CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015572
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rho GTPase-activating protein 27 
Protein Synonyms/Alias
 CIN85-associated multi-domain-containing Rho GTPase-activating protein 1; Rho-type GTPase-activating protein 27; SH3 domain-containing protein 20 
Gene Name
 ARHGAP27 
Gene Synonyms/Alias
 CAMGAP1; SH3D20; PP905 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
551GGLRQPSKFSTPEYTubiquitination[1]
743GNLATIQKLRYKVDHubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [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
 Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1 (By similarity). 
Sequence Annotation
 DOMAIN 8 69 SH3.
 DOMAIN 246 280 WW 1.
 DOMAIN 299 333 WW 2.
 DOMAIN 411 444 WW 3.
 DOMAIN 496 612 PH.
 DOMAIN 697 886 Rho-GAP.
 MOD_RES 156 156 Phosphoserine (By similarity).
 MOD_RES 216 216 Phosphoserine (By similarity).
 MOD_RES 228 228 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Endocytosis; GTPase activation; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 889 AA 
Protein Sequence
MAADVVGDVY VLVEHPFEYT GKDGRRVAIR PNERYRLLRR STEHWWHVRR EPGGRPFYLP 60
AQYVRELPAL GNPAAAAPPG PHPSPAAPEP LAYDYRFVSA AATAGPDGAP EESGGRASSL 120
CGPAQRGAAT QRSSLAPGLP ACLYLRPAAP VRPAQSLNDL ACAAVSPPAG LLGSSGSFKA 180
CSVAGSWVCP RPLARSDSEN VYEVIQDLHV PPPEESAEQV DDPPEPVYAN IERQPRATSP 240
GAAAAPLPSP VWETHTDAGT GRPYYYNPDT GVTTWESPFE AAEGAASPAT SPASVDSHVS 300
LETEWGQYWD EESRRVFFYN PLTGETAWED EAENEPEEEL EMQPGLSPGS PGDPRPPTPE 360
TDYPESLTSY PEEDYSPVGS FGEPGPTSPL TTPPGWSCHV SQDKQMLYTN HFTQEQWVRL 420
EDPHGKPYFY NPEDSSVRWE LPQVPVPAPR SIHKSSQDGD TPAQASPPEE KVPAELDEVG 480
SWEEVSPATA AVRTKTLDKA GVLHRTKTAD KGKRLRKKHW SASWTVLEGG VLTFFKDSKT 540
SAAGGLRQPS KFSTPEYTVE LRGATLSWAP KDKSSRKNVL ELRSRDGSEY LIQHDSEAII 600
STWHKAIAQG IQELSAELPP EESESSRVDF GSSERLGSWQ EKEEDARPNA AAPALGPVGL 660
ESDLSKVRHK LRKFLQRRPT LQSLREKGYI KDQVFGCALA ALCERERSRV PRFVQQCIRA 720
VEARGLDIDG LYRISGNLAT IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE 780
PLFPFSHFRQ FIAAIKLQDQ ARRSRCVRDL VRSLPAPNHD TLRMLFQHLC RVIEHGEQNR 840
MSVQSVAIVF GPTLLRPEVE ETSMPMTMVF QNQVVELILQ QCADIFPPH 889 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005622; C:intracellular; ISS:HGNC.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0030675; F:Rac GTPase activator activity; ISS:HGNC.
 GO:0017124; F:SH3 domain binding; ISS:HGNC.
 GO:0043089; P:positive regulation of Cdc42 GTPase activity; ISS:HGNC.
 GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC.
 GO:0007165; P:signal transduction; IEA:InterPro. 
Interpro
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR015767; Rho_GTPase_activating.
 IPR008936; Rho_GTPase_activation_prot.
 IPR000198; RhoGAP_dom.
 IPR001452; SH3_domain.
 IPR001202; WW_dom. 
Pfam
 PF00169; PH
 PF00620; RhoGAP
 PF00397; WW 
SMART
 SM00233; PH
 SM00324; RhoGAP
 SM00326; SH3
 SM00456; WW 
PROSITE
 PS50003; PH_DOMAIN
 PS50238; RHOGAP
 PS50002; SH3
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS