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Q9H5I1 (SUV92_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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 SUV39H2

EC=2.1.1.43
Alternative name(s):
Histone H3-K9 methyltransferase 2
Short name=H3-K9-HMTase 2
Lysine N-methyltransferase 1B
Suppressor of variegation 3-9 homolog 2
Short name=Su(var)3-9 homolog 2
Gene names
Name:SUV39H2
Synonyms:KMT1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. 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 heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. Ref.7

Catalytic activity

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

Subunit structure

Interacts with SMAD5. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Ref.8

Subcellular location

Nucleus By similarity. Chromosomecentromere By similarity. Note: Associates with centromeric constitutive heterochromatin By similarity.

Domain

Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin By similarity.

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.

Sequence similarities

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

Contains 1 chromo domain.

Contains 1 post-SET domain.

Contains 1 pre-SET domain.

Contains 1 SET domain.

Ontologies

Keywords
   Biological processBiological rhythms
Cell cycle
Differentiation
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin assembly or disassembly

Inferred from mutant phenotype PubMed 10949293. Source: UniProtKB

chromatin remodeling

Inferred from direct assay PubMed 10949293. Source: UniProtKB

histone H3-K9 dimethylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-K9 trimethylation

Inferred from sequence or structural similarity. Source: UniProtKB

male meiosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from direct assay PubMed 10949293. Source: UniProtKB

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear heterochromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase activity (H3-K9 specific)

Inferred from direct assay PubMed 10949293. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17474147PubMed 23455924. Source: IntAct

transcription regulatory region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q9H5I1-1)

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.
Note: No experimental confirmation available.
Isoform 1 (identifier: Q9H5I1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
Isoform 2 (identifier: Q9H5I1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     104-283: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Histone-lysine N-methyltransferase SUV39H2
PRO_0000186059

Regions

Domain47 – 10559Chromo
Domain189 – 24759Pre-SET
Domain250 – 373124SET
Domain394 – 41017Post-SET
Region261 – 2633S-adenosyl-L-methionine binding
Region330 – 3312S-adenosyl-L-methionine binding

Sites

Metal binding1911Zinc 1
Metal binding1911Zinc 2
Metal binding1931Zinc 1
Metal binding1961Zinc 1
Metal binding1961Zinc 3
Metal binding2011Zinc 1
Metal binding2021Zinc 2
Metal binding2291Zinc 2
Metal binding2291Zinc 3
Metal binding2331Zinc 2
Metal binding2351Zinc 3
Metal binding2391Zinc 3
Metal binding3331Zinc 4
Metal binding3981Zinc 4
Metal binding4001Zinc 4
Metal binding4051Zinc 4
Binding site3041S-adenosyl-L-methionine
Binding site3991S-adenosyl-L-methionine; via amide nitrogen

Amino acid modifications

Modified residue3811Phosphoserine Ref.11
Modified residue3841Phosphoserine Ref.9 Ref.11
Modified residue3881Phosphoserine Ref.9 Ref.11

Natural variations

Alternative sequence1 – 6060Missing in isoform 1.
VSP_002209
Alternative sequence104 – 283180Missing in isoform 2.
VSP_002210
Natural variant3831D → H in a breast cancer sample; somatic mutation. Ref.13
VAR_036344

Secondary structure

............................................ 410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: ED8BBF80AE838C69

FASTA41046,682
        10         20         30         40         50         60 
MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE YLCDYKVVKD 

        70         80         90        100        110        120 
MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVKKGKAI TPKDNNKTLK 

       130        140        150        160        170        180 
PAIAEYIVKK AKQRIALQRW QDELNRRKNH KGMIFVENTV DLEGPPSDFY YINEYKPAPG 

       190        200        210        220        230        240 
ISLVNEATFG CSCTDCFFQK CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP 

       250        260        270        280        290        300 
NRIVQKGTQY SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK 

       310        320        330        340        350        360 
GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR 

       370        380        390        400        410 
TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN 

« Hide

Isoform 1 [UniParc].

Checksum: F435E9C5EBEA8BAD
Show »

FASTA35039,946
Isoform 2 [UniParc].

