ID FNBP2_HUMAN Reviewed; 1071 AA. AC O75044; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 2. DT 09-FEB-2010, entry version 82. DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 2; DE Short=srGAP2; DE AltName: Full=Formin-binding protein 2; GN Name=SRGAP2; Synonyms=FNBP2, KIAA0456; 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], AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX MEDLINE=98116662; PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries RT from human brain."; RL DNA Res. 4:345-349(1997). RN [2] RP INTERACTION WITH ROBO1. RX MEDLINE=21526632; 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, AND MASS RP SPECTROMETRY. 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 [4] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-993; SER-994; RP SER-1053; SER-1061; SER-1064 AND THR-1065, AND MASS SPECTROMETRY. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [6] RP STRUCTURE BY NMR OF 729-787. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of human SLIT-ROBO Rho GTPase- RT activating protein 2."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Putative GTPase-activating protein for Rho family small CC GTPases. CC -!- SUBUNIT: Probably interacts with ROBO1. CC -!- INTERACTION: CC P48023:FASLG; NbExp=1; IntAct=EBI-1051034, EBI-495538; CC -!- TISSUE SPECIFICITY: Expression at low levels in placenta, kidney, CC and ovary, and little or no expression in all other tissues CC tested. CC -!- SIMILARITY: Contains 1 FCH domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB007925; BAA32301.1; ALT_INIT; mRNA. DR IPI; IPI00479125; -. DR PIR; C59437; C59437. DR RefSeq; NP_001036223.1; -. DR RefSeq; NP_056141.2; -. DR UniGene; Hs.497575; -. DR PDB; 2DL8; NMR; -; A=729-787. DR PDBsum; 2DL8; -. DR SMR; O75044; 27-348, 500-679. DR IntAct; O75044; 4. DR STRING; O75044; -. DR PhosphoSite; O75044; -. DR PRIDE; O75044; -. DR Ensembl; ENST00000414359; ENSP00000408089; ENSG00000163486; Homo sapiens. DR GeneID; 23380; -. DR KEGG; hsa:23380; -. DR CTD; 23380; -. DR GeneCards; GC01P204583; -. DR H-InvDB; HIX0001527; -. DR H-InvDB; HIX0029679; -. DR HGNC; HGNC:19751; SRGAP2. DR MIM; 606524; gene. DR PharmGKB; PA128395759; -. DR HOGENOM; HBG356471; -. DR HOVERGEN; O75044; -. DR InParanoid; O75044; -. DR PhylomeDB; O75044; -. DR Reactome; REACT_11044; Signaling by Rho GTPases. DR Reactome; REACT_18266; Axon guidance. DR NextBio; 45477; -. DR ArrayExpress; O75044; -. DR Bgee; O75044; -. DR CleanEx; HS_SRGAP2; -. DR Genevestigator; O75044; -. DR GermOnline; ENSG00000163486; Homo sapiens. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR001060; FCH. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP. DR InterPro; IPR001452; SH3_domain. DR Gene3D; G3DSA:1.10.555.10; RhoGAP; 1. 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 PROSITE; PS50133; FCH; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Complete proteome; GTPase activation; KW Phosphoprotein; Polymorphism; SH3 domain. FT CHAIN 1 1071 SLIT-ROBO Rho GTPase-activating protein FT 2. FT /FTId=PRO_0000056767. FT DOMAIN 22 87 FCH. FT DOMAIN 489 679 Rho-GAP. FT DOMAIN 728 787 SH3. FT COILED 362 401 Potential. FT COILED 940 967 Potential. FT COMPBIAS 843 909 Ser-rich. FT MOD_RES 799 799 Phosphoserine (By similarity). FT MOD_RES 916 916 Phosphoserine. FT MOD_RES 990 990 Phosphoserine. FT MOD_RES 993 993 Phosphoserine. FT MOD_RES 994 994 Phosphoserine. FT MOD_RES 1053 1053 Phosphoserine. FT MOD_RES 1061 1061 Phosphoserine. FT MOD_RES 1064 1064 Phosphoserine. FT MOD_RES 1065 1065 Phosphothreonine. FT VARIANT 874 874 R -> G (in dbSNP:rs17018890). FT /FTId=VAR_055834. FT STRAND 731 737 FT STRAND 742 746 FT STRAND 754 762 FT STRAND 765 770 FT STRAND 773 777 FT STRAND 779 784 SQ SEQUENCE 1071 AA; 120881 MW; D8BC1939D6776312 CRC64; MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLMACVT MDNLQERALH IRKVLLVLPK TTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC QAHVNELIKT IIIQHENIFP SPRELEGPVY SRGGSMEDYC DSPHGETTPV EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE IEVISEPPEE KVTARAGASC PSGGHVADIY LANINKQRKR PESGSIRKTF RSDSHGLSSS LTDSSSPGVG ASCRPSSQPI MSQSLPKEGP DKCSISGHGS LNSISRHSSL KNRLDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELREL ERQSSVKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN ATSPGVNSST SPQSTDKSCT V //