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Q9H9T3

- ELP3_HUMAN

UniProt

Q9H9T3 - ELP3_HUMAN

Protein

Elongator complex protein 3

Gene

ELP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      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.4 Publications

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

    GO - Biological processi

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

    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_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongator complex protein 3 (EC:2.3.1.48)
    Short name:
    hELP3
    Gene namesi
    Name:ELP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:20696. ELP3.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134992603.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 547547Elongator complex protein 3PRO_0000283986Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H9T3.
    PaxDbiQ9H9T3.
    PeptideAtlasiQ9H9T3.
    PRIDEiQ9H9T3.

    PTM databases

    PhosphoSiteiQ9H9T3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H9T3.
    BgeeiQ9H9T3.
    CleanExiHS_ELP3.
    GenevestigatoriQ9H9T3.

    Organism-specific databases

    HPAiHPA025812.

    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/ELP1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKBKAPO951638EBI-355217,EBI-347559

    Protein-protein interaction databases

    BioGridi120444. 13 interactions.
    IntActiQ9H9T3. 4 interactions.
    MINTiMINT-3062287.
    STRINGi9606.ENSP00000256398.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H9T3.
    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.
    HOGENOMiHOG000227514.
    HOVERGENiHBG107845.
    InParanoidiQ9H9T3.
    KOiK07739.
    OMAiGYKVVSH.
    OrthoDBiEOG7V765W.
    PhylomeDBiQ9H9T3.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H9T3-1) [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 DVIKQLIEAH EQGKDIDLNK VKTKTAAKYG    50
    LSAQPRLVDI IAAVPPQYRK VLMPKLKAKP IRTASGIAVV AVMCKPHRCP 100
    HISFTGNICV YCPGGPDSDF EYSTQSYTGY EPTSMRAIRA RYDPFLQTRH 150
    RIEQLKQLGH SVDKVEFIVM GGTFMALPEE YRDYFIRNLH DALSGHTSNN 200
    IYEAVKYSER SLTKCIGITI ETRPDYCMKR HLSDMLTYGC TRLEIGVQSV 250
    YEDVARDTNR GHTVKAVCES FHLAKDSGFK VVAHMMPDLP NVGLERDIEQ 300
    FTEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYKSY SPSDLVELVA 350
    RILALVPPWT RVYRVQRDIP MPLVSSGVEH GNLRELALAR MKDLGIQCRD 400
    VRTREVGIQE IHHKVRPYQV ELVRRDYVAN GGWETFLSYE DPDQDILIGL 450
    LRLRKCSEET FRFELGGGVS IVRELHVYGS VVPVSSRDPT KFQHQGFGML 500
    LMEEAERIAR EEHGSGKIAV ISGVGTRNYY RKIGYRLQGP YMVKMLK 547
    Length:547
    Mass (Da):62,259
    Last modified:April 17, 2007 - v2
    Checksum:i60898ADD3DBAD035
    GO
    Isoform 2 (identifier: Q9H9T3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.

    Show »
    Length:533
    Mass (Da):60,648
    Checksum:iDF8E71D8D401B90C
    GO
    Isoform 3 (identifier: Q9H9T3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: MRQKRKGDLSPA → MSTHQFYRKYMC
         13-131: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:428
    Mass (Da):49,405
    Checksum:iF11EEC322AAE8964
    GO
    Isoform 4 (identifier: Q9H9T3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-92: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:455
    Mass (Da):52,202
    Checksum:iC64BAB6FED06D973
    GO

    Sequence cautioni

    The sequence BAA91600.1 differs from that shown. Reason: Aberrant splicing.
    The sequence CAH10573.1 differs from that shown. Reason: Frameshift at position 279.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101S → G in BAA91600. (PubMed:14702039)Curated
    Sequence conflicti30 – 301H → Y in BAD96767. 1 PublicationCurated
    Sequence conflicti179 – 1791E → K in CAH10573. (PubMed:17974005)Curated
    Sequence conflicti265 – 2651K → M in BAB14138. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9292Missing in isoform 4. 1 PublicationVSP_055284Add
    BLAST
    Alternative sequencei1 – 1414Missing in isoform 2. 1 PublicationVSP_024406Add
    BLAST
    Alternative sequencei1 – 1212MRQKR…DLSPA → MSTHQFYRKYMC in isoform 3. 1 PublicationVSP_055285Add
    BLAST
    Alternative sequencei13 – 131119Missing in isoform 3. 1 PublicationVSP_055286Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001284 mRNA. Translation: BAA91600.1. Sequence problems.
    AK022626 mRNA. Translation: BAB14138.1.
    AK293424 mRNA. Translation: BAG56930.1.
    AK295574 mRNA. Translation: BAG58473.1.
    AK315985 mRNA. Translation: BAH14356.1.
    AL834273 mRNA. Translation: CAD38948.1.
    BX648011 mRNA. Translation: CAH10573.1. Frameshift.
    AC019031 Genomic DNA. No translation available.
    AC021678 Genomic DNA. No translation available.
    BC001240 mRNA. Translation: AAH01240.1.
    AK223047 mRNA. Translation: BAD96767.1.
    CCDSiCCDS6065.1. [Q9H9T3-1]
    CCDS64860.1. [Q9H9T3-5]
    CCDS64861.1. [Q9H9T3-4]
    RefSeqiNP_001271151.1. NM_001284222.1. [Q9H9T3-2]
    NP_001271153.1. NM_001284224.1.
    NP_001271154.1. NM_001284225.1.
    NP_001271155.1. NM_001284226.1.
    NP_060561.3. NM_018091.5. [Q9H9T3-1]
    XP_006716417.1. XM_006716354.1.
    UniGeneiHs.491336.

