CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019509
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 
Protein Synonyms/Alias
 Centaurin-delta-2; Cnt-d2 
Gene Name
 ARAP1 
Gene Synonyms/Alias
 CENTD2; KIAA0782 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
871RLGRLPYKAGLSLQRubiquitination[1, 2, 3]
1018DARSVHLKEGEQHVDubiquitination[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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a preference for ARF1 and ARF5 (By similarity). 
Sequence Annotation
 DOMAIN 6 70 SAM.
 DOMAIN 327 419 PH 1.
 DOMAIN 440 529 PH 2.
 DOMAIN 535 660 Arf-GAP.
 DOMAIN 743 850 PH 3.
 DOMAIN 954 1139 Rho-GAP.
 DOMAIN 1172 1261 Ras-associating.
 DOMAIN 1274 1396 PH 4.
 ZN_FING 550 576 C4-type.
 MOD_RES 229 229 Phosphoserine.
 MOD_RES 354 354 Phosphothreonine.
 MOD_RES 428 428 Phosphoserine.
 MOD_RES 431 431 Phosphotyrosine.
 MOD_RES 738 738 Phosphoserine.
 MOD_RES 1435 1435 Phosphoserine.  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Golgi apparatus; GTPase activation; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1450 AA 
Protein Sequence
MAEAGDAALS VAEWLRALHL EQYTGLFEQH GLVWATECQG LSDTRLMDMG MLLPGHRRRI 60
LAGLLRAHTS PAPAPRPTPR PVPMKRHIFR SPPVPATPPE PLPTTTEDEG LPAAPPIPPR 120
RSCLPPTCFT TPSTAAPDPV LPPLPAKRHL AELSVPPVPP RTGPPRLLVS LPTKEEESLL 180
PSLSSPPQPQ SEEPLSTLPQ GPPQPPSPPP CPPEIPPKPV RLFPEFDDSD YDEVPEEGPG 240
APARVMTKKE EPPPSRVPRA VRVASLLSEG EELSGDDQGD EEEDDHAYEG VPNGGWHTSS 300
LSLSLPSTIA APHPMDGPPG GSTPVTPVIK AGWLDKNPPQ GSYIYQKRWV RLDTDHLRYF 360
DSNKDAYSKR FISVACISHV AAIGDQKFEV ITNNRTFAFR AESDVERKEW MQALQQAMAE 420
QRARARLSSA YLLGVPGSEQ PDRAGSLELR GFKNKLYVAV VGDKVQLYKN LEEYHLGIGI 480
TFIDMSVGNV KEVDRRSFDL TTPYRIFSFS ADSELEKEQW LEAMQGAIAE ALSTSEVAER 540
IWAAAPNRFC ADCGAPQPDW ASINLCVVIC KRCAGEHRGL GAGVSKVRSL KMDRKVWTET 600
LIELFLQLGN GAGNRFWAAN VPPSEALQPS SSPSTRRCHL EAKYREGKYR RYHPLFGNQE 660
ELDKALCAAV TTTDLAETQA LLGCGAGINC FSGDPEAPTP LALAEQAGQT LQMEFLRNNR 720
TTEVPRLDSM KPLEKHYSVV LPTVSHSGFL YKTASAGKLL QDRRAREEFS RRWCVLGDGV 780
LSYFENERAV TPNGEIRASE IVCLAVPPPD THGFEHTFEV YTEGERLYLF GLESAEQAHE 840
WVKCIAKAFV PPLAEDLLAR DFERLGRLPY KAGLSLQRAQ EGWFSLSGSE LRAVFPEGPC 900
EEPLQLRKLQ ELSIQGDSEN QVLVLVERRR TLYIQGERRL DFMGWLGAIQ KAAASMGDTL 960
SEQQLGDSDI PVIVYRCVDY ITQCGLTSEG IYRKCGQTSK TQRLLESLRQ DARSVHLKEG 1020
EQHVDDVSSA LKRFLRDLPD GLFTRAQRLT WLEASEIEDE EEKVSRYREL LVRLPPVNRA 1080
TVKALISHLY CVQCFSDTNQ MNVHNLAIVF GPTLFQTDGQ DYKAGRVVED LINHYVVVFS 1140
VDEEELRKQR EEITAIVKMR VAGTASGTQH AGDFICTVYL EEKKAETEQH IKVPASMTAE 1200
ELTLEILDRR NVGIREKDYW TCFEVNEREE AERPLHFAEK VLPILHGLGT DSHLVVKKHQ 1260
AMEAMLLYLA SRVGDTKHGM MKFREDRSLL GLGLPSGGFH DRYFILNSSC LRLYKEVRSQ 1320
RPWSGAPETS HRPEKEWPIK SLKVYLGVKK KLRPPTCWGF TVVHETEKHE KQQWYLCCDT 1380
QMELREWFAT FLFVQHDGLV WPSEPSRVSR AVPEVRLGSV SLIPLRGSEN EMRRSVAAFT 1440
ADPLSLLRNV 1450 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0008060; F:ARF GTPase activator activity; IDA:UniProtKB.
 GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
 GO:0005100; F:Rho GTPase activator activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030037; P:actin filament reorganization involved in cell cycle; TAS:UniProtKB.
 GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
 GO:0043089; P:positive regulation of Cdc42 GTPase activity; IDA:UniProtKB.
 GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
 GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0051270; P:regulation of cellular component movement; IMP:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. 
Interpro
 IPR001164; ArfGAP.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR000159; Ras-assoc.
 IPR008936; Rho_GTPase_activation_prot.
 IPR000198; RhoGAP_dom.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR021129; SAM_type1. 
Pfam
 PF01412; ArfGap
 PF00169; PH
 PF00788; RA
 PF00620; RhoGAP
 PF00536; SAM_1 
SMART
 SM00105; ArfGap
 SM00233; PH
 SM00324; RhoGAP
 SM00454; SAM 
PROSITE
 PS50115; ARFGAP
 PS50003; PH_DOMAIN
 PS50200; RA
 PS50238; RHOGAP
 PS50105; SAM_DOMAIN 
PRINTS
 PR00405; REVINTRACTNG.