Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9WVM3 (APC7_MOUSE)

Entry version 149 (10 Apr 2019)
Sequence version 3 (03 Oct 2003)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Anaphase-promoting complex subunit 7

Gene

Anapc7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:3 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

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).By similarity

<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.
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

Biological processCell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-MMU-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-176407 Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
R-MMU-176408 Regulation of APC/C activators between G1/S and early anaphase
R-MMU-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-MMU-176412 Phosphorylation of the APC/C
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
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:
Anaphase-promoting complex subunit 7
Short name:
APC7
Alternative name(s):
Cyclosome subunit 7
Prediabetic NOD sera-reactive autoantigen
<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:Anapc7
Synonyms:Apc7
<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 5

Organism-specific databases

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

More...MGIi		MGI:1929711 Anapc7

<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 & Seán O’Donoghue; Source: COMPARTMENTS

<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_00001062621 – 565Anaphase-promoting complex subunit 7Add BLAST565

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei229N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9WVM3

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9WVM3

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

More...PaxDbi		Q9WVM3

PRoteomics IDEntifications database

More...PRIDEi		Q9WVM3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9WVM3

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

More...PhosphoSitePlusi		Q9WVM3

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000029466 Expressed in 275 organ(s), highest expression level in ear vesicle

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9WVM3 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9WVM3 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

V-shaped homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5.By similarity

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		207898, 6 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9WVM3

Protein interaction database and analysis system

More...IntActi		Q9WVM3, 3 interactors

Molecular INTeraction database

More...MINTi		Q9WVM3

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000113928

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9WVM3

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

More...SMRi		Q9WVM3

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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>Repeati101 – 134TPR 1Add BLAST34
Repeati169 – 202TPR 2Add BLAST34
Repeati203 – 236TPR 3Add BLAST34
Repeati237 – 270TPR 4Add BLAST34
Repeati339 – 372TPR 5Add BLAST34
Repeati373 – 406TPR 6Add BLAST34
Repeati407 – 439TPR 7Add BLAST33
Repeati442 – 474TPR 8Add BLAST33
Repeati475 – 508TPR 9Add BLAST34
Repeati509 – 531TPR 10Add BLAST23

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the APC7 family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1174 Eukaryota
ENOG410XS2B LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182950

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000007393

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG050529

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9WVM3

KEGG Orthology (KO)

More...KOi		K03354

Identification of Orthologs from Complete Genome Data

More...OMAi		CYEGLID

Database of Orthologous Groups

More...OrthoDBi		808566at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9WVM3

TreeFam database of animal gene trees

More...TreeFami		TF105445

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.10, 3 hits

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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13181 TPR_8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00028 TPR, 5 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48452 SSF48452, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50005 TPR, 5 hits
PS50293 TPR_REGION, 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9WVM3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVIDHVRDM AAAGLHSNVR LLSSLLLTMS NNNPELFSPS QKYQLLVYHA 
        60         70         80         90        100
DSLFHDKEYR NAVSKYAMAL QQKKALSKTS KVRPSTGNSA STPQSQCLPS 
       110        120        130        140        150
EIEVKYKMAE CYTMLKLDKD AIAVLDGIPS RQRTPKINMM LANLYKKAGQ 
       160        170        180        190        200
ERPSVTSYKE VLRQCPLALD AILGLLSLSV KGAEVASMTM NVIQTVPNLD 
       210        220        230        240        250
WLSVWIKAYA FVHTGDNSRA INTICSLEKK SLLRDNVDLL GSLADLYFRA 
       260        270        280        290        300
GDSKNSVLKF EQAQMLDPYL IRGMDVYGYL LAREGRLEDV ENLGCRLFNI 
       310        320        330        340        350
SDQHAEPWVV SGCHSFYSKR YSRALYLGAK AIQLNSNSVQ ALLLKGAALR 
       360        370        380        390        400
NMGRVQEAII HFREAIRLAP CRLDCYEGLI ECYLASNSIR EAMVMANNVY 
       410        420        430        440        450
KTLGANAQTL TLLATVCLED PVTQEKAKTL LDKALAQRPD YVKAVVKKAE 
       460        470        480        490        500
LLSREQKYED GIALLRNALA NQSDCVLHRI LGDFLVAVNE YQEAMDQYSI 
       510        520        530        540        550
ALSLDPNDQK SLEGMQKMEK EESPTDATQE EDVDDMEGSG EEGDLEGSDS 
       560 
EAAQWADQEQ WFGMQ
Length:565
Mass (Da):63,021
Last modified:October 3, 2003 - v3
<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:iF7DFB8D45FDCD639
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YU58D3YU58_MOUSE
Anaphase-promoting complex subunit ...
Anapc7
503Annotation 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>
F6WXH0F6WXH0_MOUSE
Anaphase-promoting complex subunit ...
Anapc7
58Annotation 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 conflicti156T → A in AAD39343 (PubMed:10515598).Curated1
Sequence conflicti188M → T in AAD39343 (PubMed:10515598).Curated1
Sequence conflicti288E → K in BAC27131 (PubMed:16141072).Curated1
Sequence conflicti340Q → K in BAC27131 (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
AF076607 mRNA Translation: AAD39343.2
AK030775 mRNA Translation: BAC27131.1
AK150764 mRNA Translation: BAE29831.1
AK150891 mRNA Translation: BAE29937.1
AK153114 mRNA Translation: BAE31731.1
AK159523 mRNA Translation: BAE35152.1
AK164202 mRNA Translation: BAE37680.1
BC006635 mRNA Translation: AAH06635.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS19649.1

