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Q9UNE7

- CHIP_HUMAN

UniProt

Q9UNE7 - CHIP_HUMAN

Protein

E3 ubiquitin-protein ligase CHIP

Gene

STUB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (25 Oct 2005)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.8 Publications

    Pathwayi

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. Hsp70 protein binding Source: HGNC
    3. Hsp90 protein binding Source: BHF-UCL
    4. kinase binding Source: BHF-UCL
    5. ligase activity Source: UniProtKB-KW
    6. misfolded protein binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. protein binding, bridging Source: HGNC
    9. protein homodimerization activity Source: UniProtKB
    10. SMAD binding Source: HGNC
    11. TPR domain binding Source: HGNC
    12. ubiquitin-protein transferase activity Source: UniProtKB
    13. ubiquitin-ubiquitin ligase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to misfolded protein Source: BHF-UCL
    2. DNA repair Source: UniProtKB-KW
    3. misfolded or incompletely synthesized protein catabolic process Source: BHF-UCL
    4. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    5. positive regulation of chaperone-mediated protein complex assembly Source: BHF-UCL
    6. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: HGNC
    7. positive regulation of protein ubiquitination Source: BHF-UCL
    8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: HGNC
    9. protein autoubiquitination Source: UniProtKB
    10. protein K63-linked ubiquitination Source: UniProtKB
    11. protein maturation Source: HGNC
    12. protein polyubiquitination Source: UniProtKB
    13. regulation of glucocorticoid metabolic process Source: HGNC
    14. transforming growth factor beta receptor signaling pathway Source: Reactome
    15. ubiquitin-dependent protein catabolic process Source: UniProtKB
    16. ubiquitin-dependent SMAD protein catabolic process Source: HGNC

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_115755. Signaling by ERBB2.
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9UNE7.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase CHIP (EC:6.3.2.-)
    Alternative name(s):
    Antigen NY-CO-7
    CLL-associated antigen KW-8
    Carboxy terminus of Hsp70-interacting protein
    STIP1 homology and U box-containing protein 1
    Gene namesi
    Name:STUB1
    Synonyms:CHIP
    ORF Names:PP1131
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11427. STUB1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. intermediate filament cytoskeleton Source: HPA
    5. nuclear inclusion body Source: BHF-UCL
    6. nucleus Source: HPA
    7. plasma membrane Source: HPA
    8. ubiquitin conjugating enzyme complex Source: HGNC
    9. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi269 – 2691P → A: Abolishes E3 ligase activity. 1 Publication

    Organism-specific databases

    Orphaneti1173. Cerebellar ataxia - hypogonadism.
    PharmGKBiPA36227.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 303303E3 ubiquitin-protein ligase CHIPPRO_0000106329Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki2 – 2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei19 – 191Phosphoserine7 Publications
    Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei23 – 231Phosphoserine2 Publications
    Modified residuei25 – 251PhosphoserineBy similarity
    Cross-linki221 – 221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki255 – 255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei273 – 2731Phosphoserine2 Publications

    Post-translational modificationi

    Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 By similarity. Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2.By similarity2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UNE7.
    PaxDbiQ9UNE7.
    PRIDEiQ9UNE7.

    PTM databases

    PhosphoSiteiQ9UNE7.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9UNE7.
    BgeeiQ9UNE7.
    CleanExiHS_STUB1.
    GenevestigatoriQ9UNE7.

    Organism-specific databases

    HPAiCAB037202.
    CAB037209.
    HPA041222.
    HPA043531.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with the C-terminal domains of HSP90AA1 and HSPA8. Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W By similarity. Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with DNAJB6.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A8K1F42EBI-357085,EBI-9357094
    ATCAYQ86WG34EBI-357085,EBI-1783328
    BAG1Q999332EBI-357085,EBI-1030678
    BAG2O958164EBI-357085,EBI-355275
    BAG3O958172EBI-357085,EBI-747185
    HSP90AA1P079009EBI-357085,EBI-296047
    HSP90AB1P082385EBI-357085,EBI-352572
    HSPA1BP081075EBI-357085,EBI-629985
    HSPA8P111425EBI-357085,EBI-351896
    MAP3K2Q9Y2U59EBI-357085,EBI-357393
    MAPTP106362EBI-357085,EBI-366182
    UBE2NP610884EBI-357085,EBI-1052908
    UBE2Q1Q7Z7E83EBI-357085,EBI-1783287
    vifP125042EBI-357085,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi115563. 193 interactions.
    DIPiDIP-29752N.
    IntActiQ9UNE7. 98 interactions.
    MINTiMINT-1132706.
    STRINGi9606.ENSP00000219548.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UNE7.
    SMRiQ9UNE7. Positions 23-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati26 – 5934TPR 1Add
    BLAST
    Repeati60 – 9334TPR 2Add
    BLAST
    Repeati95 – 12733TPR 3Add
    BLAST
    Domaini226 – 30075U-boxAdd
    BLAST

