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Q9H7B4

- SMYD3_HUMAN

UniProt

Q9H7B4 - SMYD3_HUMAN

Protein

Histone-lysine N-methyltransferase SMYD3

Gene

SMYD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 4 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.2 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Histone methyltransferase activity strongly stimulated by HSPCA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei124 – 1241S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei132 – 1321S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei181 – 1811S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei239 – 2391S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation
    Binding sitei259 – 2591S-adenosyl-L-methionine1 PublicationPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri49 – 8739MYND-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SMYD3 (EC:2.1.1.43)
    Alternative name(s):
    SET and MYND domain-containing protein 3
    Zinc finger MYND domain-containing protein 1
    Gene namesi
    Name:SMYD3
    Synonyms:ZMYND1, ZNFN3A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:15513. SMYD3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37972.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histone-lysine N-methyltransferase SMYD3PRO_0000218312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9H7B4.
    PaxDbiQ9H7B4.
    PRIDEiQ9H7B4.

    PTM databases

    PhosphoSiteiQ9H7B4.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscles and testis. Overexpressed in a majority of colorectal and hepatocellular carcinomas.1 Publication

    Gene expression databases

    ArrayExpressiQ9H7B4.
    BgeeiQ9H7B4.
    CleanExiHS_SMYD3.
    GenevestigatoriQ9H7B4.

    Organism-specific databases

    HPAiCAB012229.

    Interactioni

    Subunit structurei

    Interacts with HSPCA. Interacts with HELZ. Interacts with POLR2A; the interaction may be indirect and may be mediated by HELZ.2 Publications

    Protein-protein interaction databases

    BioGridi122268. 22 interactions.
    IntActiQ9H7B4. 12 interactions.
    MINTiMINT-1033215.
    STRINGi9606.ENSP00000373637.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Beta strandi12 – 2211
    Beta strandi29 – 335
    Beta strandi36 – 405
    Helixi42 – 443
    Turni50 – 523
    Turni63 – 653
    Beta strandi69 – 724
    Helixi73 – 786
    Helixi80 – 9213
    Turni93 – 953
    Helixi100 – 11415
    Helixi119 – 1213
    Beta strandi122 – 1243
    Helixi126 – 1283
    Helixi133 – 1353
    Helixi138 – 15417
    Turni155 – 1584
    Helixi162 – 1643
    Helixi171 – 18111
    Beta strandi183 – 1864
    Beta strandi192 – 1976
    Helixi201 – 2033
    Beta strandi211 – 2177
    Beta strandi220 – 2256
    Beta strandi234 – 2374
    Helixi246 – 25712
    Helixi264 – 2685
    Turni269 – 2713
    Helixi272 – 2754
    Helixi280 – 29819
    Helixi302 – 31312
    Turni317 – 3193
    Helixi325 – 34117
    Helixi344 – 36118
    Helixi367 – 38216
    Helixi386 – 40318
    Turni404 – 4074
    Helixi409 – 42618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MEKX-ray2.10A1-428[»]
    3OXFX-ray2.82A/B1-428[»]
    3OXGX-ray3.41A1-428[»]
    3OXLX-ray3.60A1-428[»]
    3PDNX-ray1.70A1-428[»]
    3QWPX-ray1.53A1-428[»]
    3RU0X-ray1.85A/B2-428[»]
    ProteinModelPortaliQ9H7B4.
    SMRiQ9H7B4. Positions 4-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H7B4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 240237SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 163S-adenosyl-L-methionine binding
    Regioni205 – 2062S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family.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 fingeri49 – 8739MYND-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOGENOMiHOG000007850.
    HOVERGENiHBG105004.
    InParanoidiQ9H7B4.
    KOiK11426.
    OMAiKVEKFAT.
    OrthoDBiEOG74XS68.
    PhylomeDBiQ9H7B4.
    TreeFamiTF106487.

    Family and domain databases

    InterProiIPR025805. Hist-Lys_N-MeTrfase_Smyd3.
    IPR001214. SET_dom.
    IPR002893. Znf_MYND.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view]
    SMARTiSM00317. SET. 1 hit.
    [Graphical view]
    PROSITEiPS51574. SAM_MT43_2. 1 hit.
    PS50280. SET. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H7B4-1) [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

    MEPLKVEKFA TAKRGNGLRA VTPLRPGELL FRSDPLAYTV CKGSRGVVCD    50
    RCLLGKEKLM RCSQCRVAKY CSAKCQKKAW PDHKRECKCL KSCKPRYPPD 100
    SVRLLGRVVF KLMDGAPSES EKLYSFYDLE SNINKLTEDK KEGLRQLVMT 150
    FQHFMREEIQ DASQLPPAFD LFEAFAKVIC NSFTICNAEM QEVGVGLYPS 200
    ISLLNHSCDP NCSIVFNGPH LLLRAVRDIE VGEELTICYL DMLMTSEERR 250
    KQLRDQYCFE CDCFRCQTQD KDADMLTGDE QVWKEVQESL KKIEELKAHW 300
    KWEQVLAMCQ AIISSNSERL PDINIYQLKV LDCAMDACIN LGLLEEALFY 350
    GTRTMEPYRI FFPGSHPVRG VQVMKVGKLQ LHQGMFPQAM KNLRLAFDIM 400
    RVTHGREHSL IEDLILLLEE CDANIRAS 428
    Length:428
    Mass (Da):49,097
    Last modified:November 4, 2008 - v4
    Checksum:i2079357016F200AC
    GO
    Isoform 2 (identifier: Q9H7B4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-170: Missing.
         171-176: LFEAFA → MEEEEE

    Note: No experimental confirmation available.

    Show »
    Length:258
    Mass (Da):29,759
    Checksum:iC9A509C511BA28C4
    GO
    Isoform 3 (identifier: Q9H7B4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.

    Show »
    Length:369
    Mass (Da):42,625
    Checksum:iB5A3DC1D5C8AA743
    GO

    Sequence cautioni

    The sequence CAI14744.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI16628.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131K → N in BAB86333. (PubMed:15235609)Curated
    Sequence conflicti13 – 131K → N in AAH31010. (PubMed:15489334)Curated
    Sequence conflicti140 – 1401K → R in AAH31010. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 170170Missing in isoform 2. 1 PublicationVSP_012416Add
    BLAST
    Alternative sequencei1 – 5959Missing in isoform 3. 1 PublicationVSP_035601Add
    BLAST
    Alternative sequencei171 – 1766LFEAFA → MEEEEE in isoform 2. 1 PublicationVSP_012417

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB057595 mRNA. Translation: BAB86333.1.
    AY186742 mRNA. Translation: AAO31695.1.
    AK024733 mRNA. Translation: BAB14981.1.
    AK289605 mRNA. Translation: BAF82294.1.
    AL512412, AL445468 Genomic DNA. Translation: CAI14744.1. Different initiation.
    AL512412, AL445468 Genomic DNA. Translation: CAI14745.1.
    AL512412
    , AL356583, AL358859, AL445468 Genomic DNA. Translation: CAI14746.1.
    AL358859
    , AL356583, AL445468, AL512412 Genomic DNA. Translation: CAI15419.1.
    AL356583
    , AL358859, AL445468, AL512412 Genomic DNA. Translation: CAI16395.1.
    AL445468, AL512412 Genomic DNA. Translation: CAI16628.1. Different initiation.
    AL445468, AL512412 Genomic DNA. Translation: CAI16629.1.
    AL445468
    , AL356583, AL358859, AL512412 Genomic DNA. Translation: CAI16630.1.
    CH471148 Genomic DNA. Translation: EAW77142.1.
    BC017079 mRNA. Translation: AAH17079.2.
    BC031010 mRNA. Translation: AAH31010.1.
    CCDSiCCDS31083.1. [Q9H7B4-3]
    CCDS53486.1. [Q9H7B4-1]
    RefSeqiNP_001161212.1. NM_001167740.1. [Q9H7B4-1]
    NP_073580.1. NM_022743.2. [Q9H7B4-3]
    XP_005273286.1. XM_005273229.1. [Q9H7B4-2]
    UniGeneiHs.567571.

    Genome annotation databases

    EnsembliENST00000490107; ENSP00000419184; ENSG00000185420. [Q9H7B4-3]
    GeneIDi64754.
    KEGGihsa:64754.
    UCSCiuc001ibj.3. human. [Q9H7B4-1]

