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Q9WUD1

- CHIP_MOUSE

UniProt

Q9WUD1 - CHIP_MOUSE

Protein

STIP1 homology and U box-containing protein 1

Gene

Stub1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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.1 Publication

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to misfolded protein Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB
    4. positive regulation of chaperone-mediated protein complex assembly Source: Ensembl
    5. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: HGNC
    6. positive regulation of protein ubiquitination Source: HGNC
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    8. protein autoubiquitination Source: UniProtKB
    9. protein folding Source: HGNC
    10. protein K63-linked ubiquitination Source: UniProtKB
    11. protein maturation Source: HGNC
    12. protein polyubiquitination Source: HGNC
    13. protein ubiquitination Source: HGNC
    14. regulation of glucocorticoid metabolic process Source: HGNC
    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

    BRENDAi6.3.2.19. 3474.
    ReactomeiREACT_188191. Signaling by ERBB2.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    STIP1 homology and U box-containing protein 1 (EC:6.3.2.-)
    Alternative name(s):
    Carboxy terminus of Hsp70-interacting protein
    E3 ubiquitin-protein ligase CHIP
    Gene namesi
    Name:Stub1
    Synonyms:Chip
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1891731. Stub1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. nuclear inclusion body Source: Ensembl
    3. ubiquitin conjugating enzyme complex Source: HGNC
    4. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21K → R: Impaired interaction with ATXN3; when associated with R-4 and R-7. 1 Publication
    Mutagenesisi4 – 41K → R: Impaired interaction with ATXN3; when associated with R-2 and R-7. 1 Publication
    Mutagenesisi7 – 71K → R: Impaired interaction with ATXN3; when associated with R-2 and R-4. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304STIP1 homology and U box-containing protein 1PRO_0000106330Add
    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 residuei20 – 201Phosphoserine2 Publications
    Cross-linki23 – 23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei24 – 241Phosphoserine1 Publication
    Modified residuei26 – 261Phosphoserine1 Publication
    Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki256 – 256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei274 – 2741PhosphoserineBy similarity

    Post-translational modificationi

    Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9WUD1.
    PaxDbiQ9WUD1.
    PRIDEiQ9WUD1.

    PTM databases

    PhosphoSiteiQ9WUD1.

    Expressioni

    Gene expression databases

    BgeeiQ9WUD1.
    CleanExiMM_STUB1.
    GenevestigatoriQ9WUD1.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IlkO552227EBI-773027,EBI-6690138
    UBE2NP610882EBI-773027,EBI-1052908From a different organism.

    Protein-protein interaction databases

    BioGridi207969. 35 interactions.
    DIPiDIP-29751N.
    IntActiQ9WUD1. 13 interactions.

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 3913
    Helixi43 – 5614
    Helixi61 – 7313
    Helixi77 – 9014
    Helixi95 – 10713
    Helixi111 – 12717
    Helixi135 – 15218
    Helixi161 – 17818
    Turni179 – 1813
    Helixi183 – 1853
    Turni186 – 1883
    Helixi191 – 1944
    Helixi196 – 21823
    Helixi230 – 2323
    Turni235 – 2373
    Beta strandi242 – 2465
    Beta strandi252 – 2543
    Helixi255 – 26410
    Turni270 – 2723
    Helixi278 – 2803
    Helixi285 – 29814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C2LX-ray3.30A/B/C/D24-304[»]
    2C2VX-ray2.90S/T/U/V227-304[»]
    3Q47X-ray1.70B23-155[»]
    3Q49X-ray1.54B23-155[»]
    3Q4AX-ray1.54B23-155[»]
    ProteinModelPortaliQ9WUD1.
    SMRiQ9WUD1. Positions 24-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WUD1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati27 – 6034TPR 1Add
    BLAST
    Repeati61 – 9434TPR 2Add
    BLAST
    Repeati96 – 12833TPR 3Add
    BLAST
    Domaini227 – 30175U-boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi14 – 196Poly-Gly

