Cell division cycle protein 27 homolog

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Reviewed, UniProtKB/Swiss-Prot P30260 (CDC27_HUMAN)

Last modified February 9, 2010. Version 108. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cell division cycle protein 27 homolog
      Short name=CDC27Hs
Alternative name(s):
    H-NUC

Gene names

Name:	CDC27
Synonyms:	D0S1430E, D17S978E

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	824 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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.8
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 12 subunits. Interacts with RB.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs specifically during mitosis. Ref.5 Ref.6 Ref.7 Ref.9 Ref.11 Ref.12
Sequence similarities	Belongs to the APC3/CDC27 family. Contains 9 TPR repeats.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell proliferation Traceable author statement. Source: ProtInc mitotic metaphase/anaphase transition Inferred from mutant phenotype. Source: MGI negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome protein K11-linked ubiquitination Ref.8 Inferred from direct assay. Source: UniProtKB
Cellular component	anaphase-promoting complex Ref.13 Inferred from direct assay. Source: UniProtKB centrosome Inferred from direct assay. Source: MGI cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome spindle microtubule Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ABL1	P00519	1	EBI-994813,EBI-375543
FBXO5	Q9UKT4	1	EBI-994813,EBI-852298
FYN	P06241	1	EBI-994813,EBI-515315
FZR1	Q9UM11	2	EBI-994813,EBI-724997
GRB2	P62993	1	EBI-994813,EBI-401755
MAD2L2	Q9UI95	1	EBI-994813,EBI-77889
NCK1	P16333	1	EBI-994813,EBI-389883
NEK2	P51955	1	EBI-994813,EBI-633182
PIK3R1	P27986	1	EBI-994813,EBI-79464

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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.9

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.7 Ref.9

Modified residue

366

Phosphothreonine Ref.12

Modified residue

426

Phosphoserine Ref.5 Ref.9 Ref.11

Modified residue

430

Phosphothreonine Ref.5

Modified residue

435

Phosphoserine Ref.5 Ref.6 Ref.7 Ref.9

Modified residue

438

Phosphoserine Ref.6 Ref.7 Ref.9

Modified residue

446

Phosphothreonine Ref.5 Ref.9 Ref.11

Natural variations

Natural variant

270

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

VAR_035861

Natural variant

320

S → P: dbSNP rs3208653.

VAR_052613

Natural variant

496

Y → H: dbSNP rs13666.

VAR_014489

Experimental info

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

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Sequences

Sequence

Length

Mass (Da)

Tools

P30260-1 [UniParc].

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

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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: 8234252] [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: 7756179] [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: 15489334] [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: 14657031] [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]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-438, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339; SER-435 AND SER-438, MASS SPECTROMETRY.
[8]	"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: 18485873] [Abstract] Cited for: FUNCTION OF THE APC/C.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-339; SER-426; SER-435; SER-438 AND THR-446, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426 AND THR-446, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, MASS SPECTROMETRY. Tissue: T-cell.
[13]	"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: 16364912] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE APC/C.
[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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-270.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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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. NP_001247.3.
UniGene	Hs.463295
3D structure databases
SMR	P30260. Positions 36-155, 472-769, 503-773.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30260. 14 interactions.
STRING	P30260.
PTM databases
PhosphoSite	P30260.
Proteomic databases
PRIDE	P30260.
Genome annotation databases
Ensembl	ENST00000066544; ENSP00000066544; ENSG00000004897; Homo sapiens. [Genome view]
GeneID	996.
KEGG	hsa:996.
UCSC	uc002ild.2. human.
Organism-specific databases
CTD	996.
GeneCards	GC17M042552.
H-InvDB	HIX0013917.
HGNC	HGNC:1728. CDC27.
HPA	CAB004357. CAB016315.
MIM	116946. gene.
PharmGKB	PA142672185.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07640.
HOVERGEN	P30260.
InParanoid	P30260.
PhylomeDB	P30260.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_8017. APC-Cdc20 mediated degradation of Nek2A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	P30260.
Bgee	P30260.
CleanEx	HS_CDC27.
Genevestigator	P30260.
GermOnline	ENSG00000004897. Homo sapiens.
Family and domain databases
InterPro	IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
SMART	SM00028. TPR. 8 hits. [Graphical view]
PROSITE	PS50005. TPR. 8 hits. PS50293. TPR_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	4184.
SOURCE	Search...

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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:	February 9, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents