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Q9H5I1

- SUV92_HUMAN

UniProt

Q9H5I1 - SUV92_HUMAN

Protein

Histone-lysine N-methyltransferase SUV39H2

Gene

SUV39H2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (15 Nov 2002)
      Previous versions | rss
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    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-methionine1 PublicationPROSITE-ProRule annotation
    Metal bindingi333 – 3331Zinc 4
    Metal bindingi398 – 3981Zinc 4
    Binding sitei399 – 3991S-adenosyl-L-methionine; via amide nitrogen1 PublicationPROSITE-ProRule annotation
    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. protein binding Source: IntAct
    4. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. chromatin assembly or disassembly Source: UniProtKB
    3. chromatin remodeling Source: UniProtKB
    4. histone H3-K9 dimethylation Source: UniProtKB
    5. histone H3-K9 trimethylation Source: UniProtKB
    6. male meiosis Source: Ensembl
    7. negative regulation of circadian rhythm Source: UniProtKB
    8. negative regulation of transcription, DNA-templated Source: UniProtKB
    9. rhythmic process Source: UniProtKB-KW
    10. transcription, DNA-templated Source: UniProtKB-KW

    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

    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: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17287. SUV39H2.

    Subcellular locationi

    Nucleus By similarity. Chromosomecentromere By similarity
    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

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134868807.

    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

    ArrayExpressiQ9H5I1.
    BgeeiQ9H5I1.
    CleanExiHS_SUV39H2.
    GenevestigatoriQ9H5I1.

    Organism-specific databases

    HPAiHPA045901.

    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
    CDCA4Q9BXL82EBI-723127,EBI-1773949
    KCTD17Q8N5Z52EBI-723127,EBI-743960
    KLHDC4Q8TBB52EBI-723127,EBI-8472352
    MRFAP1Q9Y6052EBI-723127,EBI-995714
    NCK1P163332EBI-723127,EBI-389883
    PHF19Q5T6S32EBI-723127,EBI-2339674
    ZNF212Q9UDV62EBI-723127,EBI-1640204

    Protein-protein interaction databases

    BioGridi122838. 39 interactions.
    IntActiQ9H5I1. 44 interactions.
    MINTiMINT-3068157.
    STRINGi9606.ENSP00000319208.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000231244.
    HOVERGENiHBG055621.
    InParanoidiQ9H5I1.
    KOiK11419.
    OMAiAWCVPCL.
    PhylomeDBiQ9H5I1.
    TreeFamiTF106452.

    Family and domain databases

    InterProiIPR023780. 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]
    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. Align

    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

    MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE    50
    YLCDYKVVKD MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY 100
    LSQVKKGKAI TPKDNNKTLK PAIAEYIVKK AKQRIALQRW QDELNRRKNH 150
    KGMIFVENTV DLEGPPSDFY YINEYKPAPG ISLVNEATFG CSCTDCFFQK 200
    CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP NRIVQKGTQY 250
    SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK 300
    GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR 350
    LPRIALFSTR TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC 400
    GAVTCRGYLN 410

    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:
    EMBL
    GenBank
    DDBJ
    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_006717503.1. [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 databases

    DMDMi25091325.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS53493.1. [Q9H5I1-3 ]
    CCDS53494.1. [Q9H5I1-1 ]
    CCDS7104.1. [Q9H5I1-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.554883.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2R3A X-ray 2.00 A 112-410 [» ]
    ProteinModelPortali Q9H5I1.
    SMRi Q9H5I1. Positions 48-96, 124-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122838. 39 interactions.
    IntActi Q9H5I1. 44 interactions.
    MINTi MINT-3068157.
    STRINGi 9606.ENSP00000319208.

    Chemistry

    BindingDBi Q9H5I1.
    ChEMBLi CHEMBL1795177.

    PTM databases

    PhosphoSitei Q9H5I1.

    Polymorphism databases

    DMDMi 25091325.

    Proteomic databases

    MaxQBi Q9H5I1.
    PaxDbi Q9H5I1.
    PRIDEi Q9H5I1.

    Protocols and materials databases

    DNASUi 79723.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313519 ; ENSP00000319208 ; ENSG00000152455 . [Q9H5I1-2 ]
    ENST00000354919 ; ENSP00000346997 ; ENSG00000152455 . [Q9H5I1-1 ]
    ENST00000378325 ; ENSP00000367576 ; ENSG00000152455 . [Q9H5I1-3 ]
    GeneIDi 79723.
    KEGGi hsa:79723.
    UCSCi uc001ing.3. human. [Q9H5I1-3 ]
    uc001inh.3. human. [Q9H5I1-1 ]

    Organism-specific databases

    CTDi 79723.
    GeneCardsi GC10P014922.
    HGNCi HGNC:17287. SUV39H2.
    HPAi HPA045901.
    MIMi 606503. gene.
    neXtProti NX_Q9H5I1.
    PharmGKBi PA134868807.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOGENOMi HOG000231244.
    HOVERGENi HBG055621.
    InParanoidi Q9H5I1.
    KOi K11419.
    OMAi AWCVPCL.
    PhylomeDBi Q9H5I1.
    TreeFami TF106452.

    Miscellaneous databases

    ChiTaRSi SUV39H2. human.
    EvolutionaryTracei Q9H5I1.
    GeneWikii SUV39H2.
    GenomeRNAii 79723.
    NextBioi 69082.
    PROi Q9H5I1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H5I1.
    Bgeei Q9H5I1.
    CleanExi HS_SUV39H2.
    Genevestigatori Q9H5I1.

    Family and domain databases

    InterProi IPR023780. 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 ]
    Pfami PF00385. Chromo. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009343. SUV39_SET. 1 hit.
    SMARTi SM00298. CHROMO. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 1 hit.
    PROSITEi PS00598. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 131 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