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Q8C267

- SETB2_MOUSE

UniProt

Q8C267 - SETB2_MOUSE

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Protein

Histone-lysine N-methyltransferase SETDB2

Gene
Setdb2, Gm293
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi296 – 2961Zinc 1 By similarity
Metal bindingi296 – 2961Zinc 2 By similarity
Metal bindingi298 – 2981Zinc 1 By similarity
Metal bindingi302 – 3021Zinc 1 By similarity
Metal bindingi302 – 3021Zinc 3 By similarity
Metal bindingi308 – 3081Zinc 1 By similarity
Metal bindingi310 – 3101Zinc 2 By similarity
Metal bindingi348 – 3481Zinc 2 By similarity
Metal bindingi348 – 3481Zinc 3 By similarity
Metal bindingi352 – 3521Zinc 2 By similarity
Metal bindingi354 – 3541Zinc 3 By similarity
Metal bindingi359 – 3591Zinc 3 By similarity
Binding sitei642 – 6421S-adenosyl-L-methionine By similarity
Metal bindingi648 – 6481Zinc 4 By similarity
Metal bindingi701 – 7011Zinc 4 By similarity
Metal bindingi703 – 7031Zinc 4 By similarity
Metal bindingi708 – 7081Zinc 4 By similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. heart looping Source: UniProtKB
  3. histone H3-K9 methylation Source: UniProtKB
  4. left/right axis specification Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETDB2 (EC:2.1.1.43)
Alternative name(s):
SET domain bifurcated 2
Gene namesi
Name:Setdb2
Synonyms:Gm293
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:2685139. Setdb2.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Histone-lysine N-methyltransferase SETDB2PRO_0000281824Add
BLAST

Proteomic databases

PaxDbiQ8C267.
PRIDEiQ8C267.

PTM databases

PhosphoSiteiQ8C267.

Expressioni

Gene expression databases

ArrayExpressiQ8C267.
BgeeiQ8C267.
CleanExiMM_SETDB2.
GenevestigatoriQ8C267.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093450.

Structurei

3D structure databases

ProteinModelPortaliQ8C267.
SMRiQ8C267. Positions 247-414, 629-709.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 23373MBDAdd
BLAST
Domaini294 – 36774Pre-SETAdd
BLAST
Domaini370 – 688319SETAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni380 – 3823S-adenosyl-L-methionine binding By similarity
Regioni645 – 6462S-adenosyl-L-methionine binding By similarity

Domaini

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

Contains 1 pre-SET domain.
Contains 1 SET domain.

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00750000117355.
HOGENOMiHOG000060314.
HOVERGENiHBG106688.
InParanoidiQ8C267.
KOiK11421.
OMAiKCHFQRR.
PhylomeDBiQ8C267.
TreeFamiTF106411.

Family and domain databases

InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8C267-1) [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

MEEKNGDAKT FWMELQDDGK VDLMFEKTQN VLHSLKQKIK DGSATNGDYV    50
QAMNLVNEAT LSNTQTLEKG MFITYSNPEV NTHRSNHTPV TQSEQENKSS 100
AVPSASCDNS CPKGCTIPSP GKKVFLPVKN KADNLVKKEA PLHISFHRHI 150
CSRTCLMETP LSLKGENPLQ LPIRCHFQRR HAKTNSHSSA LHVNYKTPCG 200
RNLRNMEEVF HYLLETECNF LFTDNFSFNT YVQLTRNHPK QNEVVSDVDI 250
SNGVESVSIP FCNEIDNSKL PRFKYRNTVW PRIYHLNFSN MFSDSCDCSE 300
GCIDIKKCAC LQLTAKNAKA CPLSSDGECA GYKYKRLQRL IPTGIYECNL 350
LCKCNKQMCQ NRVIQHGVRV RLQVFKSEKK GWGVRCLDDI DKGTFVCIYS 400
GRLLRRATPE KTNIGENGRE QQHIVKNSFS KKRKLEVVCS DCDAHCDSPK 450
AEDCPPKLSG DLKEPAVEMN HRNISRTQHH SVIRRTKSKT TVFHYSEKNM 500
GFVCSDSAAP EDKNGFKPAQ EHVNSEARRA HEDLSSNPAG DSEDTQLTES 550
DVIDITASRE DSAPAYRCKH ATIVDRKDTK QVLEVPGKKS QEEEPAASQS 600
QQALCDEELP SERTKIPSAS LMQLSKESLF LLDASKEGNV GRFLNHSCCP 650
NLWVQNVFVE THDRNFPLVA FFTNRYVKAR TELTWDYGYE AGATPAKEIL 700
CQCGFNKCRK KLI 713
Length:713
Mass (Da):80,636
Last modified:April 3, 2007 - v2
Checksum:iC4E750F01ED4231A
GO
Isoform 2 (identifier: Q8C267-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-86: GMFITYSNPEVNTHRSN → D
     119-156: SPGKKVFLPV...HRHICSRTCL → YVYVIRVSAP...NSRCLCLLVN
     157-713: Missing.

