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P22674

- CCNO_HUMAN

UniProt

P22674 - CCNO_HUMAN

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Protein

Cyclin-O

Gene

CCNO

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

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. cilium assembly Source: UniProtKB
  6. depyrimidination Source: Reactome
  7. DNA repair Source: Reactome
  8. embryo development Source: Ensembl
  9. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  10. response to drug Source: Ensembl
Complete GO annotation...

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. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: HGNC
Complete GO annotation...

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.
Orphaneti244. Primary ciliary dyskinesia.
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

MaxQBiP22674.
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. 9 interactions.
DIPiDIP-24234N.
IntActiP22674. 5 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.
GeneTreeiENSGT00760000118939.
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

        10         20         30         40         50
MVTPCPTSPS SPAARAGRRD NDQNLRAPVK KSRRPRLRRK QPLHPLNPCP
60 70 80 90 100
LPGDSGICDL FESPSSGSDG AESPSAARGG SPLPGPAQPV AQLDLQTFRD
110 120 130 140 150
YGQSCYAFRK AQESHFHPRE ALARQPQVTA ESRCKLLSWL IPVHRQFGLS
160 170 180 190 200
FESLCLTVNT LDRFLTTTPV AADCFQLLGV TSLLIACKQV EVHPPRVKQL
210 220 230 240 250
LALCCGAFSR QQLCNLECIV LHKLHFTLGA PTISFFLEHF THARVEAGQA
260 270 280 290 300
EASEALEAQA LARGVAELSL ADYAFTSYSP SLLAICCLAL ADRMLRVSRP
310 320 330 340 350
VDLRLGDHPE AALEDCMGKL QLLVAINSTS LTHMLPVQIC EKCSLPPSSK
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.Curated
The sequence CAA36728.1 differs from that shown. Reason: Sequencing errors.Curated

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:
EMBLi
GenBanki
DDBJi
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_021147.4. [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:
EMBLi
GenBanki
DDBJi
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_021147.4. [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. 9 interactions.
DIPi DIP-24234N.
IntActi P22674. 5 interactions.
MINTi MINT-1521909.
STRINGi 9606.ENSP00000282572.

PTM databases

PhosphoSitei P22674.

Polymorphism databases

DMDMi 118572733.

Proteomic databases

MaxQBi P22674.
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.
Orphaneti 244. Primary ciliary dyskinesia.
PharmGKBi PA38350.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5024.
GeneTreei ENSGT00760000118939.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 129 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