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Q9NRG4

- SMYD2_HUMAN

UniProt

Q9NRG4 - SMYD2_HUMAN

Protein

N-lysine methyltransferase SMYD2

Gene

SMYD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.6 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei240 – 2401Peptide substrate; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri52 – 9039MYND-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. p53 binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein-lysine N-methyltransferase activity Source: UniProtKB
    6. RNA polymerase II core binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of cell proliferation Source: UniProtKB
    2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    3. peptidyl-lysine dimethylation Source: UniProtKB
    4. peptidyl-lysine monomethylation Source: UniProtKB
    5. regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-lysine methyltransferase SMYD2 (EC:2.1.1.-)
    Alternative name(s):
    HSKM-B
    Histone methyltransferase SMYD2 (EC:2.1.1.43)
    Lysine N-methyltransferase 3C
    SET and MYND domain-containing protein 2
    Gene namesi
    Name:SMYD2
    Synonyms:KMT3C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:20982. SMYD2.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871E → K: Abolishes methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi189 – 1891E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi190 – 1901E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi207 – 2071H → A: Abolishes methyltransferase activity. 1 Publication
    Mutagenesisi240 – 2401Y → F: Abolishes methyltransferase activity. 2 Publications
    Mutagenesisi245 – 2451Y → F: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi252 – 2521D → R: Slightly reduces methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi253 – 2531R → Q: No effect on methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi306 – 3061R → E: No effect on methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi374 – 3741Y → A: Abolishes methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi429 – 4291E → K: Reduces methyltransferase activity on p53/TP53. 1 Publication
    Mutagenesisi431 – 4311E → K: Strongly reduces methyltransferase activity on p53/TP53. 1 Publication

    Organism-specific databases

    PharmGKBiPA134930268.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433N-lysine methyltransferase SMYD2PRO_0000218309Add
    BLAST

    Proteomic databases

    MaxQBiQ9NRG4.
    PaxDbiQ9NRG4.
    PRIDEiQ9NRG4.

    PTM databases

    PhosphoSiteiQ9NRG4.

    Expressioni

    Inductioni

    Expression is repressed by CEBPA.1 Publication

    Gene expression databases

    ArrayExpressiQ9NRG4.
    BgeeiQ9NRG4.
    CleanExiHS_SMYD2.
    GenevestigatoriQ9NRG4.

    Organism-specific databases

    HPAiHPA029023.

    Interactioni

    Subunit structurei

    Interacts with RNA polymerase II and HELZ. Interacts with SIN3A and HDAC1 By similarity. Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi121274. 12 interactions.
    DIPiDIP-50202N.
    STRINGi9606.ENSP00000355924.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Beta strandi17 – 259
    Beta strandi32 – 376
    Beta strandi39 – 435
    Helixi45 – 473
    Turni53 – 553
    Turni66 – 683
    Beta strandi72 – 754
    Helixi76 – 9621
    Helixi97 – 993
    Helixi104 – 11815
    Helixi124 – 1263
    Beta strandi127 – 1293
    Helixi131 – 1333
    Helixi138 – 1403
    Helixi143 – 16018
    Turni161 – 1633
    Helixi169 – 18214
    Beta strandi184 – 1874
    Beta strandi193 – 1986
    Helixi200 – 2034
    Beta strandi205 – 2073
    Beta strandi212 – 2187
    Beta strandi221 – 2288
    Beta strandi235 – 2384
    Helixi247 – 25812
    Helixi265 – 2695
    Helixi273 – 2764
    Helixi288 – 30821
    Turni309 – 3113
    Helixi314 – 32815
    Turni329 – 3313
    Helixi337 – 35216
    Helixi356 – 37318
    Helixi379 – 39416
    Helixi398 – 41518
    Helixi421 – 43010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RIBX-ray2.79A/B1-433[»]
    3S7BX-ray2.42A1-433[»]
    3S7DX-ray2.30A1-433[»]
    3S7FX-ray2.85A1-433[»]
    3S7JX-ray3.04A1-433[»]
    3TG4X-ray2.00A1-433[»]
    3TG5X-ray2.30A1-433[»]
    4O6FX-ray2.82A1-433[»]
    ProteinModelPortaliQ9NRG4.
    SMRiQ9NRG4. Positions 6-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 241235SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni17 – 193S-adenosyl-L-methionine binding
    Regioni183 – 1853Peptide substrate binding
    Regioni206 – 2072S-adenosyl-L-methionine binding
    Regioni258 – 2603S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri52 – 9039MYND-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOGENOMiHOG000007850.
    HOVERGENiHBG098536.
    InParanoidiQ9NRG4.
    KOiK11426.
    OMAiQPFQVGD.
    OrthoDBiEOG74XS68.
    PhylomeDBiQ9NRG4.
    TreeFamiTF106487.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR001214. SET_dom.
    IPR011990. TPR-like_helical.
    IPR002893. Znf_MYND.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view]
    SMARTiSM00317. SET. 1 hit.
    [Graphical view]
    PROSITEiPS50280. SET. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRG4-1) [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

    MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN    50
    HCEYCFTRKE GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW 100
    NPSETVRLTA RILAKQKIHP ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ 150
    SDIAALHHFY SKHLGFPDND SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP 200
    DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY IDLLYPTEDR 250
    NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN 300
    VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC 350
    LYMQDWEGAL QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA 400
    GEKALKKAIA IMEVAHGKDH PYISEIKQEI ESH 433
    Length:433
    Mass (Da):49,688
    Last modified:September 13, 2005 - v2
    Checksum:i3EEA5B8417870F5D
    GO
    Isoform 2 (identifier: Q9NRG4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         273-433: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:272
    Mass (Da):30,964
    Checksum:iF6A2B20624CED9C4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti165 – 1651G → E.3 Publications
    Corresponds to variant rs1134647 [ dbSNP | Ensembl ].
    VAR_023442
    Natural varianti430 – 4301I → M.
    Corresponds to variant rs11120301 [ dbSNP | Ensembl ].
    VAR_052991

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei273 – 433161Missing in isoform 2. 1 PublicationVSP_056005Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF226053 mRNA. Translation: AAF86953.1.
    AK313868 mRNA. Translation: BAG36596.1.
    AL929236 Genomic DNA. Translation: CAH70920.1.
    BC017080 mRNA. Translation: AAH17080.2.
    BC098276 mRNA. Translation: AAH98276.1.
    BC098133 mRNA. Translation: AAH98133.1.
    BC098305 mRNA. Translation: AAH98305.1.
    BC098335 mRNA. Translation: AAH98335.1.
    CCDSiCCDS31022.1.
    RefSeqiNP_064582.2. NM_020197.2.
    UniGeneiHs.66170.

    Genome annotation databases

    EnsembliENST00000366957; ENSP00000355924; ENSG00000143499.
    ENST00000415093; ENSP00000388682; ENSG00000143499.
    GeneIDi56950.
    KEGGihsa:56950.
    UCSCiuc021piw.1. human.

    Polymorphism databases

    DMDMi90185234.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF226053 mRNA. Translation: AAF86953.1 .
    AK313868 mRNA. Translation: BAG36596.1 .
    AL929236 Genomic DNA. Translation: CAH70920.1 .
    BC017080 mRNA. Translation: AAH17080.2 .
    BC098276 mRNA. Translation: AAH98276.1 .
    BC098133 mRNA. Translation: AAH98133.1 .
    BC098305 mRNA. Translation: AAH98305.1 .
    BC098335 mRNA. Translation: AAH98335.1 .
    CCDSi CCDS31022.1.
    RefSeqi NP_064582.2. NM_020197.2.
    UniGenei Hs.66170.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RIB X-ray 2.79 A/B 1-433 [» ]
    3S7B X-ray 2.42 A 1-433 [» ]
    3S7D X-ray 2.30 A 1-433 [» ]
    3S7F X-ray 2.85 A 1-433 [» ]
    3S7J X-ray 3.04 A 1-433 [» ]
    3TG4 X-ray 2.00 A 1-433 [» ]
    3TG5 X-ray 2.30 A 1-433 [» ]
    4O6F X-ray 2.82 A 1-433 [» ]
    ProteinModelPortali Q9NRG4.
    SMRi Q9NRG4. Positions 6-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121274. 12 interactions.
    DIPi DIP-50202N.
    STRINGi 9606.ENSP00000355924.

