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Database: UniProt
Entry: Q7Z6B7
LinkDB: Q7Z6B7
Original site: Q7Z6B7 
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   06-JUL-2016, entry version 128.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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 DOMAIN F-BAR.
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).
RN   [11]
RP   INVOLVEMENT IN NMTC2, VARIANTS NMTC2 HIS-149; THR-275; CYS-617 AND
RP   ARG-875, AND CHARACTERIZATION OF VARIANTS NMTC2 HIS-149; THR-275;
RP   CYS-617 AND ARG-875.
RX   PubMed=23539728; DOI=10.1210/jc.2012-3823;
RA   He H., Bronisz A., Liyanarachchi S., Nagy R., Li W., Huang Y.,
RA   Akagi K., Saji M., Kula D., Wojcicka A., Sebastian N., Wen B.,
RA   Puch Z., Kalemba M., Stachlewska E., Czetwertynska M., Dlugosinska J.,
RA   Dymecka K., Ploski R., Krawczyk M., Morrison P.J., Ringel M.D.,
RA   Kloos R.T., Jazdzewski K., Symer D.E., Vieland V.J., Ostrowski M.,
RA   Jarzab B., de la Chapelle A.;
RT   "SRGAP1 is a candidate gene for papillary thyroid carcinoma
RT   susceptibility.";
RL   J. Clin. Endocrinol. Metab. 98:E973-E980(2013).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-835; SER-917;
RP   SER-932 AND SER-1032, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
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. {ECO:0000269|PubMed:11672528}.
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. {ECO:0000269|PubMed:11672528,
CC       ECO:0000269|PubMed:19807924, ECO:0000305}.
CC   -!- INTERACTION:
CC       P42858:HTT; NbExp=4; IntAct=EBI-2481729, EBI-466029;
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       {ECO:0000269|PubMed:11672528}.
CC   -!- DOMAIN: The F-BAR domain mediates oligomerization, binds
CC       membranes, and constrains plasma membrane protrusions.
CC       {ECO:0000269|PubMed:22467852}.
CC   -!- DISEASE: Thyroid cancer, non-medullary, 2 (NMTC2) [MIM:188470]: A
CC       form of non-medullary thyroid cancer (NMTC), a cancer
CC       characterized by tumors originating from the thyroid follicular
CC       cells. NMTCs represent approximately 95% of all cases of thyroid
CC       cancer and are classified into papillary, follicular, Hurthle
CC       cell, and anaplastic neoplasms. {ECO:0000269|PubMed:23539728}.
CC       Note=Disease susceptibility is associated with variations
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Contains 1 F-BAR domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU01077}.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00172}.
CC   -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00192}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92542.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAA92542.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
DR   EMBL; BC053903; AAH53903.1; -; mRNA.
DR   EMBL; AB037725; BAA92542.1; ALT_INIT; mRNA.
DR   CCDS; CCDS8967.1; -. [Q7Z6B7-1]
DR   PIR; G59436; G59436.
DR   RefSeq; NP_065813.1; NM_020762.2. [Q7Z6B7-1]
DR   RefSeq; XP_005269099.1; XM_005269042.2. [Q7Z6B7-2]
DR   UniGene; Hs.210751; -.
DR   UniGene; Hs.593803; -.
DR   ProteinModelPortal; Q7Z6B7; -.
DR   SMR; Q7Z6B7; 482-694, 745-799.
DR   BioGrid; 121583; 8.
DR   DIP; DIP-53826N; -.
DR   IntAct; Q7Z6B7; 7.
DR   MINT; MINT-3308471; -.
DR   STRING; 9606.ENSP00000347198; -.
DR   iPTMnet; Q7Z6B7; -.
DR   PhosphoSite; Q7Z6B7; -.
DR   BioMuta; SRGAP1; -.
DR   DMDM; 48428624; -.
DR   EPD; Q7Z6B7; -.
DR   MaxQB; Q7Z6B7; -.
DR   PaxDb; Q7Z6B7; -.
DR   PeptideAtlas; Q7Z6B7; -.
DR   PRIDE; Q7Z6B7; -.
DR   DNASU; 57522; -.
DR   Ensembl; ENST00000355086; ENSP00000347198; ENSG00000196935. [Q7Z6B7-1]
DR   GeneID; 57522; -.
DR   KEGG; hsa:57522; -.
DR   UCSC; uc010ssp.2; human. [Q7Z6B7-1]
DR   CTD; 57522; -.
