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 - P53995 (APC1_MOUSE)

Protein

Anaphase-promoting complex subunit 1

Gene

Anapc1

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

Annotation score:4 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 - 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 1
Short name:
APC1
Alternative name(s):
Cyclosome subunit 1
Mitotic checkpoint regulator
Testis-specific gene 24 protein
<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:Anapc1
Synonyms:Mcpr, Tsg24
<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 2

Organism-specific databases

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

More...MGIi		MGI:103097 Anapc1

<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

<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_00002158721 – 1944Anaphase-promoting complex subunit 1Add BLAST1944

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 residuei51PhosphoserineBy similarity1
Modified residuei60PhosphoserineBy similarity1
Modified residuei291PhosphothreonineBy similarity1
Modified residuei313PhosphoserineBy similarity1
Modified residuei341PhosphoserineBy similarity1
Modified residuei343PhosphoserineBy similarity1
Modified residuei355PhosphoserineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei373PhosphoserineBy similarity1
Modified residuei377PhosphoserineCombined sources1
Modified residuei537PhosphothreonineBy similarity1
Modified residuei547PhosphoserineCombined sources1
Modified residuei555PhosphoserineBy similarity1
Modified residuei571PhosphotyrosineBy similarity1
Modified residuei680PhosphoserineCombined sources1
Modified residuei686PhosphoserineBy similarity1
Modified residuei688PhosphoserineCombined 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

Phosphorylated. Phosphorylation on Ser-355 occurs specifically during mitosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P53995

MaxQB - The MaxQuant DataBase

More...MaxQBi		P53995

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

More...PaxDbi		P53995

PRoteomics IDEntifications database

More...PRIDEi		P53995

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P53995

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

More...PhosphoSitePlusi		P53995

<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

Abundantly expressed in proliferating fibroblasts, juvenile testis, adult brain and epididymis.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Uniformly expressed throughout interphase of the cell cycle.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000014355 Expressed in 289 organ(s), highest expression level in embryonic stem cell

CleanEx database of gene expression profiles

More...CleanExi		MM_ANAPC1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P53995 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P53995 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

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		201352, 15 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P53995

Protein interaction database and analysis system

More...IntActi		P53995, 2 interactors

Molecular INTeraction database

More...MINTi		P53995

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000014499

<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		P53995

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>Repeati1297 – 1325PC 1Add BLAST29
Repeati1366 – 1404PC 2Add BLAST39
Repeati1467 – 1501PC 3Add BLAST35
Repeati1520 – 1552PC 4Add BLAST33

<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 APC1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1858 Eukaryota
ENOG410XQ83 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000016757

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231934

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG045326

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P53995

KEGG Orthology (KO)

More...KOi		K03348

Identification of Orthologs from Complete Genome Data

More...OMAi		AIAEWMQ

Database of Orthologous Groups

More...OrthoDBi		EOG091G00RP

TreeFam database of animal gene trees

More...TreeFami		TF105441

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR024990 Apc1
IPR002015 Proteasome/cyclosome_rpt

The PANTHER Classification System

More...PANTHERi		PTHR12827 PTHR12827, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12859 ANAPC1, 1 hit
PF01851 PC_rep, 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

P53995-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNFSEERAT MIAAGDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS 
        60         70         80         90        100
SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGDAADYD EELYVAGNMV 
       110        120        130        140        150
IWSKGSKSQA LAVYKAFTVD STVQQALWCD FIISQDKSEK IYKSHELEKC 
       160        170        180        190        200
ICILQSSCMN MHSIDGKDYI ASLPFQVANV WATKYGLLFE RCSSSHEVPP 
       210        220        230        240        250
SLPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV DPAVKIVFLN 
       260        270        280        290        300
IDPSIVMTYD AVQNVHSVWT LRRVKPEEEN AVLKFPEQAG TLQNATTSSS 
       310        320        330        340        350
LTAHLRSLSK GESPVASPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL 
       360        370        380        390        400
SRAHSPALGV HSFSGAQRFN LSSHSQSPKR HSISHSPSGS FNDSFLAPET 
       410        420        430        440        450
EPIVPELCID HLWTETLPNI REKNSQASKV FITTDLCGQK FLCFLVEAQL 
       460        470        480        490        500
QLRCVKFQES NDKTQLIFGS VTNIHAKDAA PVEKIHTMLV LEGNGNLVLY 
       510        520        530        540        550
TGVVRVGKVF IPGLPAPSLT MSNMMPRPST PLDGVGTPKP LSKLLGSMDE 
       560        570        580        590        600
VVLLSPVPEL RDSSKLNDSL YNEDCTFQQL GTYIHSVRDP VHNRVTLELS 
       610        620        630        640        650
NGSMVRITIP EVATSELVQT CLQAIKFILP KEVAIQVLVK WYNVHSAPGG 
       660        670        680        690        700
PSCHSEWSLF VICLLNMMGY NTDRLAWTRS FDFEGSLSPV IAPKKARPSD 
       710        720        730        740        750
TGSDEDWEYL LNSEYHRNVE SHLLNKSLCL TALEVSNAKD EDFSQNLSLD 
       760        770        780        790        800
SSTLLFAHIP AIFFVLHLVY EELKLNTLMG EGICSLIDLL VQLARDLKLD 
       810        820        830        840        850
SYLDHYYRDS PTLVKTTGQV CTIDQGQMGF MHHPPFFTSE PPSIYQWVSS 
       860        870        880        890        900
CLKGEGMPPY PYLPGICERS RLVVLSIALY TLGDESCVSD ETCQYLSKVT 
       910        920        930        940        950
STPQKPQAEQ EENRFTFRHS ASVSVLAERL VVWMASVGFT LRDLETLPFG 
       960        970        980        990       1000
IALPIRDAIY HCREQPDSDW SEAVCLLIGR QDLSKQACEG NLPRGKSVLS 
      1010       1020       1030       1040       1050
SEVSSGTEAE EEDDGMNDLN HEVMSLIWSE DLRVQDVRRL LQSAQPVRVN 
      1060       1070       1080       1090       1100
VVQYPELSDH EFIEEKENRL LQLCQRTMAL PVGRGMFTLF SYHPVPTEPL 
      1110       1120       1130       1140       1150
PVPKLNLTGR APPRNTTVDL NSGNIDVPPN MASWASFHNG VAAGLKIAPA 
      1160       1170       1180       1190       1200
SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG 
      1210       1220       1230       1240       1250
HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HVPALLPPTS TELDVPHNVQ 
      1260       1270       1280       1290       1300
VAAVVGIGLV YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL 
      1310       1320       1330       1340       1350
ALGMVCLGHG SNLIGMSDLN VPEQLYQYMV GGHRRFQTGM HREKHKSPSY 
      1360       1370       1380       1390       1400
QIKEGDTINV DVTCPGATLA LAMIYLKTNN RSIADWLRAP DTMYLLDFVK 
      1410       1420       1430       1440       1450
PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS LSEIELPCSE 
      1460       1470       1480       1490       1500
DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFSCLHK FAKDFMNYLS 
      1510       1520       1530       1540       1550
APNASVTGPY NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM 
      1560       1570       1580       1590       1600
NYGFHLAHHM ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR 
      1610       1620       1630       1640       1650
YHLQALRHLY VLAAEPRLLV PVDVDTNTPC YALIEVTYKG TQWYEQTKEE 
      1660       1670       1680       1690       1700
LMAPTLLPEL HLLKQMKVKG PRYWELLIDL SKGEQHLRSI LSKDGVLYVK 
      1710       1720       1730       1740       1750
LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISS FTSDPALLSF 
      1760       1770       1780       1790       1800
AEYFCKPTVS MGPKQEILDL FSSILYECVA QETPEMLPAY IAMDQALRSL 
      1810       1820       1830       1840       1850
KKRDMSDTSD LWQIKLILEF FSSRSHQDRQ HTYPKRGLFI NSEFLPVVKC 
      1860       1870       1880       1890       1900
TVDATLDQWL QAGGDVCVHA YLSGQPVEKS QLNMLACFLV YHSVPAPRHL 
      1910       1920       1930       1940 
PPMGLEGSTS FAELLYRFRH LKMPVRALLR LAPVLLGNPQ PMVM
Length:1,944
Mass (Da):215,994
Last modified:July 27, 2011 - 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:i596DD3FC07CDA321
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
A2ATQ5A2ATQ5_MOUSE
Anaphase-promoting complex subunit ...
Anapc1
1,213Annotation 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>
Q6PG65Q6PG65_MOUSE
Anapc1 protein
Anapc1
80Annotation 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 conflicti112A → Q in CAA56450 (PubMed:7929068).Curated1
Sequence conflicti348 – 349AA → GV in CAA56450 (PubMed:7929068).Curated2
Sequence conflicti643N → K in BAC34976 (PubMed:16141072).Curated1
Sequence conflicti1036D → H in CAA56450 (PubMed:7929068).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
X80169 mRNA Translation: CAA56450.1
AL928910 Genomic DNA Translation: CAM25161.1
CH466519 Genomic DNA Translation: EDL28216.1
BC139002 mRNA Translation: AAI39003.1
AK052404 mRNA Translation: BAC34976.1
AK077847 mRNA Translation: BAC37032.2

