CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015338
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATPase family AAA domain-containing protein 2 
Protein Synonyms/Alias
 AAA nuclear coregulator cancer-associated protein; ANCCA 
Gene Name
 ATAD2 
Gene Synonyms/Alias
 L16; PRO2000 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55KPAATTAKAGDGSSVubiquitination[1]
63AGDGSSVKEVETYHRubiquitination[1, 2, 3]
79RALRSLRKDAQNSSDubiquitination[1]
91SSDSSFEKNVEITEQubiquitination[1, 2]
175NQSMLFDKLITNTAEacetylation[4]
175NQSMLFDKLITNTAEubiquitination[1, 2]
187TAEAVLQKMDDMKKMacetylation[4]
187TAEAVLQKMDDMKKMubiquitination[2, 3]
311YYQAPLEKPRHQRKPubiquitination[1, 2, 3, 5, 6]
398NFRKDELKGIYKDRMubiquitination[2]
406GIYKDRMKIGASLADubiquitination[1, 2]
473YGPPGTGKTLVARALubiquitination[2, 7]
489NECSQGDKRVAFFMRubiquitination[2, 3]
504KGADCLSKWVGESERubiquitination[2]
601FLFSLPDKEARKEILubiquitination[1, 2]
609EARKEILKIHTRDWNubiquitination[2]
685DFEVAMQKMIPASQRubiquitination[1, 2, 7]
706QALSTVVKPLLQNTVubiquitination[1, 2]
772QKSSHKAKDNFNFLHacetylation[3, 8]
772QKSSHKAKDNFNFLHubiquitination[2, 3]
926FNVQLPDKEERTKFFubiquitination[1, 2]
931PDKEERTKFFEDLILubiquitination[1, 2, 5, 6]
949AKPPISKKKAVLQALubiquitination[2]
950KPPISKKKAVLQALEubiquitination[2, 3]
976SLTAEEVKRLEEQEEubiquitination[1, 2]
1011KRFRVFTKPVDPDEVubiquitination[1, 2]
1026PDYVTVIKQPMDLSSubiquitination[1, 2]
1037DLSSVISKIDLHKYLubiquitination[2]
1042ISKIDLHKYLTVKDYubiquitination[2, 5, 6]
1047LHKYLTVKDYLRDIDubiquitination[2]
1128SYYHVMPKQNSTLVGubiquitination[2]
1137NSTLVGDKRSDPEQNubiquitination[2]
1146SDPEQNEKLKTPSTPubiquitination[1]
1236QQNASESKLELRNNSubiquitination[1, 7]
1257NELEDSRKTTACTELubiquitination[2]
1314QQLITVEKALAILSQubiquitination[1]
1372RHRKDHDKTSLIQKMubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] 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]
 [6] 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]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
Functional Description
 May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. 
Sequence Annotation
 DOMAIN 1001 1071 Bromo.
 NP_BIND 467 474 ATP (Potential).
 MOD_RES 170 170 Phosphoserine.
 MOD_RES 327 327 Phosphoserine.
 MOD_RES 337 337 Phosphoserine.
 MOD_RES 746 746 Phosphoserine.
 MOD_RES 751 751 Phosphoserine.
 MOD_RES 1149 1149 Phosphothreonine.
 MOD_RES 1152 1152 Phosphothreonine.
 MOD_RES 1233 1233 Phosphoserine.
 MOD_RES 1302 1302 Phosphoserine.  
Keyword
 3D-structure; Activator; Alternative splicing; ATP-binding; Bromodomain; Coiled coil; Complete proteome; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1390 AA 
Protein Sequence
MVVLRSSLEL HNHSAASATG SLDLSSDFLS LEHIGRRRLR SAGAAQKKPA ATTAKAGDGS 60
SVKEVETYHR TRALRSLRKD AQNSSDSSFE KNVEITEQLA NGRHFTRQLA RQQADKKKEE 120
HREDKVIPVT RSLRARNIVQ STEHLHEDNG DVEVRRSCRI RSRYSGVNQS MLFDKLITNT 180
AEAVLQKMDD MKKMRRQRMR ELEDLGVFNE TEESNLNMYT RGKQKDIQRT DEETTDNQEG 240
SVESSEEGED QEHEDDGEDE DDEDDDDDDD DDDDDDDEDD EDEEDGEEEN QKRYYLRQRK 300
ATVYYQAPLE KPRHQRKPNI FYSGPASPAR PRYRLSSAGP RSPYCKRMNR RRHAIHSSDS 360
TSSSSSEDEQ HFERRRKRSR NRAINRCLPL NFRKDELKGI YKDRMKIGAS LADVDPMQLD 420
SSVRFDSVGG LSNHIAALKE MVVFPLLYPE VFEKFKIQPP RGCLFYGPPG TGKTLVARAL 480
ANECSQGDKR VAFFMRKGAD CLSKWVGESE RQLRLLFDQA YQMRPSIIFF DEIDGLAPVR 540
SSRQDQIHSS IVSTLLALMD GLDSRGEIVV IGATNRLDSI DPALRRPGRF DREFLFSLPD 600
KEARKEILKI HTRDWNPKPL DTFLEELAEN CVGYCGADIK SICAEAALCA LRRRYPQIYT 660
TSEKLQLDLS SINISAKDFE VAMQKMIPAS QRAVTSPGQA LSTVVKPLLQ NTVDKILEAL 720
QRVFPHAEFR TNKTLDSDIS CPLLESDLAY SDDDVPSVYE NGLSQKSSHK AKDNFNFLHL 780
NRNACYQPMS FRPRILIVGE PGFGQGSHLA PAVIHALEKF TVYTLDIPVL FGVSTTSPEE 840
TCAQVIREAK RTAPSIVYVP HIHVWWEIVG PTLKATFTTL LQNIPSFAPV LLLATSDKPH 900
SALPEEVQEL FIRDYGEIFN VQLPDKEERT KFFEDLILKQ AAKPPISKKK AVLQALEVLP 960
VAPPPEPRSL TAEEVKRLEE QEEDTFRELR IFLRNVTHRL AIDKRFRVFT KPVDPDEVPD 1020
YVTVIKQPMD LSSVISKIDL HKYLTVKDYL RDIDLICSNA LEYNPDRDPG DRLIRHRACA 1080
LRDTAYAIIK EELDEDFEQL CEEIQESRKK RGCSSSKYAP SYYHVMPKQN STLVGDKRSD 1140
PEQNEKLKTP STPVACSTPA QLKRKIRKKS NWYLGTIKKR RKISQAKDDS QNAIDHKIES 1200
DTEETQDTSV DHNETGNTGE SSVEENEKQQ NASESKLELR NNSNTCNIEN ELEDSRKTTA 1260
CTELRDKIAC NGDASSSQII HISDENEGKE MCVLRMTRAR RSQVEQQQLI TVEKALAILS 1320
QPTPSLVVDH ERLKNLLKTV VKKSQNYNIF QLENLYAVIS QCIYRHRKDH DKTSLIQKME 1380
QEVENFSCSR 1390 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:EC.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR011989; ARM-like.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR001487; Bromodomain.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA
 PF00439; Bromodomain 
SMART
 SM00382; AAA
 SM00297; BROMO 
PROSITE
 PS00674; AAA
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2 
PRINTS
 PR00503; BROMODOMAIN.