APC1_MOUSE
ID APC1_MOUSE Reviewed; 1944 AA.
AC P53995; A2ATQ4; Q8BP33; Q8C772;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Anaphase-promoting complex subunit 1;
DE Short=APC1;
DE AltName: Full=Cyclosome subunit 1;
DE AltName: Full=Mitotic checkpoint regulator;
DE AltName: Full=Testis-specific gene 24 protein;
GN Name=Anapc1; Synonyms=Mcpr, Tsg24;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CBA/J; TISSUE=Testis;
RX PubMed=7929068; DOI=10.1016/s0021-9258(19)51058-4;
RA Starborg M., Brundell E., Gell K., Hoeoeg C.;
RT "A novel murine gene encoding a 216-kDa protein is related to a mitotic
RT checkpoint regulator previously identified in Aspergillus nidulans.";
RL J. Biol. Chem. 269:24133-24137(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1063.
RC STRAIN=C57BL/6J; TISSUE=Embryonic lung, and Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-547; SER-680 AND
RP SER-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. {ECO:0000250|UniProtKB:Q9H1A4}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in proliferating fibroblasts,
CC juvenile testis, adult brain and epididymis.
CC -!- DEVELOPMENTAL STAGE: Uniformly expressed throughout interphase of the
CC cell cycle.
CC -!- PTM: Phosphorylated. Phosphorylation on Ser-355 occurs specifically
CC during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APC1 family. {ECO:0000305}.
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DR EMBL; X80169; CAA56450.1; -; mRNA.
DR EMBL; AL928910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28216.1; -; Genomic_DNA.
DR EMBL; BC139002; AAI39003.1; -; mRNA.
DR EMBL; AK052404; BAC34976.1; -; mRNA.
DR EMBL; AK077847; BAC37032.2; -; mRNA.
DR CCDS; CCDS16715.1; -.
DR PIR; A55117; A55117.
DR RefSeq; NP_032595.2; NM_008569.2.
DR AlphaFoldDB; P53995; -.
DR SMR; P53995; -.
DR BioGRID; 201352; 22.
DR CORUM; P53995; -.
DR IntAct; P53995; 1.
DR STRING; 10090.ENSMUSP00000014499; -.
DR iPTMnet; P53995; -.
DR PhosphoSitePlus; P53995; -.
DR EPD; P53995; -.
DR jPOST; P53995; -.
DR MaxQB; P53995; -.
DR PaxDb; P53995; -.
DR PRIDE; P53995; -.
DR ProteomicsDB; 281825; -.
DR Antibodypedia; 18056; 554 antibodies from 36 providers.
DR DNASU; 17222; -.
DR Ensembl; ENSMUST00000014499; ENSMUSP00000014499; ENSMUSG00000014355.
DR GeneID; 17222; -.
DR KEGG; mmu:17222; -.
DR UCSC; uc008mgq.2; mouse.
DR CTD; 64682; -.
DR MGI; MGI:103097; Anapc1.
DR VEuPathDB; HostDB:ENSMUSG00000014355; -.
DR eggNOG; KOG1858; Eukaryota.
DR GeneTree; ENSGT00390000016757; -.
DR HOGENOM; CLU_001202_1_0_1; -.
DR InParanoid; P53995; -.
DR OMA; MQPPDSR; -.
DR OrthoDB; 738153at2759; -.
DR PhylomeDB; P53995; -.
DR TreeFam; TF105441; -.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 17222; 22 hits in 72 CRISPR screens.
DR ChiTaRS; Anapc1; mouse.
DR PRO; PR:P53995; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P53995; protein.
DR Bgee; ENSMUSG00000014355; Expressed in metanephric loop of Henle and 261 other tissues.
DR ExpressionAtlas; P53995; baseline and differential.
DR Genevisible; P53995; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR024990; Apc1.
DR InterPro; IPR041221; APC1_C.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR PANTHER; PTHR12827; PTHR12827; 1.
DR Pfam; PF12859; ANAPC1; 1.
DR Pfam; PF18122; APC1_C; 1.
DR Pfam; PF01851; PC_rep; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway.
FT CHAIN 1..1944
FT /note="Anaphase-promoting complex subunit 1"
FT /id="PRO_0000215872"
FT REPEAT 1297..1325
FT /note="PC 1"
FT REPEAT 1366..1404
FT /note="PC 2"
FT REPEAT 1467..1501
FT /note="PC 3"
FT REPEAT 1520..1552
FT /note="PC 4"
FT REGION 312..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 571
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1A4"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 112
FT /note="A -> Q (in Ref. 1; CAA56450)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..349
FT /note="AA -> GV (in Ref. 1; CAA56450)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="N -> K (in Ref. 5; BAC34976)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="D -> H (in Ref. 1; CAA56450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1944 AA; 215994 MW; 596DD3FC07CDA321 CRC64;
MSNFSEERAT MIAAGDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS
LQEVTIHEKQ KESWQLRKGV SEIGDAADYD EELYVAGNMV IWSKGSKSQA LAVYKAFTVD
STVQQALWCD FIISQDKSEK IYKSHELEKC ICILQSSCMN MHSIDGKDYI ASLPFQVANV
WATKYGLLFE RCSSSHEVPP SLPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV
DPAVKIVFLN IDPSIVMTYD AVQNVHSVWT LRRVKPEEEN AVLKFPEQAG TLQNATTSSS
LTAHLRSLSK GESPVASPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL SRAHSPALGV
HSFSGAQRFN LSSHSQSPKR HSISHSPSGS FNDSFLAPET EPIVPELCID HLWTETLPNI
REKNSQASKV FITTDLCGQK FLCFLVEAQL QLRCVKFQES NDKTQLIFGS VTNIHAKDAA
PVEKIHTMLV LEGNGNLVLY TGVVRVGKVF IPGLPAPSLT MSNMMPRPST PLDGVGTPKP
LSKLLGSMDE VVLLSPVPEL RDSSKLNDSL YNEDCTFQQL GTYIHSVRDP VHNRVTLELS
NGSMVRITIP EVATSELVQT CLQAIKFILP KEVAIQVLVK WYNVHSAPGG PSCHSEWSLF
VICLLNMMGY NTDRLAWTRS FDFEGSLSPV IAPKKARPSD TGSDEDWEYL LNSEYHRNVE
SHLLNKSLCL TALEVSNAKD EDFSQNLSLD SSTLLFAHIP AIFFVLHLVY EELKLNTLMG
EGICSLIDLL VQLARDLKLD SYLDHYYRDS PTLVKTTGQV CTIDQGQMGF MHHPPFFTSE
PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY TLGDESCVSD ETCQYLSKVT
STPQKPQAEQ EENRFTFRHS ASVSVLAERL VVWMASVGFT LRDLETLPFG IALPIRDAIY
HCREQPDSDW SEAVCLLIGR QDLSKQACEG NLPRGKSVLS SEVSSGTEAE EEDDGMNDLN
HEVMSLIWSE DLRVQDVRRL LQSAQPVRVN VVQYPELSDH EFIEEKENRL LQLCQRTMAL
PVGRGMFTLF SYHPVPTEPL PVPKLNLTGR APPRNTTVDL NSGNIDVPPN MASWASFHNG
VAAGLKIAPA SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG
HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HVPALLPPTS TELDVPHNVQ VAAVVGIGLV
YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL ALGMVCLGHG SNLIGMSDLN
VPEQLYQYMV GGHRRFQTGM HREKHKSPSY QIKEGDTINV DVTCPGATLA LAMIYLKTNN
RSIADWLRAP DTMYLLDFVK PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS
LSEIELPCSE DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFSCLHK FAKDFMNYLS
APNASVTGPY NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM NYGFHLAHHM
ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR YHLQALRHLY VLAAEPRLLV
PVDVDTNTPC YALIEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQMKVKG PRYWELLIDL
SKGEQHLRSI LSKDGVLYVK LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISS
FTSDPALLSF AEYFCKPTVS MGPKQEILDL FSSILYECVA QETPEMLPAY IAMDQALRSL
KKRDMSDTSD LWQIKLILEF FSSRSHQDRQ HTYPKRGLFI NSEFLPVVKC TVDATLDQWL
QAGGDVCVHA YLSGQPVEKS QLNMLACFLV YHSVPAPRHL PPMGLEGSTS FAELLYRFRH
LKMPVRALLR LAPVLLGNPQ PMVM