    Chemistry

    ChEMBLi CHEMBL2169716.
    GuidetoPHARMACOLOGYi 2714.

    PTM databases

    PhosphoSitei Q9NRG4.

    Polymorphism databases

    DMDMi 90185234.

    Proteomic databases

    MaxQBi Q9NRG4.
    PaxDbi Q9NRG4.
    PRIDEi Q9NRG4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366957 ; ENSP00000355924 ; ENSG00000143499 .
    ENST00000415093 ; ENSP00000388682 ; ENSG00000143499 .
    GeneIDi 56950.
    KEGGi hsa:56950.
    UCSCi uc021piw.1. human.

    Organism-specific databases

    CTDi 56950.
    GeneCardsi GC01P214454.
    HGNCi HGNC:20982. SMYD2.
    HPAi HPA029023.
    MIMi 610663. gene.
    neXtProti NX_Q9NRG4.
    PharmGKBi PA134930268.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOGENOMi HOG000007850.
    HOVERGENi HBG098536.
    InParanoidi Q9NRG4.
    KOi K11426.
    OMAi QPFQVGD.
    OrthoDBi EOG74XS68.
    PhylomeDBi Q9NRG4.
    TreeFami TF106487.

    Miscellaneous databases

    ChiTaRSi SMYD2. human.
    GenomeRNAii 56950.
    NextBioi 62549.
    PROi Q9NRG4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRG4.
    Bgeei Q9NRG4.
    CleanExi HS_SMYD2.
    Genevestigatori Q9NRG4.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR001214. SET_dom.
    IPR011990. TPR-like_helical.
    IPR002893. Znf_MYND.
    [Graphical view ]
    Pfami PF00856. SET. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view ]
    SMARTi SM00317. SET. 1 hit.
    [Graphical view ]
    PROSITEi PS50280. SET. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel gene expressed in human liver cancer tissue."
      Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-165.
      Tissue: Liver cancer.
    2. "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), VARIANT GLU-165.
      Tissue: Testis.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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), VARIANT GLU-165.
      Tissue: Colon.
    5. Cited for: FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF HIS-207.
    6. "C/EBPalphap30 plays transcriptional regulatory roles distinct from C/EBPalphap42."
      Wang C., Chen X., Wang Y., Gong J., Hu G.
      Cell Res. 17:374-383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. Cited for: FUNCTION.
    8. "The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase."
      Abu-Farha M., Lambert J.P., Al-Madhoun A.S., Elisma F., Skerjanc I.S., Figeys D.
      Mol. Cell. Proteomics 7:560-572(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EPB41L3; HSP90AA1 AND TP53.
    9. Cited for: FUNCTION, INTERACTION WITH RB, MUTAGENESIS OF TYR-240.
    10. "Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins."
      Xu S., Zhong C., Zhang T., Ding J.
      J. Mol. Cell Biol. 3:293-300(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS.
    11. "Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation."
      Wang L., Li L., Zhang H., Luo X., Dai J., Zhou S., Gu J., Zhu J., Atadja P., Lu C., Li E., Zhao K.
      J. Biol. Chem. 286:38725-38737(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH TP53/P53 PEPTIDE; S-ADENOSYL-L-METHIONINE AND ZINC IONS, FUNCTION IN P53/TP53 METHYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-187; GLU-189; GLU-190; TYR-245; ASP-252; ARG-253; ARG-306; TYR-374; GLU-429 AND GLU-431.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH P53/TP53 PEPTIDE; S-ADENOSYL-L-METHIONINE; SYNTHETIC INHIBITOR AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-240.

    Entry informationi

    Entry nameiSMYD2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRG4
    Secondary accession number(s): B2R9P9
    , I6L9H7, Q4V765, Q5VSH9, Q96AI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 110 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 1
      Human chromosome 1: 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