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Q9UNE7 (CHIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:STUB1
Synonyms:CHIP
ORF Names:PP1131
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.10 Ref.11 Ref.12 Ref.21 Ref.22 Ref.24

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer By similarity. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with HSP90AA1. 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. Ref.2 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.22 Ref.23 Ref.30

Subcellular location

Cytoplasm Ref.2.

Tissue specificity

Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. Ref.2

Domain

The TPR domain is essential for ubiquitination mediated by UBE2D1. Ref.17

Post-translational modification

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

Miscellaneous

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

Sequence similarities

Contains 3 TPR repeats.

Contains 1 U-box domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
TPR repeat
   Molecular functionLigase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to misfolded protein

Inferred from direct assay PubMed 16831871. Source: BHF-UCL

misfolded or incompletely synthesized protein catabolic process

Inferred from direct assay PubMed 16831871. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of chaperone-mediated protein complex assembly

Inferred from direct assay PubMed 16831871. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.11. Source: HGNC

positive regulation of protein ubiquitination

Inferred from direct assay PubMed 16831871. Source: BHF-UCL

proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 15781469. Source: HGNC

protein K63-linked ubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.15Ref.17. Source: UniProtKB

protein maturation

Traceable author statement Ref.15. Source: HGNC

regulation of glucocorticoid metabolic process

Inferred from direct assay Ref.11. Source: HGNC

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

ubiquitin-dependent SMAD protein catabolic process

Inferred from direct assay PubMed 15781469. Source: HGNC

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nuclear inclusion body

Inferred from direct assay PubMed 16831871. Source: BHF-UCL

ubiquitin conjugating enzyme complex

Traceable author statement Ref.15. Source: HGNC

ubiquitin ligase complex

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionHsp70 protein binding

Inferred from direct assay Ref.2. Source: HGNC

Hsp90 protein binding

Inferred from direct assay Ref.11. Source: BHF-UCL

SMAD binding

Inferred from direct assay PubMed 15781469. Source: HGNC

TPR domain binding

Inferred from direct assay Ref.11. Source: HGNC

misfolded protein binding

Inferred from direct assay PubMed 16831871. Source: BHF-UCL

protein binding, bridging

Traceable author statement Ref.15. Source: HGNC

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-ubiquitin ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UNE7-1)

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.
Isoform 2 (identifier: Q9UNE7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303E3 ubiquitin-protein ligase CHIP
PRO_0000106329

Regions

Repeat26 – 5934TPR 1
Repeat60 – 9334TPR 2
Repeat95 – 12733TPR 3
Domain226 – 30075U-box

Amino acid modifications

Modified residue191Phosphoserine Ref.9 Ref.16 Ref.19 Ref.20 Ref.26 Ref.27 Ref.29
Modified residue231Phosphoserine Ref.20 Ref.29
Modified residue251Phosphoserine By similarity
Modified residue2731Phosphoserine Ref.20 Ref.27
Cross-link2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Cross-link221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Cross-link255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_015947

Experimental info

Sequence conflict521A → V in AAD33400. Ref.2
Sequence conflict2721R → G in AAC18038. Ref.1
Sequence conflict2801L → F in AAC18038. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: 7E7D6568B17070BF

FASTA30334,856
        10         20         30         40         50         60 
MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA 

        70         80         90        100        110        120 
VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA 

       130        140        150        160        170        180 
YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC 

       190        200        210        220        230        240 
QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM 

       250        260        270        280        290        300 
REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV 


EDY

« Hide

Isoform 2 [UniParc].

Checksum: BA7782D3C2F9E1F9
Show »

FASTA23127,067

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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, 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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[21]"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.
[22]"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair."
Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J., Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L.
EMBO J. 28:3207-3215(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POLB.
[23]"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.
[24]"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.
[25]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[27]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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, MASS SPECTROMETRY.
[30]"Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy."
Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M., McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S., Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P. expand/collapse author list , Hauser M., Katsanis N., Udd B.
Nat. Genet. 44:450-455(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJB6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00025156.
IPI00645380.
RefSeqNP_005852.2. NM_005861.2.
UniGeneHs.592081.

3D structure databases

ProteinModelPortalQ9UNE7.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29752N.
IntActQ9UNE7. 29 interactions.
MINTMINT-1132706.
STRING9606.ENSP00000219548.

PTM databases

PhosphoSiteQ9UNE7.

Polymorphism databases

DMDM78099173.

Proteomic databases

PaxDbQ9UNE7.
PRIDEQ9UNE7.

Protocols and materials databases

DNASU10273.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219548; ENSP00000219548; ENSG00000103266.
ENST00000564370; ENSP00000456875; ENSG00000103266.
ENST00000565677; ENSP00000457228; ENSG00000103266.
GeneID10273.
KEGGhsa:10273.
UCSCuc002cit.3. human.

Organism-specific databases

CTD10273.
GeneCardsGC16P000736.
H-InvDBHIX0012661.
HGNCHGNC:11427. STUB1.
HPACAB037202.
CAB037209.
HPA041222.
HPA043531.
MIM607207. gene.
neXtProtNX_Q9UNE7.
PharmGKBPA36227.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5113.
HOGENOMHOG000163725.
HOVERGENHBG053046.
InParanoidQ9UNE7.
KOK09561.
OMAQENELHS.
OrthoDBEOG4Z36F9.
PhylomeDBQ9UNE7.

Enzyme and pathway databases

Pathway_Interaction_DBalphasynuclein_pathway. Alpha-synuclein signaling.
ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkQ9UNE7.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UNE7.
BgeeQ9UNE7.
CleanExHS_STUB1.
GenevestigatorQ9UNE7.
GermOnlineENSG00000103266. Homo sapiens.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
3.30.40.10. 1 hit.
InterProIPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00515. TPR_1. 2 hits.
PF04564. U-box. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
SM00504. Ubox. 1 hit.
[Graphical view]
PROSITEPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10273.
NextBio38918.
SOURCESearch...

Entry information

Entry nameCHIP_HUMAN
AccessionPrimary (citable) accession number: Q9UNE7
Secondary accession number(s): A2IDB9 expand/collapse secondary AC list , O60526, Q969U2, Q9HBT1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 29, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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