    Domaini

    The TPR domain is essential for ubiquitination mediated by UBE2D1.1 Publication

    Sequence similaritiesi

    Contains 3 TPR repeats.PROSITE-ProRule annotation
    Contains 1 U-box domain.Curated

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG5113.
    HOGENOMiHOG000163725.
    HOVERGENiHBG053046.
    InParanoidiQ9UNE7.
    KOiK09561.
    OMAiQENELHS.
    OrthoDBiEOG79W95G.
    PhylomeDBiQ9UNE7.
    TreeFamiTF313937.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    3.30.40.10. 1 hit.
    InterProiIPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    IPR003613. Ubox_domain.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00515. TPR_1. 2 hits.
    PF04564. U-box. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 3 hits.
    SM00504. Ubox. 1 hit.
    [Graphical view]
    PROSITEiPS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    PS51698. U_BOX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNE7-1) [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

    MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG    50
    RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL 100
    GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI 150
    EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI 200
    EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI 250
    TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV 300
    EDY 303
    Length:303
    Mass (Da):34,856
    Last modified:October 25, 2005 - v2
    Checksum:i7E7D6568B17070BF
    GO
    Isoform 2 (identifier: Q9UNE7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:231
    Mass (Da):27,067
    Checksum:iBA7782D3C2F9E1F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521A → V in AAD33400. (PubMed:10330192)Curated
    Sequence conflicti272 – 2721R → G in AAC18038. (PubMed:9610721)Curated
    Sequence conflicti280 – 2801L → F in AAC18038. (PubMed:9610721)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_015947Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039689 mRNA. Translation: AAC18038.1.
    AF129085 mRNA. Translation: AAD33400.1.
    AF432221 mRNA. Translation: AAL99927.1.
    AF217968 mRNA. Translation: AAG17211.1.
    AE006464 Genomic DNA. Translation: AAK61242.1.
    Z92544 Genomic DNA. Translation: CAM26348.1.
    CH471112 Genomic DNA. Translation: EAW85758.1.
    BC007545 mRNA. Translation: AAH07545.1.
    BC017178 mRNA. Translation: AAH17178.1.
    BC022788 mRNA. Translation: AAH22788.1.
    BC063617 mRNA. Translation: AAH63617.1.
    CCDSiCCDS10419.1. [Q9UNE7-1]
    RefSeqiNP_005852.2. NM_005861.3. [Q9UNE7-1]
    UniGeneiHs.592081.

    Genome annotation databases

    EnsembliENST00000219548; ENSP00000219548; ENSG00000103266. [Q9UNE7-1]
    ENST00000564370; ENSP00000456875; ENSG00000103266. [Q9UNE7-2]
    ENST00000565677; ENSP00000457228; ENSG00000103266. [Q9UNE7-2]
    GeneIDi10273.
    KEGGihsa:10273.
    UCSCiuc002cit.3. human. [Q9UNE7-1]

    Polymorphism databases

    DMDMi78099173.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039689 mRNA. Translation: AAC18038.1 .
    AF129085 mRNA. Translation: AAD33400.1 .
    AF432221 mRNA. Translation: AAL99927.1 .
    AF217968 mRNA. Translation: AAG17211.1 .
    AE006464 Genomic DNA. Translation: AAK61242.1 .
    Z92544 Genomic DNA. Translation: CAM26348.1 .
    CH471112 Genomic DNA. Translation: EAW85758.1 .
    BC007545 mRNA. Translation: AAH07545.1 .
    BC017178 mRNA. Translation: AAH17178.1 .
    BC022788 mRNA. Translation: AAH22788.1 .
    BC063617 mRNA. Translation: AAH63617.1 .
    CCDSi CCDS10419.1. [Q9UNE7-1 ]
    RefSeqi NP_005852.2. NM_005861.3. [Q9UNE7-1 ]
    UniGenei Hs.592081.

    3D structure databases

    ProteinModelPortali Q9UNE7.
    SMRi Q9UNE7. Positions 23-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115563. 193 interactions.
    DIPi DIP-29752N.
    IntActi Q9UNE7. 98 interactions.
    MINTi MINT-1132706.
    STRINGi 9606.ENSP00000219548.

    PTM databases

    PhosphoSitei Q9UNE7.

    Polymorphism databases

    DMDMi 78099173.

    Proteomic databases

    MaxQBi Q9UNE7.
    PaxDbi Q9UNE7.
    PRIDEi Q9UNE7.

