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Q9UNE7

- CHIP_HUMAN

UniProt

Q9UNE7 - CHIP_HUMAN

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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

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. G-protein coupled receptor binding Source: ParkinsonsUK-UCL
  3. Hsp70 protein binding Source: HGNC
  4. Hsp90 protein binding Source: BHF-UCL
  5. kinase binding Source: BHF-UCL
  6. ligase activity Source: UniProtKB-KW
  7. misfolded protein binding Source: BHF-UCL
  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 ligase binding Source: ParkinsonsUK-UCL
  13. ubiquitin-protein transferase activity Source: UniProtKB
  14. 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
Complete GO annotation...

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 CHIPCurated (EC:6.3.2.-2 Publications)
Alternative name(s):
Antigen NY-CO-71 Publication
CLL-associated antigen KW-81 Publication
Carboxy terminus of Hsp70-interacting protein1 Publication
STIP1 homology and U box-containing protein 1Imported
Gene namesi
Name:STUB1Imported
Synonyms:CHIP1 Publication
ORF Names:PP1131Imported
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. endoplasmic reticulum Source: ParkinsonsUK-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. intermediate filament cytoskeleton Source: HPA
  6. nuclear inclusion body Source: BHF-UCL
  7. nucleus Source: HPA
  8. plasma membrane Source: HPA
  9. ubiquitin conjugating enzyme complex Source: HGNC
  10. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16) [MIM:615768]: Spinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR16 is characterized by truncal and limb ataxia resulting in gait instability. Additionally, patients may show dysarthria, nystagmus, spasticity of the lower limbs, and mild peripheral sensory neuropathy.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791A → D in SCAR16. 1 Publication
VAR_071293
Natural varianti79 – 791A → T in SCAR16. 1 Publication
VAR_071294
Natural varianti123 – 1231L → V in SCAR16. 1 Publication
VAR_071295
Natural varianti130 – 1301N → I in SCAR16. 1 Publication
VAR_071296
Natural varianti147 – 1471W → C in SCAR16. 1 Publication
VAR_071297
Natural varianti165 – 1651L → F in SCAR16. 1 Publication
VAR_071298
Natural varianti236 – 2361S → T in SCAR16. 1 Publication
VAR_071299
Natural varianti240 – 2401M → T in SCAR16. 1 Publication
VAR_071300
Natural varianti246 – 2461T → M in SCAR16. 1 Publication
VAR_071301

Mutagenesis

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

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi615768. phenotype.
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.2 Publications

Gene expression databases

BgeeiQ9UNE7.
CleanExiHS_STUB1.
ExpressionAtlasiQ9UNE7. baseline and differential.
GenevestigatoriQ9UNE7.

Organism-specific databases

HPAiCAB037202.
CAB037209.
HPA041222.
HPA043531.

Interactioni

Subunit structurei

Homodimer. 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. 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
EGFRP005333EBI-357085,EBI-297353
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. 209 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 U-box domain is required for the ubiquitin protein ligase activity.By similarity
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.
GeneTreeiENSGT00730000111218.
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_dom.
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

        10         20         30         40         50
MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG
60 70 80 90 100
RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL
110 120 130 140 150
GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI
160 170 180 190 200
EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI
210 220 230 240 250
EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI
260 270 280 290 300
TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV

EDY
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791A → D in SCAR16. 1 Publication
VAR_071293
Natural varianti79 – 791A → T in SCAR16. 1 Publication
VAR_071294
Natural varianti123 – 1231L → V in SCAR16. 1 Publication
VAR_071295
Natural varianti130 – 1301N → I in SCAR16. 1 Publication
VAR_071296
Natural varianti147 – 1471W → C in SCAR16. 1 Publication
VAR_071297
Natural varianti165 – 1651L → F in SCAR16. 1 Publication
VAR_071298
Natural varianti236 – 2361S → T in SCAR16. 1 Publication
VAR_071299
Natural varianti240 – 2401M → T in SCAR16. 1 Publication
VAR_071300
Natural varianti246 – 2461T → M in SCAR16. 1 Publication
VAR_071301

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_001280126.1. NM_001293197.1. [Q9UNE7-2]
NP_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_001280126.1. NM_001293197.1. [Q9UNE7-2 ]
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. 209 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 GC16P000848.
H-InvDB HIX0012661.
HGNCi HGNC:11427. STUB1.
HPAi CAB037202.
CAB037209.
HPA041222.
HPA043531.
MIMi 607207. gene.
615768. phenotype.
neXtProti NX_Q9UNE7.
Orphaneti 1173. Cerebellar ataxia - hypogonadism.
PharmGKBi PA36227.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5113.
GeneTreei ENSGT00730000111218.
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

Bgeei Q9UNE7.
CleanExi HS_STUB1.
ExpressionAtlasi Q9UNE7. baseline and differential.
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_dom.
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

« Hide 'large scale' publications
  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. "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "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, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH HSPA8; UBE2D1; UBE2D2 AND UBE2D3.
  12. "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.
  13. "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, CATALYTIC ACTIVITY, PATHWAY.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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].
  23. "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.
  24. Cited for: FUNCTION, INTERACTION WITH POLB.
  25. "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.
  26. "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.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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.
  29. "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.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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].
  32. Cited for: INTERACTION WITH DNAJB6.
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "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.
  35. "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.
  36. "Identification of CHIP as a novel causative gene for autosomal recessive cerebellar ataxia."
    Shi Y., Wang J., Li J.D., Ren H., Guan W., He M., Yan W., Zhou Y., Hu Z., Zhang J., Xiao J., Su Z., Dai M., Wang J., Jiang H., Guo J., Zhou Y., Zhang F.
    , Li N., Du J., Xu Q., Hu Y., Pan Q., Shen L., Wang G., Xia K., Zhang Z., Tang B.
    PLoS ONE 8:E81884-E81884(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCAR16 ILE-130; CYS-147; PHE-165 AND THR-236.
  37. "Ataxia and hypogonadism caused by the loss of ubiquitin ligase activity of the U box protein CHIP."
    Shi C.H., Schisler J.C., Rubel C.E., Tan S., Song B., McDonough H., Xu L., Portbury A.L., Mao C.Y., True C., Wang R.H., Wang Q.Z., Sun S.L., Seminara S.B., Patterson C., Xu Y.M.
    Hum. Mol. Genet. 23:1013-1024(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCAR16 MET-246.
  38. "Phenotype and frequency of STUB1 mutations: next-generation screenings in Caucasian ataxia and spastic paraplegia cohorts."
    Synofzik M., Schuele R., Schulze M., Gburek-Augustat J., Schweizer R., Schirmacher A., Kraegeloh-Mann I., Gonzalez M., Young P., Zuechner S., Schoels L., Bauer P.
    Orphanet J. Rare Dis. 9:57-64(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCAR16 ASP-79; THR-79; VAL-123 AND THR-240.

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 29, 2014
This is version 131 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3