ID SRGP1_HUMAN Reviewed; 1085 AA.
AC Q7Z6B7; Q9H8A3; Q9P2P2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 97.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 1;
DE Short=srGAP1;
DE AltName: Full=Rho GTPase-activating protein 13;
GN Name=SRGAP1; Synonyms=ARHGAP13, KIAA1304;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-1085 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ROBO1; CDC42 AND
RP RHOA.
RX PubMed=11672528; DOI=10.1016/S0092-8674(01)00530-X;
RA Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H.,
RA Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.;
RT "Signal transduction in neuronal migration: roles of GTPase activating
RT proteins and the small GTPase Cdc42 in the Slit-Robo pathway.";
RL Cell 107:209-221(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999; THR-1001 AND
RP SER-1032, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL
RT (CD178) by phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP HETEROOLIGOMERIZATION, AND F-BAR DOMAIN.
RX PubMed=22467852; DOI=10.1242/jcs.098962;
RA Coutinho-Budd J., Ghukasyan V., Zylka M.J., Polleux F.;
RT "The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially
RT regulate membrane deformation.";
RL J. Cell Sci. 125:3390-3401(2012).
CC -!- FUNCTION: GTPase-activating protein for RhoA and Cdc42 small
CC GTPases. Together with CDC42 seems to be involved in the pathway
CC mediating the repulsive signaling of Robo and Slit proteins in
CC neuronal migration. SLIT2, probably through interaction with
CC ROBO1, increases the interaction of SRGAP1 with ROBO1 and
CC inactivates CDC42.
CC -!- SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP2
CC and SRGAP3 through its F-BAR domain. Interacts with ROBO1, CDC42
CC and RHOA. Interacts with FASLG.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z6B7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6B7-2; Sequence=VSP_010580;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, kidney, and testis.
CC -!- DOMAIN: The F-BAR domain mediates oligomerization, binds
CC membranes, and constrains plasma membrane protrusions.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92542.1; Type=Erroneous initiation;
CC Sequence=BAA92542.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR EMBL; BC053903; AAH53903.1; -; mRNA.
DR EMBL; AB037725; BAA92542.1; ALT_INIT; mRNA.
DR IPI; IPI00376259; -.
DR IPI; IPI00414827; -.
DR PIR; G59436; G59436.
DR RefSeq; NP_065813.1; NM_020762.2.
DR UniGene; Hs.210751; -.
DR UniGene; Hs.593803; -.
DR ProteinModelPortal; Q7Z6B7; -.
DR IntAct; Q7Z6B7; 1.
DR MINT; MINT-3308471; -.
DR STRING; 9606.ENSP00000347198; -.
DR PhosphoSite; Q7Z6B7; -.
DR DMDM; 48428624; -.
DR PaxDb; Q7Z6B7; -.
DR PRIDE; Q7Z6B7; -.
DR DNASU; 57522; -.
DR Ensembl; ENST00000355086; ENSP00000347198; ENSG00000196935.
DR Ensembl; ENST00000357825; ENSP00000350480; ENSG00000196935.
DR GeneID; 57522; -.
DR KEGG; hsa:57522; -.
DR UCSC; uc001srv.2; human.
DR UCSC; uc010ssp.1; human.
DR CTD; 57522; -.
DR GeneCards; GC12P064238; -.
DR HGNC; HGNC:17382; SRGAP1.
DR HPA; HPA052416; -.
DR MIM; 606523; gene.
DR neXtProt; NX_Q7Z6B7; -.
DR PharmGKB; PA134887956; -.
DR eggNOG; NOG264793; -.
DR HOGENOM; HOG000039980; -.
DR HOVERGEN; HBG051637; -.
DR InParanoid; Q7Z6B7; -.
DR KO; K07526; -.
DR OMA; ADKSCTM; -.
DR OrthoDB; EOG4SJ5D1; -.
DR PhylomeDB; Q7Z6B7; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_96538; Developmental Biology.
DR ChiTaRS; SRGAP1; human.
DR GenomeRNAi; 57522; -.
DR NextBio; 63902; -.
DR ArrayExpress; Q7Z6B7; -.
DR Bgee; Q7Z6B7; -.
DR CleanEx; HS_SRGAP1; -.
DR Genevestigator; Q7Z6B7; -.
DR GermOnline; ENSG00000196935; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005100; F:Rho GTPase activator activity; IEA:Compara.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0016477; P:cell migration; IEA:Compara.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Compara.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; Rho_GAP; 1.
DR SUPFAM; SSF50044; SH3; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW GTPase activation; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1 1085 SLIT-ROBO Rho GTPase-activating protein
FT 1.
FT /FTId=PRO_0000056765.
FT DOMAIN 22 87 FCH.
FT DOMAIN 506 694 Rho-GAP.
FT DOMAIN 743 802 SH3.
FT REGION 1 516 F-BAR domain.
FT COILED 351 390 Potential.
FT COILED 956 985 Potential.
FT COMPBIAS 854 857 Poly-Pro.
FT COMPBIAS 909 912 Poly-Arg.
FT COMPBIAS 1027 1032 Poly-Ser.
FT MOD_RES 999 999 Phosphoserine.
FT MOD_RES 1001 1001 Phosphothreonine.
FT MOD_RES 1032 1032 Phosphoserine.
FT VAR_SEQ 479 513 RPPNVPPKPQKHRKSRPRSQYNTKLFNGDLETFVK -> SR
FT GRRNSHTRHQ (in isoform 2).
FT /FTId=VSP_010580.
SQ SEQUENCE 1085 AA; 124264 MW; D7ED1F651344F0D9 CRC64;
MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ DFFRKKAEIE
TEYSRNLEKL AERFMAKTRS TKDHQQYKKD QNLLSPVNCW YLLLNQVRRE SKDHATLSDI
YLNNVIMRFM QISEDSTRMF KKSKEIAFQL HEDLMKVLNE LYTVMKTYHM YHAESISAES
KLKEAEKQEE KQIGRSGDPV FHIRLEERHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR
NEYLLTLEAT NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD
IIENAVDNLE PRSDKQRFME MYPAAFCPPM KFEFQSHMGD EVCQVSAQQP VQAELMLRYQ
QLQSRLATLK IENEEVKKTT EATLQTIQDM VTIEDYDVSE CFQHSRSTES VKSTVSETYL
SKPSIAKRRA NQQETEQFYF MKLREYLEGS NLITKLQAKH DLLQRTLGEG HRAEYMTTRP
PNVPPKPQKH RKSRPRSQYN TKLFNGDLET FVKDSGQVIP LIVESCIRFI NLYGLQHQGI
FRVSGSQVEV NDIKNSFERG ENPLADDQSN HDINSVAGVL KLYFRGLENP LFPKERFNDL
ISCIRIDNLY ERALHIRKLL LTLPRSVLIV MRYLFAFLNH LSQYSDENMM DPYNLAICFG
PTLMPVPEIQ DQVSCQAHVN EIIKTIIIHH ETIFPDAKEL DGPVYEKCMA GDDYCDSPYS
EHGTLEEVDQ DAGTEPHTSE DECEPIEAIA KFDYVGRSAR ELSFKKGASL LLYHRASEDW
WEGRHNGIDG LVPHQYIVVQ DMDDTFSDTL SQKADSEASS GPVTEDKSSS KDMNSPTDRH
PDGYLARQRK RGEPPPPVRR PGRTSDGHCP LHPPHALSNS SVDLGSPSLA SHPRGLLQNR
GLNNDSPERR RRPGHGSLTN ISRHDSLKKI DSPPIRRSTS SGQYTGFNDH KPLDPETIAQ
DIEETMNTAL NELRELERQS TAKHAPDVVL DTLEQVKNSP TPATSTESLS PLHNVALRSS
EPQIRRSTSS SSDTMSTFKP MVAPRMGVQL KPPALRPKPA VLPKTNPTIG PAPPPQGPTD
KSCTM
//
