CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012477
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone-lysine N-methyltransferase SETDB1 
Protein Synonyms/Alias
 ERG-associated protein with SET domain; ESET; Histone H3-K9 methyltransferase 4; H3-K9-HMTase 4; Lysine N-methyltransferase 1E; SET domain bifurcated 1 
Gene Name
 SETDB1 
Gene Synonyms/Alias
 KIAA0067; KMT1E 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58MDCVQQRKKQLAELEubiquitination[1]
59DCVQQRKKQLAELETubiquitination[1, 2, 3]
173KFMDAVNKKSSSQDLubiquitination[1]
174FMDAVNKKSSSQDLHubiquitination[1]
182SSSQDLHKGTLSQMSubiquitination[3, 4]
349NRPMVLLKSGQLIKTubiquitination[5]
355LKSGQLIKTEWEGTWubiquitination[1]
364EWEGTWWKSRVEEVDubiquitination[5]
383RILFLDDKRCEWIYRubiquitination[1]
570SYRAPMEKLFYLPHVubiquitination[1]
597RNEQYRGKNPLLVPLubiquitination[1, 2, 3]
715SKERIPGKGVFINTGubiquitination[1]
786YECNKRCKCDPNMCTubiquitination[1]
809QVRLQLFKTQNKGWGubiquitination[1]
1187TNMASVDKGESAPVRubiquitination[1]
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] 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]
 [3] 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]
 [4] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [5] 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] 
Functional Description
 Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. 
Sequence Annotation
 DOMAIN 257 320 Tudor 1.
 DOMAIN 347 403 Tudor 2.
 DOMAIN 594 665 MBD.
 DOMAIN 727 800 Pre-SET.
 DOMAIN 803 1266 SET.
 DOMAIN 1275 1291 Post-SET.
 MOD_RES 976 976 Phosphothreonine; by NLK (Probable).
 MOD_RES 1066 1066 Phosphoserine.
 CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Chromosome; Coiled coil; Complete proteome; Isopeptide bond; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1291 AA 
Protein Sequence
MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK MDCVQQRKKQ 60
LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY SKLGLQYRDS SSEDESSRPT 120
EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL 180
HKGTLSQMSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS 240
LLSGNHIAYD YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 300
YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS GQLIKTEWEG 360
TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASALE KKQGQLRTRP 420
NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL 480
AQSRKQVAKK STSFRPGSVG SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS 540
ALPAPPAPPV FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL 600
LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC DFLFLEMFCL 660
DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT PPPQVAYSKE RIPGKGVFIN 720
TGPEFLVGCD CKDGCRDKSK CACHQLTIQA TACTPGGQIN PNSGYQYKRL EECLPTGVYE 780
CNKRCKCDPN MCTNRLVQHG LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD 840
FADKEGLEMG DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE 900
SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP DLGPPHIPVP 960
PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS HSSFKTNEGG EGRAGGSRME 1020
AEKASTSGLG IKDEGDIKQA KKEDTDDRNK MSVVTESSRN YGYNPSPVKP EGLRRPPSKT 1080
SMHQSRRLMA SAQSNPDDVL TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS 1140
EGDDFEDKKN MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF 1200
YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF ASKRIRAGTE 1260
LTWDYNYEVG SVEGKELLCC CGAIECRGRL L 1291 
Gene Ontology
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0001833; P:inner cell mass cell proliferation; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016177; DNA-bd_integrase-typ.
 IPR025796; Hist-Lys_N-MeTrfase_SETDB1.
 IPR001739; Methyl_CpG_DNA-bd.
 IPR003616; Post-SET_dom.
 IPR007728; Pre-SET_dom.
 IPR003606; Pre-SET_Zn-bd_sub.
 IPR001214; SET_dom.
 IPR002999; Tudor. 
Pfam
 PF01429; MBD
 PF05033; Pre-SET
 PF00856; SET 
SMART
 SM00391; MBD
 SM00508; PostSET
 SM00468; PreSET
 SM00317; SET
 SM00333; TUDOR 
PROSITE
 PS50982; MBD
 PS50868; POST_SET
 PS50867; PRE_SET
 PS51573; SAM_MT43_SUVAR39_1
 PS50280; SET
 PS50304; TUDOR 
PRINTS