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UniProtKB - Q9WUD1 (CHIP_MOUSE)

Entry version 173 (13 Feb 2019)
Sequence version 1 (01 Nov 1999)
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Protein

STIP1 homology and U box-containing protein 1

Gene

Stub1

Organism
Mus musculus (Mouse)
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. 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). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. 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 (By similarity). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (By similarity).By similarity3 Publications

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-2173788 Downregulation of TGF-beta receptor signaling
R-MMU-8863795 Downregulation of ERBB2 signaling
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

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

More...UniPathwayi
UPA00143

<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:
STIP1 homology and U box-containing protein 1Curated (EC:2.3.2.272 Publications)
Alternative name(s):
Carboxy terminus of Hsp70-interacting protein1 Publication
E3 ubiquitin-protein ligase CHIPCurated
RING-type E3 ubiquitin transferase CHIPCurated
<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1891731 Stub1

<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

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>Mutagenesisi2K → R: Impaired interaction with ATXN3; when associated with R-4 and R-7. 1 Publication1
Mutagenesisi4K → R: Impaired interaction with ATXN3; when associated with R-2 and R-7. 1 Publication1
Mutagenesisi7K → R: Impaired interaction with ATXN3; when associated with R-2 and R-4. 1 Publication1
Mutagenesisi261H → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication1
Mutagenesisi270P → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication1

<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_00001063301 – 304STIP1 homology and U box-containing protein 1Add BLAST304

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 residuei20PhosphoserineCombined sources1
Cross-linki23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei24PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei150PhosphoserineBy similarity1
Cross-linki222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei274PhosphoserineBy similarity1

<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

Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9WUD1

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9WUD1

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9WUD1

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

More...PaxDbi		Q9WUD1

PeptideAtlas

More...PeptideAtlasi		Q9WUD1

PRoteomics IDEntifications database

More...PRIDEi		Q9WUD1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9WUD1

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

More...PhosphoSitePlusi		Q9WUD1

<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 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 Treg regulatory T-cells (Treg).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000039615 Expressed in 39 organ(s), highest expression level in brain

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9WUD1 MM

<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 (PubMed:16307917). 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 DNAAF4 and POLB (By similarity). Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity (PubMed:16307917). Interacts (when monoubiquitinated) with ATXN3 (PubMed:21855799). Interacts with UBE2W (PubMed:21855799). Interacts with DNAJB6 (By similarity). Interacts with FOXP3 (PubMed:23973223). Interacts with FLCN and HSP90AA1. Interacts with HSP90. Interacts with UBE2N and UBE2V1. Interacts (via TPR repeats) with the C-terminal domains of HSPA8 and HSPA1A. Interacts with the non-acetylated form of HSPA1A and HSPA1B. Interacts with SMAD3 and HSP90AB1 (By similarity). Interacts with UBE4B (By similarity). Interacts with RIPK3 (By similarity).By similarity3 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		207969, 49 interactors

Database of interacting proteins

More...DIPi		DIP-29751N

Protein interaction database and analysis system

More...IntActi		Q9WUD1, 16 interactors

Molecular INTeraction database

More...MINTi		Q9WUD1

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000040431

<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

1304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2C2LX-ray3.30A/B/C/D24-304[»]
2C2VX-ray2.90S/T/U/V227-304[»]
3Q47X-ray1.70B23-155[»]
3Q49X-ray1.54B23-155[»]
3Q4AX-ray1.54B23-155[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9WUD1

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

More...SMRi		Q9WUD1

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9WUD1

<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>Repeati27 – 60TPR 1Add BLAST34
Repeati61 – 94TPR 2Add BLAST34
Repeati96 – 128TPR 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>Domaini227 – 301U-boxAdd BLAST75

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi14 – 19Poly-Gly6

<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.1 Publication
The TPR domain is essential for ubiquitination mediated by UBE2D1.By similarity

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4642 Eukaryota
ENOG410ZC2R LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00930000151045

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000163725

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG053046

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9WUD1

KEGG Orthology (KO)

More...KOi		K09561

Identification of Orthologs from Complete Genome Data

More...OMAi		QERVVPD

Database of Orthologous Groups

More...OrthoDBi		1422450at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9WUD1

TreeFam database of animal gene trees

More...TreeFami		TF313937

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

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

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48452 SSF48452, 1 hit

PROSITE; a protein domain and family database

More...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>Sequencei

<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.

