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P30260 (CDC27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division cycle protein 27 homolog
Alternative name(s):
Anaphase-promoting complex subunit 3
Short name=APC3
CDC27 homolog
Short name=CDC27Hs
H-NUC
Gene names
Name:CDC27
Synonyms:ANAPC3, D0S1430E, D17S978E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Ref.9

Pathway

Protein modification; protein ubiquitination.

Subunit structure

The APC/C is composed of at least 12 subunits. Interacts with RB. Interacts with FAM168B/MANI By similarity. Interacts with MCPH1.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs specifically during mitosis. Ref.7 Ref.16

Sequence similarities

Belongs to the APC3/CDC27 family.

Contains 9 TPR repeats.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement PubMed 7736578. Source: ProtInc

metaphase/anaphase transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 7736578. Source: MGI

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic spindle assembly checkpoint

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein K11-linked ubiquitination

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentanaphase-promoting complex

Inferred from direct assay Ref.15PubMed 21926987. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 7736578. Source: MGI

cytoplasm

Inferred from direct assay. Source: LIFEdb

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

spindle

Traceable author statement PubMed 7736578. Source: ProtInc

spindle microtubule

Inferred from direct assay PubMed 7736578. Source: MGI

   Molecular_functionprotein phosphatase binding

Inferred from physical interaction PubMed 21241890. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30260-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P30260-2)

The sequence of this isoform differs from the canonical sequence as follows:
     319-319: K → KTFRVLQ
Note: No experimental confirmation available. May be due to competing acceptor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 824824Cell division cycle protein 27 homolog
PRO_0000106273

Regions

Repeat84 – 11431TPR 1
Repeat115 – 14834TPR 2
Repeat499 – 53234TPR 3
Repeat567 – 60034TPR 4
Repeat602 – 63433TPR 5
Repeat635 – 66834TPR 6
Repeat670 – 70233TPR 7
Repeat704 – 73633TPR 8
Repeat737 – 77034TPR 9

Amino acid modifications

Modified residue2051Phosphothreonine Ref.7 Ref.10
Modified residue2091Phosphothreonine Ref.7
Modified residue2441Phosphothreonine Ref.7
Modified residue2911Phosphoserine Ref.7
Modified residue3131Phosphothreonine Ref.7
Modified residue3391Phosphoserine Ref.10
Modified residue3661Phosphothreonine Ref.12
Modified residue3861Phosphoserine Ref.13
Modified residue4261Phosphoserine Ref.7 Ref.10
Modified residue4301Phosphothreonine Ref.7
Modified residue4351Phosphoserine Ref.7
Modified residue4381Phosphoserine Ref.10
Modified residue4461Phosphothreonine Ref.7 Ref.10
Modified residue8211Phosphoserine Ref.16

Natural variations

Alternative sequence3191K → KTFRVLQ in isoform 2.
VSP_047225
Natural variant2701G → A in a breast cancer sample; somatic mutation. Ref.17
VAR_035861
Natural variant3201S → P.
Corresponds to variant rs3208653 [ dbSNP | Ensembl ].
VAR_052613
Natural variant4961Y → H.
Corresponds to variant rs13666 [ dbSNP | Ensembl ].
VAR_014489

Experimental info

Mutagenesis8211S → A: Abolishes binding to MCPH1. Ref.16
Sequence conflict4031K → E in AAH11656. Ref.6
Sequence conflict4601Missing in AAA60471. Ref.1
Sequence conflict7151A → R in AAA60471. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: E6C8F59C1EF1DCBA

FASTA82491,867
        10         20         30         40         50         60 
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL 

        70         80         90        100        110        120 
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDIVTEF GDSACFTLSL 

       130        140        150        160        170        180 
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKF TSLQNFSNCL 

       190        200        210        220        230        240 
PNSCTTQVPN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI 

       250        260        270        280        290        300 
SPDTVPLGTG TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN 

       310        320        330        340        350        360 
YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ SSGPQTSTTP 

       370        380        390        400        410        420 
QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF PPKIPNRKTK SKTNKGGITQ 

       430        440        450        460        470        480 
PNINDSLEIT KLDSSIISEG KISTITPQIQ AFNLQKAAAE GLMSLLREMG KGYLALCSYN 