Note: No experimental confirmation available.

Show »
Length:140
Mass (Da):15,493
Checksum:i37E19B746B1A9205
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei70 – 8617GMFIT…THRSN → D in isoform 2. VSP_024063Add
BLAST
Alternative sequencei119 – 15638SPGKK…SRTCL → YVYVIRVSAPSVCCLLNIPK SLTPFIKFNSRCLCLLVN in isoform 2. VSP_024064Add
BLAST
Alternative sequencei157 – 713557Missing in isoform 2. VSP_024065Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK089197 mRNA. Translation: BAC40789.1.
AC114007 Genomic DNA. No translation available.
CCDSiCCDS36939.1. [Q8C267-1]
RefSeqiNP_001074493.1. NM_001081024.1. [Q8C267-1]
UniGeneiMm.205022.

Genome annotation databases

EnsembliENSMUST00000095775; ENSMUSP00000093450; ENSMUSG00000071350. [Q8C267-1]
ENSMUST00000111253; ENSMUSP00000106884; ENSMUSG00000071350. [Q8C267-2]
GeneIDi239122.
KEGGimmu:239122.
UCSCiuc007uei.1. mouse. [Q8C267-1]
uc007uej.1. mouse. [Q8C267-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK089197 mRNA. Translation: BAC40789.1 .
AC114007 Genomic DNA. No translation available.
CCDSi CCDS36939.1. [Q8C267-1 ]
RefSeqi NP_001074493.1. NM_001081024.1. [Q8C267-1 ]
UniGenei Mm.205022.

3D structure databases

ProteinModelPortali Q8C267.
SMRi Q8C267. Positions 247-414, 629-709.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000093450.

PTM databases

PhosphoSitei Q8C267.

Proteomic databases

PaxDbi Q8C267.
PRIDEi Q8C267.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000095775 ; ENSMUSP00000093450 ; ENSMUSG00000071350 . [Q8C267-1 ]
ENSMUST00000111253 ; ENSMUSP00000106884 ; ENSMUSG00000071350 . [Q8C267-2 ]
GeneIDi 239122.
KEGGi mmu:239122.
UCSCi uc007uei.1. mouse. [Q8C267-1 ]
uc007uej.1. mouse. [Q8C267-2 ]

Organism-specific databases

CTDi 83852.
MGIi MGI:2685139. Setdb2.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00750000117355.
HOGENOMi HOG000060314.
HOVERGENi HBG106688.
InParanoidi Q8C267.
KOi K11421.
OMAi KCHFQRR.
PhylomeDBi Q8C267.
TreeFami TF106411.

Miscellaneous databases

NextBioi 383999.
PROi Q8C267.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8C267.
Bgeei Q8C267.
CleanExi MM_SETDB2.
Genevestigatori Q8C267.

Family and domain databases

InterProi IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50982. MBD. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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] (ISOFORM 2).
    Strain: NOD.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiSETB2_MOUSE
AccessioniPrimary (citable) accession number: Q8C267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 90 of the entry and version 2 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

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