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Q14CW9

- AT7L3_HUMAN

UniProt

Q14CW9 - AT7L3_HUMAN

Protein

Ataxin-7-like protein 3

Gene

ATXN7L3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      Previous versions | rss
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    Functioni

    Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex.2 PublicationsUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri84 – 10522SGF11-typeUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transcription coactivator activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone deubiquitination Source: UniProtKB
    3. positive regulation of transcription, DNA-templated Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ataxin-7-like protein 3UniRule annotation
    Alternative name(s):
    SAGA-associated factor 11 homologUniRule annotation
    Gene namesi
    Name:ATXN7L3UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:25416. ATXN7L3.

    Subcellular locationi

    Nucleus UniRule annotation

    GO - Cellular componenti

    1. DUBm complex Source: UniProtKB-HAMAP
    2. SAGA complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134991793.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 347347Ataxin-7-like protein 3PRO_0000278301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei129 – 1291Phosphoserine1 Publication
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei278 – 2781Phosphoserine1 Publication
    Modified residuei281 – 2811Phosphoserine4 Publications
    Modified residuei326 – 3261Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14CW9.
    PaxDbiQ14CW9.
    PRIDEiQ14CW9.

    PTM databases

    PhosphoSiteiQ14CW9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14CW9.
    BgeeiQ14CW9.
    CleanExiHS_ATXN7L3.
    GenevestigatoriQ14CW9.

    Organism-specific databases

    HPAiHPA050625.
    HPA052419.

    Interactioni

    Subunit structurei

    Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with ENY2 and USP22.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi121289. 16 interactions.
    IntActiQ14CW9. 6 interactions.
    MINTiMINT-6774236.
    STRINGi9606.ENSP00000397259.

    Structurei

    Secondary structure

    1
    347
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi199 – 2046
    Turni205 – 2073
    Turni214 – 2174
    Beta strandi226 – 2283
    Helixi231 – 24111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KKTNMR-A197-276[»]
    ProteinModelPortaliQ14CW9.
    SMRiQ14CW9. Positions 198-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14CW9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini196 – 26368SCA7UniRule annotationAdd
    BLAST

    Domaini

    The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.1 PublicationUniRule annotation
    The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the SAGA deubiquitination module.UniRule annotation

    Sequence similaritiesi

    Belongs to the SGF11 family.UniRule annotation
    Contains 1 SCA7 domain.UniRule annotation
    Contains 1 SGF11-type zinc finger.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri84 – 10522SGF11-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG271996.
    HOGENOMiHOG000006954.
    HOVERGENiHBG071455.
    InParanoidiQ14CW9.
    KOiK11363.
    OMAiPFKYSNS.
    PhylomeDBiQ14CW9.
    TreeFamiTF324580.

    Family and domain databases

    HAMAPiMF_03047. Sgf11.
    InterProiIPR013246. SAGA_su_Sgf11.
    IPR013243. SCA7_dom.
    [Graphical view]
    PfamiPF08313. SCA7. 1 hit.
    PF08209. Sgf11. 1 hit.
    [Graphical view]
    PROSITEiPS51505. SCA7. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14CW9-1) [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

    MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL    50
    DDTDPDSMKD FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP 100
    HLEKCLGMGR NSSRIANRRI ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK 150
    KAKKRKSDKN PNSPRRSKSL KHKNGELSNS DPFKYNNSTG ISYETLGPEE 200
    LRSLLTTQCG VISEHTKKMC TRSLRCPQHT DEQRRTVRIY FLGPSAVLPE 250
    VESSLDNDSF DMTDSQALIS RLQWDGSSDL SPSDSGSSKT SENQGWGLGT 300
    NSSESRKTKK KKSHLSLVGT ASGLGSNKKK KPKPPAPPTP SIYDDIN 347
    Length:347
    Mass (Da):38,651
    Last modified:August 22, 2006 - v1
    Checksum:i742D85BFF4ADD0C0
    GO
    Isoform 2 (identifier: Q14CW9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         159-159: K → KLWYLPFQ

    Show »
    Length:354
    Mass (Da):39,599
    Checksum:iEDB618080F2200D6
    GO

    Sequence cautioni

    The sequence AAH37418.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB71070.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei159 – 1591K → KLWYLPFQ in isoform 2. 1 PublicationVSP_036721

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC037418 mRNA. Translation: AAH37418.1. Different initiation.
    BC113595 mRNA. Translation: AAI13596.1.
    BC126113 mRNA. Translation: AAI26114.1.
    AK056002 mRNA. Translation: BAB71070.1. Different initiation.
    AL390158 mRNA. Translation: CAB99093.1.
    CCDSiCCDS42345.1. [Q14CW9-1]
    CCDS45697.1. [Q14CW9-2]
    RefSeqiNP_001092303.1. NM_001098833.1. [Q14CW9-1]
    NP_064603.1. NM_020218.1. [Q14CW9-2]
    UniGeneiHs.512651.

