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Protein

Histone-lysine N-methyltransferase SUV39H2

Gene

SUV39H2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi191 – 1911Zinc 1
Metal bindingi191 – 1911Zinc 2
Metal bindingi193 – 1931Zinc 1
Metal bindingi196 – 1961Zinc 1
Metal bindingi196 – 1961Zinc 3
Metal bindingi201 – 2011Zinc 1
Metal bindingi202 – 2021Zinc 2
Metal bindingi229 – 2291Zinc 2
Metal bindingi229 – 2291Zinc 3
Metal bindingi233 – 2331Zinc 2
Metal bindingi235 – 2351Zinc 3
Metal bindingi239 – 2391Zinc 3
Binding sitei304 – 3041S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Metal bindingi333 – 3331Zinc 4
Metal bindingi398 – 3981Zinc 4
Binding sitei399 – 3991S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication
Metal bindingi400 – 4001Zinc 4
Metal bindingi405 – 4051Zinc 4

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  3. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. cellular response to hypoxia Source: MGI
  3. chromatin assembly or disassembly Source: UniProtKB
  4. chromatin organization Source: Reactome
  5. chromatin remodeling Source: UniProtKB
  6. histone H3-K9 dimethylation Source: UniProtKB
  7. histone H3-K9 trimethylation Source: UniProtKB
  8. male meiosis Source: Ensembl
  9. negative regulation of circadian rhythm Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  12. rhythmic process Source: UniProtKB-KW
  13. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_268728. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SUV39H2
Synonyms:KMT1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17287. SUV39H2.

Subcellular locationi

  1. Nucleus By similarity
  2. Chromosomecentromere By similarity

  3. Note: Associates with centromeric constitutive heterochromatin.By similarity

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. chromosome, centromeric region Source: UniProtKB-SubCell
  3. nuclear heterochromatin Source: Ensembl
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868807.

Polymorphism and mutation databases

BioMutaiSUV39H2.
DMDMi25091325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Histone-lysine N-methyltransferase SUV39H2PRO_0000186059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei384 – 3841Phosphoserine2 Publications
Modified residuei388 – 3881Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H5I1.
PaxDbiQ9H5I1.
PRIDEiQ9H5I1.

PTM databases

PhosphoSiteiQ9H5I1.

Expressioni

Gene expression databases

BgeeiQ9H5I1.
CleanExiHS_SUV39H2.
ExpressionAtlasiQ9H5I1. baseline and differential.
GenevestigatoriQ9H5I1.

Organism-specific databases

HPAiHPA045901.
HPA057554.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL2Q8NEU84EBI-723127,EBI-741261
CDCA4Q9BXL82EBI-723127,EBI-1773949
HEL25V9HWG03EBI-723127,EBI-10183977
KCTD17Q8N5Z52EBI-723127,EBI-743960
KLHDC4Q8TBB52EBI-723127,EBI-8472352
MRFAP1Q9Y6052EBI-723127,EBI-995714
NCK1P163332EBI-723127,EBI-389883
PHF19Q5T6S32EBI-723127,EBI-2339674
PNMA1Q8ND904EBI-723127,EBI-302345
ZNF212Q9UDV62EBI-723127,EBI-1640204

Protein-protein interaction databases

BioGridi122838. 46 interactions.
IntActiQ9H5I1. 46 interactions.
MINTiMINT-3068157.
STRINGi9606.ENSP00000319208.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi125 – 14723Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi159 – 1613Combined sources
Turni196 – 1983Combined sources
Helixi202 – 2054Combined sources
Helixi244 – 2463Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi276 – 2805Combined sources
Beta strandi283 – 2864Combined sources
Helixi287 – 2959Combined sources
Helixi299 – 3035Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi313 – 3186Combined sources
Beta strandi320 – 3234Combined sources
Helixi325 – 3284Combined sources
Beta strandi336 – 34510Combined sources
Beta strandi353 – 3608Combined sources
Beta strandi367 – 3704Combined sources
Helixi372 – 3743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R3AX-ray2.00A112-410[»]
ProteinModelPortaliQ9H5I1.
SMRiQ9H5I1. Positions 48-96, 124-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H5I1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 10559ChromoPROSITE-ProRule annotationAdd
BLAST
Domaini189 – 24759Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini250 – 373124SETPROSITE-ProRule annotationAdd
BLAST
Domaini394 – 41017Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 2633S-adenosyl-L-methionine binding
Regioni330 – 3312S-adenosyl-L-methionine binding

Domaini

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).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 similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 chromo 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

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiQ9H5I1.
KOiK11419.
OMAiAWCVPCL.
PhylomeDBiQ9H5I1.
TreeFamiTF106452.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9H5I1-1) [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
MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE
60 70 80 90 100
YLCDYKVVKD MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY
110 120 130 140 150
LSQVKKGKAI TPKDNNKTLK PAIAEYIVKK AKQRIALQRW QDELNRRKNH
160 170 180 190 200
KGMIFVENTV DLEGPPSDFY YINEYKPAPG ISLVNEATFG CSCTDCFFQK
210 220 230 240 250
CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP NRIVQKGTQY
260 270 280 290 300
SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK
310 320 330 340 350
GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR
360 370 380 390 400
LPRIALFSTR TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC
410
GAVTCRGYLN

Note: No experimental confirmation available.

Length:410
Mass (Da):46,682
Last modified:November 15, 2002 - v2
Checksum:iED8BBF80AE838C69
GO
Isoform 1 (identifier: Q9H5I1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:350
Mass (Da):39,946
Checksum:iF435E9C5EBEA8BAD
GO
Isoform 2 (identifier: Q9H5I1-3) [UniParc]FASTAAdd to basket

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

Show »
Length:230
Mass (Da):26,350
Checksum:iBB9EF88E02C4D74A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti383 – 3831D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_036344

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060Missing in isoform 1. 3 PublicationsVSP_002209Add
BLAST
Alternative sequencei104 – 283180Missing in isoform 2. 1 PublicationVSP_002210Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS53493.1. [Q9H5I1-3]
CCDS53494.1. [Q9H5I1-1]
CCDS7104.1. [Q9H5I1-2]
RefSeqiNP_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_006717503.2. [Q9H5I1-2]
UniGeneiHs.554883.

Genome annotation databases

EnsembliENST00000313519; ENSP00000319208; ENSG00000152455. [Q9H5I1-2]
ENST00000354919; ENSP00000346997; ENSG00000152455. [Q9H5I1-1]
ENST00000378325; ENSP00000367576; ENSG00000152455. [Q9H5I1-3]
GeneIDi79723.
KEGGihsa:79723.
UCSCiuc001ing.3. human. [Q9H5I1-3]
uc001inh.3. human. [Q9H5I1-1]

Polymorphism and mutation databases

BioMutaiSUV39H2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS53493.1. [Q9H5I1-3]
CCDS53494.1. [Q9H5I1-1]
CCDS7104.1. [Q9H5I1-2]
RefSeqiNP_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_006717503.2. [Q9H5I1-2]
UniGeneiHs.554883.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R3AX-ray2.00A112-410[»]
ProteinModelPortaliQ9H5I1.
SMRiQ9H5I1. Positions 48-96, 124-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122838. 46 interactions.
IntActiQ9H5I1. 46 interactions.
MINTiMINT-3068157.
STRINGi9606.ENSP00000319208.

Chemistry

BindingDBiQ9H5I1.
ChEMBLiCHEMBL1795177.

PTM databases

PhosphoSiteiQ9H5I1.

Polymorphism and mutation databases

BioMutaiSUV39H2.
DMDMi25091325.

Proteomic databases

MaxQBiQ9H5I1.
PaxDbiQ9H5I1.
PRIDEiQ9H5I1.

Protocols and materials databases

DNASUi79723.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313519; ENSP00000319208; ENSG00000152455. [Q9H5I1-2]
ENST00000354919; ENSP00000346997; ENSG00000152455. [Q9H5I1-1]
ENST00000378325; ENSP00000367576; ENSG00000152455. [Q9H5I1-3]
GeneIDi79723.
KEGGihsa:79723.
UCSCiuc001ing.3. human. [Q9H5I1-3]
uc001inh.3. human. [Q9H5I1-1]

Organism-specific databases

CTDi79723.
GeneCardsiGC10P014922.
HGNCiHGNC:17287. SUV39H2.
HPAiHPA045901.
HPA057554.
MIMi606503. gene.
neXtProtiNX_Q9H5I1.
PharmGKBiPA134868807.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiQ9H5I1.
KOiK11419.
OMAiAWCVPCL.
PhylomeDBiQ9H5I1.
TreeFamiTF106452.

Enzyme and pathway databases

ReactomeiREACT_268728. PKMTs methylate histone lysines.

Miscellaneous databases

ChiTaRSiSUV39H2. human.
EvolutionaryTraceiQ9H5I1.
GeneWikiiSUV39H2.
GenomeRNAii79723.
NextBioi69082.
PROiQ9H5I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H5I1.
CleanExiHS_SUV39H2.
ExpressionAtlasiQ9H5I1. baseline and differential.
GenevestigatoriQ9H5I1.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR011381. Histone_H3-K9_MeTrfase.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 112-410 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-383.

Entry informationi

Entry nameiSUV92_HUMAN
AccessioniPrimary (citable) accession number: Q9H5I1
Secondary accession number(s): D3DRT4
, Q5JSS4, Q5JSS5, Q6I9Y3, Q8ND06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: April 29, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.