CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014726
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AT-rich interactive domain-containing protein 2 
Protein Synonyms/Alias
 ARID domain-containing protein 2; BRG1-associated factor 200; BAF200; Zinc finger protein with activation potential; Zipzap/p200 
Gene Name
 ARID2 
Gene Synonyms/Alias
 KIAA1557 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MANSTGKAPPDERRubiquitination[1, 2, 3]
15APPDERRKGLAFLDEubiquitination[2, 4, 5]
43KIPAVGGKELDLHGLubiquitination[2]
62TTLGGFAKVSEKNQWubiquitination[2, 3, 4, 5]
195KHVMQLEKDPKIITLubiquitination[2]
238RDFVKFWKDIVDDNEubiquitination[2]
275SLFHPPRKLGINDIEubiquitination[2]
371MSRDRFLKMRGMEILubiquitination[2]
581VFPNHTVKRVEDSSSubiquitination[2]
1701DALLAGLKQDEPGQAubiquitination[2]
1716GSQKSSTKQPTVGGTubiquitination[2]
1731SSTPRAQKAIVNHPSubiquitination[4, 5]
1760FRDFTDEKEGPITKHubiquitination[2]
1777LTAALILKNIGKYSEubiquitination[2, 4, 5]
1781LILKNIGKYSECGRRubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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]
 [5] 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
 Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. 
Sequence Annotation
 DOMAIN 13 105 ARID.
 DNA_BIND 524 603 RFX-type winged-helix.
 ZN_FING 1632 1657 C2H2-type.
 MOTIF 313 317 LXXLL.
 MOD_RES 631 631 Phosphoserine.
 MOD_RES 635 635 Phosphoserine.
 MOD_RES 653 653 Phosphothreonine.
 MOD_RES 689 689 Phosphoserine.
 MOD_RES 692 692 Phosphothreonine.
 MOD_RES 1496 1496 Phosphoserine.  
Keyword
 Alternative splicing; Chromatin regulator; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1835 AA 
Protein Sequence
MANSTGKAPP DERRKGLAFL DELRQFHHSR GSPFKKIPAV GGKELDLHGL YTRVTTLGGF 60
AKVSEKNQWG EIVEEFNFPR SCSNAAFALK QYYLRYLEKY EKVHHFGEDD DEVPPGNPKP 120
QLPIGAIPSS YNYQQHSVSD YLRQSYGLSM DFNSPNDYNK LVLSLLSGLP NEVDFAINVC 180
TLLSNESKHV MQLEKDPKII TLLLANAGVF DDTLGSFSTV FGEEWKEKTD RDFVKFWKDI 240
VDDNEVRDLI SDRNKSHEGT SGEWIWESLF HPPRKLGIND IEGQRVLQIA VILRNLSFEE 300
GNVKLLAANR TCLRFLLLSA HSHFISLRQL GLDTLGNIAA ELLLDPVDFK TTHLMFHTVT 360
KCLMSRDRFL KMRGMEILGN LCKAEDNGVL ICEYVDQDSY REIICHLTLP DVLLVISTLE 420
VLYMLTEMGD VACTKIAKVE KSIDMLVCLV SMDIQMFGPD ALAAVKLIEH PSSSHQMLSE 480
IRPQAIEQVQ TQTHVASAPA SRAVVAQHVA PPPGIVEIDS EKFACQWLNA HFEVNPDCSV 540
SRAEMYSEYL STCSKLARGG ILTSTGFYKC LRTVFPNHTV KRVEDSSSNG QAHIHVVGVK 600
RRAIPLPIQM YYQQQPVSTS VVRVDSVPDV SPAPSPAGIP HGSQTIGNHF QRTPVANQSS 660
NLTATQMSFP VQGVHTVAQT VSRIPQNPSP HTHQQQNAPV TVIQSKAPIP CEVVKATVIQ 720
NSIPQTGVPV SIAVGGGPPQ SSVVQNHSTG PQPVTVVNSQ TLLHHPSVIP QQSPLHTVVP 780
GQIPSGTPVT VIQQAVPQSH MFGRVQNIPA CTSTVSQGQQ LITTSPQPVQ TSSQQTSAGS 840
QSQDTVIIAP PQYVTTSASN IVSATSVQNF QVATGQMVTI AGVPSPQASR VGFQNIAPKP 900
LPSQQVSSTV VQQPIQQPQQ PTQQSVVIVS QPAQQGQTYA PAIHQIVLAN PAALPAGQTV 960
QLTGQPNITP SSSPSPVPAT NNQVPTAMSS SSTPQSQGPP PTVSQMLSVK RQQQQQHSPA 1020
PPPQQVQVQV QQPQQVQMQV QPQQSNAGVG QPASGESSLI KQLLLPKRGP STPGGKLILP 1080
APQIPPPNNA RAPSPQVVYQ VASNQAAGFG VQGQTPAQQL LVGQQNVQLV PSAMPPSGGV 1140
QTVPISNLQI LPGPLISNSP ATIFQGTSGN QVTITVVPNT SFAPATVSQG NATQLIAPAG 1200
ITMSGTQTGV GLPVQTLPAT QASPAGQSSC TTATPPFKGD KIICQKEEEA KEATGLHVHE 1260
RKIEVMENPS CRRGATNTSN GDTKENEMHV GSLLNGRKYS DSSLPPSNSG KIQSETNQCS 1320
LISNGPSLEL GENGASGKQN SEQIDMQDIK SDLRKPLVNG ICDFDKGDGS HLSKNIPNHK 1380
TSNHVGNGEI SPMEPQGTLD ITQQDTAKGD QLERISNGPV LTLGGSSVSS IQEASNAATQ 1440
QFSGTDLLNG PLASSLNSDV PQQRPSVVVS PHSTTSVIQG HQIIAVPDSG SKVSHSPALS 1500
SDVRSTNGTA ECKTVKRPAE DTDRETVAGI PNKVGVRIVT ISDPNNAGCS ATMVAVPAGA 1560
DPSTVAKVAI ESAVQQKQQH PPTYVQNVVP QNTPMPPSPA VQVQGQPNSS QPSPFSGSSQ 1620
PGDPMRKPGQ NFMCLWQSCK KWFQTPSQVF YHAATEHGGK DVYPGQCLWE GCEPFQRQRF 1680
SFITHLQDKH CSKDALLAGL KQDEPGQAGS QKSSTKQPTV GGTSSTPRAQ KAIVNHPSAA 1740
LMALRRGSRN LVFRDFTDEK EGPITKHIRL TAALILKNIG KYSECGRRLL KRHENNLSVL 1800
AISNMEASST LAKCLYELNF TVQSKEQEKD SEMLQ 1835 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IDA:GDB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001606; ARID/BRIGHT_DNA-bd.
 IPR003150; DNA-bd_RFX.
 IPR011991; WHTH_DNA-bd_dom.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like. 
Pfam
 PF01388; ARID
 PF02257; RFX_DNA_binding 
SMART
 SM00501; BRIGHT
 SM00355; ZnF_C2H2 
PROSITE
 PS51011; ARID
 PS51526; RFX_DBD
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS