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O95619

- YETS4_HUMAN

UniProt

O95619 - YETS4_HUMAN

Protein

YEATS domain-containing protein 4

Gene

YEATS4

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 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. protein binding Source: IntAct
    3. protein C-terminus binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. structural constituent of cytoskeleton Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H2A acetylation Source: UniProtKB
    3. histone H4 acetylation Source: UniProtKB
    4. mitotic nuclear division Source: UniProtKB
    5. positive regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of growth Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Growth regulation, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    YEATS domain-containing protein 4
    Alternative name(s):
    Glioma-amplified sequence 41
    Short name:
    Gas41
    NuMA-binding protein 1
    Short name:
    NuBI-1
    Short name:
    NuBI1
    Gene namesi
    Name:YEATS4
    Synonyms:GAS41
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:24859. YEATS4.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. NuA4 histone acetyltransferase complex Source: UniProtKB
    2. nuclear matrix Source: UniProtKB
    3. nucleoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134992686.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 227227YEATS domain-containing protein 4PRO_0000066204Add
    BLAST

    Proteomic databases

    MaxQBiO95619.
    PaxDbiO95619.
    PeptideAtlasiO95619.
    PRIDEiO95619.

    PTM databases

    PhosphoSiteiO95619.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO95619.
    BgeeiO95619.
    CleanExiHS_YEATS4.
    GenevestigatoriO95619.

    Interactioni

    Subunit structurei

    Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. YEATS4 interacts with MLLT10/AF10. YEATS4 may also interact with the SWI/SNF component SMARCB1/BAF47, TACC1 and TACC2, and the nuclear matrix protein NUMA1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TACC1O754106EBI-399269,EBI-624237

    Protein-protein interaction databases

    BioGridi113761. 28 interactions.
    IntActiO95619. 10 interactions.
    MINTiMINT-3003084.
    STRINGi9606.ENSP00000247843.

    Structurei

    3D structure databases

    ProteinModelPortaliO95619.
    SMRiO95619. Positions 13-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 126105YEATSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni163 – 22765Interaction with MLLT10Add
    BLAST
    Regioni168 – 22760Interaction with TACC1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili178 – 22649Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 YEATS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5033.
    HOGENOMiHOG000190181.
    HOVERGENiHBG061271.
    InParanoidiO95619.
    KOiK11341.
    OrthoDBiEOG73FQNN.
    PhylomeDBiO95619.

    Family and domain databases

    InterProiIPR005033. YEATS.
    [Graphical view]
    PANTHERiPTHR23195. PTHR23195. 1 hit.
    PfamiPF03366. YEATS. 1 hit.
    [Graphical view]
    PROSITEiPS51037. YEATS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95619-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKRMAEFGP DSGGRVKGVT IVKPIVYGNV ARYFGKKREE DGHTHQWTVY    50
    VKPYRNEDMS AYVKKIQFKL HESYGNPLRV VTKPPYEITE TGWGEFEIII 100
    KIFFIDPNER PVTLYHLLKL FQSDTNAMLG KKTVVSEFYD EMIFQDPTAM 150
    MQQLLTTSRQ LTLGAYKHET EFAELEVKTR EKLEAAKKKT SFEIAELKER 200
    LKASRETINC LKNEIRKLEE DDQAKDI 227
    Length:227
    Mass (Da):26,499
    Last modified:May 1, 1999 - v1
    Checksum:i34C4692B227A7B85
    GO

    Sequence cautioni

    The sequence CAC01935.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591R → C in CAC01935. (PubMed:10913114)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U61384 mRNA. Translation: AAD12188.1.
    AJ245746 mRNA. Translation: CAC01935.1. Different initiation.
    AK001413 mRNA. Translation: BAA91678.1.
    BC000994 mRNA. Translation: AAH00994.1.
    CCDSiCCDS8990.1.
    RefSeqiNP_006521.1. NM_006530.2.
    UniGeneiHs.4029.

    Genome annotation databases

    EnsembliENST00000247843; ENSP00000247843; ENSG00000127337.
    GeneIDi8089.
    KEGGihsa:8089.
    UCSCiuc001sux.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U61384 mRNA. Translation: AAD12188.1 .
    AJ245746 mRNA. Translation: CAC01935.1 . Different initiation.
    AK001413 mRNA. Translation: BAA91678.1 .
    BC000994 mRNA. Translation: AAH00994.1 .
    CCDSi CCDS8990.1.
    RefSeqi NP_006521.1. NM_006530.2.
    UniGenei Hs.4029.

    3D structure databases

    ProteinModelPortali O95619.
    SMRi O95619. Positions 13-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113761. 28 interactions.
    IntActi O95619. 10 interactions.
    MINTi MINT-3003084.
    STRINGi 9606.ENSP00000247843.

    PTM databases

    PhosphoSitei O95619.

    Proteomic databases

    MaxQBi O95619.
    PaxDbi O95619.
    PeptideAtlasi O95619.
    PRIDEi O95619.

    Protocols and materials databases

    DNASUi 8089.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247843 ; ENSP00000247843 ; ENSG00000127337 .
    GeneIDi 8089.
    KEGGi hsa:8089.
    UCSCi uc001sux.3. human.

    Organism-specific databases

    CTDi 8089.
    GeneCardsi GC12P069753.
    HGNCi HGNC:24859. YEATS4.
    MIMi 602116. gene.
    neXtProti NX_O95619.
    PharmGKBi PA134992686.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5033.
    HOGENOMi HOG000190181.
    HOVERGENi HBG061271.
    InParanoidi O95619.
    KOi K11341.
    OrthoDBi EOG73FQNN.
    PhylomeDBi O95619.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Miscellaneous databases

    GenomeRNAii 8089.
    NextBioi 30722.
    PROi O95619.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95619.
    Bgeei O95619.
    CleanExi HS_YEATS4.
    Genevestigatori O95619.

    Family and domain databases

    InterProi IPR005033. YEATS.
    [Graphical view ]
    PANTHERi PTHR23195. PTHR23195. 1 hit.
    Pfami PF03366. YEATS. 1 hit.
    [Graphical view ]
    PROSITEi PS51037. YEATS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a novel transcription factor-like gene amplified in human glioma including astrocytoma grade I."
      Fischer U., Heckel D., Michel A., Janka M., Hulsebos T., Meese E.
      Hum. Mol. Genet. 6:1817-1822(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "GAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMA."
      Harborth J., Weber K., Osborn M.
      J. Biol. Chem. 275:31979-31985(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH NUMA1, TISSUE SPECIFICITY.
    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].
    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].
    5. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
      Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-15; 18-32; 56-64; 120-131; 168-178 AND 217-227, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes in human cells."
      Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.
      Biochem. J. 363:195-200(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TACC1.
    7. "The MLL fusion partner AF10 binds GAS41, a protein that interacts with the human SWI/SNF complex."
      Debernardi S., Bassini A., Jones L.K., Chaplin T., Linder B., de Bruijn D.R.H., Meese E., Young B.D.
      Blood 99:275-281(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLLT10 AND SMARCB1.
    8. "Molecular cloning, genomic structure and interactions of the putative breast tumor suppressor TACC2."
      Lauffart B., Gangisetty O., Still I.H.
      Genomics 81:192-201(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TACC2.
    9. "The highly conserved and multifunctional NuA4 HAT complex."
      Doyon Y., Cote J.
      Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON NUA4 COMPLEX.
    10. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiYETS4_HUMAN
    AccessioniPrimary (citable) accession number: O95619
    Secondary accession number(s): Q9NQD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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