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Q8NHZ8

- CDC26_HUMAN

UniProt

Q8NHZ8 - CDC26_HUMAN

Protein

Anaphase-promoting complex subunit CDC26

Gene

CDC26

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. mitotic cell cycle Source: Reactome
    3. mitotic nuclear division Source: UniProtKB-KW
    4. mitotic spindle assembly checkpoint Source: Reactome
    5. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    6. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    7. protein K11-linked ubiquitination Source: UniProtKB
    8. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome

    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_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.
    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17839. CDC26.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25974.

    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.
    GenevestigatoriQ8NHZ8.

    Organism-specific databases

    HPAiHPA044130.

    Interactioni

    Subunit structurei

    The APC/C is composed of at least 12 subunits.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC16Q130423EBI-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 – 163
    Helixi17 – 259

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000231545.
    HOVERGENiHBG057346.
    InParanoidiQ8NHZ8.
    KOiK03359.
    OMAiNENQNER.
    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

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi74751322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF503918 mRNA. Translation: AAM34207.1 .
    AL449305 Genomic DNA. Translation: CAI10967.1 .
    BC042534 mRNA. Translation: AAH42534.1 .
    BC066300 mRNA. Translation: AAH66300.1 .
    CCDSi CCDS6790.1.
    RefSeqi NP_644815.1. NM_139286.3.
    UniGenei Hs.727648.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HYM X-ray 2.80 A/C/E/G/I/K 1-29 [» ]
    ProteinModelPortali Q8NHZ8.
    SMRi Q8NHZ8. Positions 1-26.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128878. 25 interactions.
    DIPi DIP-48551N.
    IntActi Q8NHZ8. 24 interactions.
    STRINGi 9606.ENSP00000363322.

    PTM databases

    PhosphoSitei Q8NHZ8.

    Polymorphism databases

    DMDMi 74751322.

    Proteomic databases

    MaxQBi Q8NHZ8.
    PaxDbi Q8NHZ8.
    PRIDEi Q8NHZ8.

    Protocols and materials databases

    DNASUi 246184.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374206 ; ENSP00000363322 ; ENSG00000176386 .
    GeneIDi 246184.
    KEGGi hsa:246184.
    UCSCi uc004bgw.2. human.

    Organism-specific databases

    CTDi 246184.
    GeneCardsi GC09M116018.
    HGNCi HGNC:17839. CDC26.
    HPAi HPA044130.
    MIMi 614533. gene.
    neXtProti NX_Q8NHZ8.
    PharmGKBi PA25974.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42592.
    HOGENOMi HOG000231545.
    HOVERGENi HBG057346.
    InParanoidi Q8NHZ8.
    KOi K03359.
    OMAi NENQNER.
    OrthoDBi EOG7Q2N8D.
    PhylomeDBi Q8NHZ8.
    TreeFami TF101057.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_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_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.

    Miscellaneous databases

    EvolutionaryTracei Q8NHZ8.
    GenomeRNAii 246184.
    NextBioi 91885.
    PROi Q8NHZ8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8NHZ8.
    CleanExi HS_CDC26.
    Genevestigatori Q8NHZ8.

    Family and domain databases

    InterProi IPR018860. APC_suCDC26.
    [Graphical view ]
    Pfami PF10471. APC_CDC26. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 107 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