    Polymorphism databases

    DMDMi212276523.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB057595 mRNA. Translation: BAB86333.1 .
    AY186742 mRNA. Translation: AAO31695.1 .
    AK024733 mRNA. Translation: BAB14981.1 .
    AK289605 mRNA. Translation: BAF82294.1 .
    AL512412 , AL445468 Genomic DNA. Translation: CAI14744.1 . Different initiation.
    AL512412 , AL445468 Genomic DNA. Translation: CAI14745.1 .
    AL512412
    , AL356583 , AL358859 , AL445468 Genomic DNA. Translation: CAI14746.1 .
    AL358859
    , AL356583 , AL445468 , AL512412 Genomic DNA. Translation: CAI15419.1 .
    AL356583
    , AL358859 , AL445468 , AL512412 Genomic DNA. Translation: CAI16395.1 .
    AL445468 , AL512412 Genomic DNA. Translation: CAI16628.1 . Different initiation.
    AL445468 , AL512412 Genomic DNA. Translation: CAI16629.1 .
    AL445468
    , AL356583 , AL358859 , AL512412 Genomic DNA. Translation: CAI16630.1 .
    CH471148 Genomic DNA. Translation: EAW77142.1 .
    BC017079 mRNA. Translation: AAH17079.2 .
    BC031010 mRNA. Translation: AAH31010.1 .
    CCDSi CCDS31083.1. [Q9H7B4-3 ]
    CCDS53486.1. [Q9H7B4-1 ]
    RefSeqi NP_001161212.1. NM_001167740.1. [Q9H7B4-1 ]
    NP_073580.1. NM_022743.2. [Q9H7B4-3 ]
    XP_005273286.1. XM_005273229.1. [Q9H7B4-2 ]
    UniGenei Hs.567571.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MEK X-ray 2.10 A 1-428 [» ]
    3OXF X-ray 2.82 A/B 1-428 [» ]
    3OXG X-ray 3.41 A 1-428 [» ]
    3OXL X-ray 3.60 A 1-428 [» ]
    3PDN X-ray 1.70 A 1-428 [» ]
    3QWP X-ray 1.53 A 1-428 [» ]
    3RU0 X-ray 1.85 A/B 2-428 [» ]
    ProteinModelPortali Q9H7B4.
    SMRi Q9H7B4. Positions 4-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122268. 22 interactions.
    IntActi Q9H7B4. 12 interactions.
    MINTi MINT-1033215.
    STRINGi 9606.ENSP00000373637.

    Chemistry

    ChEMBLi CHEMBL2321643.

    PTM databases

    PhosphoSitei Q9H7B4.

    Polymorphism databases

    DMDMi 212276523.

    Proteomic databases

    MaxQBi Q9H7B4.
    PaxDbi Q9H7B4.
    PRIDEi Q9H7B4.

    Protocols and materials databases

    DNASUi 64754.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000490107 ; ENSP00000419184 ; ENSG00000185420 . [Q9H7B4-3 ]
    GeneIDi 64754.
    KEGGi hsa:64754.
    UCSCi uc001ibj.3. human. [Q9H7B4-1 ]

    Organism-specific databases

    CTDi 64754.
    GeneCardsi GC01M245912.
    HGNCi HGNC:15513. SMYD3.
    HPAi CAB012229.
    MIMi 608783. gene.
    neXtProti NX_Q9H7B4.
    PharmGKBi PA37972.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOGENOMi HOG000007850.
    HOVERGENi HBG105004.
    InParanoidi Q9H7B4.
    KOi K11426.
    OMAi KVEKFAT.
    OrthoDBi EOG74XS68.
    PhylomeDBi Q9H7B4.
    TreeFami TF106487.

    Miscellaneous databases

    ChiTaRSi SMYD3. human.
    EvolutionaryTracei Q9H7B4.
    GeneWikii SMYD3.
    GenomeRNAii 64754.
    NextBioi 66717.
    PROi Q9H7B4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H7B4.
    Bgeei Q9H7B4.
    CleanExi HS_SMYD3.
    Genevestigatori Q9H7B4.

    Family and domain databases

    InterProi IPR025805. Hist-Lys_N-MeTrfase_Smyd3.
    IPR001214. SET_dom.
    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 PS51574. SAM_MT43_2. 1 hit.
    PS50280. SET. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells."
      Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., Nakamura Y.
      Nat. Cell Biol. 6:731-740(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HSPCA; HELZ AND POLR2A, DNA-BINDING.
    2. Sha J.H., Zhou Z.M., Xu M.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. "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] (ISOFORMS 1 AND 3).
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Colon and Melanoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: CATALYTIC ACTIVITY, FUNCTION.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of human histone-lysine n-methyltransferase SMYD3 in complex with S-adenosyl-L-methionine."
      Structural genomics consortium (SGC)
      Submitted (APR-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS.

    Entry informationi

    Entry nameiSMYD3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H7B4
    Secondary accession number(s): A8K0P0
    , B1AN38, Q86TL8, Q8N5Z6, Q96AI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 119 of the entry and version 4 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3