CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001460
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Metastasis-associated protein MTA2 
Protein Synonyms/Alias
 Metastasis-associated 1-like 1; MTA1-L1 protein; p53 target protein in deacetylase complex 
Gene Name
 MTA2 
Gene Synonyms/Alias
 MTA1L1; PID 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32RRIEELNKTANGNVEubiquitination[1, 2]
41ANGNVEAKVVCLFRRubiquitination[3]
71REFEEESKQPGVSEQubiquitination[1, 3, 4, 5]
152GEIRVGCKYQAEIPDacetylation[5, 6, 7, 8]
152GEIRVGCKYQAEIPDubiquitination[2, 3, 5, 9, 10]
173SDNRNQQKMEMKVWDubiquitination[3, 5]
177NQQKMEMKVWDPDNPubiquitination[3]
332AEADSKLKQVYIPTYacetylation[11]
341VYIPTYTKPNPNQIIacetylation[7, 11]
460TFLLQTTKLTRLARRubiquitination[2, 3, 12, 13]
504IRLPKAAKTPLKIHPubiquitination[4]
508KAAKTPLKIHPLVRLubiquitination[3, 4, 5, 12, 13]
522LPLATIVKDLVAQAPubiquitination[2, 4, 12, 13]
531LVAQAPLKPKTPRGTacetylation[8]
531LVAQAPLKPKTPRGTubiquitination[3, 4]
611PVVFVATKDTRALRKubiquitination[3, 4, 5, 12, 13]
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] 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]
 [3] 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]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [10] 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]
 [11] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [12] 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]
 [13] 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
 May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins. 
Sequence Annotation
 DOMAIN 1 144 BAH.
 DOMAIN 145 256 ELM2.
 DOMAIN 263 315 SANT.
 ZN_FING 367 394 GATA-type; atypical.
 MOD_RES 152 152 N6-acetyllysine.
 MOD_RES 433 433 Phosphoserine.
 MOD_RES 435 435 Phosphoserine.
 MOD_RES 534 534 Phosphothreonine.
 MOD_RES 548 548 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 668 AA 
Protein Sequence
MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD 60
SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILSQY 120
LEKEDCFFYS LVFDPVQKTL LADQGEIRVG CKYQAEIPDR LVEGESDNRN QQKMEMKVWD 180
PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR 240
NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL 300
ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG 360
FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGATRGTTEP 420
HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR 480
RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT 540
PINRNQLSQN RGLGGIMVKR AYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD 600
APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLIAVRPPVP LPAPSHPAST 660
NEPIVLED 668 
Gene Ontology
 GO:0016581; C:NuRD complex; IDA:UniProtKB.
 GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0004407; F:histone deacetylase activity; IEA:Compara.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0000989; F:transcription factor binding transcription factor activity; IEA:Compara.
 GO:0044212; F:transcription regulatory region DNA binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006333; P:chromatin assembly or disassembly; TAS:ProtInc.
 GO:0006306; P:DNA methylation; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara. 
Interpro
 IPR001025; BAH_dom.
 IPR000949; ELM2_dom.
 IPR009057; Homeodomain-like.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR000679; Znf_GATA. 
Pfam
 PF01426; BAH
 PF01448; ELM2
 PF00320; GATA 
SMART
 SM00439; BAH
 SM00717; SANT
 SM00401; ZnF_GATA 
PROSITE
 PS51038; BAH
 PS51156; ELM2
 PS00344; GATA_ZN_FINGER_1
 PS50114; GATA_ZN_FINGER_2
 PS51293; SANT 
PRINTS