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Protein

E3 ubiquitin-protein ligase CHIP

Gene

STUB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). 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). Likely mediates polyubiquitination and downregulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609).13 Publications

Miscellaneous

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

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.2 Publications

Pathwayi: protein 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

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processDNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B10 2681
ReactomeiR-HSA-2173788 Downregulation of TGF-beta receptor signaling
R-HSA-8863795 Downregulation of ERBB2 signaling
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkiQ9UNE7
SIGNORiQ9UNE7
UniPathwayi
UPA00143

Protein family/group databases

MoonDBiQ9UNE7 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CHIPCurated (EC:2.3.2.272 Publications)
Alternative name(s):
Antigen NY-CO-71 Publication
CLL-associated antigen KW-81 Publication
Carboxy terminus of Hsp70-interacting protein1 Publication
RING-type E3 ubiquitin transferase CHIPCurated
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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000103266.10
HGNCiHGNC:11427 STUB1
MIMi607207 gene
neXtProtiNX_Q9UNE7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07234828E → K in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. 1 Publication1
Natural variantiVAR_07234965N → S in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination. 1 PublicationCorresponds to variant dbSNP:rs690016544EnsemblClinVar.1
Natural variantiVAR_07129379A → D in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777347EnsemblClinVar.1
Natural variantiVAR_07129479A → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777346EnsemblClinVar.1
Natural variantiVAR_071295123L → V in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777344EnsemblClinVar.1
Natural variantiVAR_071296130N → I in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777341EnsemblClinVar.1
Natural variantiVAR_072350145K → Q in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs146251364EnsemblClinVar.1
Natural variantiVAR_071297147W → C in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777342EnsemblClinVar.1
Natural variantiVAR_071298165L → F in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777340EnsemblClinVar.1
Natural variantiVAR_071299236S → T in SCAR16. 1 Publication1
Natural variantiVAR_071300240M → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777345EnsemblClinVar.1
Natural variantiVAR_071301246T → M in SCAR16; inhibits ubiquitin ligase activity and autoubiquitination. 2 PublicationsCorresponds to variant dbSNP:rs587777343EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi30K → A: Loss of interaction with FOXP3 and its ability to ubiquitinate FOXP3. Loss of interaction with SMAD3, HSPA8, HSP90AA1 and HSP90AB1. 2 Publications1
Mutagenesisi260H → Q: Loss of ability to ubiquitinate FOXP3. 1 Publication1
Mutagenesisi269P → A: Abolishes E3 ligase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi10273
MalaCardsiSTUB1
MIMi615768 phenotype
OpenTargetsiENSG00000103266
Orphaneti412057 Autosomal recessive cerebellar ataxia due to STUB1 deficiency
PharmGKBiPA36227

Polymorphism and mutation databases

BioMutaiSTUB1
DMDMi78099173

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001063291 – 303E3 ubiquitin-protein ligase CHIPAdd BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei19PhosphoserineCombined sources1 Publication1
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei23PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei149PhosphoserineCombined sources1
Cross-linki221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei273PhosphoserineCombined sources1

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

EPDiQ9UNE7
PaxDbiQ9UNE7
PeptideAtlasiQ9UNE7
PRIDEiQ9UNE7
ProteomicsDBi85282
85283 [Q9UNE7-2]

PTM databases

iPTMnetiQ9UNE7
PhosphoSitePlusiQ9UNE7

Expressioni

Tissue specificityi

Expressed in differentiated myotubes (at protein level) (PubMed:17369820). Highly expressed in skeletal muscle, heart, pancreas, brain and placenta (PubMed:10330192, PubMed:11435423). Detected in kidney, liver and lung (PubMed:10330192, PubMed:11435423).3 Publications

Inductioni

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

Gene expression databases

BgeeiENSG00000103266 Expressed in 227 organ(s), highest expression level in lateral nuclear group of thalamus
CleanExiHS_STUB1
ExpressionAtlasiQ9UNE7 baseline and differential
GenevisibleiQ9UNE7 HS

Organism-specific databases

HPAiCAB037202
CAB037209
HPA041222
HPA043531

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with BAG2 (PubMed:16169850). Interacts with E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (PubMed:11557750). Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1 (PubMed:15215316). Interacts with MKKS (PubMed:18094050). Interacts with DNAAF4 (PubMed:19423554). Interacts with POLB (PubMed:19713937). 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 (By similarity). Interacts with DNAJB6 (PubMed:22366786). Interacts with FOXP3 (PubMed:23973223). Interacts with FLCN (PubMed:27353360). Interacts with HSP90AA1 (PubMed:27353360, PubMed:24613385). Interacts with HSP90 (PubMed:11146632). Interacts with UBE2N and UBE2V1 (PubMed:16307917). Interacts (via TPR repeats) with the C-terminal domain of HSPA1A (PubMed:10330192). Interacts with the non-acetylated form of HSPA1A and HSPA1B (PubMed:27708256). Interacts (via TPR repeats) with the C-terminal domain of HSPA8 (PubMed:10330192, PubMed:11557750, PubMed:23990462, PubMed:27708256). Interacts with SMAD3 and HSP90AB1 (PubMed:24613385). Interacts with UBE4B (PubMed:17369820). Interacts with RIPK3 (PubMed:29883609).By similarity17 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115563, 348 interactors
CORUMiQ9UNE7
DIPiDIP-29752N
IntActiQ9UNE7, 152 interactors
MINTiQ9UNE7
STRINGi9606.ENSP00000219548

Structurei

Secondary structure

1303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9UNE7
SMRiQ9UNE7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati26 – 59TPR 1Add BLAST34
Repeati60 – 93TPR 2Add BLAST34
Repeati95 – 127TPR 3Add BLAST33
Domaini226 – 300U-boxAdd BLAST75

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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG4642 Eukaryota
ENOG410ZC2R LUCA
GeneTreeiENSGT00930000151045
HOGENOMiHOG000163725
HOVERGENiHBG053046
InParanoidiQ9UNE7
KOiK09561
OMAiQERVVPD
OrthoDBiEOG091G0FJB
PhylomeDBiQ9UNE7
TreeFamiTF313937

Family and domain databases

Gene3Di1.25.40.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
IPR003613 Ubox_domain
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF04564 U-box, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 3 hits
SM00504 Ubox, 1 hit
SUPFAMiSSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 1 hit
PS51698 U_BOX, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BS86H3BS86_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
213Annotation score:
H3BUD0H3BUD0_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
185Annotation score:
H3BTA3H3BTA3_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
157Annotation score:
V9GYH3V9GYH3_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
24Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52A → V in AAD33400 (PubMed:10330192).Curated1
Sequence conflicti272R → G in AAC18038 (PubMed:9610721).Curated1
Sequence conflicti280L → F in AAC18038 (PubMed:9610721).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07234828E → K in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. 1 Publication1
Natural variantiVAR_07234965N → S in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination. 1 PublicationCorresponds to variant dbSNP:rs690016544EnsemblClinVar.1
Natural variantiVAR_07129379A → D in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777347EnsemblClinVar.1
Natural variantiVAR_07129479A → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777346EnsemblClinVar.1
Natural variantiVAR_071295123L → V in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777344EnsemblClinVar.1
Natural variantiVAR_071296130N → I in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777341EnsemblClinVar.1
Natural variantiVAR_072350145K → Q in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs146251364EnsemblClinVar.1
Natural variantiVAR_071297147W → C in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777342EnsemblClinVar.1
Natural variantiVAR_071298165L → F in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777340EnsemblClinVar.1
Natural variantiVAR_071299236S → T in SCAR16. 1 Publication1
Natural variantiVAR_071300240M → T in SCAR16. 1 PublicationCorresponds to variant dbSNP:rs587777345EnsemblClinVar.1
Natural variantiVAR_071301246T → M in SCAR16; inhibits ubiquitin ligase activity and autoubiquitination. 2 PublicationsCorresponds to variant dbSNP:rs587777343EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0159471 – 72Missing in isoform 2. 1 PublicationAdd BLAST72

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 No translation available.
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 [Q9UNE7-1]
ENST00000564370; ENSP00000456875; ENSG00000103266 [Q9UNE7-2]
ENST00000565677; ENSP00000457228; ENSG00000103266 [Q9UNE7-2]
GeneIDi10273
KEGGihsa:10273
UCSCiuc002cit.4 human [Q9UNE7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

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 No translation available.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KBQX-ray2.91A/B21-154[»]
ProteinModelPortaliQ9UNE7
SMRiQ9UNE7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115563, 348 interactors
CORUMiQ9UNE7
DIPiDIP-29752N
IntActiQ9UNE7, 152 interactors
MINTiQ9UNE7
STRINGi9606.ENSP00000219548

Protein family/group databases

MoonDBiQ9UNE7 Predicted

PTM databases

iPTMnetiQ9UNE7
PhosphoSitePlusiQ9UNE7

Polymorphism and mutation databases

BioMutaiSTUB1
DMDMi78099173

Proteomic databases

EPDiQ9UNE7
PaxDbiQ9UNE7
PeptideAtlasiQ9UNE7
PRIDEiQ9UNE7
ProteomicsDBi85282
85283 [Q9UNE7-2]

Protocols and materials databases

DNASUi10273
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219548; ENSP00000219548; ENSG00000103266 [Q9UNE7-1]
ENST00000564370; ENSP00000456875; ENSG00000103266 [Q9UNE7-2]
ENST00000565677; ENSP00000457228; ENSG00000103266 [Q9UNE7-2]
GeneIDi10273
KEGGihsa:10273
UCSCiuc002cit.4 human [Q9UNE7-1]

Organism-specific databases

CTDi10273
DisGeNETi10273
EuPathDBiHostDB:ENSG00000103266.10
GeneCardsiSTUB1
H-InvDBiHIX0012661
HGNCiHGNC:11427 STUB1
HPAiCAB037202
CAB037209
HPA041222
HPA043531
MalaCardsiSTUB1
MIMi607207 gene
615768 phenotype
neXtProtiNX_Q9UNE7
OpenTargetsiENSG00000103266
Orphaneti412057 Autosomal recessive cerebellar ataxia due to STUB1 deficiency
PharmGKBiPA36227
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4642 Eukaryota
ENOG410ZC2R LUCA
GeneTreeiENSGT00930000151045
HOGENOMiHOG000163725
HOVERGENiHBG053046
InParanoidiQ9UNE7
KOiK09561
OMAiQERVVPD
OrthoDBiEOG091G0FJB
PhylomeDBiQ9UNE7
TreeFamiTF313937

Enzyme and pathway databases

UniPathwayi
UPA00143

BRENDAi2.3.2.B10 2681
ReactomeiR-HSA-2173788 Downregulation of TGF-beta receptor signaling
R-HSA-8863795 Downregulation of ERBB2 signaling
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SignaLinkiQ9UNE7
SIGNORiQ9UNE7

Miscellaneous databases

ChiTaRSiSTUB1 human
GeneWikiiSTUB1
GenomeRNAii10273
PROiPR:Q9UNE7
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103266 Expressed in 227 organ(s), highest expression level in lateral nuclear group of thalamus
CleanExiHS_STUB1
ExpressionAtlasiQ9UNE7 baseline and differential
GenevisibleiQ9UNE7 HS

Family and domain databases

Gene3Di1.25.40.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
IPR003613 Ubox_domain
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF04564 U-box, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 3 hits
SM00504 Ubox, 1 hit
SUPFAMiSSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 1 hit
PS51698 U_BOX, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCHIP_HUMAN
AccessioniPrimary (citable) accession number: Q9UNE7
Secondary accession number(s): A2IDB9
, O60526, Q969U2, Q9HBT1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 7, 2018
This is version 176 of the entry and version 2 of the sequence. See 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

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
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