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Q9CZX0

- ELP3_MOUSE

UniProt

Q9CZX0 - ELP3_MOUSE

Protein

Elongator complex protein 3

Gene

Elp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. May also have a methyltransferase activity. Involved in cell migration.1 Publication

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Cofactori

    Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi99 – 991Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi109 – 1091Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi112 – 1121Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

    GO - Molecular functioni

    1. DNA binding Source: Ensembl
    2. histone acetyltransferase activity Source: UniProtKB-EC
    3. iron-sulfur cluster binding Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. phosphorylase kinase regulator activity Source: UniProtKB

    GO - Biological processi

    1. positive regulation of cell migration Source: UniProtKB
    2. regulation of protein kinase activity Source: GOC
    3. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. transcription elongation from RNA polymerase II promoter Source: Ensembl

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongator complex protein 3 (EC:2.3.1.48)
    Gene namesi
    Name:Elp3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1921445. Elp3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. DNA-directed RNA polymerase II, holoenzyme Source: Ensembl
    3. Elongator holoenzyme complex Source: UniProtKB
    4. nucleolus Source: Ensembl
    5. transcription elongation factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 547547Elongator complex protein 3PRO_0000283987Add
    BLAST

    Proteomic databases

    PaxDbiQ9CZX0.
    PRIDEiQ9CZX0.

    PTM databases

    PhosphoSiteiQ9CZX0.

    Expressioni

    Gene expression databases

    BgeeiQ9CZX0.
    CleanExiMM_ELP3.
    GenevestigatoriQ9CZX0.

    Interactioni

    Subunit structurei

    Component of the RNA polymerase II elongator complex (Elongator), which consists of IKBKAP/ELP1, STIP1/ELP2, ELP3, ELP4, ELP5 and ELP6. IKBKAP/ELP1, STIP1/ELP2 and ELP3 form the Elongator core complex. Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit. Interacts with IKBKAP/ELP1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi216566. 1 interaction.
    IntActiQ9CZX0. 1 interaction.
    MINTiMINT-4126289.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CZX0.
    SMRiQ9CZX0. Positions 490-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini396 – 547152N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ELP3 family.Curated
    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1243.
    GeneTreeiENSGT00390000013141.
    HOGENOMiHOG000227514.
    HOVERGENiHBG107845.
    InParanoidiQ9CZX0.
    KOiK07739.
    OMAiGYKVVSH.
    OrthoDBiEOG7V765W.
    PhylomeDBiQ9CZX0.
    TreeFamiTF105752.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    3.80.30.20. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR006638. Elp3/MiaB/NifB.
    IPR000182. GNAT_dom.
    IPR005910. Hist_AcTrfase_ELP3.
    IPR007197. rSAM.
    IPR023404. rSAM_horseshoe.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
    SMARTiSM00729. Elp3. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    TIGRFAMsiTIGR01211. ELP3. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9CZX0-1) [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

    MRQKRKGDLS PAELMMLTIG DVIKQLVEAH EQGKDVDLNK MKTKTAAKYG    50
    LASQPRLVDI IAAVPPHYRK ILIPKLKAKP VRTASGIAVV AVMCKPHRCP 100
    HISFTGNICI YCPGGPDSDF EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH 150
    RIEQLKQLGH SVDKVEFIVM GGTFMALPEE YRDYFIRSLH DALSGHTSNN 200
    IHEAIKYSER SFTKCVGITI ETRPDYCMKR HLSDMLTYGC TRLEIGVQSV 250
    YEDVARDTNR GHTVKAACES FHLAKDSGFK VVTHMMPDLP NVGLERDIEQ 300
    FIEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYRSY SPSDLIELVA 350
    RILALVPPWT RVYRVQRDIP MPLVSSGVEH GNLRELAFAR MKDLGIQCRD 400
    VRTREVGIQE IHHRVRPYQV ELVRRDYVAN GGWETFLSYE DPDQDILIGL 450
    LRLRKCSEET FRFELGGGVS IVRELHVYGS VVPVSSRDPT KFQHQGFGML 500
    LMEEAERIAR EEHGSGKMAV ISGVGTRNYY RKIGYRLQGP YMVKMLK 547
    Length:547
    Mass (Da):62,385
    Last modified:June 1, 2001 - v1
    Checksum:i9234BB4DDD145FF4
    GO
    Isoform 2 (identifier: Q9CZX0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-7: G → GAKYVGQGRKGGSGFSEITG

