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Q15047 (SETB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase SETDB1

EC=2.1.1.43
Alternative name(s):
ERG-associated protein with SET domain
Short name=ESET
Histone H3-K9 methyltransferase 4
Short name=H3-K9-HMTase 4
Lysine N-methyltransferase 1E
SET domain bifurcated 1
Gene names
Name:SETDB1
Synonyms:KIAA0067, KMT1E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.15

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Subunit structure

Interacts with MBD1; interaction is abolished when MBD1 is sumoylated. Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is required to stimulate histone methyltransferase activity and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9'. During DNA replication, it is recruited by SETDB1 to form a S phase-specific complex that facilitates methylation of H3 'Lys-9' during replication-coupled chromatin assembly and is at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1. Interacts with ERG, TRIM28/TIF1B, CBX1, CBX5, CHD7, DNMT3A, HDAC1, HDAC2, NLK, PPARG, SIN3A, SIN3B, DNMT3B and SUMO2. Interacts with MPHOSPH8. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.19

Subcellular location

Nucleus. Chromosome. Note: Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin.

Tissue specificity

Widely expressed. High expression in testis.

Domain

The pre-SET, SET and post-SET domains are all required for methyltransferase activity. The 347-amino-acid insertion in the SET domain has no effect on the catalytic activity.

Isoform 2 lacks all domains required for histone methyltransferase activity.

Miscellaneous

Highly up-regulated in Huntington disease patients, suggesting that participates in the altered chromatin modulation and transcription dysfunction observed in Huntington disease. Its down-regulation has salubrious effects on patients, suggesting that it may be a promising treatment in Huntington disease patients.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.

Contains 1 MBD (methyl-CpG-binding) domain.

Contains 1 post-SET domain.

Contains 1 pre-SET domain.

Contains 1 SET domain.

Contains 2 Tudor domains.

Sequence caution

The sequence BAA06689.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAI13325.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI13326.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15047-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15047-2)

The sequence of this isoform differs from the canonical sequence as follows:
     381-397: DDKRCEWIYRGSTRLEP → VLFFSTILEAEVGGGGT
     398-1291: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q15047-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1254-1254: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12911291Histone-lysine N-methyltransferase SETDB1
PRO_0000186064

Regions

Domain257 – 32064Tudor 1
Domain347 – 40357Tudor 2
Domain594 – 66572MBD
Domain727 – 80074Pre-SET
Domain803 – 1266464SET
Domain1275 – 129117Post-SET
Coiled coil18 – 6447 Potential

Amino acid modifications

Modified residue9761Phosphothreonine; by NLK Probable
Modified residue10661Phosphoserine Ref.16 Ref.18 Ref.21
Cross-link182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence381 – 39717DDKRC…TRLEP → VLFFSTILEAEVGGGGT in isoform 2.
VSP_002217
Alternative sequence398 – 1291894Missing in isoform 2.
VSP_002218
Alternative sequence12541Missing in isoform 3.
VSP_034600
Natural variant2361N → S.
Corresponds to variant rs2271075 [ dbSNP | Ensembl ].
VAR_014284
Natural variant5061P → S. Ref.4
Corresponds to variant rs17852587 [ dbSNP | Ensembl ].
VAR_031281
Natural variant8241A → G.
Corresponds to variant rs2691551 [ dbSNP | Ensembl ].
VAR_014286
Natural variant8241A → P.
Corresponds to variant rs2814054 [ dbSNP | Ensembl ].
VAR_014285

Experimental info

Mutagenesis729 – 7313CDC → LDP: Abolishes methyltransferase activity. Ref.5
Mutagenesis9761T → A: Abrogates interaction with CHD7, NLK and PPARG. Reduces phosphorylation by NLK. Reduces transcriptional repression. Ref.15
Mutagenesis12241H → K: Abolishes methyltransferase activity. Ref.5
Mutagenesis12261C → A: Abolishes methyltransferase activity. Ref.5
Mutagenesis12791C → Y: Abolishes methyltransferase activity. Ref.5

