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Q9CWR2

- SMYD3_MOUSE

UniProt

Q9CWR2 - SMYD3_MOUSE

Protein

Histone-lysine N-methyltransferase SMYD3

Gene

Smyd3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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 By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Histone methyltransferase activity strongly stimulated by HSPCA.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei124 – 1241S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei132 – 1321S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei239 – 2391S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei259 – 2591S-adenosyl-L-methioninePROSITE-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
    3. protein binding Source: MGI
    4. RNA polymerase II core binding Source: MGI
    5. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
    6. RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding Source: MGI

    GO - Biological processi

    1. cellular response to dexamethasone stimulus Source: MGI
    2. establishment of protein localization Source: MGI
    3. myotube cell development Source: MGI
    4. negative regulation of protein kinase activity Source: MGI
    5. nucleosome assembly Source: MGI
    6. positive regulation of peptidyl-serine phosphorylation Source: MGI
    7. positive regulation of transcription from RNA polymerase II promoter Source: MGI

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.1.1.43. 3474.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1916976. Smyd3.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Histone-lysine N-methyltransferase SMYD3PRO_0000218313Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9CWR2.
    PaxDbiQ9CWR2.
    PRIDEiQ9CWR2.

    PTM databases

    PhosphoSiteiQ9CWR2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CWR2.
    BgeeiQ9CWR2.
    CleanExiMM_SMYD3.
    GenevestigatoriQ9CWR2.

    Interactioni

    Subunit structurei

    Interacts with HSPCA. Interacts with HELZ. Interacts with POLR2A; the interaction may be indirect and may be mediated by HELZ By similarity.By similarity

    Protein-protein interaction databases

    BioGridi213640. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CWR2.
    SMRiQ9CWR2. Positions 4-428.
    ModBaseiSearch...
    MobiDBiSearch...

    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 bindingBy similarity
    Regioni205 – 2062S-adenosyl-L-methionine bindingBy similarity

    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.
    GeneTreeiENSGT00530000063077.
    HOGENOMiHOG000007850.
    HOVERGENiHBG105004.
    InParanoidiQ9CWR2.
    KOiK11426.
    OMAiKVEKFAT.
    OrthoDBiEOG74XS68.
    PhylomeDBiQ9CWR2.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9CWR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEALKVEKFT TANRGNGLRA VAPLRPGELL FRSDPLAYTV CKGSRGVVCD    50
    RCLLGKEKLM RCSQCRIAKY CSAKCQKKAW PDHRRECSCL KSCKPRYPPD 100
    SVRLLGRVIV KLMDEKPSES EKLYSFYDLE SNISKLTEDK KEGLRQLAMT 150
    FQHFMREEIQ DASQLPPSFD LFEAFAKVIC NSFTICNAEM QEVGVGLYPS 200
    MSLLNHSCDP NCSIVFNGPH LLLRAVREIE AGEELTICYL DMLMTSEERR 250
    KQLRDQYCFE CDCIRCQTQD KDADMLTGDE QIWKEVQESL KKIEELKAHW 300
    KWEQVLALCQ AIINSNSNRL PDINIYQLKV LDCAMDACIN LGMLEEALFY 350
    AMRTMEPYRI FFPGSHPVRG VQVMKVGKLQ LHQGMFPQAM KNLRLAFDIM 400
    KVTHGREHSL IEDLILLLEE CDANIRAS 428
    Length:428
    Mass (Da):49,126
    Last modified:June 1, 2001 - v1
    Checksum:i1EC765044E1FB0DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti318 – 3181N → D in AAH61485. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010447 mRNA. Translation: BAB26947.1.
    AK044168 mRNA. Translation: BAC31804.1.
    AK046829 mRNA. Translation: BAC32887.1.
    BC052431 mRNA. Translation: AAH52431.1.
    BC061485 mRNA. Translation: AAH61485.1.
    CCDSiCCDS15560.1.
    RefSeqiNP_081464.1. NM_027188.3.
    XP_006497043.1. XM_006496980.1.
    XP_006497044.1. XM_006496981.1.
    XP_006497045.1. XM_006496982.1.
    UniGeneiMm.222338.

    Genome annotation databases

    EnsembliENSMUST00000128302; ENSMUSP00000117410; ENSMUSG00000055067.
    GeneIDi69726.
    KEGGimmu:69726.
    UCSCiuc007dvj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010447 mRNA. Translation: BAB26947.1 .
    AK044168 mRNA. Translation: BAC31804.1 .
    AK046829 mRNA. Translation: BAC32887.1 .
    BC052431 mRNA. Translation: AAH52431.1 .
    BC061485 mRNA. Translation: AAH61485.1 .
    CCDSi CCDS15560.1.
    RefSeqi NP_081464.1. NM_027188.3.
    XP_006497043.1. XM_006496980.1.
    XP_006497044.1. XM_006496981.1.
    XP_006497045.1. XM_006496982.1.
    UniGenei Mm.222338.

    3D structure databases

    ProteinModelPortali Q9CWR2.
    SMRi Q9CWR2. Positions 4-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213640. 1 interaction.

    PTM databases

    PhosphoSitei Q9CWR2.

    Proteomic databases

    MaxQBi Q9CWR2.
    PaxDbi Q9CWR2.
    PRIDEi Q9CWR2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000128302 ; ENSMUSP00000117410 ; ENSMUSG00000055067 .
    GeneIDi 69726.
    KEGGi mmu:69726.
    UCSCi uc007dvj.1. mouse.

    Organism-specific databases

    CTDi 64754.
    MGIi MGI:1916976. Smyd3.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00530000063077.
    HOGENOMi HOG000007850.
    HOVERGENi HBG105004.
    InParanoidi Q9CWR2.
    KOi K11426.
    OMAi KVEKFAT.
    OrthoDBi EOG74XS68.
    PhylomeDBi Q9CWR2.
    TreeFami TF106487.

    Enzyme and pathway databases

    BRENDAi 2.1.1.43. 3474.

    Miscellaneous databases

    ChiTaRSi SMYD3. mouse.
    NextBioi 330194.
    PROi Q9CWR2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CWR2.
    Bgeei Q9CWR2.
    CleanExi MM_SMYD3.
    Genevestigatori Q9CWR2.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Brain cortex, Embryonic stem cell and Medulla oblongata.
    2. "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].
      Strain: C57BL/6 and FVB/N-3.
      Tissue: Brain and Mammary tumor.

    Entry informationi

    Entry nameiSMYD3_MOUSE
    AccessioniPrimary (citable) accession number: Q9CWR2
    Secondary accession number(s): Q6P7V6, Q8BG90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3