CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014112
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A deubiquitinase MYSM1 
Protein Synonyms/Alias
 2A-DUB; Myb-like, SWIRM and MPN domain-containing protein 1 
Gene Name
 MYSM1 
Gene Synonyms/Alias
 KIAA1915 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67ENRAVIEKMLLEEEYubiquitination[1]
78EEEYYLSKKSQPEKVubiquitination[1, 2, 3, 4]
79EEYYLSKKSQPEKVWubiquitination[3]
84SKKSQPEKVWLDQKEubiquitination[1, 5, 6]
90EKVWLDQKEDDKKYMubiquitination[1, 3]
95DQKEDDKKYMKSLQKubiquitination[3]
98EDDKKYMKSLQKTAKubiquitination[3]
135LFEQGLAKFGRRWTKubiquitination[1, 5, 6, 7]
173KVKCGLDKETPNQKTubiquitination[3]
284RGCLQNEKQDETLSSubiquitination[1]
533LSAEELAKRREEEKGubiquitination[1]
675RDIDTQAKYQSYFSRubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
810NLFLSNYKSNQENGVubiquitination[4]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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] 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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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]
 [10] 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] 
Functional Description
 Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation. 
Sequence Annotation
 DOMAIN 116 167 SANT.
 DOMAIN 372 470 SWIRM.
 DOMAIN 572 682 MPN.
 MOTIF 656 669 JAMM motif.
 MOTIF 774 778 LXXLL motif.
 METAL 656 656 Zinc; catalytic (By similarity).
 METAL 658 658 Zinc; catalytic (By similarity).
 METAL 669 669 Zinc; catalytic (Probable).
 MOD_RES 218 218 Phosphoserine.
 MOD_RES 236 236 Phosphothreonine.
 MOD_RES 340 340 Phosphoserine.  
Keyword
 3D-structure; Activator; Alternative splicing; Chromatin regulator; Complete proteome; DNA-binding; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Polymorphism; Protease; Reference proteome; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 828 AA 
Protein Sequence
MAAEEADVDI EGDVVAAAGA QPGSGENTAS VLQKDHYLDS SWRTENGLIP WTLDNTISEE 60
NRAVIEKMLL EEEYYLSKKS QPEKVWLDQK EDDKKYMKSL QKTAKIMVHS PTKPASYSVK 120
WTIEEKELFE QGLAKFGRRW TKISKLIGSR TVLQVKSYAR QYFKNKVKCG LDKETPNQKT 180
GHNLQVKNED KGTKAWTPSC LRGRADPNLN AVKIEKLSDD EEVDITDEVD ELSSQTPQKN 240
SSSDLLLDFP NSKMHETNQG EFITSDSQEA LFSKSSRGCL QNEKQDETLS SSEITLWTEK 300
QSNGDKKSIE LNDQKFNELI KNCNKHDGRG IIVDARQLPS PEPCEIQKNL NDNEMLFHSC 360
QMVEESHEEE ELKPPEQEIE IDRNIIQEEE KQAIPEFFEG RQAKTPERYL KIRNYILDQW 420
EICKPKYLNK TSVRPGLKNC GDVNCIGRIH TYLELIGAIN FGCEQAVYNR PQTVDKVRIR 480
DRKDAVEAYQ LAQRLQSMRT RRRRVRDPWG NWCDAKDLEG QTFEHLSAEE LAKRREEEKG 540
RPVKSLKVPR PTKSSFDPFQ LIPCNFFSEE KQEPFQVKVA SEALLIMDLH AHVSMAEVIG 600
LLGGRYSEVD KVVEVCAAEP CNSLSTGLQC EMDPVSQTQA SETLAVRGFS VIGWYHSHPA 660
FDPNPSLRDI DTQAKYQSYF SRGGAKFIGM IVSPYNRNNP LPYSQITCLV ISEEISPDGS 720
YRLPYKFEVQ QMLEEPQWGL VFEKTRWIIE KYRLSHSSVP MDKIFRRDSD LTCLQKLLEC 780
MRKTLSKVTN CFMAEEFLTE IENLFLSNYK SNQENGVTEE NCTKELLM 828 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
 GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR009057; Homeodomain-like.
 IPR000555; JAB1_Mov34_MPN_PAD1.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR007526; SWIRM.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01398; JAB
 PF00249; Myb_DNA-binding
 PF04433; SWIRM 
SMART
 SM00232; JAB_MPN
 SM00717; SANT 
PROSITE
 PS51293; SANT
 PS50934; SWIRM 
PRINTS