LOCUS NP_001247 824 aa linear PRI 28-APR-2025
DEFINITION cell division cycle protein 27 homolog isoform 2 [Homo sapiens].
ACCESSION NP_001247
VERSION NP_001247.3
DBSOURCE REFSEQ: accession NM_001256.6
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 824)
AUTHORS Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
TITLE Functional and Genetic Analyses Unveil the Implication of CDC27 in
Hemifacial Microsomia
JOURNAL Int J Mol Sci 25 (9), 4707 (2024)
PUBMED 38731925
REMARK GeneRIF: Functional and Genetic Analyses Unveil the Implication of
CDC27 in Hemifacial Microsomia.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 824)
AUTHORS Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
TITLE Circ_0000775 promotes the migration, invasion and EMT of hepatic
carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
JOURNAL Pathol Res Pract 235, 153908 (2022)
PUBMED 35561648
REMARK GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE 3 (residues 1 to 824)
AUTHORS Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
Zhang,M.J., Chen,X. and Li,Q.
TITLE A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
Activity
JOURNAL Front Immunol 13, 876963 (2022)
PUBMED 35418986
REMARK GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
Disease Activity.
Publication Status: Online-Only
REFERENCE 4 (residues 1 to 824)
AUTHORS Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
and Leonetti,M.D.
TITLE OpenCell: Endogenous tagging for the cartography of human cellular
organization
JOURNAL Science 375 (6585), eabi6983 (2022)
PUBMED 35271311
REFERENCE 5 (residues 1 to 824)
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
REFERENCE 6 (residues 1 to 824)
AUTHORS Ollendorff,V. and Donoghue,D.J.
TITLE The serine/threonine phosphatase PP5 interacts with CDC16 and
CDC27, two tetratricopeptide repeat-containing subunits of the
anaphase-promoting complex
JOURNAL J Biol Chem 272 (51), 32011-32018 (1997)
PUBMED 9405394
REFERENCE 7 (residues 1 to 824)
AUTHORS Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
TITLE Localization of the human homolog of the yeast cell division
control 27 gene (CDC27) proximal to ITGB3 on human chromosome
17q21.3
JOURNAL Somat Cell Mol Genet 21 (5), 351-355 (1995)
PUBMED 8619132
REFERENCE 8 (residues 1 to 824)
AUTHORS Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
TITLE CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
spindle and is essential for the metaphase to anaphase transition
JOURNAL Cell 81 (2), 261-268 (1995)
PUBMED 7736578
REFERENCE 9 (residues 1 to 824)
AUTHORS Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
Lee,W.H.
TITLE Identification of a human homologue of yeast nuc2 which interacts
with the retinoblastoma protein in a specific manner
JOURNAL Cell Growth Differ 6 (2), 199-210 (1995)
PUBMED 7756179
REFERENCE 10 (residues 1 to 824)
AUTHORS Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
TITLE Linking yeast genetics to mammalian genomes: identification and
mapping of the human homolog of CDC27 via the expressed sequence
tag (EST) data base
JOURNAL Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
PUBMED 8234252
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from HY023336.1, S78234.1,
AC002558.2 and AA927469.1.
On Feb 8, 2008 this sequence version replaced NP_001247.2.
Summary: The protein encoded by this gene shares strong similarity
with Saccharomyces cerevisiae protein Cdc27, and the gene product
of Schizosaccharomyces pombe nuc 2. This protein is a component of
the anaphase-promoting complex (APC), which is composed of eight
protein subunits and is highly conserved in eukaryotic cells. This
complex catalyzes the formation of cyclin B-ubiquitin conjugate,
which is responsible for the ubiquitin-mediated proteolysis of
B-type cyclins. The protein encoded by this gene and three other
members of the APC complex contain tetratricopeptide (TPR) repeats,
which are important for protein-protein interactions. This protein
was shown to interact with mitotic checkpoint proteins including
Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
the timing of mitosis. Alternative splicing of this gene results in
multiple transcript variants. Related pseudogenes have been
identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
2014].
Transcript Variant: This variant (2) uses an alternate in-frame
splice site in the central coding region, compared to variant 1,
resulting in an isoform (2) that is shorter than isoform 1.
Sequence Note: This RefSeq record was created from transcript and
genomic sequence data to make the sequence consistent with the
reference genome assembly. The genomic coordinates used for the
transcript record were based on transcript alignments.
