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Protein Page:
SETDB1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
SETDB1 a protein lysine methyltransferase that specifically trimethylates K9 of histone H3 (H3K9me3), a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Unlike SUV39H H3K9 methyltransferase, which functions mainly in heterochromatin regions such as pericentric heterochromatin, SETDB1 functions mainly in euchromatic regions, playing a central role in the silencing of euchromatic genes. H3K9me3 is coordinated with DNA methylation. Interacts with a variety of proteins, including transcription factors (ERG), histone deacetylases (HDAC1/2), DNA methyltransferases (DNMT3A/B) and transcriptional co-repressors (mSin3A/B, MBD1, KAP-1, the ATFa-associated modulator mAM). Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. Contains Tudor and methyl-CpG-binding domains, which may coordinate binding to methylated histones and methylated DNA, respectively. Is targeted to histone H3 by TIF1B, a factor recruited by KRAB zinc-finger proteins. Recruited by DNMT3A to silenced promoters in cancer cells. May play a role in the pathogenesis of Huntington's disease, since levels of SETDB1 and H3K9me3 are both increased in diseased brains. Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Three isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Methyltransferase, protein lysine; EC 2.1.1.43; Amino Acid Metabolism - lysine degradation; Methyltransferase
Cellular Component: Golgi apparatus; cytoplasm; plasma membrane; nucleolus; chromosome; nucleus
Molecular Function: protein binding; DNA binding; zinc ion binding; histone-lysine N-methyltransferase activity
Biological Process: regulation of transcription, DNA-dependent; transcription, DNA-dependent; inner cell mass cell proliferation
Reference #:  Q15047 (UniProtKB)
Alt. Names/Synonyms: ERG-associated protein with a SET domain, ESET; ERG-associated protein with SET domain; ESET; H3-K9-HMTase 4; H3-K9-HMTase4; Histone H3-K9 methyltransferase 4; Histone-lysine N-methyltransferase SETDB1; histone-lysine N-methyltransferase, H3lysine-9 specific 4; KG1T; KIAA0067; KMT1E; Lysine N-methyltransferase 1E; SET domain bifurcated 1; SET domain, bifurcated 1; SETB1; SETDB1
Gene Symbols: SETDB1
Molecular weight: 143,157 Da
Basal Isoelectric point: 5.74  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SETDB1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K59-u DCVQQRKkQLAELET
0 1 Y107 YSKLGLQYRDsssED
0 2 S110-p LGLQYRDsssEDESS
0 2 S111-p GLQYRDsssEDESSR
0 2 S112-p LQYRDsssEDESSRP
0 1 S117 sssEDESSRPTEIIE
0 1 T120 EDESSRPTEIIEIPD
0 1 S134-p DEDDDVLsIDsGDAG
0 1 S137-p DDVLsIDsGDAGSRT
0 1 S175-p MDAVNKKsSSQDLHk
0 1 K182-u sSSQDLHkGTLSQMS
0 2 Y230-p TVGPGKKyKVKFDNK
0 1 S468-p FPPAPPLsPQAGDsD
0 1 S474-p LsPQAGDsDLESQLA
0 1 K490-m3 SRKQVAKkSTSFRPG
0 1 S501-p FRPGSVGsGHssPtS
0 1 S504-p GSVGsGHssPtSPAL
0 1 S505-p SVGsGHssPtSPALS
0 1 T507-p GsGHssPtSPALSEN
0 3 K597-u RNEQYRGkNPLLVPL
0 1 T838-p IYAGKILtDDFADKE
0 1 S862-p ANLDHIEsVENFKEG
0 1 S872-p NFKEGYEsDAPCSSD
0 1 S905-p PEESNDDssDDNFCK
0 1 S906-p EESNDDssDDNFCKD
0 1 S1000 GGFADSDSHSSFKTN
0 2 S1025-p RMEAEKAsTSGLGIK
0 1 G1030 KAsTSGLGIKDEGDI
0 2 K1050-u EDTDDRNkMSVVTES
1 17 S1066-p RNYGYNPsPVKPEGL
0 1 T1101-p SNPDDVLtLssStEs
0 1 S1103-p PDDVLtLssStEsEG
0 1 S1104-p DDVLtLssStEsEGE
0 1 T1106-p VLtLssStEsEGESG
0 1 S1108-p tLssStEsEGESGTS
0 3 S1130-p TSATAVDsDDIQtIs
0 4 T1135-p VDsDDIQtIssGsEG
0 3 S1137-p sDDIQtIssGsEGDD
0 3 S1138-p DDIQtIssGsEGDDF
0 3 S1140-p IQtIssGsEGDDFED
0 2 K1170-m1 STRGFALkSTHGIAI
0 1 K1170-m2 STRGFALkSTHGIAI
0 1 K1170-m3 STRGFALkSTHGIAI
0 1 K1178-m2 STHGIAIkStNMASV
0 1 K1178-m3 STHGIAIkStNMASV
0 1 S1179 THGIAIkStNMASVD
0 2 T1180-p HGIAIkStNMASVDK
0 1 S1190-p ASVDKGEsAPVRKNt
0 1 T1197-p sAPVRKNtRQFYDGE
  mouse

 
K59 DCIQQRKKQLAELET
Y107-p YSKLGLQyHDsssED
S110-p LGLQyHDsssEDEAs
S111-p GLQyHDsssEDEAsR
S112-p LQyHDsssEDEAsRP
S117-p sssEDEAsRPtEIIE
T120-p EDEAsRPtEIIEIPD
S134 DEDDDVLSIDSGDAG
S137 DDVLSIDSGDAGSRT
S175 MDAVNKKSSSQDLHK
K182 SSSQDLHKGTLGQVS
Y230 TVGLGKKYKVKFDNK
S467 PLPIPPLSPQAADTD
T473 LSPQAADTDLESQLA
K489 SRKQVAKKSTSFRPG
S500 FRPGSVGSGHSSPTS
S503 GSVGSGHSSPTSSTL
S504 SVGSGHSSPTSSTLS
T506 GSGHSSPTSSTLSEN
K614 RNEQYRGKNPLLVPL
T855 IYAGKILTDDFADKE
S879 ANLDHIESVENFKEG
S889 NFKEGYESDVPTSSD
S922 PEESNDDSSDDNFCK
S923 EESNDDSSDDNFCKD
S1017-p GGFADSDsRSSFKTS
S1042 RGEAERASTSGLsFK
S1047-p RASTSGLsFKDEGDN
K1067 EDPENRNKMPVVTEG
- gap
T1117 SNPDDILTLSSSTES
S1119 PDDILTLSSSTESEG
S1120 DDILTLSSSTESEGE
T1122 ILTLSSSTESEGESG
S1124 TLSSSTESEGESGTS
S1146 TSATAVDSDDIQTIS
T1151 VDSDDIQTISSGSDG
S1153 SDDIQTISSGSDGDD
S1154 DDIQTISSGSDGDDF
S1156 IQTISSGSDGDDFED
K1186-m1 STRGFALkSTHGIAI
K1186 STRGFALKSTHGIAI
K1186 STRGFALKSTHGIAI
K1194 STHGIAIKstNMASV
K1194 STHGIAIKstNMASV
S1195-p THGIAIKstNMASVD
T1196-p HGIAIKstNMASVDK
S1206 ASVDKGESAPVRKNT
T1213 SAPVRKNTRQFYDGE
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