LOCUS NP_073153 1944 aa linear PRI 27-APR-2025
DEFINITION anaphase-promoting complex subunit 1 [Homo sapiens].
ACCESSION NP_073153 XP_943596
VERSION NP_073153.1
DBSOURCE REFSEQ: accession NM_022662.4
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 1944)
AUTHORS Mann,G., Sulkshane,P., Sadhu,P., Ziv,T., Glickman,M.H. and Brik,A.
TITLE Antibody for Serine 65 Phosphorylated Ubiquitin Identifies
PLK1-Mediated Phosphorylation of Mitotic Proteins and APC1
JOURNAL Molecules 27 (15), 4867 (2022)
PUBMED 35956818
REMARK GeneRIF: Antibody for Serine 65 Phosphorylated Ubiquitin Identifies
PLK1-Mediated Phosphorylation of Mitotic Proteins and APC1.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 1944)
AUTHORS Liess,A.K.L., Kucerova,A., Schweimer,K., Schlesinger,D., Dybkov,O.,
Urlaub,H., Mansfeld,J. and Lorenz,S.
TITLE Dimerization regulates the human APC/C-associated
ubiquitin-conjugating enzyme UBE2S
JOURNAL Sci Signal 13 (654) (2020)
PUBMED 33082289
REMARK GeneRIF: Dimerization regulates the human APC/C-associated
ubiquitin-conjugating enzyme UBE2S.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 1944)
AUTHORS Ajeawung,N.F., Nguyen,T.T.M., Lu,L., Kucharski,T.J., Rousseau,J.,
Molidperee,S., Atienza,J., Gamache,I., Jin,W., Plon,S.E., Lee,B.H.,
Teodoro,J.G., Wang,L.L. and Campeau,P.M.
TITLE Mutations in ANAPC1, Encoding a Scaffold Subunit of the
Anaphase-Promoting Complex, Cause Rothmund-Thomson Syndrome Type 1
JOURNAL Am J Hum Genet 105 (3), 625-630 (2019)
PUBMED 31303264
REMARK GeneRIF: Fibroblast studies showed that the intronic mutation
causes the activation of a 95 bp pseudoexon, leading to mRNAs with
premature termination codons and nonsense-mediated decay, decreased
ANAPC1 protein levels, and prolongation of interphase
REFERENCE 4 (residues 1 to 1944)
AUTHORS Ivarsdottir,E.V., Benonisdottir,S., Thorleifsson,G., Sulem,P.,
Oddsson,A., Styrkarsdottir,U., Kristmundsdottir,S.,
Arnadottir,G.A., Thorgeirsson,G., Jonsdottir,I., Zoega,G.M.,
Thorsteinsdottir,U., Gudbjartsson,D.F., Jonasson,F., Holm,H. and
Stefansson,K.
TITLE Sequence variation at ANAPC1 accounts for 24% of the variability in
corneal endothelial cell density
JOURNAL Nat Commun 10 (1), 1284 (2019)
PUBMED 30894546
REMARK GeneRIF: Sequence variation at ANAPC1 accounts for 24% of the
variability in corneal endothelial cell density.
Publication Status: Online-Only
REFERENCE 5 (residues 1 to 1944)
AUTHORS Watson,E.R., Brown,N.G., Peters,J.M., Stark,H. and Schulman,B.A.
TITLE Posing the APC/C E3 Ubiquitin Ligase to Orchestrate Cell Division
JOURNAL Trends Cell Biol 29 (2), 117-134 (2019)
PUBMED 30482618
REMARK GeneRIF: The anaphase promoting complex/cyclosome (APC/C) E3 ligase
is not simply an interaction hub, but a dynamic, multifunctional
molecular machine whose structure is remodeled by binding partners
to achieve temporal ubiquitylation regulating cell division
[Review].
Review article
REFERENCE 6 (residues 1 to 1944)
AUTHORS Kramer,E.R., Scheuringer,N., Podtelejnikov,A.V., Mann,M. and
Peters,J.M.