Q9WUD1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY 
        60         70         80         90        100
GRAITRNPLV AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF 
       110        120        130        140        150
LGQCQLEMES YDEAIANLQR AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS 
       160        170        180        190        200
IEERRIHQES ELHSYLTRLI AAERERELEE CQRNHEGHED DGHIRAQQAC 
       210        220        230        240        250
IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL MREPCITPSG 
       260        270        280        290        300
ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW 

VEDY
Length:304
Mass (Da):34,909
Last modified:November 1, 1999 - v1
<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:i18BD2728908025A8
GO

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 conflicti20S → T in BAB22329 (PubMed:16141072).Curated1

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
AF129086 mRNA Translation: AAD33401.1
AK002752 mRNA Translation: BAB22329.1
AK004464 mRNA Translation: BAB23315.1
AK045776 mRNA Translation: BAC32489.1
AK166630 mRNA Translation: BAE38905.1
BC027427 mRNA Translation: AAH27427.1
BC038939 mRNA Translation: AAH38939.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS28533.1

NCBI Reference Sequences

More...RefSeqi		NP_062693.1, NM_019719.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.277599
Mm.491120

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615

Database of genes from NCBI RefSeq genomes

More...GeneIDi		56424

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:56424

UCSC genome browser

More...UCSCi		uc008bcf.1 mouse

<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
AF129086 mRNA Translation: AAD33401.1
AK002752 mRNA Translation: BAB22329.1
AK004464 mRNA Translation: BAB23315.1
AK045776 mRNA Translation: BAC32489.1
AK166630 mRNA Translation: BAE38905.1
BC027427 mRNA Translation: AAH27427.1
BC038939 mRNA Translation: AAH38939.1
CCDSiCCDS28533.1
RefSeqiNP_062693.1, NM_019719.3
UniGeneiMm.277599
Mm.491120

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C2LX-ray3.30A/B/C/D24-304[»]
2C2VX-ray2.90S/T/U/V227-304[»]
3Q47X-ray1.70B23-155[»]
3Q49X-ray1.54B23-155[»]
3Q4AX-ray1.54B23-155[»]
ProteinModelPortaliQ9WUD1
SMRiQ9WUD1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207969, 49 interactors
DIPiDIP-29751N
IntActiQ9WUD1, 16 interactors
MINTiQ9WUD1
STRINGi10090.ENSMUSP00000040431

PTM databases

iPTMnetiQ9WUD1
PhosphoSitePlusiQ9WUD1

Proteomic databases

EPDiQ9WUD1
jPOSTiQ9WUD1
MaxQBiQ9WUD1
PaxDbiQ9WUD1
PeptideAtlasiQ9WUD1
PRIDEiQ9WUD1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615
GeneIDi56424
KEGGimmu:56424
UCSCiuc008bcf.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10273
MGIiMGI:1891731 Stub1

Phylogenomic databases

eggNOGiKOG4642 Eukaryota
ENOG410ZC2R LUCA
GeneTreeiENSGT00930000151045
HOGENOMiHOG000163725
HOVERGENiHBG053046
InParanoidiQ9WUD1
KOiK09561
OMAiQERVVPD
OrthoDBi1422450at2759
PhylomeDBiQ9WUD1
TreeFamiTF313937

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-MMU-2173788 Downregulation of TGF-beta receptor signaling
R-MMU-8863795 Downregulation of ERBB2 signaling
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

EvolutionaryTraceiQ9WUD1

Protein Ontology

More...PROi		PR:Q9WUD1

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000039615 Expressed in 39 organ(s), highest expression level in brain
GenevisibleiQ9WUD1 MM

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_MOUSE
<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: Q9WUD1
Secondary accession number(s): Q9DCJ0
<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: November 1, 1999
Last modified: February 13, 2019
This is version 173 of the entry and version 1 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

<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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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