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Protein

Cell division cycle protein 27 homolog

Gene

CDC27

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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.1 Publication

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 - Molecular functioni

  • protein phosphatase binding Source: BHF-UCL

GO - Biological processi

  • anaphase-promoting complex-dependent catabolic process Source: Reactome
  • cell proliferation Source: ProtInc
  • metaphase/anaphase transition of mitotic cell cycle Source: MGI
  • protein K11-linked ubiquitination Source: UniProtKB

Keywordsi

Biological processUbl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-HSA-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176407 Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
R-HSA-176408 Regulation of APC/C activators between G1/S and early anaphase
R-HSA-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-HSA-176412 Phosphorylation of the APC/C
R-HSA-179409 APC-Cdc20 mediated degradation of Nek2A
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiP30260
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
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 namesi
Name:CDC27
Synonyms:ANAPC3, D0S1430E, D17S978E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000004897.11
HGNCiHGNC:1728 CDC27
MIMi116946 gene
neXtProtiNX_P30260

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi821S → A: Abolishes binding to MCPH1. 1 Publication1

Organism-specific databases

DisGeNETi996
OpenTargetsiENSG00000004897
PharmGKBiPA26261

Polymorphism and mutation databases

BioMutaiCDC27
DMDMi12644198

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001062731 – 824Cell division cycle protein 27 homologAdd BLAST824

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei205PhosphothreonineCombined sources1 Publication1
Modified residuei209Phosphothreonine1 Publication1
Modified residuei244Phosphothreonine1 Publication1
Modified residuei291Phosphoserine1 Publication1
Modified residuei313Phosphothreonine1 Publication1
Modified residuei339PhosphoserineCombined sources1
Modified residuei366PhosphothreonineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Modified residuei386PhosphoserineCombined sources1
Modified residuei426PhosphoserineCombined sources1 Publication1
Modified residuei430Phosphothreonine1 Publication1
Modified residuei435Phosphoserine1 Publication1
Modified residuei438PhosphoserineCombined sources1
Modified residuei446PhosphothreonineCombined sources1 Publication1
Modified residuei821Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs specifically during mitosis.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP30260
MaxQBiP30260
PaxDbiP30260
PeptideAtlasiP30260
PRIDEiP30260
ProteomicsDBi54645

PTM databases

iPTMnetiP30260
PhosphoSitePlusiP30260

Expressioni

Gene expression databases

BgeeiENSG00000004897
CleanExiHS_CDC27
ExpressionAtlasiP30260 baseline and differential
GenevisibleiP30260 HS

Organism-specific databases

HPAiCAB016315
HPA028129
HPA052399

Interactioni

Subunit structurei

Homodimer. The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa. Interacts with RB. Interacts with FAM168B/MANI (By similarity). Interacts with MCPH1.By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein phosphatase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107431, 141 interactors
CORUMiP30260
DIPiDIP-36422N
ELMiP30260
IntActiP30260, 69 interactors
MINTiP30260
STRINGi9606.ENSP00000434614

Structurei

Secondary structure

1824
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 17Combined sources10
Helixi21 – 34Combined sources14
Helixi38 – 50Combined sources13
Helixi54 – 63Combined sources10
Helixi69 – 81Combined sources13
Helixi85 – 93Combined sources9
Beta strandi96 – 98Combined sources3
Helixi103 – 110Combined sources8
Helixi111 – 113Combined sources3
Helixi114 – 127Combined sources14
Helixi131 – 144Combined sources14
Helixi149 – 158Combined sources10
Helixi164 – 167Combined sources4
Helixi457 – 477Combined sources21
Helixi481 – 489Combined sources9
Helixi493 – 497Combined sources5
Helixi499 – 512Combined sources14
Helixi515 – 528Combined sources14
Turni529 – 531Combined sources3
Helixi536 – 546Combined sources11
Helixi549 – 562Combined sources14
Helixi567 – 579Combined sources13
Helixi583 – 596Combined sources14
Helixi601 – 613Combined sources13
Helixi617 – 630Combined sources14
Helixi635 – 648Combined sources14
Helixi651 – 664Combined sources14
Helixi668 – 681Combined sources14
Helixi685 – 690Combined sources6
Helixi693 – 698Combined sources6
Turni699 – 701Combined sources3
Helixi703 – 715Combined sources13
Helixi719 – 732Combined sources14
Beta strandi733 – 735Combined sources3
Helixi737 – 748Combined sources12
Helixi754 – 766Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3T1NX-ray2.60C/D821-824[»]
4RG6X-ray3.30A/B1-824[»]
4RG7X-ray4.25A/B1-824[»]
4RG9X-ray3.25A/B1-824[»]
4UI9electron microscopy3.60F/H1-824[»]
5A31electron microscopy4.30F/H1-824[»]
5G04electron microscopy4.00F/H1-824[»]
5G05electron microscopy3.40F/H1-824[»]
5KHRelectron microscopy6.10F/H1-824[»]
5KHUelectron microscopy4.80F/H1-824[»]
5L9Telectron microscopy6.40F/H1-824[»]
5L9Uelectron microscopy6.40F/H1-824[»]
5LCWelectron microscopy4.00F/H1-824[»]
ProteinModelPortaliP30260
SMRiP30260
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati6 – 35TPR 1Add BLAST30
Repeati38 – 65TPR 2Add BLAST28
Repeati67 – 99TPR 3Add BLAST33
Repeati115 – 145TPR 4Add BLAST31
Repeati465 – 495TPR 5Add BLAST31
Repeati499 – 528TPR 6Add BLAST30
Repeati533 – 563TPR 7Add BLAST31
Repeati567 – 598TPR 8Add BLAST32
Repeati601 – 631TPR 9Add BLAST31
Repeati635 – 667TPR 10Add BLAST33
Repeati670 – 702TPR 11Add BLAST33
Repeati704 – 734TPR 12Add BLAST31
Repeati737 – 768TPR 13Add BLAST32

Sequence similaritiesi

Belongs to the APC3/CDC27 family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1126 Eukaryota
COG0457 LUCA
GeneTreeiENSGT00550000074887
HOGENOMiHOG000231056
HOVERGENiHBG050859
InParanoidiP30260
KOiK03350
OMAiMPLTSPC
OrthoDBiEOG091G03JF
PhylomeDBiP30260
TreeFamiTF101058

Family and domain databases

Gene3Di1.25.40.10, 4 hits
InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR001440 TPR_1
IPR019734 TPR_repeat
PfamiView protein in Pfam
PF00515 TPR_1, 2 hits
PF13181 TPR_8, 2 hits
SMARTiView protein in SMART
SM00028 TPR, 8 hits
SUPFAMiSSF48452 SSF48452, 3 hits
PROSITEiView protein in PROSITE
PS50005 TPR, 8 hits
PS50293 TPR_REGION, 2 hits

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P30260-1) [UniParc]FASTAAdd to basket

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.

« 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
KSHDDIVTEF GDSACFTLSL LGHVYCKTDR LAKGSECYQK SLSLNPFLWS
160 170 180 190 200
PFESLCEIGE KPDPDQTFKF TSLQNFSNCL PNSCTTQVPN HSLSHRQPET
210 220 230 240 250
VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI SPDTVPLGTG
260 270 280 290 300
TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN
310 320 330 340 350
YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ
360 370 380 390 400
SSGPQTSTTP QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF
410 420 430 440 450
PPKIPNRKTK SKTNKGGITQ PNINDSLEIT KLDSSIISEG KISTITPQIQ
460 470 480 490 500
AFNLQKAAAE GLMSLLREMG KGYLALCSYN CKEAINILSH LPSHHYNTGW
510 520 530 540 550
VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS 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):91,867
Last modified:December 1, 2000 - v2
Checksum:iE6C8F59C1EF1DCBA
GO
Isoform 2 (identifier: P30260-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:830
Mass (Da):92,612
Checksum:i00CE7174F8165CA1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti403K → E in AAH11656 (PubMed:15489334).Curated1
Sequence conflicti460Missing in AAA60471 (PubMed:8234252).Curated1
Sequence conflicti715A → R in AAA60471 (PubMed:8234252).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035861270G → A in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_014489496Y → H. Corresponds to variant dbSNP:rs13666Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_047225319K → KTFRVLQ in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS11509.1 [P30260-1]
CCDS45720.1 [P30260-2]
PIRiI52835
RefSeqiNP_001107563.1, NM_001114091.2 [P30260-2]
NP_001247.3, NM_001256.4 [P30260-1]
UniGeneiHs.463295
Hs.602766

Genome annotation databases

EnsembliENST00000066544; ENSP00000066544; ENSG00000004897 [P30260-1]
ENST00000531206; ENSP00000434614; ENSG00000004897 [P30260-2]
GeneIDi996
KEGGihsa:996
UCSCiuc002ild.5 human [P30260-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCDC27_HUMAN
AccessioniPrimary (citable) accession number: P30260
Secondary accession number(s): G3V1C4, Q16349, Q96F35
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 1, 2000
Last modified: June 20, 2018
This is version 192 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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