    Genome annotation databases

    EnsembliENST00000256398; ENSP00000256398; ENSG00000134014. [Q9H9T3-1]
    ENST00000380353; ENSP00000369711; ENSG00000134014. [Q9H9T3-5]
    ENST00000521015; ENSP00000428449; ENSG00000134014. [Q9H9T3-2]
    ENST00000537665; ENSP00000445558; ENSG00000134014. [Q9H9T3-4]
    GeneIDi55140.
    KEGGihsa:55140.
    UCSCiuc003xgn.4. human. [Q9H9T3-1]

    Polymorphism databases

    DMDMi145558902.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001284 mRNA. Translation: BAA91600.1 . Sequence problems.
    AK022626 mRNA. Translation: BAB14138.1 .
    AK293424 mRNA. Translation: BAG56930.1 .
    AK295574 mRNA. Translation: BAG58473.1 .
    AK315985 mRNA. Translation: BAH14356.1 .
    AL834273 mRNA. Translation: CAD38948.1 .
    BX648011 mRNA. Translation: CAH10573.1 . Frameshift.
    AC019031 Genomic DNA. No translation available.
    AC021678 Genomic DNA. No translation available.
    BC001240 mRNA. Translation: AAH01240.1 .
    AK223047 mRNA. Translation: BAD96767.1 .
    CCDSi CCDS6065.1. [Q9H9T3-1 ]
    CCDS64860.1. [Q9H9T3-5 ]
    CCDS64861.1. [Q9H9T3-4 ]
    RefSeqi NP_001271151.1. NM_001284222.1. [Q9H9T3-2 ]
    NP_001271153.1. NM_001284224.1.
    NP_001271154.1. NM_001284225.1.
    NP_001271155.1. NM_001284226.1.
    NP_060561.3. NM_018091.5. [Q9H9T3-1 ]
    XP_006716417.1. XM_006716354.1.
    UniGenei Hs.491336.

    3D structure databases

    ProteinModelPortali Q9H9T3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120444. 13 interactions.
    IntActi Q9H9T3. 4 interactions.
    MINTi MINT-3062287.
    STRINGi 9606.ENSP00000256398.

    PTM databases

    PhosphoSitei Q9H9T3.

    Polymorphism databases

    DMDMi 145558902.

    Proteomic databases

    MaxQBi Q9H9T3.
    PaxDbi Q9H9T3.
    PeptideAtlasi Q9H9T3.
    PRIDEi Q9H9T3.

    Protocols and materials databases

    DNASUi 55140.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256398 ; ENSP00000256398 ; ENSG00000134014 . [Q9H9T3-1 ]
    ENST00000380353 ; ENSP00000369711 ; ENSG00000134014 . [Q9H9T3-5 ]
    ENST00000521015 ; ENSP00000428449 ; ENSG00000134014 . [Q9H9T3-2 ]
    ENST00000537665 ; ENSP00000445558 ; ENSG00000134014 . [Q9H9T3-4 ]
    GeneIDi 55140.
    KEGGi hsa:55140.
    UCSCi uc003xgn.4. human. [Q9H9T3-1 ]

    Organism-specific databases

    CTDi 55140.
    GeneCardsi GC08P028006.
    HGNCi HGNC:20696. ELP3.
    HPAi HPA025812.
    MIMi 612722. gene.
    neXtProti NX_Q9H9T3.
    PharmGKBi PA134992603.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1243.
    HOGENOMi HOG000227514.
    HOVERGENi HBG107845.
    InParanoidi Q9H9T3.
    KOi K07739.
    OMAi GYKVVSH.
    OrthoDBi EOG7V765W.
    PhylomeDBi Q9H9T3.
    TreeFami TF105752.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    GeneWikii ELP3.
    GenomeRNAii 55140.
    NextBioi 35471088.
    PROi Q9H9T3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H9T3.
    Bgeei Q9H9T3.
    CleanExi HS_ELP3.
    Genevestigatori Q9H9T3.

    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. "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; 3 AND 4).
      Tissue: Amygdala and Hippocampus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Amygdala and Endometrium.
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(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] (ISOFORM 1).
      Tissue: Cervix.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-547 (ISOFORM 1).
      Tissue: Thyroid.
    6. Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Human Elongator facilitates RNA polymerase II transcription through chromatin."
      Kim J.H., Lane W.S., Reinberg D.
      Proc. Natl. Acad. Sci. U.S.A. 99:1241-1246(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR CORE COMPLEX, INTERACTION WITH IKBKAP, SUBCELLULAR LOCATION, FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast."
      Li F., Lu J., Han Q., Zhang G., Huang B.
      Mol. Genet. Genomics 273:264-272(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Transcription impairment and cell migration defects in elongator-depleted cells: implication for familial dysautonomia."
      Close P., Hawkes N., Cornez I., Creppe C., Lambert C.A., Rogister B., Siebenlist U., Merville M.P., Slaugenhaupt S.A., Bours V., Svejstrup J.Q., Chariot A.
      Mol. Cell 22:521-531(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RNA POLYMERASE II ELONGATOR COMPLEX.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, SUBCELLULAR LOCATION.
    14. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiELP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9T3
    Secondary accession number(s): B4DE19
    , B4DIG1, E2QRI5, Q53G84, Q6AWB0, Q9BVF7, Q9NVZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 117 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3