DR   GeneCards; SRGAP1; -.
DR   HGNC; HGNC:17382; SRGAP1.
DR   HPA; HPA052416; -.
DR   MIM; 188470; phenotype.
DR   MIM; 606523; gene.
DR   neXtProt; NX_Q7Z6B7; -.
DR   PharmGKB; PA134887956; -.
DR   eggNOG; KOG3565; Eukaryota.
DR   eggNOG; ENOG410XS44; LUCA.
DR   GeneTree; ENSGT00760000118863; -.
DR   HOGENOM; HOG000039980; -.
DR   HOVERGEN; HBG051637; -.
DR   InParanoid; Q7Z6B7; -.
DR   KO; K07526; -.
DR   OMA; MEMYPTA; -.
DR   OrthoDB; EOG7966FQ; -.
DR   PhylomeDB; Q7Z6B7; -.
DR   TreeFam; TF315892; -.
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
DR   Reactome; R-HSA-428543; Inactivation of Cdc42 and Rac.
DR   ChiTaRS; SRGAP1; human.
DR   GeneWiki; SRGAP1; -.
DR   GenomeRNAi; 57522; -.
DR   PRO; PR:Q7Z6B7; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; Q7Z6B7; -.
DR   CleanEx; HS_SRGAP1; -.
DR   ExpressionAtlas; Q7Z6B7; baseline and differential.
DR   Genevisible; Q7Z6B7; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0048365; F:Rac GTPase binding; IBA:GO_Central.
DR   GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR031160; F_BAR.
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; SSF48350; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS51741; F_BAR; 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   Disease mutation; GTPase activation; Phosphoprotein;
KW   Reference proteome; SH3 domain.
FT   CHAIN         1   1085       SLIT-ROBO Rho GTPase-activating protein
FT                                1.
FT                                /FTId=PRO_0000056765.
FT   DOMAIN       19    314       F-BAR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01077}.
FT   DOMAIN      506    694       Rho-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00172}.
FT   DOMAIN      743    802       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   COILED      351    390       {ECO:0000255}.
FT   COILED      956    985       {ECO:0000255}.
FT   COMPBIAS    854    857       Poly-Pro.
FT   COMPBIAS    909    912       Poly-Arg.
FT   COMPBIAS   1027   1032       Poly-Ser.
FT   MOD_RES     196    196       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:D4A208}.
FT   MOD_RES     416    416       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     515    515       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q91Z67}.
FT   MOD_RES     835    835       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     917    917       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     932    932       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     999    999       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1001   1001       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1010   1010       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O75044}.
FT   MOD_RES    1029   1029       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O75044}.
FT   MOD_RES    1032   1032       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ     479    513       RPPNVPPKPQKHRKSRPRSQYNTKLFNGDLETFVK -> SR
FT                                GRRNSHTRHQ (in isoform 2).
FT                                {ECO:0000303|PubMed:10718198}.
FT                                /FTId=VSP_010580.
FT   VARIANT     149    149       Q -> H (in NMTC2; does not affect the
FT                                interaction with ROBO1; decreased GTPase
FT                                activator activity; in SLIT2 and ROBO1-
FT                                mediated inhibition of CDC42).
FT                                {ECO:0000269|PubMed:23539728}.
FT                                /FTId=VAR_075879.
FT   VARIANT     275    275       A -> T (in NMTC2; does not affect the
FT                                interaction with ROBO1; slightly
FT                                increased GTPase activator activity; in
FT                                SLIT2 and ROBO1-mediated inhibition of
FT                                CDC42). {ECO:0000269|PubMed:23539728}.
FT                                /FTId=VAR_075880.
FT   VARIANT     512    512       V -> I. {ECO:0000269|PubMed:23539728}.
FT                                /FTId=VAR_075881.
FT   VARIANT     617    617       R -> C (in NMTC2; does not affect the
FT                                interaction with ROBO1; decreased GTPase
FT                                activator activity; in SLIT2 and ROBO1-
FT                                mediated inhibition of CDC42).
FT                                {ECO:0000269|PubMed:23539728}.
FT                                /FTId=VAR_075882.
FT   VARIANT     875    875       H -> R (in NMTC2; does not affect the
FT                                interaction with ROBO1; slightly
FT                                increased GTPase activator activity; in
FT                                SLIT2 and ROBO1-mediated inhibition of
FT                                CDC42). {ECO:0000269|PubMed:23539728}.
FT                                /FTId=VAR_075883.
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
//
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