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Reviewed, UniProtKB/Swiss-Prot P30260 (CDC27_HUMAN)

Last modified July 7, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Subunit structure

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.9

Sequence similarities

Belongs to the APC3/CDC27 family.

Contains 9 TPR repeats.

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.5 Ref.6
Modified residue2091Phosphothreonine Ref.5
Modified residue2441Phosphothreonine Ref.5
Modified residue2911Phosphoserine Ref.5
Modified residue3131Phosphothreonine Ref.5
Modified residue3391Phosphoserine Ref.6
Modified residue4261Phosphoserine Ref.5 Ref.6
Modified residue4301Phosphothreonine Ref.5
Modified residue4351Phosphoserine Ref.5 Ref.6 Ref.9
Modified residue4381Phosphoserine Ref.6 Ref.9
Modified residue4461Phosphothreonine Ref.5 Ref.6

Natural variations

Natural variant2701G → A in a breast cancer sample; somatic mutation. Ref.10
VAR_035861
Natural variant3201S → P: dbSNP rs3208653.
VAR_052613
Natural variant4961Y → H: dbSNP rs13666.
VAR_014489

Experimental info

Sequence conflict3191K → KTFRVLQ in AAH11656. Ref.4
Sequence conflict4031K → E in AAH11656. Ref.4
Sequence conflict4601Missing in AAA60471. Ref.1
Sequence conflict7151A → R in AAA60471. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30260-1 [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

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: 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]"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.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"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.
[9]"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.
[10]"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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-270.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

U00001 mRNA. Translation: AAA60471.1.
S78234 mRNA. Translation: AAB34378.1.
AY518321 Genomic DNA. Translation: AAR89911.1.
BC011656 mRNA. Translation: AAH11656.1.
IPIIPI00294575.
PIRI52835.
RefSeqNP_001107563.1.
NP_001247.3.
UniGeneHs.463295

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP30260. 14 interactions.

PTM databases

PhosphoSiteP30260.

Proteomic databases

PRIDEP30260.

Genome annotation databases

EnsemblENSG00000004897. Homo sapiens. [Contig view]
GeneID996.
KEGGhsa:996.
UCSCuc002ild.2. human.

Organism-specific databases

GeneCardsGC17M042552.
H-InvDBHIX0013917.
HGNCHGNC:1728. CDC27.
HPACAB004357.
CAB016315.
MIM116946. gene.
PharmGKBPA142672185.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP30260.
HOVERGENP30260.
OMAP30260. KMKFPPK.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP30260.
BgeeP30260.
CleanExHS_CDC27.
GermOnlineENSG00000004897. Homo sapiens.

Family and domain databases

InterProIPR001440. TPR-1.
IPR011990. TPR-like_helical.
IPR013026. TPR_region.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF00515. TPR_1. 6 hits.
[Graphical view]
SMARTSM00028. TPR. 8 hits.
[Graphical view]
PROSITEPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio4184.
SOURCESearch...

Entry information

Entry nameCDC27_HUMAN
AccessionPrimary (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: July 7, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

SIMILARITY comments

Index of protein domains and families

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