Secondary structure

....................................... 1291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D8841B4C41B911C5

FASTA1,291143,157
        10         20         30         40         50         60 
MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK MDCVQQRKKQ 

        70         80         90        100        110        120 
LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY SKLGLQYRDS SSEDESSRPT 

       130        140        150        160        170        180 
EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL 

       190        200        210        220        230        240 
HKGTLSQMSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS 

       250        260        270        280        290        300 
LLSGNHIAYD YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 

       310        320        330        340        350        360 
YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS GQLIKTEWEG 

       370        380        390        400        410        420 
TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASALE KKQGQLRTRP 

       430        440        450        460        470        480 
NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL 

       490        500        510        520        530        540 
AQSRKQVAKK STSFRPGSVG SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS 

       550        560        570        580        590        600 
ALPAPPAPPV FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL 

       610        620        630        640        650        660 
LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC DFLFLEMFCL 

       670        680        690        700        710        720 
DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT PPPQVAYSKE RIPGKGVFIN 

       730        740        750        760        770        780 
TGPEFLVGCD CKDGCRDKSK CACHQLTIQA TACTPGGQIN PNSGYQYKRL EECLPTGVYE 

       790        800        810        820        830        840 
CNKRCKCDPN MCTNRLVQHG LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD 

       850        860        870        880        890        900 
FADKEGLEMG DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE 

       910        920        930        940        950        960 
SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP DLGPPHIPVP 

       970        980        990       1000       1010       1020 
PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS HSSFKTNEGG EGRAGGSRME 

      1030       1040       1050       1060       1070       1080 
AEKASTSGLG IKDEGDIKQA KKEDTDDRNK MSVVTESSRN YGYNPSPVKP EGLRRPPSKT 

      1090       1100       1110       1120       1130       1140 
SMHQSRRLMA SAQSNPDDVL TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS 

      1150       1160       1170       1180       1190       1200 
EGDDFEDKKN MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF 

      1210       1220       1230       1240       1250       1260 
YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF ASKRIRAGTE 

      1270       1280       1290 
LTWDYNYEVG SVEGKELLCC CGAIECRGRL L 

« Hide

Isoform 2 [UniParc].

Checksum: A880C9152E11A900
Show »

FASTA39744,689
Isoform 3 [UniParc].

Checksum: BBF5516339BE6C17
Show »

FASTA1,290143,001

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-506.
Tissue: Muscle and Uterus.
[5]"SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins."
Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III
Genes Dev. 16:919-932(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF 729-CYS--CYS-731; HIS-1224; CYS-1226 AND CYS-1279, INTERACTION WITH TRIM28.
[6]"Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation."
Ayyanathan K., Lechner M.S., Bell P., Maul G.G., Schultz D.C., Yamada Y., Tanaka K., Torigoe K., Rauscher F.J. III
Genes Dev. 17:1855-1869(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression."
Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B., Tempst P., Roeder R.G., Zhang Y.
Mol. Cell 12:475-487(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH ATF7IP.
[8]"Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
Sarraf S.A., Stancheva I.
Mol. Cell 15:595-605(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MBD1 AND CHAF1A.
[9]"In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation."
Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., Carpenter A.E., Belmont A.S., van Driel R.
Mol. Cell. Biol. 25:4552-4564(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX1 AND CBX5.
[10]"Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins."
Lyst M.J., Nan X., Stancheva I.
EMBO J. 25:5317-5328(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBD1.
[11]"Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
[12]"The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells."
Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.
J. Biol. Chem. 281:19489-19500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNMT3A AND DNMT3B.
[13]"NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression."
Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G.
Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUMO2.
[14]"ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease."
Ryu H., Lee J., Hagerty S.W., Soh B.Y., McAlpin S.E., Cormier K.A., Smith K.M., Ferrante R.J.
Proc. Natl. Acad. Sci. U.S.A. 103:19176-19181(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPRESSION IN HUNTINGTON DISEASE.
[15]"A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-gamma transactivation."
Takada I., Mihara M., Suzawa M., Ohtake F., Kobayashi S., Igarashi M., Youn M.Y., Takeyama K., Nakamura T., Mezaki Y., Takezawa S., Yogiashi Y., Kitagawa H., Yamada G., Takada S., Minami Y., Shibuya H., Matsumoto K., Kato S.
Nat. Cell Biol. 9:1273-1285(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHD7; NLK1 AND PPARG, PHOSPHORYLATION AT THR-976, MUTAGENESIS OF THR-976.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH REST; CDYL; WIZ; EHMT1 AND EHMT2.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion."
Kokura K., Sun L., Bedford M.T., Fang J.
EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPHOSPH8.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"The crystal structure of Tudor domain of human histone-lysine N-methyltransferase SETDB1."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 196-402.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31891 mRNA. Translation: BAA06689.2. Different initiation.
AL590133 Genomic DNA. Translation: CAI13325.1. Sequence problems.
AL590133 Genomic DNA. Translation: CAI13326.1. Sequence problems.
AL590133 Genomic DNA. Translation: CAI13327.1.
AL590133 Genomic DNA. Translation: CAI13328.1.
CH471121 Genomic DNA. Translation: EAW53506.1.
BC009362 mRNA. Translation: AAH09362.1.
BC028671 mRNA. Translation: AAH28671.1.
RefSeqNP_001138887.1. NM_001145415.1.
NP_001230420.1. NM_001243491.1.
NP_036564.3. NM_012432.3.
UniGeneHs.643565.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DLMX-ray1.77A196-402[»]
ProteinModelPortalQ15047.
SMRQ15047. Positions 196-397, 603-881, 1129-1290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115202. 115 interactions.
DIPDIP-31029N.
IntActQ15047. 98 interactions.
MINTMINT-1184137.
STRING9606.ENSP00000357965.

Chemistry

ChEMBLCHEMBL2321646.

PTM databases

PhosphoSiteQ15047.

Polymorphism databases

DMDM25091210.

Proteomic databases

PaxDbQ15047.
PRIDEQ15047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271640; ENSP00000271640; ENSG00000143379. [Q15047-1]
ENST00000368962; ENSP00000357958; ENSG00000143379. [Q15047-2]
ENST00000368969; ENSP00000357965; ENSG00000143379. [Q15047-3]
GeneID9869.
KEGGhsa:9869.
UCSCuc001evu.2. human. [Q15047-1]
uc001evv.2. human. [Q15047-3]
uc001evw.4. human. [Q15047-2]

Organism-specific databases

CTD9869.
GeneCardsGC01P150898.
HGNCHGNC:10761. SETDB1.
HPAHPA018142.
MIM604396. gene.
neXtProtNX_Q15047.
PharmGKBPA35679.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG061013.
InParanoidQ15047.
KOK11421.
OMAGSVGSGH.
OrthoDBEOG7ZD1TG.
PhylomeDBQ15047.
TreeFamTF106411.

Gene expression databases

ArrayExpressQ15047.
BgeeQ15047.
CleanExHS_SETDB1.
GenevestigatorQ15047.

Family and domain databases

InterProIPR016177. DNA-bd_dom.
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.
[Graphical view]
PfamPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMSSF54171. SSF54171. 1 hit.
PROSITEPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51573. SAM_MT43_SUVAR39_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSETDB1. human.
EvolutionaryTraceQ15047.
GeneWikiSETDB1.
GenomeRNAi9869.
NextBio37203.
PROQ15047.
SOURCESearch...

Entry information

Entry nameSETB1_HUMAN
AccessionPrimary (citable) accession number: Q15047
Secondary accession number(s): A6NEW2 expand/collapse secondary AC list , Q5SZD8, Q5SZD9, Q5SZE0, Q5SZE7, Q96GM9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM