LOCUS NP_057321 755 aa linear PRI 27-APR-2025
DEFINITION anaphase-promoting complex subunit 5 isoform a [Homo sapiens].
ACCESSION NP_057321
VERSION NP_057321.2
DBSOURCE REFSEQ: accession NM_016237.5
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 755)
AUTHORS Yau,R.G., Doerner,K., Castellanos,E.R., Haakonsen,D.L., Werner,A.,
Wang,N., Yang,X.W., Martinez-Martin,N., Matsumoto,M.L., Dixit,V.M.
and Rape,M.
TITLE Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle
and Protein Quality Control
JOURNAL Cell 171 (4), 918-933 (2017)
PUBMED 29033132
REFERENCE 2 (residues 1 to 755)
AUTHORS Xu,M., Liu,X., Xu,Y., Zhu,S. and Gao,Y.
TITLE Co-expression of Axin and APC gene fragments inhibits colorectal
cancer cell growth via regulation of the Wnt signaling pathway
JOURNAL Mol Med Rep 16 (4), 3783-3790 (2017)
PUBMED 28731177
REMARK GeneRIF: coexpression of APC5 and Axin genes significantly
downregulated Wnt signaling in human SW480 CRC cells and inhibited
cell growth.
REFERENCE 3 (residues 1 to 755)
AUTHORS Zhang,S., Chang,L., Alfieri,C., Zhang,Z., Yang,J., Maslen,S.,
Skehel,M. and Barford,D.
TITLE Molecular mechanism of APC/C activation by mitotic phosphorylation
JOURNAL Nature 533 (7602), 260-264 (2016)
PUBMED 27120157
REFERENCE 4 (residues 1 to 755)
AUTHORS Song,M.S., Carracedo,A., Salmena,L., Song,S.J., Egia,A.,
Malumbres,M. and Pandolfi,P.P.
TITLE Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a
phosphatase-independent manner
JOURNAL Cell 144 (2), 187-199 (2011)
PUBMED 21241890
REFERENCE 5 (residues 1 to 755)
AUTHORS Tran,K., Kamil,J.P., Coen,D.M. and Spector,D.H.
TITLE Inactivation and disassembly of the anaphase-promoting complex
during human cytomegalovirus infection is associated with
degradation of the APC5 and APC4 subunits and does not require
UL97-mediated phosphorylation of Cdh1
JOURNAL J Virol 84 (20), 10832-10843 (2010)
PUBMED 20686030
REMARK GeneRIF: Inactivation and disassembly of the anaphase-promoting
complex during human cytomegalovirus infection is associated with
degradation of the APC5 and APC4 subunits and does not require
UL97-mediated phosphorylation of Cdh1.
REFERENCE 6 (residues 1 to 755)
AUTHORS Kraft,C., Herzog,F., Gieffers,C., Mechtler,K., Hagting,A., Pines,J.
and Peters,J.M.
TITLE Mitotic regulation of the human anaphase-promoting complex by
phosphorylation
JOURNAL EMBO J 22 (24), 6598-6609 (2003)
PUBMED 14657031
REFERENCE 7 (residues 1 to 755)
AUTHORS Vodermaier,H.C., Gieffers,C., Maurer-Stroh,S., Eisenhaber,F. and
Peters,J.M.
TITLE TPR subunits of the anaphase-promoting complex mediate binding to
the activator protein CDH1
JOURNAL Curr Biol 13 (17), 1459-1468 (2003)
PUBMED 12956947
REFERENCE 8 (residues 1 to 755)
AUTHORS Autieri,M.V.
TITLE Expression of anaphase-promoting complex 5 in balloon
angioplasty-injured rat carotid arteries and mitogen-stimulated
human vascular smooth muscle cells
JOURNAL Biochem Biophys Res Commun 282 (3), 723-728 (2001)
PUBMED 11401522
REFERENCE 9 (residues 1 to 755)
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 755)
AUTHORS Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
Kirschner,M.W.
TITLE Identification of a cullin homology region in a subunit of the
anaphase-promoting complex
JOURNAL Science 279 (5354), 1219-1222 (1998)
PUBMED 9469815
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AI879332.1, BC001950.1,
AA349724.1 and BX381618.2.
On Apr 10, 2002 this sequence version replaced NP_057321.1.
Summary: This gene encodes a tetratricopeptide repeat-containing
component of the anaphase promoting complex/cyclosome (APC/C), a
large E3 ubiquitin ligase that controls cell cycle progression by
targeting a number of cell cycle regulators such as B-type cyclins
for 26S proteasome-mediated degradation through ubiquitination. The
encoded protein is required for the proper ubiquitination function
of APC/C and for the interaction of APC/C with transcription
coactivators. It also interacts with polyA binding protein and
represses internal ribosome entry site-mediated translation.
Multiple transcript variants encoding different isoforms have been
found for this gene. These differences cause translation initiation
at a downstream AUG and result in a shorter protein (isoform b),
compared to isoform a. [provided by RefSeq, Nov 2008].
Transcript Variant: This variant (1) represents the longer
transcript and encodes the longer isoform (a).
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 :: SRR14038191.4105352.1, BC001081.2
[ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000261819.8/ ENSP00000261819.3
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..755
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="12"
/map="12q24.31"
Protein 1..755
/product="anaphase-promoting complex subunit 5 isoform a"
/note="cyclosome subunit 5"
/calculated_mol_wt=84946
Region 32..165
/region_name="Apc5_N"
/note="N-terminal domain of the anaphase-promoting complex
subunit Apc5 (or Anapc5); cd16270"
/db_xref="CDD:293878"
Site order(44..45,54,57..58,61..62,64..65,69,124,129..132)
/site_type="other"
/note="Apc4 interaction interface [polypeptide binding]"
/db_xref="CDD:293878"
Site order(104..106,109,113,143,147..150,152..153)
/site_type="other"
/note="CDC23 interaction interface [polypeptide binding]"
/db_xref="CDD:293878"
Site order(134,137..138,141,144..145)
/site_type="other"
/note="APC subunit 15 interaction interface [polypeptide
binding]"
/db_xref="CDD:293878"
Site 195
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 209..249
/region_name="TPR 1"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Site 232
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 248..282
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276806"
Region 250..300
/region_name="TPR 2"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 254..354
/region_name="ANAPC5"
/note="Anaphase-promoting complex subunit 5; pfam12862"
/db_xref="CDD:432838"
Region 300..333
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276806"
Region 301..337
/region_name="TPR 3"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 338..378
/region_name="TPR 4"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 379..418
/region_name="TPR 5"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 419..466
/region_name="TPR 6"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 452..>645
/region_name="TPR_MalT"
/note="MalT-like TPR region; pfam17874"
/db_xref="CDD:436107"
Region 467..500
/region_name="TPR 7"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 467..495
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Site order(468,471..472,475..476,478,502,504..505,508..509,
511..512,542,545..546,549..550,553)
/site_type="other"
/note="putative protein binding surface [polypeptide
binding]"
/db_xref="CDD:276809"
Region 500..531
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 501..540
/region_name="TPR 8"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 541..580
/region_name="TPR 9"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 541..568
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 581..620
/region_name="TPR 10"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 621..660
/region_name="TPR 11"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 661..696
/region_name="TPR 12"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
Region 697..736
/region_name="TPR 13"
/note="propagated from UniProtKB/Swiss-Prot (Q9UJX4.2)"
CDS 1..755
/gene="ANAPC5"
/gene_synonym="APC5"
/coded_by="NM_016237.5:72..2339"
/note="isoform a is encoded by transcript variant 1"
/db_xref="CCDS:CCDS9220.1"
/db_xref="GeneID:51433"
/db_xref="HGNC:HGNC:15713"
/db_xref="MIM:606948"
ORIGIN
1 masvheslyf npmmtngvvh anvfgikdwv tpykiavlvl lnemsrtgeg avslmerrrl
61 nqlllpllqg pditlsklyk lieescpqla nsvqiriklm aegelkdmeq ffddlsdsfs
121 gtepevhkts vvglflrhmi laysklsfsq vfklytalqq yfqngekktv edadmeltsr
181 degerkmeke eldvsvreee vscsgplsqk qaefflsqqa sllkndetka ltpaslqkel
241 nnllkfnpdf aeahylsyln nlrvqdvfss thsllhyfdr liltgaesks ngeegygrsl
301 ryaalnlaal hcrfghyqqa elalqeairi aqesndhvcl qhclswlyvl gqkrsdsyvl
361 lehsvkkavh fglpylaslg iqslvqqraf agktanklmd alkdsdllhw khslselidi
421 siaqktaiwr lygrstmalq qaqmllsmns leavnagvqq nntesfaval chlaelhaeq
481 gcfaaasevl khlkerfppn sqhaqlwmlc dqkiqfdram ndgkyhlads lvtgitalns
541 iegvyrkavv lqaqnqmsea hkllqkllvh cqklkntemv isvllsvael ywrsssptia
601 lpmllqalal skeyrlqyla setvlnlafa qlilgipeqa lsllhmaiep iladgaildk
661 gramflvakc qvasaasydq pkkaealeaa ienlneakny fakvdckeri rdvvyfqarl
721 yhtlgktqer nrcamlfrql hqelpshgvp linhl
//
