Cell division cycle protein 27 homolog

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P30260 (CDC27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. History...

Clusters with 100%, 90%, 50% identity |

Documents (7) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	824 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7
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.5 Ref.13
Sequence similarities	Belongs to the APC3/CDC27 family. Contains 9 TPR repeats.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell proliferation Traceable author statement PubMed 7736578. Source: ProtInc mitotic metaphase/anaphase transition Inferred from mutant phenotype PubMed 7736578. Source: MGI 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.7. Source: UniProtKB
Cellular_component	anaphase-promoting complex Inferred from direct assay Ref.12 PubMed 21926987. Source: UniProtKB centrosome Inferred from direct assay PubMed 7736578. Source: MGI cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome spindle microtubule Inferred from direct assay PubMed 7736578. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CDC20	Q12834	6	EBI-994813,EBI-367462
CDH1	P12830	2	EBI-994813,EBI-727477
FBXO5	Q9UKT4	2	EBI-994813,EBI-852298
FZR1	Q9UM11	8	EBI-994813,EBI-724997
MAD2L2	Q9UI95	2	EBI-994813,EBI-77889
NCK1	P16333	3	EBI-994813,EBI-389883
NEK2	P51955	2	EBI-994813,EBI-633182
PTEN	P60484	7	EBI-994813,EBI-696162

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 824

824

Cell division cycle protein 27 homolog

PRO_0000106273

Regions

Repeat

84 – 114

TPR 1

Repeat

115 – 148

TPR 2

Repeat

499 – 532

TPR 3

Repeat

567 – 600

TPR 4

Repeat

602 – 634

TPR 5

Repeat

635 – 668

TPR 6

Repeat

670 – 702

TPR 7

Repeat

704 – 736

TPR 8

Repeat

737 – 770

TPR 9

Amino acid modifications

Modified residue

205

Phosphothreonine Ref.5 Ref.8

Modified residue

209

Phosphothreonine Ref.5

Modified residue

244

Phosphothreonine Ref.5

Modified residue

291

Phosphoserine Ref.5

Modified residue

313

Phosphothreonine Ref.5

Modified residue

339

Phosphoserine Ref.8

Modified residue

366

Phosphothreonine Ref.9

Modified residue

386

Phosphoserine Ref.10

Modified residue

426

Phosphoserine Ref.5 Ref.8

Modified residue

430

Phosphothreonine Ref.5

Modified residue

435

Phosphoserine Ref.5

Modified residue

438

Phosphoserine Ref.8

Modified residue

446

Phosphothreonine Ref.5 Ref.8

Modified residue

821

Phosphoserine Ref.13

Natural variations

Natural variant

270

G → A in a breast cancer sample; somatic mutation. Ref.14

VAR_035861

Natural variant

320

S → P.
Corresponds to variant rs3208653 [ dbSNP | Ensembl ].

VAR_052613

Natural variant

496

Y → H.
Corresponds to variant rs13666 [ dbSNP | Ensembl ].

VAR_014489

Experimental info

Mutagenesis

821

S → A: Abolishes binding to MCPH1. Ref.13

Sequence conflict

319

K → KTFRVLQ in AAH11656. Ref.4

Sequence conflict

403

K → E in AAH11656. Ref.4

Sequence conflict

460

Missing in AAA60471. Ref.1

Sequence conflict

715

A → R in AAA60471. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P30260 [UniParc].

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

FASTA

824

91,867

        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

References

	« Hide 'large scale' referencesShow '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].
[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].
[3]	NIEHS SNPs program Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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]. Tissue: Uterus.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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.
[13]	"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.
[14]	"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. 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

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00001 mRNA. Translation: AAA60471.1.
S78234 mRNA. Translation: AAB34378.1.
AY518321 Genomic DNA. Translation: AAR89911.1.
BC011656 mRNA. Translation: AAH11656.1.

IPI

IPI00294575.

PIR

I52835.

RefSeq

NP_001107563.1. NM_001114091.1.
NP_001247.3. NM_001256.3.

UniGene

Hs.463295.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3T1N	X-ray	2.60	C/D	821-824	[»]

ProteinModelPortal

P30260.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36422N.

IntAct

P30260. 41 interactions.

MINT

MINT-86425.

STRING

9606.ENSP00000399255.

PTM databases

PhosphoSite

P30260.

Polymorphism databases

DMDM

12644198.

Proteomic databases

PaxDb

P30260.

PRIDE

P30260.

Protocols and materials databases

DNASU

996.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000066544; ENSP00000066544; ENSG00000004897.

GeneID

996.

KEGG

hsa:996.

UCSC

uc002ild.4. human.

Organism-specific databases

CTD

996.

GeneCards

GC17M045195.

H-InvDB

HIX0176461.

HGNC

HGNC:1728. CDC27.

HPA

CAB004357.
CAB016315.
HPA028129.

MIM

116946. gene.

neXtProt

NX_P30260.

PharmGKB

PA26261.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0457.

HOGENOM

HOG000231056.

HOVERGEN

HBG050859.

InParanoid

P30260.

K03350.

OrthoDB

EOG4MW85D.

PhylomeDB

P30260.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
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.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P30260.

Bgee

P30260.

CleanEx

HS_CDC27.

Genevestigator

P30260.

GermOnline

ENSG00000004897. Homo sapiens.

Family and domain databases

InterPro

IPR026803. CDC27.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]

PANTHER

PTHR12558:SF5. PTHR12558:SF5. 1 hit.

Pfam

PF00515. TPR_1. 4 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]

SMART

SM00028. TPR. 8 hits.
[Graphical view]

PROSITE

PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CDC27. human.

GenomeRNAi

996.

NextBio

4184.

SOURCE

Search...

Entry information

Entry name

CDC27_HUMAN

Accession

Primary (citable) accession number: P30260
Secondary accession number(s): Q16349, Q96F35

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 17

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents