CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024540
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rho GTPase-activating protein 32 
Protein Synonyms/Alias
 Brain-specific Rho GTPase-activating protein; GAB-associated Cdc42/Rac GTPase-activating protein; GC-GAP; GTPase regulator interacting with TrkA; 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 
Gene Name
 ARHGAP32 
Gene Synonyms/Alias
 GRIT; KIAA0712; RICS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
688ESEPSEMKAMALKGGacetylation[1]
1699YNPRLQGKSLYSYAGubiquitination[2]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). 
Sequence Annotation
 DOMAIN 131 245 PX; atypical.
 DOMAIN 259 321 SH3.
 DOMAIN 372 567 Rho-GAP.
 REGION 1391 1711 Interaction with GAB2.
 REGION 1685 2087 Interaction with FYN.
 MOD_RES 706 706 Phosphoserine.
 MOD_RES 856 856 Phosphoserine (By similarity).
 MOD_RES 892 892 Phosphoserine (By similarity).
 MOD_RES 952 952 Phosphoserine (By similarity).
 MOD_RES 1203 1203 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Endoplasmic reticulum; Endosome; Golgi apparatus; GTPase activation; Membrane; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; SH3 domain; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2087 AA 
Protein Sequence
METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED DFVPELHRNV 60
HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC 120
AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD 180
KHLHLCIYDR RFSQLSELPR SDTLKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME 240
IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW 300
RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK 360
QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH 420
EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI 480
KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF 540
SGTAAFMEVR IQSVVVEFIL NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL 600
EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN KMKKSPVGSW 660
RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS 720
KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEGGLLHIP ALMSPHSAED 780
VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS 840
SQCQTPGSTA SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS 900
KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN RSPTQIVKMK 960
TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS KAVASGQTQT GAVTHDPPQD 1020
SVPVSSVSLI PPPPPPKNVA RMLALALAES AQQASTQSLK RPGTSQAGYT NYGDIAVATT 1080
EDNLSSSYSA VALDKAYFQT DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE 1140
QHHQVDLTGN QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ 1200
DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG SPEENTSTAT 1260
MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH RTNRPLPPPP SQRSAEQPPV 1320
VGQVQAATNI GLNNSHKVQG VVPVPERPPE PRAMDDPASA FISDSGAAAA QCPMATAVQP 1380
GLPEKVRDGA RVPLLHLRAE SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY 1440
HSFVTASSTS VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC 1500
QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK PCSRVEYVSS 1560
LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS RTEVPPDDEP AYCPRPLYQY 1620
KPYQSSQARS DYHVTQLQPY FENGRVHYRY SPYSSSSSSY YSPDGALCDV DAYGTVQLRP 1680
LHRLPNRDFA FYNPRLQGKS LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT 1740
SWDLEDMEKY RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK 1800
TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP EKPSLPQKQS 1860
SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG AGQLDYGSKG IPDTSEPVSY 1920
HNSGVKYAAS GQESLRLNHK EVRLSKEMER PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP 1980
PKPERSHSLK LHHTQNVERD PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF 2040
GGGGMGTYVP PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE 2087 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
 GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
 GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
 GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. 
Interpro
 IPR001683; Phox.
 IPR008936; Rho_GTPase_activation_prot.
 IPR000198; RhoGAP_dom.
 IPR001452; SH3_domain. 
Pfam
 PF00787; PX
 PF00620; RhoGAP
 PF00018; SH3_1 
SMART
 SM00324; RhoGAP
 SM00326; SH3 
PROSITE
 PS50195; PX
 PS50238; RHOGAP
 PS50002; SH3 
PRINTS