       490        500        510        520        530        540 
CKEAINILSH LPSHHYNTGW VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS 

       550        560        570        580        590        600 
TTLWHLQKDV ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY 

       610        620        630        640        650        660 
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK FSLAEMHFQK 

       670        680        690        700        710        720 
ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP KNPLCKFHRA SVLFANEKYK 

       730        740        750        760        770        780 
SALQELEELK QIVPKESLVY FLIGKVYKKL GQTHLALMNF SWAMDLDPKG ANNQIKEAID 

       790        800        810        820 
KRYLPDDEEP ITQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF 

« Hide

Isoform 2 [UniParc].

Checksum: 00CE7174F8165CA1
Show »

FASTA83092,612

References

« Hide 'large scale' references
[1]"Linking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data base."
Tugendreich S., Boguski M.S., Seldin M., Hieter P.A.
Proc. Natl. Acad. Sci. U.S.A. 90:10031-10035(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification of a human homologue of yeast nuc2 which interacts with the retinoblastoma protein in a specific manner."
Chen P.L., Ueng Y.C., Durfee T., Chen K.C., Yang-Feng T., Lee W.H.
Cell Growth Differ. 6:199-210(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[7]"Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-205; THR-209; THR-244; SER-291; THR-313; SER-426; THR-430; SER-435 AND THR-446.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE APC/C.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-339; SER-426; SER-438 AND THR-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE APC/C.
[16]"Molecular basis for the association of microcephalin (MCPH1) protein with the cell division cycle protein 27 (Cdc27) subunit of the anaphase-promoting complex."
Singh N., Wiltshire T.D., Thompson J.R., Mer G., Couch F.J.
J. Biol. Chem. 287:2854-2862(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 821-824 IN COMPLEX WITH MCPH1, PHOSPHORYLATION AT SER-821, MUTAGENESIS OF SER-821.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-270.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00001 mRNA. Translation: AAA60471.1.
S78234 mRNA. Translation: AAB34378.1.
AY518321 Genomic DNA. Translation: AAR89911.1.
AC002558 Genomic DNA. No translation available.
CH471231 Genomic DNA. Translation: EAW57687.1.
BC011656 mRNA. Translation: AAH11656.1.
PIRI52835.
RefSeqNP_001107563.1. NM_001114091.1.
NP_001247.3. NM_001256.3.
UniGeneHs.463295.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T1NX-ray2.60C/D821-824[»]
ProteinModelPortalP30260.
SMRP30260. Positions 487-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107431. 88 interactions.
DIPDIP-36422N.
IntActP30260. 44 interactions.
MINTMINT-86425.
STRING9606.ENSP00000399255.

PTM databases

PhosphoSiteP30260.

Polymorphism databases

DMDM12644198.

Proteomic databases

PaxDbP30260.
PRIDEP30260.

Protocols and materials databases

DNASU996.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000066544; ENSP00000066544; ENSG00000004897. [P30260-1]
ENST00000531206; ENSP00000434614; ENSG00000004897. [P30260-2]
GeneID996.
KEGGhsa:996.
UCSCuc002ild.4. human. [P30260-1]
uc002ile.4. human.

Organism-specific databases

CTD996.
GeneCardsGC17M045195.
H-InvDBHIX0176461.
HGNCHGNC:1728. CDC27.
HPACAB004357.
CAB016315.
HPA028129.
HPA052399.
MIM116946. gene.
neXtProtNX_P30260.
PharmGKBPA26261.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000231056.
HOVERGENHBG050859.
InParanoidP30260.
KOK03350.
OMANRKTKCK.
OrthoDBEOG751NDX.
PhylomeDBP30260.
TreeFamTF101058.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP30260.
BgeeP30260.
CleanExHS_CDC27.
GenevestigatorP30260.

Family and domain databases

InterProIPR013026. TPR-contain_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 4 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 8 hits.
[Graphical view]
PROSITEPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC27. human.
GeneWikiCDC27.
GenomeRNAi996.
NextBio4184.
PROP30260.
SOURCESearch...

Entry information

Entry nameCDC27_HUMAN
AccessionPrimary (citable) accession number: P30260
Secondary accession number(s): G3V1C4, Q16349, Q96F35
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM