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O88974

- SETB1_MOUSE

UniProt

O88974 - SETB1_MOUSE

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Protein

Histone-lysine N-methyltransferase SETDB1

Gene

Setdb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi746 – 7461Zinc 1By similarity
Metal bindingi746 – 7461Zinc 2By similarity
Metal bindingi748 – 7481Zinc 1By similarity
Metal bindingi752 – 7521Zinc 1By similarity
Metal bindingi752 – 7521Zinc 3By similarity
Metal bindingi758 – 7581Zinc 1By similarity
Metal bindingi760 – 7601Zinc 2By similarity
Metal bindingi798 – 7981Zinc 2By similarity
Metal bindingi798 – 7981Zinc 3By similarity
Metal bindingi802 – 8021Zinc 2By similarity
Metal bindingi804 – 8041Zinc 3By similarity
Metal bindingi809 – 8091Zinc 3By similarity
Binding sitei868 – 8681S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei870 – 8701S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei1236 – 12361S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi1242 – 12421Zinc 4By similarity
Metal bindingi1295 – 12951Zinc 4By similarity
Metal bindingi1297 – 12971Zinc 4By similarity
Metal bindingi1302 – 13021Zinc 4By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. bone development Source: MGI
  2. histone H3-K9 trimethylation Source: MGI
  3. inner cell mass cell proliferation Source: MGI
  4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETDB1 (EC:2.1.1.43)
Alternative name(s):
ERG-associated protein with SET domain
Short name:
ESET
SET domain bifurcated 1
Gene namesi
Name:Setdb1
Synonyms:Eset, Kiaa0067
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1934229. Setdb1.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity
Note: Associated with non-pericentromeric regions of chromatin.By similarity

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi798 – 7981C → T: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi1242 – 12421C → T: Abolishes methyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13071307Histone-lysine N-methyltransferase SETDB1PRO_0000186065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei993 – 9931Phosphothreonine; by NLKBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88974.
PaxDbiO88974.
PRIDEiO88974.

PTM databases

PhosphoSiteiO88974.

Expressioni

Tissue specificityi

Ubiquitously expressed. Strong expression in liver and testis.1 Publication

Gene expression databases

CleanExiMM_SETDB1.
GenevestigatoriO88974.

Interactioni

Subunit structurei

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 TRIM28/TIF1B, CBX1, CBX5, CHD7, DNMT3A, DNMT3B, NLK, PPARG and SUMO2. Interacts with MPHOSPH8 (By similarity). Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Interacts with ERG, HDAC1, HDAC2, SIN3A, SIN3B.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ErgP812703EBI-79658,EBI-79647

Protein-protein interaction databases

IntActiO88974. 9 interactions.
MINTiMINT-1753431.
STRINGi10090.ENSMUSP00000102788.

Structurei

3D structure databases

ProteinModelPortaliO88974.
SMRiO88974. Positions 196-397, 698-903, 1181-1306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini257 – 32064Tudor 1Add
BLAST
Domaini347 – 40357Tudor 2Add
BLAST
Domaini611 – 68272MBDPROSITE-ProRule annotationAdd
BLAST
Domaini744 – 81774Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini820 – 1282463SETPROSITE-ProRule annotationAdd
BLAST
Domaini1291 – 130717Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni830 – 8323S-adenosyl-L-methionine bindingBy similarity
Regioni1239 – 12402S-adenosyl-L-methionine bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili30 – 6536Sequence AnalysisAdd
BLAST

Domaini

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.
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation
Contains 2 Tudor domains.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG2940.
HOVERGENiHBG061013.
InParanoidiO88974.

Family and domain databases

InterProiIPR016177. 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]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. 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]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: O88974-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSLPGCMSL AAAPAAADSA EIAELQQAVV EELGISMEEL RQYIDEELEK
60 70 80 90 100
MDCIQQRKKQ LAELETWVLQ KESEVAYVDR LFDDASREVT NCESLVKDFY
110 120 130 140 150
SKLGLQYHDS SSEDEASRPT EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL
160 170 180 190 200
REAMAALRKS AQDVQKFMDA VNKKSSSQDL HKGTLGQVSG ELSKDGDLIV
210 220 230 240 250
SMRILGKKRT KTWHKGTLIA IQTVGLGKKY KVKFDNKGKS LLSGNHIAYD
260 270 280 290 300
YHPPADKLFV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG
310 320 330 340 350
YASYVTQSEL YPICRPLKKT WEDIEDSSCR DFIEEYITAY PNRPMVLLKS
360 370 380 390 400
GQLIKTEWEG TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS
410 420 430 440 450
MKTSSASAME KKQGGQLRTR PNMGAVRSKG PVVQYTQDLT GTGIQFKPME
460 470 480 490 500
PLQPIAPPAP LPIPPLSPQA ADTDLESQLA QSRKQVAKKS TSFRPGSVGS
510 520 530 540 550
GHSSPTSSTL SENVSAGKLG INQTYRSPLA SVTSTPASAA PPVPPVPPGP
560 570 580 590 600
PTPPGPPAPP GPLAPPAFHG MLERAPAEPS YRAPMEKLFY LPHVCSYTCL
610 620 630 640 650
SRIRPMRNEQ YRGKNPLLVP LLYDFRRMTA RRRVNRKMGF HVIYKTPCGL
660 670 680 690 700
CLRTMQEIER YLFETGCDFL FLEMFCLDPY VLVDRKFQPF KPFYYILDIT
710 720 730 740 750
YGKEDVPLSC VNEIDTTPPP QVAYSKERIP GKGVFINTGP EFLVGCDCKD
760 770 780 790 800
GCRDKSKCAC HQLTIQATAC TPGGQVNPNS GYQYKRLEEC LPTGVYECNK
810 820 830 840 850
RCNCDPNMCT NRLVQHGLQV RLQLFKTQNK GWGIRCLDDI AKGSFVCIYA
860 870 880 890 900
GKILTDDFAD KEGLEMGDEY FANLDHIESV ENFKEGYESD VPTSSDSSGV
910 920 930 940 950
DMKDQEDGNS GSEDPEESND DSSDDNFCKD EDFSTSSVWR SYATRRQTRG
960 970 980 990 1000
QKENELSEMT SKDSRPPDLG PPHVPIPSSV SVGGCNPPSS EETPKNKVAS
1010 1020 1030 1040 1050
WLSCNSVSEG GFADSDSRSS FKTSEGGDGR AGGGRGEAER ASTSGLSFKD
1060 1070 1080 1090 1100
EGDNKQPKKE DPENRNKMPV VTEGSQNHGH NPPMKSEGLR RPASKMSVLQ
1110 1120 1130 1140 1150
SQRVVTSTQS NPDDILTLSS STESEGESGT SRKPTAGHTS ATAVDSDDIQ
1160 1170 1180 1190 1200
TISSGSDGDD FEDKKNLSGP TKRQVAVKST RGFALKSTHG IAIKSTNMAS
1210 1220 1230 1240 1250
VDKGESAPVR KNTRQFYDGE ESCYIIDAKL EGNLGRYLNH SCSPNLFVQN
1260 1270 1280 1290 1300
VFVDTHDLRF PWVAFFASKR IRAGTELTWD YNYEVGSVEG KELLCCCGAI

ECRGRLL
Length:1,307
Mass (Da):144,549
Last modified:November 1, 1998 - v1
Checksum:i326AED6371D156C2
GO
Isoform 2 (identifier: O88974-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     482-486: SRKQV → AQSQK
     489-1307: Missing.

Show »
Length:488
Mass (Da):54,696
Checksum:i8874BF6A963B5415
GO
Isoform 3 (identifier: O88974-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-807: Missing.

Show »
Length:500
Mass (Da):54,477
Checksum:i164B400024020B2F
GO
Isoform 4 (identifier: O88974-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     474-474: D → ES

Show »
Length:1,308
Mass (Da):144,650
Checksum:iE224818F50D56E25
GO
Isoform 5 (identifier: O88974-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-1307: Missing.

Show »
Length:526
Mass (Da):58,617
Checksum:iF5B6903C06D91D11
GO
Isoform 6 (identifier: O88974-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     474-474: D → ES
     527-1307: Missing.

Show »
Length:527
Mass (Da):58,719
Checksum:iF2B3561EAA10EC06
GO
Isoform 7 (identifier: O88974-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     756-1307: Missing.

Note: No experimental confirmation available.

