 MW; 6E7680AE32155B3A CRC64;
MCFASSIIEA HRKLFIAPPD LDHSDPATPT ISTRSKMPRG KSRLQTEVCG DCGAGDPSWA
SINRGILLCA DCCSVHRSLG RHISIVKSLR QGNWEPSVLN FVNSLNAHGA NSVWEHHLLD
GSTNSTGGKH VPRWRKPTPK DALHPTKSDF IKAKHVNLTF VLKPSLQDDD DGNGSAGCLE
QELSRQLHAS VRTSNLETSL RFLVQGADPN YYHEDKLSTP LHMAAKFGQA SQIEMLLIYG
ADVNALDGNG MTPLELARAN NHNTIAERLL DAMYDVTDRI ITFLGGKKPD HASGRHMIIP
DANGADISEQ LKIARGKLQL VPNKMFEELV MDLYDEVDRR ECEAIWSTST LNADHATVPF
LPANPFLSAT RNQGRQKLAR FNRAEFTGLL TDVLVDAMRR QNMANLRPMD APVAGHQSLQ
SLPYANNSML LGSFEQGGHD PNLSDDEPIY DPVASDDDYA PVPPMAQQAI VHTPPRSANS
HNEMETLRKQ LNDYKSEINQ LKNVVQMLSS ENTQLKSKFS SASNNSVYDE PLRIDLSLSS
PDTEHEPLSL PEGGTANGES GSSNDSSNQS TIKRPASMYE RRLVPNVAKG NTDIRNTTSM
YQMAGDGKPF GEEVKVRSDL VTRRLKELIR AMQPVPEDQK QSIAPHGELI RSAVTDLIAL
YANLPPNASD PSRETLKLLT RQNILIQHEC ENLQKAIEAD DKQAIQKNTL EVRDCAFHIA
SAIKTLVLQF Y


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Related Genes :
[Git arfgap2 CG16728] ARF GTPase-activating protein Git (ARF GAP GIT) (dGIT protein) (G protein-coupled receptor kinase interacting ArfGAP)
[ARFGAP1 ARF1GAP] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[Arfgap1 Arf1gap] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[ASAP1 DDEF1 KIAA1249 PAG2] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[AGD3 FKD2 SFC VAN3 At5g13300 T31B5.120] ADP-ribosylation factor GTPase-activating protein AGD3 (ARF GAP AGD3) (Protein ARF-GAP DOMAIN 3) (AtAGD3) (Protein FORKED 2) (Protein SCARFACE) (Protein VASCULAR NETWORK 3)
[AGAP3 CENTG3] Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3 (AGAP-3) (CRAM-associated GTPase) (CRAG) (Centaurin-gamma-3) (Cnt-g3) (MR1-interacting protein) (MRIP-1)
[Asap1 Ddef1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[AGD1 At5g61980 K22G18.9] ADP-ribosylation factor GTPase-activating protein AGD1 (ARF GAP AGD1) (Protein ARF-GAP DOMAIN 1) (AtAGD1)
[Arfgap1 Arf1gap] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[ASAP1 DDEF1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[AGFG1 HRB RAB RIP] Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein)
[ACAP1 CENTB1 KIAA0050] Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (Centaurin-beta-1) (Cnt-b1)
[Grk5 Gprk5] G protein-coupled receptor kinase 5 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK5)
[Agfg1 Hrb Rip] Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein homolog) (Nucleoporin-like protein RIP)
[GRK5 GPRK5] G protein-coupled receptor kinase 5 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK5)
[Arhgap32 Grit Kiaa0712 Rics] Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)
[Pak DPAK Dpak1 CG10295] Serine/threonine-protein kinase Pak (EC 2.7.11.1)
[ARFGEF1 ARFGEP1 BIG1] Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)
[TRIP12 KIAA0045 ULF] E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) (E3 ubiquitin-protein ligase for Arf) (ULF) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12)
[RALGAPA1 GARNL1 KIAA0884 TULIP1] Ral GTPase-activating protein subunit alpha-1 (GAP-related-interacting partner to E12) (GRIPE) (GTPase-activating Rap/Ran-GAP domain-like 1) (Tuberin-like protein 1) (p240)
[F2RL1 GPR11 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]
[ARHGAP35 GRF1 GRLF1 KIAA1722 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Glucocorticoid receptor repression factor 1) (GRF-1) (Rho GAP p190A) (p190-A)
[GRK6 GPRK6] G protein-coupled receptor kinase 6 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK6)
[ARF1] ADP-ribosylation factor 1
[Arhgap35 Grlf1 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (GAP-associated protein p190) (Glucocorticoid receptor DNA-binding factor 1)
[G3BP1 G3BP] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1)
[git5 gpb1 pi017 SPBC32H8.07] Guanine nucleotide-binding protein subunit beta
[RASA1 GAP RASA] Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP)
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)

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