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Protein

Anaphase-promoting complex subunit CDC26

Gene

CDC26

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. May recruit the E2 ubiquitin-conjugating enzymes to the complex.1 Publication

Pathway: 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

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit CDC26
Alternative name(s):
Anaphase-promoting complex subunit 12
Short name:
APC12
Cell division cycle protein 26 homolog
Gene namesi
Name:CDC26
Synonyms:ANAPC12, C9orf17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17839. CDC26.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25974.

Polymorphism and mutation databases

BioMutaiCDC26.
DMDMi74751322.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8585Anaphase-promoting complex subunit CDC26PRO_0000271194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine2 Publications
Modified residuei82 – 821Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NHZ8.
PaxDbiQ8NHZ8.
PRIDEiQ8NHZ8.

PTM databases

PhosphoSiteiQ8NHZ8.

Expressioni

Gene expression databases

BgeeiQ8NHZ8.
CleanExiHS_CDC26.
ExpressionAtlasiQ8NHZ8. baseline.
GenevisibleiQ8NHZ8. HS.

Organism-specific databases

HPAiHPA044130.

Interactioni

Subunit structurei

V-shaped homodimer. Interacts with CDC16. 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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC16Q130428EBI-2555941,EBI-994830

Protein-protein interaction databases

BioGridi128878. 25 interactions.
DIPiDIP-48551N.
IntActiQ8NHZ8. 24 interactions.
STRINGi9606.ENSP00000363322.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Helixi17 – 259Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HYMX-ray2.80A/C/E/G/I/K1-29[»]
ProteinModelPortaliQ8NHZ8.
SMRiQ8NHZ8. Positions 1-26.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NHZ8.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili7 – 3832Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the CDC26 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG42592.
GeneTreeiENSGT00390000008457.
HOGENOMiHOG000231545.
HOVERGENiHBG057346.
InParanoidiQ8NHZ8.
KOiK03359.
OMAiQFGNFEF.
OrthoDBiEOG7Q2N8D.
PhylomeDBiQ8NHZ8.
TreeFamiTF101057.

Family and domain databases

InterProiIPR018860. APC_suCDC26.
[Graphical view]
PfamiPF10471. APC_CDC26. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NHZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL
60 70 80
SSDPKSREQM INDRIGYKPQ PKPNNRSSQF GSLEF
Length:85
Mass (Da):9,777
Last modified:October 1, 2002 - v1
Checksum:i134970EE68F0142C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503918 mRNA. Translation: AAM34207.1.
AL449305 Genomic DNA. Translation: CAI10967.1.
BC042534 mRNA. Translation: AAH42534.1.
BC066300 mRNA. Translation: AAH66300.1.
CCDSiCCDS6790.1.
RefSeqiNP_644815.1. NM_139286.3.
UniGeneiHs.727648.

Genome annotation databases

EnsembliENST00000374206; ENSP00000363322; ENSG00000176386.
GeneIDi246184.
KEGGihsa:246184.
UCSCiuc004bgw.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503918 mRNA. Translation: AAM34207.1.
AL449305 Genomic DNA. Translation: CAI10967.1.
BC042534 mRNA. Translation: AAH42534.1.
BC066300 mRNA. Translation: AAH66300.1.
CCDSiCCDS6790.1.
RefSeqiNP_644815.1. NM_139286.3.
UniGeneiHs.727648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HYMX-ray2.80A/C/E/G/I/K1-29[»]
ProteinModelPortaliQ8NHZ8.
SMRiQ8NHZ8. Positions 1-26.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128878. 25 interactions.
DIPiDIP-48551N.
IntActiQ8NHZ8. 24 interactions.
STRINGi9606.ENSP00000363322.

PTM databases

PhosphoSiteiQ8NHZ8.

Polymorphism and mutation databases

BioMutaiCDC26.
DMDMi74751322.

Proteomic databases

MaxQBiQ8NHZ8.
PaxDbiQ8NHZ8.
PRIDEiQ8NHZ8.

Protocols and materials databases

DNASUi246184.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374206; ENSP00000363322; ENSG00000176386.
GeneIDi246184.
KEGGihsa:246184.
UCSCiuc004bgw.2. human.

Organism-specific databases

CTDi246184.
GeneCardsiGC09M116018.
HGNCiHGNC:17839. CDC26.
HPAiHPA044130.
MIMi614533. gene.
neXtProtiNX_Q8NHZ8.
PharmGKBiPA25974.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42592.
GeneTreeiENSGT00390000008457.
HOGENOMiHOG000231545.
HOVERGENiHBG057346.
InParanoidiQ8NHZ8.
KOiK03359.
OMAiQFGNFEF.
OrthoDBiEOG7Q2N8D.
PhylomeDBiQ8NHZ8.
TreeFamiTF101057.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Miscellaneous databases

EvolutionaryTraceiQ8NHZ8.
GenomeRNAii246184.
NextBioi91885.
PROiQ8NHZ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NHZ8.
CleanExiHS_CDC26.
ExpressionAtlasiQ8NHZ8. baseline.
GenevisibleiQ8NHZ8. HS.

Family and domain databases

InterProiIPR018860. APC_suCDC26.
[Graphical view]
PfamiPF10471. APC_CDC26. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex."
    Gmachl M., Gieffers C., Podtelejnikov A.V., Mann M., Peters J.-M.
    Proc. Natl. Acad. Sci. U.S.A. 97:8973-8978(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE APC/C COMPLEX.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Brain and Skin.
  4. "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.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-42 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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.
  10. "Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure."
    Wang J., Dye B.T., Rajashankar K.R., Kurinov I., Schulman B.A.
    Nat. Struct. Mol. Biol. 16:987-989(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-29 IN COMPLEX WITH CDC16.
  11. "Molecular architecture and mechanism of the anaphase-promoting complex."
    Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.
    Nature 513:388-393(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, SUBUNIT.

Entry informationi

Entry nameiCDC26_HUMAN
AccessioniPrimary (citable) accession number: Q8NHZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2002
Last modified: June 24, 2015
This is version 115 of the entry and version 1 of the sequence. [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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.