The Consensus CDS (CCDS) project

More...CCDSi		CCDS16715.1

Protein sequence database of the Protein Information Resource

More...PIRi		A55117

NCBI Reference Sequences

More...RefSeqi		NP_032595.2, NM_008569.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.277408
Mm.449185

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000014499; ENSMUSP00000014499; ENSMUSG00000014355

Database of genes from NCBI RefSeq genomes

More...GeneIDi		17222

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:17222

UCSC genome browser

More...UCSCi		uc008mgq.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
X80169 mRNA Translation: CAA56450.1
AL928910 Genomic DNA Translation: CAM25161.1
CH466519 Genomic DNA Translation: EDL28216.1
BC139002 mRNA Translation: AAI39003.1
AK052404 mRNA Translation: BAC34976.1
AK077847 mRNA Translation: BAC37032.2
CCDSiCCDS16715.1
PIRiA55117
RefSeqiNP_032595.2, NM_008569.2
UniGeneiMm.277408
Mm.449185

3D structure databases

ProteinModelPortaliP53995
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201352, 15 interactors
CORUMiP53995
IntActiP53995, 2 interactors
MINTiP53995
STRINGi10090.ENSMUSP00000014499

PTM databases

iPTMnetiP53995
PhosphoSitePlusiP53995

Proteomic databases

EPDiP53995
MaxQBiP53995
PaxDbiP53995
PRIDEiP53995

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014499; ENSMUSP00000014499; ENSMUSG00000014355
GeneIDi17222
KEGGimmu:17222
UCSCiuc008mgq.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		64682
MGIiMGI:103097 Anapc1

Phylogenomic databases

eggNOGiKOG1858 Eukaryota
ENOG410XQ83 LUCA
GeneTreeiENSGT00390000016757
HOGENOMiHOG000231934
HOVERGENiHBG045326
InParanoidiP53995
KOiK03348
OMAiAIAEWMQ
OrthoDBiEOG091G00RP
TreeFamiTF105441

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:P53995

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000014355 Expressed in 289 organ(s), highest expression level in embryonic stem cell
CleanExiMM_ANAPC1
ExpressionAtlasiP53995 baseline and differential
GenevisibleiP53995 MM

Family and domain databases

InterProiView protein in InterPro
IPR024990 Apc1
IPR002015 Proteasome/cyclosome_rpt
PANTHERiPTHR12827 PTHR12827, 1 hit
PfamiView protein in Pfam
PF12859 ANAPC1, 1 hit
PF01851 PC_rep, 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 nameiAPC1_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: P53995
Secondary accession number(s): A2ATQ4, Q8BP33, Q8C772
<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 1, 1996
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 131 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

<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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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