CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031204
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone-lysine N-methyltransferase SUV39H1 
Protein Synonyms/Alias
 Suppressor of variegation 3-9 homolog 1 (Drosophila), isoform CRA_b; cDNA FLJ57812, highly similar to Histone-lysine N-methyltransferase, H3 lysine-9 specific 1 (EC 2.1.1.43) 
Gene Name
 SUV39H1 
Gene Synonyms/Alias
 hCG_19814 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48CPALGISKRNLYDFEubiquitination[1]
98LKCVRILKQFHKDLEubiquitination[1]
132LANYLVQKAKQRRALubiquitination[2, 3]
134NYLVQKAKQRRALRRubiquitination[1]
149WEQELNAKRSHLGRIubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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
  
Sequence Annotation
  
Keyword
 Chromosome; Complete proteome; Methyltransferase; Nucleus; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 423 AA 
Protein Sequence
MVGMSRLRND RLADPLTGCS VCCKSSWNQL QDLCRLAKLS CPALGISKRN LYDFEVEYLC 60
DYKKIREQEY YLVKWRGYPD SESTWEPRQN LKCVRILKQF HKDLERELLR RHHRSKTPRH 120
LDPSLANYLV QKAKQRRALR RWEQELNAKR SHLGRITVEN EVDLDGPPRA FVYINEYRVG 180
EGITLNQVAV GCECQDCLWA PTGGCCPGAS LHKFAYNDQG QVRLRAGLPI YECNSRCRCG 240
YDCPNRVVQK GIRYDLCIFR TDDGRGWGVR TLEKIRKNSF VMEYVGEIIT SEEAERRGQI 300
YDRQGATYLF DLDYVEDVYT VDAAYYGNIS HFVNHSCDPN LQVYNVFIDN LDERLPRIAF 360
FATRTIRAGE ELTFDYNMQV DPVDMESTRM DSNFGLAGLP GSPKKRVRIE CKCGTESCRK 420
YLF 423 
Gene Ontology
 GO:0005694; C:chromosome; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR023779; Chromodomain_CS.
 IPR011381; Histone_H3-K9_MeTrfase.
 IPR003616; Post-SET_dom.
 IPR007728; Pre-SET_dom.
 IPR003606; Pre-SET_Zn-bd_sub.
 IPR001214; SET_dom. 
Pfam
 PF00385; Chromo
 PF05033; Pre-SET
 PF00856; SET 
SMART
 SM00298; CHROMO
 SM00508; PostSET
 SM00468; PreSET
 SM00317; SET 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2
 PS50868; POST_SET
 PS50867; PRE_SET
 PS51579; SAM_MT43_SUVAR39_3
 PS50280; SET 
PRINTS