    Domaini

    The TPR domain is essential for ubiquitination mediated by UBE2D1.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiNOG260504.
    GeneTreeiENSGT00730000111218.
    HOGENOMiHOG000163725.
    HOVERGENiHBG053046.
    InParanoidiQ9WUD1.
    KOiK09561.
    OMAiQENELHS.
    OrthoDBiEOG79W95G.
    PhylomeDBiQ9WUD1.
    TreeFamiTF313937.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    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. 1 hit.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9WUD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY    50
    GRAITRNPLV AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF 100
    LGQCQLEMES YDEAIANLQR AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS 150
    IEERRIHQES ELHSYLTRLI AAERERELEE CQRNHEGHED DGHIRAQQAC 200
    IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL MREPCITPSG 250
    ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW 300
    VEDY 304
    Length:304
    Mass (Da):34,909
    Last modified:November 1, 1999 - v1
    Checksum:i18BD2728908025A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201S → T in BAB22329. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129086 mRNA. Translation: AAD33401.1.
    AK002752 mRNA. Translation: BAB22329.1.
    AK004464 mRNA. Translation: BAB23315.1.
    AK045776 mRNA. Translation: BAC32489.1.
    AK166630 mRNA. Translation: BAE38905.1.
    BC027427 mRNA. Translation: AAH27427.1.
    BC038939 mRNA. Translation: AAH38939.1.
    CCDSiCCDS28533.1.
    RefSeqiNP_062693.1. NM_019719.3.
    UniGeneiMm.277599.
    Mm.491120.

    Genome annotation databases

    EnsembliENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615.
    GeneIDi56424.
    KEGGimmu:56424.
    UCSCiuc008bcf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129086 mRNA. Translation: AAD33401.1 .
    AK002752 mRNA. Translation: BAB22329.1 .
    AK004464 mRNA. Translation: BAB23315.1 .
    AK045776 mRNA. Translation: BAC32489.1 .
    AK166630 mRNA. Translation: BAE38905.1 .
    BC027427 mRNA. Translation: AAH27427.1 .
    BC038939 mRNA. Translation: AAH38939.1 .
    CCDSi CCDS28533.1.
    RefSeqi NP_062693.1. NM_019719.3.
    UniGenei Mm.277599.
    Mm.491120.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C2L X-ray 3.30 A/B/C/D 24-304 [» ]
    2C2V X-ray 2.90 S/T/U/V 227-304 [» ]
    3Q47 X-ray 1.70 B 23-155 [» ]
    3Q49 X-ray 1.54 B 23-155 [» ]
    3Q4A X-ray 1.54 B 23-155 [» ]
    ProteinModelPortali Q9WUD1.
    SMRi Q9WUD1. Positions 24-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207969. 35 interactions.
    DIPi DIP-29751N.
    IntActi Q9WUD1. 13 interactions.

    PTM databases

    PhosphoSitei Q9WUD1.

    Proteomic databases

    MaxQBi Q9WUD1.
    PaxDbi Q9WUD1.
    PRIDEi Q9WUD1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044911 ; ENSMUSP00000040431 ; ENSMUSG00000039615 .
    GeneIDi 56424.
    KEGGi mmu:56424.
    UCSCi uc008bcf.1. mouse.

    Organism-specific databases

    CTDi 10273.
    MGIi MGI:1891731. Stub1.

    Phylogenomic databases

    eggNOGi NOG260504.
    GeneTreei ENSGT00730000111218.
    HOGENOMi HOG000163725.
    HOVERGENi HBG053046.
    InParanoidi Q9WUD1.
    KOi K09561.
    OMAi QENELHS.
    OrthoDBi EOG79W95G.
    PhylomeDBi Q9WUD1.
    TreeFami TF313937.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BRENDAi 6.3.2.19. 3474.
    Reactomei REACT_188191. Signaling by ERBB2.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    Miscellaneous databases

    EvolutionaryTracei Q9WUD1.
    NextBioi 312582.
    PROi Q9WUD1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9WUD1.
    CleanExi MM_STUB1.
    Genevestigatori Q9WUD1.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    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. 1 hit.
    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. "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].
    2. "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].
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina, Embryo and Kidney.
    3. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor and Salivary gland.
    4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. Cited for: FUNCTION, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
    8. "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: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.

    Entry informationi

    Entry nameiCHIP_MOUSE
    AccessioniPrimary (citable) accession number: Q9WUD1
    Secondary accession number(s): Q9DCJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 131 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3