TITLE Mitotic regulation of the APC activator proteins CDC20 and CDH1
JOURNAL Mol Biol Cell 11 (5), 1555-1569 (2000)
PUBMED 10793135
REFERENCE 7 (residues 1 to 1944)
AUTHORS Lukas,C., Sorensen,C.S., Kramer,E., Santoni-Rugiu,E., Lindeneg,C.,
Peters,J.M., Bartek,J. and Lukas,J.
TITLE Accumulation of cyclin B1 requires E2F and cyclin-A-dependent
rearrangement of the anaphase-promoting complex
JOURNAL Nature 401 (6755), 815-818 (1999)
PUBMED 10548110
REFERENCE 8 (residues 1 to 1944)
AUTHORS Gieffers,C., Peters,B.H., Kramer,E.R., Dotti,C.G. and Peters,J.M.
TITLE Expression of the CDH1-associated form of the anaphase-promoting
complex in postmitotic neurons
JOURNAL Proc Natl Acad Sci U S A 96 (20), 11317-11322 (1999)
PUBMED 10500174
REFERENCE 9 (residues 1 to 1944)
AUTHORS Grossberger,R., Gieffers,C., Zachariae,W., Podtelejnikov,A.V.,
Schleiffer,A., Nasmyth,K., Mann,M. and Peters,J.M.
TITLE Characterization of the DOC1/APC10 subunit of the yeast and the
human anaphase-promoting complex
JOURNAL J Biol Chem 274 (20), 14500-14507 (1999)
PUBMED 10318877
REFERENCE 10 (residues 1 to 1944)
AUTHORS Wang,L.L. and Plon,S.E.
TITLE Rothmund-Thomson Syndrome
JOURNAL (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
Amemiya A (Eds.);
GENEREVIEWS(R);
(1993)
PUBMED 20301415
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
AC104651.2 and AC093166.6.
On Mar 4, 2006 this sequence version replaced XP_943596.1.
Summary: This gene encodes a subunit of the anaphase-promoting
complex. This complex is an E3 ubiquitin ligase that regulates
progression through the metaphase to anaphase portion of the cell
cycle by ubiquitinating proteins which targets them for
degradation. [provided by RefSeq, Dec 2011].
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR18074967.1049856.1,
SRR14038193.2038024.1 [ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000341068.8/ ENSP00000339109.3
RefSeq Select criteria :: based on conservation, expression
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..1944
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="2"
/map="2q13"
Protein 1..1944
/product="anaphase-promoting complex subunit 1"
/note="anaphase-promoting complex 1 (meiotic checkpoint
regulator); cyclosome subunit 1; mitotic checkpoint
regulator; testis-specific gene 24 protein"
/calculated_mol_wt=216370
Region 1..136
/region_name="Apc1_N"
/note="Anaphase-promoting complex subunit 1 N-terminal;
pfam19521"
/db_xref="CDD:437353"
Site 51
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 60
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 151..359
/region_name="ANAPC1"
/note="Anaphase-promoting complex subunit 1 WD40
beta-propeller domain; pfam12859"
/db_xref="CDD:463732"
Site 202
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 286
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 291
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 305..343
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 313
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 341
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 343
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 355
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 362
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 373..396
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 373
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 377
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 537
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 547
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:20068231; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 555
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 571