Checksum: BB9EF88E02C4D74A
Show »

FASTA23026,350

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 AND 2).
Tissue: Bone marrow and Muscle.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-410.
Tissue: Testis.
[7]"A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells."
Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R., Naguibneva I., Robin P., Cabon F., Polesskaya A., Harel-Bellan A.
EMBO J. 23:605-615(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression."
Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M., Lechleider R.J.
Oncogene 23:5242-5251(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMAD5.
[9]"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-384 AND SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-381; SER-384 AND SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Structural biology of human H3K9 methyltransferases."
Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H., Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H., Plotnikov A.N., Schapira M.
PLoS ONE 5:E8570-E8570(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 112-410 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-383.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027067 mRNA. Translation: BAB15645.1.
CR457372 mRNA. Translation: CAG33653.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40028.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40029.1.
AL360083, AC069544 Genomic DNA. Translation: CAI40032.1.
CH471072 Genomic DNA. Translation: EAW86254.1.
CH471072 Genomic DNA. Translation: EAW86253.1.
CH471072 Genomic DNA. Translation: EAW86255.1.
CH471072 Genomic DNA. Translation: EAW86256.1.
BC007754 mRNA. Translation: AAH07754.1.
BC029360 mRNA. Translation: AAH29360.1.
AL834488 mRNA. Translation: CAD39146.1.
CCDSCCDS53493.1. [Q9H5I1-3]
CCDS53494.1. [Q9H5I1-1]
CCDS7104.1. [Q9H5I1-2]
RefSeqNP_001180353.1. NM_001193424.1. [Q9H5I1-1]
NP_001180354.1. NM_001193425.1. [Q9H5I1-2]
NP_001180355.1. NM_001193426.1. [Q9H5I1-3]
NP_001180356.1. NM_001193427.1.
NP_078946.1. NM_024670.3. [Q9H5I1-2]
XP_006717566.1. XM_006717503.1. [Q9H5I1-2]
UniGeneHs.554883.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R3AX-ray2.00A112-410[»]
ProteinModelPortalQ9H5I1.
SMRQ9H5I1. Positions 48-96, 124-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122838. 39 interactions.
IntActQ9H5I1. 44 interactions.
MINTMINT-3068157.
STRING9606.ENSP00000319208.

Chemistry

BindingDBQ9H5I1.
ChEMBLCHEMBL1795177.

PTM databases

PhosphoSiteQ9H5I1.

Polymorphism databases

DMDM25091325.

Proteomic databases

MaxQBQ9H5I1.
PaxDbQ9H5I1.
PRIDEQ9H5I1.

Protocols and materials databases

DNASU79723.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313519; ENSP00000319208; ENSG00000152455. [Q9H5I1-2]
ENST00000354919; ENSP00000346997; ENSG00000152455. [Q9H5I1-1]
ENST00000378325; ENSP00000367576; ENSG00000152455. [Q9H5I1-3]
GeneID79723.
KEGGhsa:79723.
UCSCuc001ing.3. human. [Q9H5I1-3]
uc001inh.3. human. [Q9H5I1-1]

Organism-specific databases

CTD79723.
GeneCardsGC10P014922.
HGNCHGNC:17287. SUV39H2.
HPAHPA045901.
MIM606503. gene.
neXtProtNX_Q9H5I1.
PharmGKBPA134868807.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOGENOMHOG000231244.
HOVERGENHBG055621.
InParanoidQ9H5I1.
KOK11419.
OMAAWCVPCL.
PhylomeDBQ9H5I1.
TreeFamTF106452.

Gene expression databases

ArrayExpressQ9H5I1.
BgeeQ9H5I1.
CleanExHS_SUV39H2.
GenevestigatorQ9H5I1.

Family and domain databases

InterProIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF009343. SUV39_SET. 1 hit.
SMARTSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51579. SAM_MT43_SUVAR39_3. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUV39H2. human.
EvolutionaryTraceQ9H5I1.
GeneWikiSUV39H2.
GenomeRNAi79723.
NextBio69082.
PROQ9H5I1.
SOURCESearch...

Entry information

Entry nameSUV92_HUMAN
AccessionPrimary (citable) accession number: Q9H5I1
Secondary accession number(s): D3DRT4 expand/collapse secondary AC list , Q5JSS4, Q5JSS5, Q6I9Y3, Q8ND06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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 10

Human chromosome 10: entries, gene names and cross-references to MIM