CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015536
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 
Protein Synonyms/Alias
 Centaurin-beta-2; Cnt-b2 
Gene Name
 Acap2 
Gene Synonyms/Alias
 Centb2; Kiaa0041 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
57KAFCVANKQFMNGIRubiquitination[1]
125RKFKDAKKQFEKVSEacetylation[2]
129DAKKQFEKVSEEKENacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] 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
 GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) (By similarity). 
Sequence Annotation
 DOMAIN 1 226 BAR.
 DOMAIN 266 361 PH.
 DOMAIN 399 520 Arf-GAP.
 REPEAT 632 661 ANK 1.
 REPEAT 665 694 ANK 2.
 REPEAT 698 727 ANK 3.
 ZN_FING 414 437 C4-type.
 MOD_RES 384 384 Phosphoserine (By similarity).
 MOD_RES 521 521 Phosphoserine.
 MOD_RES 734 734 Phosphotyrosine (By similarity).  
Keyword
 Alternative splicing; ANK repeat; Coiled coil; Complete proteome; GTPase activation; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 770 AA 
Protein Sequence
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM 60
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF 120
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEAANILT ATRKCFRHIA LDYVLQINVL 180
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ 240
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK 300
KFKDSPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI 360
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NTSCCDCGLA 420
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE 480
AKLEKMGVKK PQPGQRQEKE AYIRAKYVER KFVDKYSALL SPSEQEKRII SKSCEDQRLS 540
HARASVHTPV KSNDSGIQQC SEDGRESLPS TVSANSLYEP EGERQESSVF LDSKHLNPGL 600
QLYRASYEKN LPKMAEALAH GADVNWANSD ENQATPLIQA VLGGSLVTCE FLLQNGANVN 660
QRDVQGRGPL HHATVLGHTG QVCLFLKRGA NQHATDEEGK DPLSIAVEAA NADIVTLLRL 720
ARMNEEMRES EGLYGQPGDE TYQDIFRDFS QMASNNPEKL NRFQQDSQKF 770 
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:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 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. 
Pfam
 PF12796; Ank_2
 PF01412; ArfGap
 PF00169; PH 
SMART
 SM00248; ANK
 SM00105; ArfGap
 SM00233; PH 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50115; ARFGAP
 PS51021; BAR
 PS50003; PH_DOMAIN 
PRINTS
 PR00405; REVINTRACTNG.