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 :: SRR11853558.10627.1,
SRR14038193.4312364.1 [ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000066544.8/ ENSP00000066544.3
RefSeq Select criteria :: based on conservation, expression
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..824
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="17"
/map="17q21.32"
Protein 1..824
/product="cell division cycle protein 27 homolog isoform
2"
/note="anaphase promoting complex subunit 3; nuc2 homolog;
anaphase-promoting complex, protein 3; cell division cycle
27 homolog; D0S1430E, D17S978E"
/calculated_mol_wt=91737
Region 6..35
/region_name="TPR 1"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 17..92
/region_name="ANAPC3"
/note="Anaphase-promoting complex, cyclosome, subunit 3;
pfam12895"
/db_xref="CDD:463743"
Region 38..65
/region_name="TPR 2"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 67..99
/region_name="TPR 3"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 115..145
/region_name="TPR 4"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Site 205
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (P30260.2)"
Site 209
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 244
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Region 287..422
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Site 291
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 313
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 339
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 366
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:19690332; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 379
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 386
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:20068231; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 426
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (P30260.2)"
Site 430
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 435
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 438
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
Site 446
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000269|PubMed:14657031,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 448..>671
/region_name="Spy"
/note="Predicted O-linked N-acetylglucosamine transferase,
SPINDLY family [Posttranslational modification, protein
turnover, chaperones]; COG3914"
/db_xref="CDD:443119"
Region 465..495
/region_name="TPR 5"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 499..528
/region_name="TPR 6"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 501..527
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 533..563
/region_name="TPR 7"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 561..>731
/region_name="TPR"
/note="Tetratricopeptide (TPR) repeat [General function
prediction only]; COG0457"
/db_xref="CDD:440225"
Region 567..598
/region_name="TPR 8"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 567..595
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Site order(568,571..572,575..576,578,602,605..606,609..610,
612..613,636,639..640,643..644,647)
/site_type="other"
/note="putative protein binding surface [polypeptide
binding]"
/db_xref="CDD:276809"
Region 600..630
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 601..631
/region_name="TPR 9"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 635..667
/region_name="TPR 10"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 635..663
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region <665..804
/region_name="NlpI"
/note="Lipoprotein NlpI, contains TPR repeats [Cell
wall/membrane/envelope biogenesis]; COG4785"
/db_xref="CDD:443815"
Region 669..696
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 670..702
/region_name="TPR 11"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 703..731
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 704..734
/region_name="TPR 12"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 737..768
/region_name="TPR 13"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Region 737..765
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 781..824
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
Site 821
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:22139841; propagated from
UniProtKB/Swiss-Prot (P30260.2)"
CDS 1..824
/gene="CDC27"
/gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
H-NUC; HNUC; NUC2"
/coded_by="NM_001256.6:124..2598"
/note="isoform 2 is encoded by transcript variant 2"
/db_xref="CCDS:CCDS11509.1"
/db_xref="GeneID:996"
/db_xref="HGNC:HGNC:1728"
/db_xref="MIM:116946"
ORIGIN
1 mtvlqepvqa aiwqalnhya yrdavflaer lyaevhseea lfllatcyyr sgkaykayrl
61 lkghscttpq ckyllakccv dlsklaegeq ilsggvfnkq kshddivtef gdsacftlsl
121 lghvycktdr lakgsecyqk slslnpflws pfeslceige kpdpdqtfkf tslqnfsncl
181 pnscttqvpn hslshrqpet vltetpqdti elnrlnless nskyslntds svsyidsavi
241 spdtvplgtg tsilskqvqn kpktgrsllg gpaalspltp sfgilpletp spgdgsylqn
301 ytntppvidv pstgapskks varigqtgtk svfsqsgnsr evtpilaqtq ssgpqtsttp
361 qvlsptitsp pnalprrssr lftsdssttk enskklkmkf ppkipnrktk sktnkggitq
421 pnindsleit kldssiiseg kistitpqiq afnlqkaaae glmsllremg kgylalcsyn
481 ckeainilsh lpshhyntgw vlcqigrayf elseymqaer ifsevrrien yrvegmeiys
541 ttlwhlqkdv alsvlskdlt dmdknspeaw caagncfslq rehdiaikff qraiqvdpny
601 ayaytllghe fvlteeldka lacfrnairv nprhynawyg lgmiyykqek fslaemhfqk
661 aldinpqssv llchigvvqh alkksekald tlnkaividp knplckfhra svlfanekyk
721 salqeleelk qivpkeslvy fligkvykkl gqthlalmnf swamdldpkg annqikeaid
781 krylpddeep itqeeqimgt desqessmtd addtqlhaae sdef
//
