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Protein

E3 ubiquitin-protein ligase CHIP

Gene

STUB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223).9 Publications

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • G-protein coupled receptor binding Source: ParkinsonsUK-UCL
  • Hsp70 protein binding Source: HGNC
  • Hsp90 protein binding Source: BHF-UCL
  • kinase binding Source: BHF-UCL
  • ligase activity Source: UniProtKB-KW
  • misfolded protein binding Source: BHF-UCL
  • protein binding, bridging Source: HGNC
  • protein homodimerization activity Source: UniProtKB
  • SMAD binding Source: HGNC
  • TPR domain binding Source: HGNC
  • ubiquitin protein ligase activity Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase activity involved in ERAD pathway Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • ubiquitin-ubiquitin ligase activity Source: UniProtKB

GO - Biological processi

  • cellular response to misfolded protein Source: BHF-UCL
  • DNA repair Source: UniProtKB-KW
  • endoplasmic reticulum unfolded protein response Source: Ensembl
  • ERAD pathway Source: GOC
  • misfolded or incompletely synthesized protein catabolic process Source: BHF-UCL
  • negative regulation of protein binding Source: Ensembl
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  • positive regulation of chaperone-mediated protein complex assembly Source: BHF-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: HGNC
  • positive regulation of protein ubiquitination Source: HGNC
  • positive regulation of ubiquitin-protein transferase activity Source: Ensembl
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: HGNC
  • protein autoubiquitination Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein maturation Source: HGNC
  • protein polyubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • regulation of glucocorticoid metabolic process Source: HGNC
  • transforming growth factor beta receptor signaling pathway Source: Reactome
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
  • 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

BRENDAi2.3.2.B10. 2681.
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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11427. STUB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • extracellular exosome Source: UniProtKB
  • intermediate filament cytoskeleton Source: HPA
  • nuclear inclusion body Source: BHF-UCL
  • nucleoplasm Source: HPA
  • plasma membrane Source: HPA
  • ubiquitin conjugating enzyme complex Source: HGNC
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionSpinocerebellar 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.

See also OMIM:615768
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281E → K in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. 1 Publication
VAR_072348
Natural varianti65 – 651N → S in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination. 1 Publication
VAR_072349
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 varianti145 – 1451K → Q in SCAR16. 1 Publication
VAR_072350
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; inhibits ubiquitin ligase activity and autoubiquitination. 2 Publications
VAR_071301

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301K → A: Loss of interaction with FOXP3 and its ability to ubiquitinate FOXP3. 1 Publication
Mutagenesisi260 – 2601H → Q: Loss of ability to ubiquitinate FOXP3. 1 Publication
Mutagenesisi269 – 2691P → A: Abolishes E3 ligase activity. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi615768. phenotype.
Orphaneti1173. Cerebellar ataxia - hypogonadism.
PharmGKBiPA36227.

Polymorphism and mutation databases

BioMutaiSTUB1.
DMDMi78099173.

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 – 191Phosphoserine8 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

Inductioni

Up-regulated by inflammatory signals in regulatory T-cells (Treg).1 Publication

Gene expression databases

BgeeiQ9UNE7.
CleanExiHS_STUB1.
ExpressionAtlasiQ9UNE7. baseline and differential.
GenevisibleiQ9UNE7. HS.

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. Interacts with FOXP3.By similarity12 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
CCL28Q9NRJ33EBI-357085,EBI-7783254
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
OLFM3Q96PB73EBI-357085,EBI-10292253
RUSC1Q9BVN23EBI-357085,EBI-6257312
TXN2Q997573EBI-357085,EBI-2932492
UBE2NP610885EBI-357085,EBI-1052908
UBE2Q1Q7Z7E83EBI-357085,EBI-1783287
vifP125042EBI-357085,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi115563. 227 interactions.
DIPiDIP-29752N.
IntActiQ9UNE7. 108 interactions.
MINTiMINT-1132706.
STRINGi9606.ENSP00000219548.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 3813Combined sources
Helixi42 – 5514Combined sources
Helixi60 – 7213Combined sources
Helixi76 – 8914Combined sources
Helixi94 – 10613Combined sources
Helixi110 – 12617Combined sources
Helixi134 – 14714Combined sources
Turni148 – 1514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KBQX-ray2.91A/B21-154[»]
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. AlignAdd to basket

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 varianti28 – 281E → K in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. 1 Publication
VAR_072348
Natural varianti65 – 651N → S in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination. 1 Publication
VAR_072349
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 varianti145 – 1451K → Q in SCAR16. 1 Publication
VAR_072350
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; inhibits ubiquitin ligase activity and autoubiquitination. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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]
CCDS76797.1. [Q9UNE7-2]
RefSeqiNP_001280126.1. NM_001293197.1. [Q9UNE7-2]
NP_005852.2. NM_005861.3. [Q9UNE7-1]
UniGeneiHs.592081.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS76797.1. [Q9UNE7-2]
RefSeqiNP_001280126.1. NM_001293197.1. [Q9UNE7-2]
NP_005852.2. NM_005861.3. [Q9UNE7-1]
UniGeneiHs.592081.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KBQX-ray2.91A/B21-154[»]
ProteinModelPortaliQ9UNE7.
SMRiQ9UNE7. Positions 23-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115563. 227 interactions.
DIPiDIP-29752N.
IntActiQ9UNE7. 108 interactions.
MINTiMINT-1132706.
STRINGi9606.ENSP00000219548.

PTM databases

PhosphoSiteiQ9UNE7.

Polymorphism and mutation databases

BioMutaiSTUB1.
DMDMi78099173.

Proteomic databases

MaxQBiQ9UNE7.
PaxDbiQ9UNE7.
PRIDEiQ9UNE7.

Protocols and materials databases

DNASUi10273.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10273.
GeneCardsiGC16P000848.
H-InvDBHIX0012661.
HGNCiHGNC:11427. STUB1.
HPAiCAB037202.
CAB037209.
HPA041222.
HPA043531.
MIMi607207. gene.
615768. phenotype.
neXtProtiNX_Q9UNE7.
Orphaneti1173. Cerebellar ataxia - hypogonadism.
PharmGKBiPA36227.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5113.
GeneTreeiENSGT00730000111218.
HOGENOMiHOG000163725.
HOVERGENiHBG053046.
InParanoidiQ9UNE7.
KOiK09561.
OMAiQENELHS.
OrthoDBiEOG79W95G.
PhylomeDBiQ9UNE7.
TreeFamiTF313937.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 2681.
ReactomeiREACT_115755. Signaling by ERBB2.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9UNE7.

Miscellaneous databases

ChiTaRSiSTUB1. human.
GeneWikiiSTUB1.
GenomeRNAii10273.
NextBioi38918.
PROiQ9UNE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNE7.
CleanExiHS_STUB1.
ExpressionAtlasiQ9UNE7. baseline and differential.
GenevisibleiQ9UNE7. HS.

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]
ProtoNetiSearch...

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. "The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3."
    Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H., Li Y.
    , Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.
    Immunity 39:272-285(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, INTERACTION WITH FOXP3, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-30 AND HIS-260.
  36. "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.
  37. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  38. "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, INVOLVEMENT IN SCAR16.
  39. "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.
  40. "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.
  41. "Autosomal recessive cerebellar ataxia of adult onset due to STUB1 mutations."
    Depondt C., Donatello S., Simonis N., Rai M., van Heurck R., Abramowicz M., D'Hooghe M., Pandolfo M.
    Neurology 82:1749-1750(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCAR16 GLN-145.
  42. Cited for: VARIANTS SCAR16 LYS-28; SER-65 AND MET-246, CHARACTERIZATION OF VARIANTS SCAR16 LYS-28; SER-65 AND MET-246.

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: July 22, 2015
This is version 140 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.