Show »
Length:755
Mass (Da):84,400
Checksum:i3AE0FFE5C3542A60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti463 – 4631I → M in BAC40439. (PubMed:16141072)Curated
Sequence conflicti1092 – 10921P → S in BAC65480. (PubMed:12693553)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 807807Missing in isoform 3. 1 PublicationVSP_002221Add
BLAST
Alternative sequencei474 – 4741D → ES in isoform 4 and isoform 6. 2 PublicationsVSP_024031
Alternative sequencei482 – 4865SRKQV → AQSQK in isoform 2. 1 PublicationVSP_002219
Alternative sequencei489 – 1307819Missing in isoform 2. 1 PublicationVSP_002220Add
BLAST
Alternative sequencei527 – 1307781Missing in isoform 5 and isoform 6. 1 PublicationVSP_024032Add
BLAST
Alternative sequencei756 – 1307552Missing in isoform 7. 1 PublicationVSP_024033Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091628 mRNA. Translation: AAC43039.1.
AY091600 mRNA. Translation: AAM13922.1.
AF546078 mRNA. Translation: AAN52358.1.
AY226577 Genomic DNA. Translation: AAO73535.2.
AY226577 Genomic DNA. Translation: AAO73536.2.
BC007176 mRNA. Translation: AAH07176.1.
BC079537 mRNA. Translation: AAH79537.1.
AK122198 Transcribed RNA. Translation: BAC65480.3.
AK088590 mRNA. Translation: BAC40439.1.
CCDSiCCDS17613.1. [O88974-4]
CCDS50991.1. [O88974-1]
PIRiT17453.
UniGeneiMm.490259.

Genome annotation databases

UCSCiuc008qjo.2. mouse. [O88974-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091628 mRNA. Translation: AAC43039.1 .
AY091600 mRNA. Translation: AAM13922.1 .
AF546078 mRNA. Translation: AAN52358.1 .
AY226577 Genomic DNA. Translation: AAO73535.2 .
AY226577 Genomic DNA. Translation: AAO73536.2 .
BC007176 mRNA. Translation: AAH07176.1 .
BC079537 mRNA. Translation: AAH79537.1 .
AK122198 Transcribed RNA. Translation: BAC65480.3 .
AK088590 mRNA. Translation: BAC40439.1 .
CCDSi CCDS17613.1. [O88974-4 ]
CCDS50991.1. [O88974-1 ]
PIRi T17453.
UniGenei Mm.490259.

3D structure databases

ProteinModelPortali O88974.
SMRi O88974. Positions 196-397, 698-903, 1181-1306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O88974. 9 interactions.
MINTi MINT-1753431.
STRINGi 10090.ENSMUSP00000102788.

PTM databases

PhosphoSitei O88974.

Proteomic databases

MaxQBi O88974.
PaxDbi O88974.
PRIDEi O88974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi uc008qjo.2. mouse. [O88974-5 ]

Organism-specific databases

MGIi MGI:1934229. Setdb1.
Rougei Search...

Phylogenomic databases

eggNOGi COG2940.
HOVERGENi HBG061013.
InParanoidi O88974.

Miscellaneous databases

ChiTaRSi Setdb1. mouse.
PROi O88974.
SOURCEi Search...

Gene expression databases

CleanExi MM_SETDB1.
Genevestigatori O88974.

Family and domain databases

InterProi IPR016177. 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 ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50982. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor."
    Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H., Hickstein D.D., Zhang Y.
    Oncogene 21:148-152(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, INTERACTION WITH ERG, MUTAGENESIS OF CYS-798 AND CYS-1242.
    Strain: BDF1.
    Tissue: Blood.
  2. "Genomic structure and expression of the mouse ESET gene encoding an ERG-associated histone methyltransferase with a SET domain."
    Blackburn M.L., Chansky H.A., Zielinska-Kwiatkowska A., Matsui Y., Yang L.
    Biochim. Biophys. Acta 1629:8-14(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 6), TISSUE SPECIFICITY.
    Strain: BDF1 and C57BL/6J X DBA/2.
  3. "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 3 AND 7).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1307 (ISOFORM 4).
    Tissue: Brain.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 4).
    Strain: NOD.
    Tissue: Thymus.
  6. "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."
    Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.
    Biochem. J. 369:651-657(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1; HDAC2; SIN3A AND SIN3B.

Entry informationi

Entry nameiSETB1_MOUSE
AccessioniPrimary (citable) accession number: O88974
Secondary accession number(s): Q6AXH8
, Q78N64, Q78N65, Q80U84, Q8BTV6, Q8CIX7, Q922K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3