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Protein

Cyclin-Y

Gene

Ccny

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Positive regulatory subunit of the cyclin-dependent kinase CDK14/PFTK1. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway (By similarity). Recruits CDK16 to the plasma membrane (By similarity). Positive regulatory subunit of the cyclin-dependent kinase CDK16.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-Y
Alternative name(s):
Cyclin fold protein 1
Gene namesi
Name:Ccny
Synonyms:Cfp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1915224. Ccny.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 341340Cyclin-YPRO_0000080515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei25 – 251PhosphoserineBy similarity
Modified residuei30 – 301PhosphothreonineBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei37 – 371PhosphothreonineBy similarity
Modified residuei67 – 671Phosphothreonine; by CDK14By similarity
Modified residuei71 – 711Phosphoserine; by CDK14By similarity
Modified residuei73 – 731Phosphoserine; by CDK14By similarity
Modified residuei75 – 751PhosphothreonineBy similarity
Modified residuei83 – 831Phosphoserine; by CDK14By similarity
Modified residuei99 – 991PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei280 – 2801PhosphoserineCombined sources
Modified residuei288 – 2881Phosphoserine; by CDK14By similarity
Modified residuei295 – 2951Phosphoserine; by CDK14By similarity
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated; leading to its degradation.By similarity
Heavily phosphorylated. Phosphorylation at Ser-71 and Ser-73 by CDK14 is enhanced during the G2 and M cell cycle phases, and creates a phosphodegron triggering SCF-dependent ubiquitination.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8BGU5.
MaxQBiQ8BGU5.
PaxDbiQ8BGU5.
PRIDEiQ8BGU5.

PTM databases

iPTMnetiQ8BGU5.
PhosphoSiteiQ8BGU5.
SwissPalmiQ8BGU5.

Expressioni

Tissue specificityi

Detected in brain, heart, lung, skeletal muscle, ovary, thymus and testis (at protein level).1 Publication

Gene expression databases

BgeeiQ8BGU5.
CleanExiMM_CCNY.
GenevisibleiQ8BGU5. MM.

Interactioni

Subunit structurei

Interacts with CDK14 and LRP6 (By similarity). Interacts with CDK16.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdk16Q047352EBI-772904,EBI-11615670

Protein-protein interaction databases

IntActiQ8BGU5. 4 interactions.
MINTiMINT-4125949.
STRINGi10090.ENSMUSP00000050001.

Structurei

3D structure databases

ProteinModelPortaliQ8BGU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 265123Cyclin N-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family. Cyclin Y subfamily.Curated
Contains 1 cyclin N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG1675. Eukaryota.
ENOG410XNQX. LUCA.
GeneTreeiENSGT00390000006626.
HOGENOMiHOG000021397.
HOVERGENiHBG058985.
InParanoidiQ8BGU5.
OMAiYDKHDPE.
OrthoDBiEOG7DC24W.
PhylomeDBiQ8BGU5.
TreeFamiTF314464.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR006671. Cyclin_N.
IPR012399. Cyclin_Y.
[Graphical view]
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF028934. Cyclin_CG14939. 1 hit.
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q8BGU5-1) [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
MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI
60 70 80 90 100
DDLNMEFNPS DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQTSRKYSS
110 120 130 140 150
CSTIFLDDST VSQPNLKYTI KCVALAIYYH IKNRDPDGRM LLDIFDENLH
160 170 180 190 200
PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS AAQLTAECAI VTLVYLERLL
210 220 230 240 250
TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI LKDITVEDMN
260 270 280 290 300
ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH
310 320 330 340
KLEAISRLCE DKYKDLRKPM RKRSASADNL ILPRWSPAII S
Length:341
Mass (Da):39,395
Last modified:March 1, 2003 - v1
Checksum:i6F16CE5B14559FCB
GO
Isoform 2 (identifier: Q8BGU5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-76: Missing.

Show »
Length:316
Mass (Da):36,562
Checksum:i22558710C92190FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571L → P in BAB30772 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei52 – 7625Missing in isoform 2. 1 PublicationVSP_014835Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017493 mRNA. Translation: BAB30772.1.
AK028696 mRNA. Translation: BAC26071.1.
AK076556 mRNA. Translation: BAC36391.1.
BC023321 mRNA. Translation: AAH23321.1.
BC035524 mRNA. Translation: AAH35524.1.
CCDSiCCDS29050.1. [Q8BGU5-1]
RefSeqiNP_080760.2. NM_026484.3. [Q8BGU5-1]
UniGeneiMm.376607.
Mm.86523.

Genome annotation databases

EnsembliENSMUST00000053917; ENSMUSP00000050001; ENSMUSG00000024286. [Q8BGU5-1]
GeneIDi67974.
KEGGimmu:67974.
UCSCiuc008eai.1. mouse. [Q8BGU5-1]
uc012azd.1. mouse. [Q8BGU5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017493 mRNA. Translation: BAB30772.1.
AK028696 mRNA. Translation: BAC26071.1.
AK076556 mRNA. Translation: BAC36391.1.
BC023321 mRNA. Translation: AAH23321.1.
BC035524 mRNA. Translation: AAH35524.1.
CCDSiCCDS29050.1. [Q8BGU5-1]
RefSeqiNP_080760.2. NM_026484.3. [Q8BGU5-1]
UniGeneiMm.376607.
Mm.86523.

3D structure databases

ProteinModelPortaliQ8BGU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BGU5. 4 interactions.
MINTiMINT-4125949.
STRINGi10090.ENSMUSP00000050001.

PTM databases

iPTMnetiQ8BGU5.
PhosphoSiteiQ8BGU5.
SwissPalmiQ8BGU5.

Proteomic databases

EPDiQ8BGU5.
MaxQBiQ8BGU5.
PaxDbiQ8BGU5.
PRIDEiQ8BGU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053917; ENSMUSP00000050001; ENSMUSG00000024286. [Q8BGU5-1]
GeneIDi67974.
KEGGimmu:67974.
UCSCiuc008eai.1. mouse. [Q8BGU5-1]
uc012azd.1. mouse. [Q8BGU5-2]

Organism-specific databases

CTDi219771.
MGIiMGI:1915224. Ccny.

Phylogenomic databases

eggNOGiKOG1675. Eukaryota.
ENOG410XNQX. LUCA.
GeneTreeiENSGT00390000006626.
HOGENOMiHOG000021397.
HOVERGENiHBG058985.
InParanoidiQ8BGU5.
OMAiYDKHDPE.
OrthoDBiEOG7DC24W.
PhylomeDBiQ8BGU5.
TreeFamiTF314464.

Miscellaneous databases

ChiTaRSiCcny. mouse.
NextBioi326110.
PROiQ8BGU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGU5.
CleanExiMM_CCNY.
GenevisibleiQ8BGU5. MM.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR006671. Cyclin_N.
IPR012399. Cyclin_Y.
[Graphical view]
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF028934. Cyclin_CG14939. 1 hit.
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo, Skin and Testis.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: Czech II and FVB/N.
    Tissue: Kidney and Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis."
    Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M., Pelliniemi L.J., Boesl M., Geley S.
    Mol. Cell. Biol. 32:868-879(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDK16, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCCNY_MOUSE
AccessioniPrimary (citable) accession number: Q8BGU5
Secondary accession number(s): Q8CI87, Q9CYN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.