    Show »
    Length:566
    Mass (Da):64,266
    Checksum:i2FF7F992FFFB3EC6
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 71G → GAKYVGQGRKGGSGFSEITG in isoform 2. 1 PublicationVSP_024408

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012072 mRNA. Translation: BAB28009.1.
    AK088457 mRNA. Translation: BAC40364.1.
    BC026461 mRNA. Translation: AAH26461.1.
    BC057453 mRNA. Translation: AAH57453.1.
    CCDSiCCDS56965.1. [Q9CZX0-2]
    RefSeqiNP_001240741.1. NM_001253812.1. [Q9CZX0-2]
    NP_083087.1. NM_028811.3. [Q9CZX0-1]
    UniGeneiMm.29719.
    Mm.474894.

    Genome annotation databases

    EnsembliENSMUST00000022609; ENSMUSP00000022609; ENSMUSG00000022031. [Q9CZX0-2]
    GeneIDi74195.
    KEGGimmu:74195.
    UCSCiuc007ujk.2. mouse. [Q9CZX0-1]
    uc007ujl.2. mouse. [Q9CZX0-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012072 mRNA. Translation: BAB28009.1 .
    AK088457 mRNA. Translation: BAC40364.1 .
    BC026461 mRNA. Translation: AAH26461.1 .
    BC057453 mRNA. Translation: AAH57453.1 .
    CCDSi CCDS56965.1. [Q9CZX0-2 ]
    RefSeqi NP_001240741.1. NM_001253812.1. [Q9CZX0-2 ]
    NP_083087.1. NM_028811.3. [Q9CZX0-1 ]
    UniGenei Mm.29719.
    Mm.474894.

    3D structure databases

    ProteinModelPortali Q9CZX0.
    SMRi Q9CZX0. Positions 490-539.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 216566. 1 interaction.
    IntActi Q9CZX0. 1 interaction.
    MINTi MINT-4126289.

    PTM databases

    PhosphoSitei Q9CZX0.

    Proteomic databases

    PaxDbi Q9CZX0.
    PRIDEi Q9CZX0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022609 ; ENSMUSP00000022609 ; ENSMUSG00000022031 . [Q9CZX0-2 ]
    GeneIDi 74195.
    KEGGi mmu:74195.
    UCSCi uc007ujk.2. mouse. [Q9CZX0-1 ]
    uc007ujl.2. mouse. [Q9CZX0-2 ]

    Organism-specific databases

    CTDi 55140.
    MGIi MGI:1921445. Elp3.

    Phylogenomic databases

    eggNOGi COG1243.
    GeneTreei ENSGT00390000013141.
    HOGENOMi HOG000227514.
    HOVERGENi HBG107845.
    InParanoidi Q9CZX0.
    KOi K07739.
    OMAi GYKVVSH.
    OrthoDBi EOG7V765W.
    PhylomeDBi Q9CZX0.
    TreeFami TF105752.

    Enzyme and pathway databases

    Reactomei REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    NextBioi 340066.
    PROi Q9CZX0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CZX0.
    CleanExi MM_ELP3.
    Genevestigatori Q9CZX0.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    3.80.30.20. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR006638. Elp3/MiaB/NifB.
    IPR000182. GNAT_dom.
    IPR005910. Hist_AcTrfase_ELP3.
    IPR007197. rSAM.
    IPR023404. rSAM_horseshoe.
    [Graphical view ]
    Pfami PF00583. Acetyltransf_1. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    TIGRFAMsi TIGR01211. ELP3. 1 hit.
    PROSITEi PS51186. GNAT. 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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Thymus.
    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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of melanoma cells as subunits of Elongator."
      Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., Nguyen L., Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., Chariot A.
      J. Biol. Chem. 287:32535-32545(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiELP3_MOUSE
    AccessioniPrimary (citable) accession number: Q9CZX0
    Secondary accession number(s): Q8C2K2, Q8R369
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 108 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