    Protocols and materials databases

    DNASUi 10273.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219548 ; ENSP00000219548 ; ENSG00000103266 . [Q9UNE7-1 ]
    ENST00000564370 ; ENSP00000456875 ; ENSG00000103266 . [Q9UNE7-2 ]
    ENST00000565677 ; ENSP00000457228 ; ENSG00000103266 . [Q9UNE7-2 ]
    GeneIDi 10273.
    KEGGi hsa:10273.
    UCSCi uc002cit.3. human. [Q9UNE7-1 ]

    Organism-specific databases

    CTDi 10273.
    GeneCardsi GC16P000823.
    H-InvDB HIX0012661.
    HGNCi HGNC:11427. STUB1.
    HPAi CAB037202.
    CAB037209.
    HPA041222.
    HPA043531.
    MIMi 607207. gene.
    neXtProti NX_Q9UNE7.
    Orphaneti 1173. Cerebellar ataxia - hypogonadism.
    PharmGKBi PA36227.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5113.
    HOGENOMi HOG000163725.
    HOVERGENi HBG053046.
    InParanoidi Q9UNE7.
    KOi K09561.
    OMAi QENELHS.
    OrthoDBi EOG79W95G.
    PhylomeDBi Q9UNE7.
    TreeFami TF313937.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115755. Signaling by ERBB2.
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9UNE7.

    Miscellaneous databases

    GeneWikii STUB1.
    GenomeRNAii 10273.
    NextBioi 38918.
    PROi Q9UNE7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNE7.
    Bgeei Q9UNE7.
    CleanExi HS_STUB1.
    Genevestigatori Q9UNE7.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    3.30.40.10. 1 hit.
    InterProi IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    IPR003613. Ubox_domain.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00515. TPR_1. 2 hits.
    PF04564. U-box. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 3 hits.
    SM00504. Ubox. 1 hit.
    [Graphical view ]
    PROSITEi PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    PS51698. U_BOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of human colon cancer antigens recognized by autologous antibodies."
      Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
      Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN.
      Tissue: Colon carcinoma.
    2. "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
      Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
      Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HSPA8 AND HSPA1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Heart.
    3. "Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX."
      Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
      Blood 100:2123-2131(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN.
    4. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
      Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
      Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Colon and Skin.
    9. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 13-30; 56-66; 86-119; 129-140; 155-167; 235-241; 256-263 AND 273-287, PHOSPHORYLATION AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    10. "CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation."
      Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hoehfeld J., Patterson C.
      J. Biol. Chem. 276:42938-42944(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSPA8; UBE2D1; UBE2D2 AND UBE2D3.
    11. "The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins."
      Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hoehfeld J., Patterson C.
      Nat. Cell Biol. 3:93-96(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP90.
    12. "Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase."
      Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M., Patterson C., Pratt W.B., Osawa Y.
      J. Biol. Chem. 279:52970-52977(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator."
      Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.
      Mol. Biol. Cell 15:4003-4010(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPA1A AND HSPBP1.
    14. "Regulation of the cytoplasmic quality control protein degradation pathway by BAG2."
      Dai Q., Qian S.B., Li H.-H., McDonough H., Borchers C., Huang D., Takayama S., Younger J.M., Ren H.Y., Cyr D.M., Patterson C.
      J. Biol. Chem. 280:38673-38681(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BAG2.
    15. "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
      Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
      Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2N AND UBE2V1.
    16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology."
      Windheim M., Peggie M., Cohen P.
      Biochem. J. 409:723-729(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYUBIQUITINATION AT LYS-22; LYS-221 AND LYS-255, DOMAIN TPR.
    18. "MKKS is a centrosome-shuttling protein degraded by disease-causing mutations via CHIP-mediated ubiquitination."
      Hirayama S., Yamazaki Y., Kitamura A., Oda Y., Morito D., Okawa K., Kimura H., Cyr D.M., Kubota H., Nagata K.
      Mol. Biol. Cell 19:899-911(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MKKS.
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases."
      Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.
      Arch. Biochem. Biophys. 483:66-74(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. Cited for: FUNCTION, INTERACTION WITH POLB.
    24. "Functional interaction of DYX1C1 with estrogen receptors suggests involvement of hormonal pathways in dyslexia."
      Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E., Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E., Kere J.
      Hum. Mol. Genet. 18:2802-2812(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYX1C1.
    25. "Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis."
      Annamalai B., Liu X., Gopal U., Isaacs J.S.
      Mol. Cancer Res. 7:1021-1032(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    28. "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-19 AND SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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-19 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. Cited for: INTERACTION WITH DNAJB6.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini."
      Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.
      Biochem. J. 453:137-145(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-2.
    34. "Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase."
      Matsumura Y., Sakai J., Skach W.R.
      J. Biol. Chem. 288:31069-31079(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSPA8, MUTAGENESIS OF PRO-269.

    Entry informationi

    Entry nameiCHIP_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNE7
    Secondary accession number(s): A2IDB9
    , O60526, Q969U2, Q9HBT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 130 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

    Miscellaneous

    Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3