    Genome annotation databases

    EnsembliENST00000389384; ENSP00000374035; ENSG00000087152. [Q14CW9-1]
    ENST00000454077; ENSP00000397259; ENSG00000087152. [Q14CW9-2]
    GeneIDi56970.
    KEGGihsa:56970.
    UCSCiuc002ifz.3. human. [Q14CW9-2]
    uc002iga.3. human. [Q14CW9-1]

    Polymorphism databases

    DMDMi121948758.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC037418 mRNA. Translation: AAH37418.1 . Different initiation.
    BC113595 mRNA. Translation: AAI13596.1 .
    BC126113 mRNA. Translation: AAI26114.1 .
    AK056002 mRNA. Translation: BAB71070.1 . Different initiation.
    AL390158 mRNA. Translation: CAB99093.1 .
    CCDSi CCDS42345.1. [Q14CW9-1 ]
    CCDS45697.1. [Q14CW9-2 ]
    RefSeqi NP_001092303.1. NM_001098833.1. [Q14CW9-1 ]
    NP_064603.1. NM_020218.1. [Q14CW9-2 ]
    UniGenei Hs.512651.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KKT NMR - A 197-276 [» ]
    ProteinModelPortali Q14CW9.
    SMRi Q14CW9. Positions 198-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121289. 16 interactions.
    IntActi Q14CW9. 6 interactions.
    MINTi MINT-6774236.
    STRINGi 9606.ENSP00000397259.

    PTM databases

    PhosphoSitei Q14CW9.

    Polymorphism databases

    DMDMi 121948758.

    Proteomic databases

    MaxQBi Q14CW9.
    PaxDbi Q14CW9.
    PRIDEi Q14CW9.

    Protocols and materials databases

    DNASUi 56970.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389384 ; ENSP00000374035 ; ENSG00000087152 . [Q14CW9-1 ]
    ENST00000454077 ; ENSP00000397259 ; ENSG00000087152 . [Q14CW9-2 ]
    GeneIDi 56970.
    KEGGi hsa:56970.
    UCSCi uc002ifz.3. human. [Q14CW9-2 ]
    uc002iga.3. human. [Q14CW9-1 ]

    Organism-specific databases

    CTDi 56970.
    GeneCardsi GC17M042269.
    HGNCi HGNC:25416. ATXN7L3.
    HPAi HPA050625.
    HPA052419.
    neXtProti NX_Q14CW9.
    PharmGKBi PA134991793.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271996.
    HOGENOMi HOG000006954.
    HOVERGENi HBG071455.
    InParanoidi Q14CW9.
    KOi K11363.
    OMAi PFKYSNS.
    PhylomeDBi Q14CW9.
    TreeFami TF324580.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    EvolutionaryTracei Q14CW9.
    GenomeRNAii 56970.
    NextBioi 62612.
    PROi Q14CW9.

    Gene expression databases

    ArrayExpressi Q14CW9.
    Bgeei Q14CW9.
    CleanExi HS_ATXN7L3.
    Genevestigatori Q14CW9.

    Family and domain databases

    HAMAPi MF_03047. Sgf11.
    InterProi IPR013246. SAGA_su_Sgf11.
    IPR013243. SCA7_dom.
    [Graphical view ]
    Pfami PF08313. SCA7. 1 hit.
    PF08209. Sgf11. 1 hit.
    [Graphical view ]
    PROSITEi PS51505. SCA7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-347 (ISOFORM 2).
      Tissue: Lymph.
    2. "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] OF 123-347 (ISOFORM 1).
      Tissue: Teratocarcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-347.
      Tissue: Amygdala.
    4. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
      Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
      Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SAGA COMPLEX, INTERACTION WITH ENY2 AND USP22, DOMAIN.
    5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements."
      Lang G., Bonnet J., Umlauf D., Karmodiya K., Koffler J., Stierle M., Devys D., Tora L.
      Mol. Cell. Biol. 31:3734-3744(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-131 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties."
      Bonnet J., Wang Y.H., Spedale G., Atkinson R.A., Romier C., Hamiche A., Pijnappel W.W., Timmers H.T., Tora L., Devys D., Kieffer B.
      EMBO Rep. 11:612-618(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 197-276 IN COMPLEX WITH ZINC.

    Entry informationi

    Entry nameiAT7L3_HUMAN
    AccessioniPrimary (citable) accession number: Q14CW9
    Secondary accession number(s): Q8IY68, Q96N40, Q9NPU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 76 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3