/site_type="phosphorylation"
/note="Phosphotyrosine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 615..985
/region_name="Apc1_MidN"
/note="Anaphase-promoting complex subunit 1 middle domain;
pfam20518"
/db_xref="CDD:466667"
Site 686
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:20068231; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 688
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Site 916
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 994..1016
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 1297..1325
/region_name="PC 1"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 1366..1404
/region_name="PC 2"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 1467..1501
/region_name="PC 3"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 1467..1501
/region_name="PC_rep"
/note="Proteasome/cyclosome repeat; pfam01851"
/db_xref="CDD:460361"
Region 1520..1552
/region_name="PC 4"
/note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
Region 1739..1895
/region_name="APC1_C"
/note="Anaphase-promoting complex sub unit 1 C-terminal
domain; pfam18122"
/db_xref="CDD:465659"
CDS 1..1944
/gene="ANAPC1"
/gene_synonym="APC1; MCPR; TSG24"
/coded_by="NM_022662.4:277..6111"
/db_xref="CCDS:CCDS2093.1"
/db_xref="GeneID:64682"
/db_xref="HGNC:HGNC:19988"
/db_xref="MIM:608473"
ORIGIN
1 msnfyeertt miaardlqef vpfgrdhckh hpnalnlqlr qlqpaselws sdgaaglvgs
61 lqevtihekq keswqlrkgv seigedvdyd eelyvagnmv iwskgsksqa lavykaftvd
121 spvqqalwcd fiisqdksek ayssnevekc icilqsscin mhsiegkdyi aslpfqvanv
181 wptkygllfe rsasshevpp gspreplptm fsmlhpldei tplvcksgsl fgssrvqyvv
241 dhamkivfln tdpsivmtyd avqnvhsvwt lrrvkseeen vvlkfseqgg tpqnvatsss
301 ltahlrslsk gdspvtspfq nyssihsqsr stsspslhsr spsisnmaal srahspalgv
361 hsfsgvqrfn isshnqspkr hsishspnsn sngsflapet epivpelcid hlwtetitni
421 reknsqaskv fitsdlcgqk flcflvesql qlrcvkfqes ndktqlifgs vtnipakdaa
481 pvekidtmlv legsgnlvly tgvvrvgkvf ipglpapslt msntmprpst pldgvstpkp
541 lskllgslde vvllspvpel rdssklhdsl ynedctfqql gtyihsirdp vhnrvtlels
601 ngsmvritip eiatselvqt clqaikfilp keiavqmlvk wynvhsapgg psyhsewnlf
661 vtclmnmmgy ntdrlawtrn fdfegslspv iapkkarpse tgsdddweyl lnsdyhqnve
721 shllnrslcl spseasqmkd edfsqnlsld sstllfthip aiffvlhlvy eelklntlmg
781 egicslvell vqlardlklg pyvdhyyrdy ptlvrttgqv ctidpgqtgf mhhpsfftse
841 ppsiyqwvss clkgegmppy pylpgicers rlvvlsialy ilgdeslvsd essqyltrit
901 iapqklqveq eenrfsfrhs tsvsslaerl vvwmtnvgft lrdletlpfg ialpirdaiy
961 hcreqpasdw peavclligr qdlskqaceg nlpkgksvls sdvpsgtete eeddgmndmn
1021 hevmsliwse dlrvqdvrrl lqsahpvrvn vvqypelsdh efieekenrl lqlcqrtmal
1081 pvgrgmftlf syhpvptepl pipklnltgr apprnttvdl nsgnidvppn mtswasfhng
1141 vaaglkiapa sqidsawivy nkpkhaelan eyagflmalg lnghltklat lnihdyltkg
1201 hemtsiglll gvsaaklgtm dmsitrllsi hipallppts teldvphnvq vaavvgiglv
1261 yqgtahrhta evllaeigrp pgpemeyctd resyslaagl algmvclghg snligmsdln
1321 vpeqlyqymv gghrrfqtgm hrekhkspsy qikegdtinv dvtcpgatla lamiylktnn
1381 rsiadwlrap dtmylldfvk peflllrtla rclilwddil pnskwvdsnv pqiirensis
1441 lseielpcse dlnletlsqa hvyiiagacl slgfrfagse nlsafnclhk fakdfmtyls
1501 apnasvtgph nletclsvvl lslamvmags gnlkvlqlcr flhmktggem nygfhlahhm
1561 algllflggg ryslstsnss iaallcalyp hfpahstdnr yhlqalrhly vlaaeprllv
1621 pvdvdtntpc yallevtykg tqwyeqtkee lmaptllpel hllkqikvkg prywellidl
1681 skgtqhlksi lskdgvlyvk lragqlsyke dpmgwqslla qtvanrnsea rafkpetisa
1741 ftsdpallsf aeyfckptvn mgqkqeildl fssvlyecvt qetpemlpay iamdqairrl
1801 grremsetse lwqiklvlef fssrshqerl qnhpkrglfm nseflpvvkc tidntldqwl
1861 qvggdmcvha ylsgqplees qlsmlacflv yhsvpapqhl ppiglegsts faellfkfkq
1921 lkmpvrallr laplllgnpq pmvm
//
