CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038719
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 Asap1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
664HYCSMYGKPECLKLLacetylation[1]
675LKLLLRSKPTVDIVNphosphoglycerylation[2]
830SSSKTANKFEGLSQQacetylation[3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
  
Sequence Annotation
  
Keyword
 ANK repeat; Complete proteome; Metal-binding; Reference proteome; Repeat; SH3 domain; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1090 AA 
Protein Sequence
MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL 60
EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK 120
FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI 180
EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL 240
IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD 300
PKEVGGLYVA SRANSVIRDS QSRQGGYSMH QLQGNKEYGS EKKGFLLKKS DGIRKVWQRR 360
KCAVKNGILT ISHATSNRQP AKLNLLTCQV KPNAEDKKSF DLISHNRTYH FQAEDEQDYI 420
AWISVLTNSK EEALTMAFRG EQSTGENSLE DLTKAIIEDV QRLPGNDICC DCGSSEPTWL 480
STNLGILTCI ECSGIHREMG VHISRIQSLE LDKLGTSELL LAKNVGNNSF NDIMEANLPS 540
PSPKPTPSSD MTVRKEYITA KYVDHRFSRK TCASSSAKLN ELLEAIKSRD LLALIQVYAE 600
GVELMEPLLE PGQELGETAL HLAVRTADQT SLHLVDFLVQ NCGNLDKQTS VGNTVLHYCS 660
MYGKPECLKL LLRSKPTVDI VNQNGETALD IAKRLKATQC EDLLSQAKSG KFNPHVHVEY 720
EWNLRQDEMD ESDDDLDDKP SPIKKERSPR PQSFCHSSSI SPQDKLALPG FSTPRDKQRL 780
SYGAFTNQIF ASTSTDLPTS PTSEAPPLPP RNAGKGNDVG PLSSSKTANK FEGLSQQAST 840
SSAKTALGPR VLPKLPQKVA LRKTETSHHL SLDRTNIPPE TFQKSSQLTE LPQKPPLGEL 900
PPKPVELAPK PQVGELPPKP GELPPKPQLG DLPPKPQLSD LPPKPQMKDL PPKPQLGDLL 960
AKSQAGDVSA KVQPPSEVTQ RSHTGDLSPN VQSRDAIQKQ ASEDSNDLTP TLPETPVPLP 1020
RKINTGKNKV RRVKTIYDCQ ADNDDELTFI EGEVIIVTGE EDQEWWIGHI EGQPERKGVF 1080
PVSFVHILSD 1090 
Gene Ontology
 GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro. 
Interpro
 IPR027267; AH/BAR-dom.
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR001164; ArfGAP.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR001452; SH3_domain. 
Pfam
 PF12796; Ank_2
 PF01412; ArfGap
 PF00169; PH
 PF00018; SH3_1 
SMART
 SM00248; ANK
 SM00105; ArfGap
 SM00233; PH
 SM00326; SH3 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50115; ARFGAP
 PS50003; PH_DOMAIN
 PS50002; SH3 
PRINTS
 PR00405; REVINTRACTNG.