CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018336
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 
Protein Synonyms/Alias
 Centaurin-delta-3; Cnt-d3 
Gene Name
 ARAP3 
Gene Synonyms/Alias
 CENTD3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
296LLSGWLDKLSPQGNYubiquitination[1]
Reference
 [1] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
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. Acts on ARF6, RAC1, RHOA and CDC42. Plays a role in the internalization of anthrax toxin. 
Sequence Annotation
 DOMAIN 4 68 SAM.
 DOMAIN 287 379 PH 1.
 DOMAIN 394 483 PH 2.
 DOMAIN 480 611 Arf-GAP.
 DOMAIN 907 1088 Rho-GAP.
 DOMAIN 1117 1210 Ras-associating.
 DOMAIN 1223 1325 PH 3.
 ZN_FING 504 527 C4-type.
 MOD_RES 1403 1403 Phosphotyrosine (By similarity).
 MOD_RES 1408 1408 Phosphotyrosine (By similarity).
 MOD_RES 1444 1444 Phosphoserine.
 MOD_RES 1480 1480 Phosphoserine.  
Keyword
 3D-structure; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; GTPase activation; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1544 AA 
Protein Sequence
MAAPQDLDIA VWLATVHLEQ YADTFRRHGL ATAGAARGLG HEELKQLGIS ATGHRKRILR 60
LLQTGTEEGS LDPKSDSAME PSPSPAPQAQ PPKPVPKPRT VFGGLSGPAT TQRPGLSPAL 120
GGPGVSRSPE PSPRPPPLPT SSSEQSSALN TVEMMPNSIY FGLDSRGRAQ AAQDKAPDSS 180
QISAPTPALR PTTGTVHIMD PGCLYYGVQP VGTPGAPDRR ESRGVCQGRA EHRLSRQDLE 240
AREDAGYASL ELPGDSTLLS PTLETEETSD DLISPYASFS FTADRLTPLL SGWLDKLSPQ 300
GNYVFQRRFV QFNGRSLMYF GSDKDPFPKG VIPLTAIEMT RSSKDNKFQV ITGQRVFVFR 360
TESEAQRDMW CSTLQSCLKE QRLLGHPRPP QPPRPLRTGM LELRGHKAKV FAALSPGELA 420
LYKSEQAFSL GIGICFIELQ GCSVRETKSR SFDLLTPHRC FSFTAESGGA RQSWAAALQE 480
AVTETLSDYE VAEKIWSNRA NRQCADCGSS RPDWAAVNLG VVICKQCAGQ HRALGSGISK 540
VQSLKLDTSV WSNEIVQLFI VLGNDRANRF WAGTLPPGEG LHPDATPGPR GEFISRKYRL 600
GLFRKPHPQY PDHSQLLQAL CAAVARPNLL KNMTQLLCVE AFEGEEPWFP PAPDGSCPGL 660
LPSDPSPGVY NEVVVRATYS GFLYCSPVSN KAGPSPPRRG RDAPPRLWCV LGAALEMFAS 720
ENSPEPLSLI QPQDIVCLGV SPPPTDPGDR FPFSFELILA GGRIQHFGTD GADSLEAWTS 780
AVGKWFSPLS CHQLLGPGLL RLGRLWLRSP SHTAPAPGLW LSGFGLLRGD HLFLCSAPGP 840
GPPAPEDMVH LRRLQEISVV SAADTPDKKE HLVLVETGRT LYLQGEGRLD FTAWNAAIGG 900
AAGGGGTGLQ EQQMSRGDIP IIVDACISFV TQHGLRLEGV YRKGGARARS LRLLAEFRRD 960
ARSVKLRPGE HFVEDVTDTL KRFFRELDDP VTSARLLPRW REAAELPQKN QRLEKYKDVI 1020
GCLPRVNRRT LATLIGHLYR VQKCAALNQM CTRNLALLFA PSVFQTDGRG EHEVRVLQEL 1080
IDGYISVFDI DSDQVAQIDL EVSLITTWKD VQLSQAGDLI MEVYIEQQLP DNCVTLKVSP 1140
TLTAEELTNQ VLEMRGTAAG MDLWVTFEIR EHGELERPLH PKEKVLEQAL QWCQLPEPCS 1200
ASLLLKKVPL AQAGCLFTGI RRESPRVGLL RCREEPPRLL GSRFQERFFL LRGRCLLLLK 1260
EKKSSKPERE WPLEGAKVYL GIRKKLKPPT PWGFTLILEK MHLYLSCTDE DEMWDWTTSI 1320
LKAQHDDQQP VVLRRHSSSD LARQKFGTMP LLPIRGDDSG ATLLSANQTL RRLHNRRTLS 1380
MFFPMKSSQG SVEEQEELEE PVYEEPVYEE VGAFPELIQD TSTSFSTTRE WTVKPENPLT 1440
SQKSLDQPFL SKSSTLGQEE RPPEPPPGPP SKSSPQARGS LEEQLLQELS SLILRKGETT 1500
AGLGSPSQPS SPQSPSPTGL PTQTPGFPTQ PPCTSSPPSS QPLT 1544 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0008060; F:ARF GTPase activator activity; ISS:UniProtKB.
 GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
 GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
 GO:0005100; F:Rho GTPase activator activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
 GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
 GO:0035021; P:negative regulation of Rac protein signal transduction; IEA:Compara.
 GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
 GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
 GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB. 
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.
 IPR011510; SAM_2. 
Pfam
 PF01412; ArfGap
 PF00169; PH
 PF00788; RA
 PF00620; RhoGAP
 PF07647; SAM_2 
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.