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Protein

Cell division cycle protein 27 homolog

Gene

Cdc27

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-RNO-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-RNO-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-RNO-174154. APC/C:Cdc20 mediated degradation of Securin.
R-RNO-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-RNO-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-RNO-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-RNO-176412. Phosphorylation of the APC/C.
R-RNO-179409. APC-Cdc20 mediated degradation of Nek2A.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2559582. Senescence-Associated Secretory Phenotype (SASP).
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 27 homolog
Gene namesi
Name:Cdc27
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1304921. Cdc27.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003904741 – 824Cell division cycle protein 27 homologAdd BLAST824

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei205PhosphothreonineBy similarity1
Modified residuei209PhosphothreonineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei313PhosphothreonineBy similarity1
Modified residuei339PhosphoserineBy similarity1
Modified residuei367PhosphothreonineBy similarity1
Modified residuei380PhosphoserineBy similarity1
Modified residuei387PhosphoserineBy similarity1
Modified residuei427PhosphoserineBy similarity1
Modified residuei431PhosphothreonineBy similarity1
Modified residuei436PhosphoserineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei447PhosphothreonineBy similarity1
Modified residuei821PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs specifically during mitosis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ4V8A2.
PRIDEiQ4V8A2.

PTM databases

iPTMnetiQ4V8A2.
PhosphoSitePlusiQ4V8A2.

Expressioni

Gene expression databases

BgeeiENSRNOG00000005904.
GenevisibleiQ4V8A2. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi262095. 5 interactors.
IntActiQ4V8A2. 1 interactor.
STRINGi10116.ENSRNOP00000007963.

Structurei

3D structure databases

ProteinModelPortaliQ4V8A2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati84 – 114TPR 1Add BLAST31
Repeati115 – 148TPR 2Add BLAST34
Repeati499 – 532TPR 3Add BLAST34
Repeati567 – 600TPR 4Add BLAST34
Repeati602 – 634TPR 5Add BLAST33
Repeati635 – 668TPR 6Add BLAST34
Repeati670 – 702TPR 7Add BLAST33
Repeati704 – 736TPR 8Add BLAST33
Repeati737 – 770TPR 9Add BLAST34

Sequence similaritiesi

Belongs to the APC3/CDC27 family.Curated
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1126. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00550000074887.
HOGENOMiHOG000231056.
HOVERGENiHBG050859.
InParanoidiQ4V8A2.
KOiK03350.
OMAiNSCTTQV.
OrthoDBiEOG091G03JF.

Family and domain databases

InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 2 hits.
PF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4V8A2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR
60 70 80 90 100
SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ
110 120 130 140 150
KSHDDLVTEF GDSACFTLSL LGHVYCKTDR LAKGSECYQK SLSLNPFLWS
160 170 180 190 200
PFESLCEIGE KPDPDQTFKL TSLQNFSSCL PNTCTALVSN HSLSHRQPET
210 220 230 240 250
VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI SPDNVPLGTG
260 270 280 290 300
PSILSKQVQN KPKTGRSLLG GPTALSPLTP SFGILPLETP SPGDGSYLQN
310 320 330 340 350
YTNTPSVIDV PSTGAPTKKS VARMGHTGAK SVFSQSGNSR EATPVLVAQT
360 370 380 390 400
QSSGPQTSTT PQVLSPTITS PPNALPRRSS RLFTSDSSTT KENSKKLKMK
410 420 430 440 450
FPPKIPNRKT KSKTNKGGIT QPNINDSLEI TKLDSSIISE GKISTITPQI
460 470 480 490 500
QAFNLQKAAA GLMSLLREMG KGYLALCSYN CKEAINILSH LPSHHYSTGW
510 520 530 540 550
VLCQIGRAYF ELSEYMQAER IFSEVRRIES FRVEGMEIYS TTLWHLQKDV
560 570 580 590 600
ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY
610 620 630 640 650
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK
660 670 680 690 700
FSLAEMHFQK ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP
710 720 730 740 750
KNPLCKFHRA SVLFANEKYK SALQELEELK QIVPKESLVY FLIGKVYKKL
760 770 780 790 800
GQTHLALMNF SWAMDLDPKG ANNQIKEAID KRYLPDDEEP ITQEEQIMGT
810 820
DESQESSMTD ADDTQLHAAE SDEF
Length:824
Mass (Da):91,663
Last modified:July 5, 2005 - v1
Checksum:i24B02A896A0463A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC097475 mRNA. Translation: AAH97475.1.
RefSeqiNP_001019964.1. NM_001024793.1.
UniGeneiRn.198335.

Genome annotation databases

EnsembliENSRNOT00000007963; ENSRNOP00000007963; ENSRNOG00000005904.
GeneIDi360643.
KEGGirno:360643.
UCSCiRGD:1304921. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC097475 mRNA. Translation: AAH97475.1.
RefSeqiNP_001019964.1. NM_001024793.1.
UniGeneiRn.198335.

3D structure databases

ProteinModelPortaliQ4V8A2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi262095. 5 interactors.
IntActiQ4V8A2. 1 interactor.
STRINGi10116.ENSRNOP00000007963.

PTM databases

iPTMnetiQ4V8A2.
PhosphoSitePlusiQ4V8A2.

Proteomic databases

PaxDbiQ4V8A2.
PRIDEiQ4V8A2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007963; ENSRNOP00000007963; ENSRNOG00000005904.
GeneIDi360643.
KEGGirno:360643.
UCSCiRGD:1304921. rat.

Organism-specific databases

CTDi996.
RGDi1304921. Cdc27.

Phylogenomic databases

eggNOGiKOG1126. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00550000074887.
HOGENOMiHOG000231056.
HOVERGENiHBG050859.
InParanoidiQ4V8A2.
KOiK03350.
OMAiNSCTTQV.
OrthoDBiEOG091G03JF.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-RNO-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-RNO-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-RNO-174154. APC/C:Cdc20 mediated degradation of Securin.
R-RNO-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-RNO-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-RNO-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-RNO-176412. Phosphorylation of the APC/C.
R-RNO-179409. APC-Cdc20 mediated degradation of Nek2A.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2559582. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

PROiQ4V8A2.

Gene expression databases

BgeeiENSRNOG00000005904.
GenevisibleiQ4V8A2. RN.

Family and domain databases

InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 2 hits.
PF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDC27_RAT
AccessioniPrimary (citable) accession number: Q4V8A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.