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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.3.2.B10 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q9UNE7

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9UNE7

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00143

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
Q9UNE7 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:STUB1Imported
Synonyms:CHIP1 Publication
ORF Names:PP1131Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000103266.10

Human Gene Nomenclature Database

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HGNCi
HGNC:11427 STUB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
607207 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9UNE7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
10273

MalaCards human disease database

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MalaCardsi
STUB1
MIMi615768 phenotype

Open Targets

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OpenTargetsi
ENSG00000103266

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
412057 Autosomal recessive cerebellar ataxia due to STUB1 deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36227

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
STUB1

Domain mapping of disease mutations (DMDM)

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DMDMi
78099173

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001063291 – 303E3 ubiquitin-protein ligase CHIPAdd BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
Q9UNE7

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9UNE7

PeptideAtlas

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PeptideAtlasi
Q9UNE7

PRoteomics IDEntifications database

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PRIDEi
Q9UNE7

ProteomicsDB human proteome resource

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ProteomicsDBi
85282
85283 [Q9UNE7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9UNE7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9UNE7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000103266 Expressed in 227 organ(s), highest expression level in lateral nuclear group of thalamus

CleanEx database of gene expression profiles

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CleanExi
HS_STUB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9UNE7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9UNE7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB037202
CAB037209
HPA041222
HPA043531

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115563, 354 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9UNE7

Database of interacting proteins

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DIPi
DIP-29752N

Protein interaction database and analysis system

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IntActi
Q9UNE7, 153 interactors

Molecular INTeraction database

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MINTi
Q9UNE7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000219548

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9UNE7

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9UNE7

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati26 – 59TPR 1Add BLAST34
Repeati60 – 93TPR 2Add BLAST34
Repeati95 – 127TPR 3Add BLAST33
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini226 – 300U-boxAdd BLAST75

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4642 Eukaryota
ENOG410ZC2R LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00930000151045

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000163725

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053046

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9UNE7

KEGG Orthology (KO)

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KOi
K09561

Identification of Orthologs from Complete Genome Data

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OMAi
QERVVPD

Database of Orthologous Groups

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OrthoDBi
EOG091G0FJB

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UNE7

TreeFam database of animal gene trees

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TreeFami
TF313937

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
IPR003613 Ubox_domain
IPR013083 Znf_RING/FYVE/PHD

Pfam protein domain database

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Pfami
View protein in Pfam
PF04564 U-box, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00028 TPR, 3 hits
SM00504 Ubox, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48452 SSF48452, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 1 hit
PS51698 U_BOX, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BUD0H3BUD0_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
185Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BTA3H3BTA3_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
157Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GYH3V9GYH3_HUMAN
E3 ubiquitin-protein ligase CHIP
STUB1
24Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0159471 – 72Missing in isoform 2. 1 PublicationAdd BLAST72

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10419.1 [Q9UNE7-1]
CCDS76797.1 [Q9UNE7-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001280126.1, NM_001293197.1 [Q9UNE7-2]
NP_005852.2, NM_005861.3 [Q9UNE7-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.592081

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000219548; ENSP00000219548; ENSG00000103266 [Q9UNE7-1]
ENST00000564370; ENSP00000456875; ENSG00000103266 [Q9UNE7-2]
ENST00000565677; ENSP00000457228; ENSG00000103266 [Q9UNE7-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
10273

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10273

UCSC genome browser

More...
UCSCi
uc002cit.4 human [Q9UNE7-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KBQX-ray2.91A/B21-154[»]
ProteinModelPortaliQ9UNE7
SMRiQ9UNE7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115563, 354 interactors
CORUMiQ9UNE7
DIPiDIP-29752N
IntActiQ9UNE7, 153 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

The DNASU plasmid repository

More...
DNASUi
10273
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

Comparative Toxicogenomics Database

More...
CTDi
10273
DisGeNETi10273
EuPathDBiHostDB:ENSG00000103266.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
STUB1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0012661
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

GenAtlas: human gene database

More...
GenAtlasi
Search...

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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
STUB1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
STUB1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
10273

Protein Ontology

More...
PROi
PR:Q9UNE7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCHIP_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UNE7
Secondary accession number(s): A2IDB9
, O60526, Q969U2, Q9HBT1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: December 5, 2018
This is version 177 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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