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P53995

- APC1_MOUSE

UniProt

P53995 - APC1_MOUSE

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Protein

Anaphase-promoting complex subunit 1

Gene
Anapc1, Mcpr, Tsg24
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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.

Pathwayi

GO - Molecular functioni

  1. protein binding Source: MGI

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. protein K11-linked ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_205250. Phosphorylation of the APC/C.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
UniPathwayiUPA00143.

Names & Taxonomyi

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
Gene namesi
Name:Anapc1
Synonyms:Mcpr, Tsg24
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:103097. Anapc1.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: UniProtKB
  2. nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19441944Anaphase-promoting complex subunit 1PRO_0000215872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511Phosphoserine By similarity
Modified residuei60 – 601Phosphoserine By similarity
Modified residuei291 – 2911Phosphothreonine By similarity
Modified residuei341 – 3411Phosphoserine By similarity
Modified residuei355 – 3551Phosphoserine By similarity
Modified residuei362 – 3621Phosphoserine By similarity
Modified residuei373 – 3731Phosphoserine By similarity
Modified residuei377 – 3771Phosphoserine By similarity
Modified residuei537 – 5371Phosphothreonine By similarity
Modified residuei547 – 5471Phosphoserine By similarity
Modified residuei555 – 5551Phosphoserine By similarity
Modified residuei571 – 5711Phosphotyrosine By similarity
Modified residuei686 – 6861Phosphoserine By similarity
Modified residuei688 – 6881Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53995.
PaxDbiP53995.
PRIDEiP53995.

PTM databases

PhosphoSiteiP53995.

Expressioni

Tissue specificityi

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

Developmental stagei

Uniformly expressed throughout interphase of the cell cycle.

Gene expression databases

ArrayExpressiP53995.
BgeeiP53995.
CleanExiMM_ANAPC1.
GenevestigatoriP53995.

Interactioni

Subunit structurei

The APC/C is composed of at least 12 subunits By similarity.

Protein-protein interaction databases

BioGridi201352. 14 interactions.
IntActiP53995. 1 interaction.
MINTiMINT-4087721.
STRINGi10090.ENSMUSP00000014499.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1297 – 132529PC 1Add
BLAST
Repeati1366 – 140439PC 2Add
BLAST
Repeati1467 – 150135PC 3Add
BLAST
Repeati1520 – 155233PC 4Add
BLAST

Sequence similaritiesi

Belongs to the APC1 family.
Contains 4 PC repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG316940.
GeneTreeiENSGT00390000016757.
HOGENOMiHOG000231934.
HOVERGENiHBG045326.
InParanoidiA2ATQ4.
KOiK03348.
OMAiLAWTRNF.
OrthoDBiEOG77WWCQ.
TreeFamiTF105441.

Family and domain databases

InterProiIPR024990. Apc1.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PANTHERiPTHR12827. PTHR12827. 1 hit.
PfamiPF12859. Apc1. 1 hit.
PF01851. PC_rep. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53995-1 [UniParc]FASTAAdd to Basket

« Hide

MSNFSEERAT MIAAGDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS     50
SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGDAADYD EELYVAGNMV 100
IWSKGSKSQA LAVYKAFTVD STVQQALWCD FIISQDKSEK IYKSHELEKC 150
ICILQSSCMN MHSIDGKDYI ASLPFQVANV WATKYGLLFE RCSSSHEVPP 200
SLPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV DPAVKIVFLN 250
IDPSIVMTYD AVQNVHSVWT LRRVKPEEEN AVLKFPEQAG TLQNATTSSS 300
LTAHLRSLSK GESPVASPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL 350
SRAHSPALGV HSFSGAQRFN LSSHSQSPKR HSISHSPSGS FNDSFLAPET 400
EPIVPELCID HLWTETLPNI REKNSQASKV FITTDLCGQK FLCFLVEAQL 450
QLRCVKFQES NDKTQLIFGS VTNIHAKDAA PVEKIHTMLV LEGNGNLVLY 500
TGVVRVGKVF IPGLPAPSLT MSNMMPRPST PLDGVGTPKP LSKLLGSMDE 550
VVLLSPVPEL RDSSKLNDSL YNEDCTFQQL GTYIHSVRDP VHNRVTLELS 600
NGSMVRITIP EVATSELVQT CLQAIKFILP KEVAIQVLVK WYNVHSAPGG 650
PSCHSEWSLF VICLLNMMGY NTDRLAWTRS FDFEGSLSPV IAPKKARPSD 700
TGSDEDWEYL LNSEYHRNVE SHLLNKSLCL TALEVSNAKD EDFSQNLSLD 750
SSTLLFAHIP AIFFVLHLVY EELKLNTLMG EGICSLIDLL VQLARDLKLD 800
SYLDHYYRDS PTLVKTTGQV CTIDQGQMGF MHHPPFFTSE PPSIYQWVSS 850
CLKGEGMPPY PYLPGICERS RLVVLSIALY TLGDESCVSD ETCQYLSKVT 900
STPQKPQAEQ EENRFTFRHS ASVSVLAERL VVWMASVGFT LRDLETLPFG 950
IALPIRDAIY HCREQPDSDW SEAVCLLIGR QDLSKQACEG NLPRGKSVLS 1000
SEVSSGTEAE EEDDGMNDLN HEVMSLIWSE DLRVQDVRRL LQSAQPVRVN 1050
VVQYPELSDH EFIEEKENRL LQLCQRTMAL PVGRGMFTLF SYHPVPTEPL 1100
PVPKLNLTGR APPRNTTVDL NSGNIDVPPN MASWASFHNG VAAGLKIAPA 1150
SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG 1200
HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HVPALLPPTS TELDVPHNVQ 1250
VAAVVGIGLV YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL 1300
ALGMVCLGHG SNLIGMSDLN VPEQLYQYMV GGHRRFQTGM HREKHKSPSY 1350
QIKEGDTINV DVTCPGATLA LAMIYLKTNN RSIADWLRAP DTMYLLDFVK 1400
PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS LSEIELPCSE 1450
DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFSCLHK FAKDFMNYLS 1500
APNASVTGPY NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM 1550
NYGFHLAHHM ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR 1600
YHLQALRHLY VLAAEPRLLV PVDVDTNTPC YALIEVTYKG TQWYEQTKEE 1650
LMAPTLLPEL HLLKQMKVKG PRYWELLIDL SKGEQHLRSI LSKDGVLYVK 1700
LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISS FTSDPALLSF 1750
AEYFCKPTVS MGPKQEILDL FSSILYECVA QETPEMLPAY IAMDQALRSL 1800
KKRDMSDTSD LWQIKLILEF FSSRSHQDRQ HTYPKRGLFI NSEFLPVVKC 1850
TVDATLDQWL QAGGDVCVHA YLSGQPVEKS QLNMLACFLV YHSVPAPRHL 1900
PPMGLEGSTS FAELLYRFRH LKMPVRALLR LAPVLLGNPQ PMVM 1944
Length:1,944
Mass (Da):215,994
Last modified:July 27, 2011 - v2
Checksum:i596DD3FC07CDA321
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121A → Q in CAA56450. 1 Publication
Sequence conflicti348 – 3492AA → GV in CAA56450. 1 Publication
Sequence conflicti643 – 6431N → K in BAC34976. 1 Publication
Sequence conflicti1036 – 10361D → H in CAA56450. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS16715.1.
PIRi A55117.
RefSeqi NP_032595.2. NM_008569.2.
UniGenei Mm.277408.
Mm.449185.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201352. 14 interactions.
IntActi P53995. 1 interaction.
MINTi MINT-4087721.
STRINGi 10090.ENSMUSP00000014499.

PTM databases

PhosphoSitei P53995.

Proteomic databases

MaxQBi P53995.
PaxDbi P53995.
PRIDEi P53995.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000014499 ; ENSMUSP00000014499 ; ENSMUSG00000014355 .
GeneIDi 17222.
KEGGi mmu:17222.
UCSCi uc008mgq.2. mouse.

Organism-specific databases

CTDi 64682.
MGIi MGI:103097. Anapc1.

Phylogenomic databases

eggNOGi NOG316940.
GeneTreei ENSGT00390000016757.
HOGENOMi HOG000231934.
HOVERGENi HBG045326.
InParanoidi A2ATQ4.
KOi K03348.
OMAi LAWTRNF.
OrthoDBi EOG77WWCQ.
TreeFami TF105441.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_205250. Phosphorylation of the APC/C.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

Miscellaneous databases

NextBioi 291630.
PROi P53995.
SOURCEi Search...

Gene expression databases

ArrayExpressi P53995.
Bgeei P53995.
CleanExi MM_ANAPC1.
Genevestigatori P53995.

Family and domain databases

InterProi IPR024990. Apc1.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view ]
PANTHERi PTHR12827. PTHR12827. 1 hit.
Pfami PF12859. Apc1. 1 hit.
PF01851. PC_rep. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel murine gene encoding a 216-kDa protein is related to a mitotic checkpoint regulator previously identified in Aspergillus nidulans."
    Starborg M., Brundell E., Gell K., Hoeoeg C.
    J. Biol. Chem. 269:24133-24137(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CBA.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1063.
    Strain: C57BL/6J.
    Tissue: Embryonic lung and Forelimb.

Entry informationi

Entry nameiAPC1_MOUSE
AccessioniPrimary (citable) accession number: P53995
Secondary accession number(s): A2ATQ4, Q8BP33, Q8C772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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