NCBI Reference Sequences

More...RefSeqi		NP_062779.3, NM_019805.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.37341

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000031422; ENSMUSP00000031422; ENSMUSG00000029466
ENSMUST00000122010; ENSMUSP00000113928; ENSMUSG00000029466

Database of genes from NCBI RefSeq genomes

More...GeneIDi		56317

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:56317

UCSC genome browser

More...UCSCi		uc008zlh.2 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
AF076607 mRNA Translation: AAD39343.2
AK030775 mRNA Translation: BAC27131.1
AK150764 mRNA Translation: BAE29831.1
AK150891 mRNA Translation: BAE29937.1
AK153114 mRNA Translation: BAE31731.1
AK159523 mRNA Translation: BAE35152.1
AK164202 mRNA Translation: BAE37680.1
BC006635 mRNA Translation: AAH06635.1
CCDSiCCDS19649.1
RefSeqiNP_062779.3, NM_019805.4
UniGeneiMm.37341

3D structure databases

ProteinModelPortaliQ9WVM3
SMRiQ9WVM3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207898, 6 interactors
CORUMiQ9WVM3
IntActiQ9WVM3, 3 interactors
MINTiQ9WVM3
STRINGi10090.ENSMUSP00000113928

PTM databases

iPTMnetiQ9WVM3
PhosphoSitePlusiQ9WVM3

Proteomic databases

EPDiQ9WVM3
MaxQBiQ9WVM3
PaxDbiQ9WVM3
PRIDEiQ9WVM3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031422; ENSMUSP00000031422; ENSMUSG00000029466
ENSMUST00000122010; ENSMUSP00000113928; ENSMUSG00000029466
GeneIDi56317
KEGGimmu:56317
UCSCiuc008zlh.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		51434
MGIiMGI:1929711 Anapc7

Phylogenomic databases

eggNOGiKOG1174 Eukaryota
ENOG410XS2B LUCA
GeneTreeiENSGT00950000182950
HOGENOMiHOG000007393
HOVERGENiHBG050529
InParanoidiQ9WVM3
KOiK03354
OMAiCYEGLID
OrthoDBi808566at2759
PhylomeDBiQ9WVM3
TreeFamiTF105445

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-MMU-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-MMU-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-176407 Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
R-MMU-176408 Regulation of APC/C activators between G1/S and early anaphase
R-MMU-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-MMU-176412 Phosphorylation of the APC/C
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9WVM3

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000029466 Expressed in 275 organ(s), highest expression level in ear vesicle
ExpressionAtlasiQ9WVM3 baseline and differential
GenevisibleiQ9WVM3 MM

Family and domain databases

Gene3Di1.25.40.10, 3 hits
InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
PfamiView protein in Pfam
PF13181 TPR_8, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 5 hits
SUPFAMiSSF48452 SSF48452, 2 hits
PROSITEiView protein in PROSITE
PS50005 TPR, 5 hits
PS50293 TPR_REGION, 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 nameiAPC7_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: Q9WVM3
Secondary accession number(s): Q3UBM7, Q8BSR2, Q91W13
<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 3, 2003
Last sequence update: October 3, 2003
Last modified: April 10, 2019
This is version 149 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again