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P22674

- CCNO_HUMAN

UniProt

P22674 - CCNO_HUMAN

Protein

Cyclin-O

Gene

CCNO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of MCIDAS to promote mother centriole amplification and maturation in preparation for apical docking.1 Publication

    GO - Molecular functioni

    1. uracil DNA N-glycosylase activity Source: HGNC

    GO - Biological processi

    1. base-excision repair Source: HGNC
    2. base-excision repair, AP site formation Source: Reactome
    3. cell cycle Source: UniProtKB
    4. cell division Source: UniProtKB
    5. depyrimidination Source: Reactome
    6. DNA repair Source: Reactome
    7. embryo development Source: Ensembl
    8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    9. response to drug Source: Ensembl

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division, Cilium biogenesis/degradation

    Enzyme and pathway databases

    ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
    REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
    SignaLinkiP22674.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-O
    Gene namesi
    Name:CCNO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:18576. CCNO.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localizes to the apical part of cytoplasm.1 Publication

    GO - Cellular componenti

    1. nucleoplasm Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Ciliary dyskinesia, primary, 29 (CILD29) [MIM:615872]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia. CILD29 patients do not exhibit situs inversus, a congenital abnormality in which visceral organs are opposite to their normal positions (situs solitus) due to lateral transposition.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. Marked reduction of cilia in multiciliate cells due to defective mother centriole generation and placement. Remaining cilia correctly express axonemal motor proteins, are motile and do not show beating defects. Defects are probably caused by a strong reduction in the number of multiple motile cilia covering the cell surface in respiratory epithelial cells (PubMed:24747639).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti239 – 2391H → R in CILD29. 1 Publication
    VAR_071197

    Keywords - Diseasei

    Ciliopathy, Disease mutation, Primary ciliary dyskinesia

    Organism-specific databases

    MIMi615872. phenotype.
    PharmGKBiPA38350.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 350350Cyclin-OPRO_0000176175Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei81 – 811Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP22674.
    PRIDEiP22674.

    PTM databases

    PhosphoSiteiP22674.

    Expressioni

    Tissue specificityi

    Present in respiratory cells (at protein level).1 Publication

    Developmental stagei

    Maximum levels during G1 phase. Levels decrease through S and G2 phases.1 Publication

    Gene expression databases

    BgeeiP22674.
    CleanExiHS_CCNO.
    GenevestigatoriP22674.

    Organism-specific databases

    HPAiHPA050090.

    Interactioni

    Protein-protein interaction databases

    BioGridi115595. 8 interactions.
    DIPiDIP-24234N.
    IntActiP22674. 4 interactions.
    MINTiMINT-1521909.
    STRINGi9606.ENSP00000282572.

    Structurei

    3D structure databases

    ProteinModelPortaliP22674.
    SMRiP22674. Positions 122-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cyclin family.Curated

    Phylogenomic databases

    eggNOGiCOG5024.
    HOGENOMiHOG000060283.
    HOVERGENiHBG062171.
    InParanoidiP22674.
    KOiK10861.
    OMAiLDLQTFR.
    OrthoDBiEOG77DJ6P.
    PhylomeDBiP22674.
    TreeFamiTF332057.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR028864. Ccno.
    IPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR004367. Cyclin_C-dom.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10177:SF14. PTHR10177:SF14. 1 hit.
    PfamiPF02984. Cyclin_C. 1 hit.
    PF00134. Cyclin_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
    SMARTiSM00385. CYCLIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P22674-1) [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

    MVTPCPTSPS SPAARAGRRD NDQNLRAPVK KSRRPRLRRK QPLHPLNPCP    50
    LPGDSGICDL FESPSSGSDG AESPSAARGG SPLPGPAQPV AQLDLQTFRD 100
    YGQSCYAFRK AQESHFHPRE ALARQPQVTA ESRCKLLSWL IPVHRQFGLS 150
    FESLCLTVNT LDRFLTTTPV AADCFQLLGV TSLLIACKQV EVHPPRVKQL 200
    LALCCGAFSR QQLCNLECIV LHKLHFTLGA PTISFFLEHF THARVEAGQA 250
    EASEALEAQA LARGVAELSL ADYAFTSYSP SLLAICCLAL ADRMLRVSRP 300
    VDLRLGDHPE AALEDCMGKL QLLVAINSTS LTHMLPVQIC EKCSLPPSSK 350
    Length:350
    Mass (Da):38,096
    Last modified:November 28, 2006 - v2
    Checksum:iAF1C1D1C34334BED
    GO
    Isoform 2 (identifier: P22674-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         129-131: TAE → RCW
         132-350: Missing.

    Show »
    Length:131
    Mass (Da):14,297
    Checksum:i75705330B7735297
    GO

    Sequence cautioni

    The sequence AAB05817.1 differs from that shown. Reason: Sequencing errors.
    The sequence CAA36728.1 differs from that shown. Reason: Sequencing errors.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti246 – 2461E → G in BAB15351. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti161 – 1611L → M.
    Corresponds to variant rs13169396 [ dbSNP | Ensembl ].
    VAR_029081
    Natural varianti239 – 2391H → R in CILD29. 1 Publication
    VAR_071197

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei129 – 1313TAE → RCW in isoform 2. 2 PublicationsVSP_021655
    Alternative sequencei132 – 350219Missing in isoform 2. 2 PublicationsVSP_021656Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52486 mRNA. Translation: CAA36728.1. Sequence problems.
    M87499 Genomic DNA. Translation: AAB05817.1. Sequence problems.
    AK026075 mRNA. Translation: BAB15351.1.
    AK290030 mRNA. Translation: BAF82719.1.
    AC026704 Genomic DNA. No translation available.
    CH471123 Genomic DNA. Translation: EAW54913.1.
    BC004877 mRNA. Translation: AAH04877.1.
    CCDSiCCDS34157.1. [P22674-1]
    PIRiS14266.
    RefSeqiNP_066970.3. NM_021147.3. [P22674-1]
    UniGeneiHs.3041.

    Genome annotation databases

    EnsembliENST00000282572; ENSP00000282572; ENSG00000152669. [P22674-1]
    ENST00000501463; ENSP00000422485; ENSG00000152669. [P22674-2]
    GeneIDi10309.
    KEGGihsa:10309.
    UCSCiuc003jpw.3. human. [P22674-1]

    Polymorphism databases

    DMDMi118572733.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52486 mRNA. Translation: CAA36728.1 . Sequence problems.
    M87499 Genomic DNA. Translation: AAB05817.1 . Sequence problems.
    AK026075 mRNA. Translation: BAB15351.1 .
    AK290030 mRNA. Translation: BAF82719.1 .
    AC026704 Genomic DNA. No translation available.
    CH471123 Genomic DNA. Translation: EAW54913.1 .
    BC004877 mRNA. Translation: AAH04877.1 .
    CCDSi CCDS34157.1. [P22674-1 ]
    PIRi S14266.
    RefSeqi NP_066970.3. NM_021147.3. [P22674-1 ]
    UniGenei Hs.3041.

    3D structure databases

    ProteinModelPortali P22674.
    SMRi P22674. Positions 122-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115595. 8 interactions.
    DIPi DIP-24234N.
    IntActi P22674. 4 interactions.
    MINTi MINT-1521909.
    STRINGi 9606.ENSP00000282572.

    PTM databases

    PhosphoSitei P22674.

    Polymorphism databases

    DMDMi 118572733.

    Proteomic databases

    PaxDbi P22674.
    PRIDEi P22674.

    Protocols and materials databases

    DNASUi 10309.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282572 ; ENSP00000282572 ; ENSG00000152669 . [P22674-1 ]
    ENST00000501463 ; ENSP00000422485 ; ENSG00000152669 . [P22674-2 ]
    GeneIDi 10309.
    KEGGi hsa:10309.
    UCSCi uc003jpw.3. human. [P22674-1 ]

    Organism-specific databases

    CTDi 10309.
    GeneCardsi GC05M054526.
    H-InvDB HIX0022318.
    HIX0200729.
    HGNCi HGNC:18576. CCNO.
    HPAi HPA050090.
    MIMi 607752. gene.
    615872. phenotype.
    neXtProti NX_P22674.
    PharmGKBi PA38350.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5024.
    HOGENOMi HOG000060283.
    HOVERGENi HBG062171.
    InParanoidi P22674.
    KOi K10861.
    OMAi LDLQTFR.
    OrthoDBi EOG77DJ6P.
    PhylomeDBi P22674.
    TreeFami TF332057.

    Enzyme and pathway databases

    Reactomei REACT_1064. Displacement of DNA glycosylase by APE1.
    REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
    SignaLinki P22674.

    Miscellaneous databases

    GeneWikii Cyclin_O.
    GenomeRNAii 10309.
    NextBioi 39071.
    PROi P22674.
    SOURCEi Search...

    Gene expression databases

    Bgeei P22674.
    CleanExi HS_CCNO.
    Genevestigatori P22674.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR028864. Ccno.
    IPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR004367. Cyclin_C-dom.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10177:SF14. PTHR10177:SF14. 1 hit.
    Pfami PF02984. Cyclin_C. 1 hit.
    PF00134. Cyclin_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001771. Cyclin_A_B_D_E. 1 hit.
    SMARTi SM00385. CYCLIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase."
      Muller S.J., Caradonna S.
      Biochim. Biophys. Acta 1088:197-207(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: T-cell.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus and Kidney epithelium.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
      Tissue: Pancreas.
    6. "Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase."
      Muller S.J., Caradonna S.
      J. Biol. Chem. 268:1310-1319(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, DEVELOPMENTAL STAGE.
    7. "The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its relationship to human and chimpanzee homologues."
      Hirst R., Gosden R., Miller D.
      Gene 375:95-102(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: VARIANT CILD29 ARG-239, INVOLVEMENT IN CILD29, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCCNO_HUMAN
    AccessioniPrimary (citable) accession number: P22674
    Secondary accession number(s): A8K1W5
    , Q0P6J2, Q9H6B0, Q9UMD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    Caution

    Was originally thought to have uracil-DNA glycosylase (UDG) activity and wrongly named UNG2 and UDG2 (PubMed:2001396). It was later shown that it is a member of the cyclin family (PubMed:8419333). UNG2 corresponds to the isoform 2 of UNG gene.2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3