GenomeNet

Database: RefSeq
Entry: NP_001247
LinkDB: NP_001247
Original site: NP_001247 
LOCUS       NP_001247                824 aa            linear   PRI 04-JUL-2020
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   Xin Y, Ning S, Zhang L and Cui M.
  TITLE     CDC27 Facilitates Gastric Cancer Cell Proliferation, Invasion and
            Metastasis via Twist-Induced Epithelial-Mesenchymal Transition
  JOURNAL   Cell. Physiol. Biochem. 50 (2), 501-511 (2018)
   PUBMED   30308498
  REMARK    GeneRIF: CDC27 facilitated cells invasion and metastasis via Twist
            pathway, leading to initiation of epithelial-mesenchymal transition
            and silencing of Twist expression could reverse this process.
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Wang C, Su Z, Hou H, Li D, Pan Z, Tian W and Mo C.
  TITLE     Inhibition of Anaphase-Promoting Complex by Silence APC/C(Cdh1) to
            Enhance Radiosensitivity of Nasopharyngeal Carcinoma Cells
  JOURNAL   J. Cell. Biochem. 118 (10), 3150-3157 (2017)
   PUBMED   28004426
  REMARK    GeneRIF: The levels of CDC20 and CylinB1 increased and the levels
            of Ku70 and APC3 decreased after irradiation. APC/C(Cdh1) is
            involved in regulation of radiosensitivity in human NPC CNE-1
            cells.
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Yoshimura S, Kasamatsu A, Nakashima D, Iyoda M, Kasama H, Saito T,
            Takahara T, Endo-Sakamoto Y, Shiiba M, Tanzawa H and Uzawa K.
  TITLE     UBE2S associated with OSCC proliferation by promotion of P21
            degradation via the ubiquitin-proteasome system
  JOURNAL   Biochem. Biophys. Res. Commun. 485 (4), 820-825 (2017)
   PUBMED   28257844
  REMARK    GeneRIF: Data indicate that UBE2S and APC3 co-regulate the
            expression level of P21 at G2/M check point via the
            ubiquitin-proteasome system.
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Feng Z, Zhang L, Zhou J, Zhou S, Li L, Guo X, Feng G, Ma Z, Huang W
            and Huang F.
  TITLE     mir-218-2 promotes glioblastomas growth, invasion and drug
            resistance by targeting CDC27
  JOURNAL   Oncotarget 8 (4), 6304-6318 (2017)
   PUBMED   27974673
  REMARK    GeneRIF: mir-218-2 promotes glioblastomas growth, invasion and drug
            resistance by targeting CDC27 expression.
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Yu H, Peters JM, King RW, Page AM, Hieter P and Kirschner MW.
  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 DJ.
  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 PP, Couch FJ, Brody LC, Abel KJ, Boehnke M, Shearon TH,
            Chandrasekharappa SC, Collins FS and Weber BL.
  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 PL, Ueng YC, Durfee T, Chen KC, Yang-Feng T and Lee WH.
  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 MS, Seldin MS 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 :: SRR1660807.224122.1,
                                           SRR1803615.70207.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##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:289650"
     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:0000244|PubMed:18669648,
                     ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031;
                     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)"
     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:0000244|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000244|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000244|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000244|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000244|PubMed:18669648,
                     ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031;
                     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:0000244|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000244|PubMed:18669648,
                     ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          457..528
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:290160"
     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..762
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:223533"
     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          567..600
                     /region_name="TPR_1"
                     /note="Tetratricopeptide repeat; pfam00515"
                     /db_xref="CDD:278916"
     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..634
                     /region_name="TPR_1"
                     /note="Tetratricopeptide repeat; pfam00515"
                     /db_xref="CDD:278916"
     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..667
                     /region_name="TPR_1"
                     /note="Tetratricopeptide repeat; pfam00515"
                     /db_xref="CDD:278916"
     Region          635..663
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     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          672..702
                     /region_name="TPR_1"
                     /note="Tetratricopeptide repeat; pfam00515"
                     /db_xref="CDD:278916"
     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"
     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
//
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