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Protein
Submitted name:

Ccne1 protein

Gene

Ccne1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

CyclinUniRule annotationSAAS annotation

Enzyme and pathway databases

ReactomeiR-RNO-113510. E2F mediated regulation of DNA replication.
R-RNO-1538133. G0 and Early G1.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-RNO-6804116. TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
R-RNO-69200. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
R-RNO-69202. Cyclin E associated events during G1/S transition.
R-RNO-69205. G1/S-Specific Transcription.
R-RNO-69563. p53-Dependent G1 DNA Damage Response.

Names & Taxonomyi

Protein namesi
Submitted name:
Ccne1 proteinImported
Submitted name:
G1/S-specific cyclin-E1Imported
Gene namesi
Name:Ccne1Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2294. Ccne1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

PeptideAtlasiB1WC54.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020014.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini146 – 17732Cyclin N-terminalInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG0655. Eukaryota.
ENOG410XS2J. LUCA.
GeneTreeiENSGT00760000118939.
HOVERGENiHBG050834.
KOiK06626.
OMAiPLLQPKM.
OrthoDBiEOG7HB595.
TreeFamiTF101005.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR028858. Cyclin_E.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF71. PTHR10177:SF71. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1WC54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRERKERDS KDHSNMKEEG GSDLSVRSRK RKANVAVFLQ DPDEEIAKID
60 70 80 90 100
KTVKSQDSSQ PWDDDSACVD PCSFIPTPNK EEDNELEYPK TAFQPRKIRP
110 120 130 140 150
PRASPLPVLN WGNREEVWRI MLNKEKTYLR DEHFLQRHPL LQARMRAVLL
160 170 180 190 200
DWLMEVCEVY KLHRETFYLA QDFFDRYMAS QQNIIKTLLQ LIGISALFIA
210 220 230 240 250
SKLEEIYPPK LHQFAYVTDG ACSGDEILTM ELMMMKALKW RLSPLTIVSW
260 270 280 290 300
LNVYVQVAYV NDTGEVLMPQ YPQQVFVQIA ELLDLCVLDV GCLEFPYGVL
310 320 330 340 350
AASALYHFSS LELMQKVSGY QWCDIEKCVK WMVPFAMVIR EMGSSKLKHF
360 370 380 390 400
RGVPMEDSHN IQTHTNSLDL LDKAQAKKAI LSEQNRISPP PSGVLTPPHS
410
SKKQSSEQET E
Length:411
Mass (Da):47,388
Last modified:May 20, 2008 - v1
Checksum:i3B84BFBEBB8564D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07003041 Genomic DNA. No translation available.
BC162008 mRNA. Translation: AAI62008.1.
RefSeqiNP_001094291.1. NM_001100821.1.
XP_006228966.1. XM_006228904.2.
UniGeneiRn.15455.

Genome annotation databases

EnsembliENSRNOT00000020014; ENSRNOP00000020014; ENSRNOG00000014786.
GeneIDi25729.
KEGGirno:25729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07003041 Genomic DNA. No translation available.
BC162008 mRNA. Translation: AAI62008.1.
RefSeqiNP_001094291.1. NM_001100821.1.
XP_006228966.1. XM_006228904.2.
UniGeneiRn.15455.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020014.

Proteomic databases

PeptideAtlasiB1WC54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020014; ENSRNOP00000020014; ENSRNOG00000014786.
GeneIDi25729.
KEGGirno:25729.

Organism-specific databases

CTDi898.
RGDi2294. Ccne1.

Phylogenomic databases

eggNOGiKOG0655. Eukaryota.
ENOG410XS2J. LUCA.
GeneTreeiENSGT00760000118939.
HOVERGENiHBG050834.
KOiK06626.
OMAiPLLQPKM.
OrthoDBiEOG7HB595.
TreeFamiTF101005.

Enzyme and pathway databases

ReactomeiR-RNO-113510. E2F mediated regulation of DNA replication.
R-RNO-1538133. G0 and Early G1.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-RNO-6804116. TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
R-RNO-69200. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
R-RNO-69202. Cyclin E associated events during G1/S transition.
R-RNO-69205. G1/S-Specific Transcription.
R-RNO-69563. p53-Dependent G1 DNA Damage Response.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR028858. Cyclin_E.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10177:SF71. PTHR10177:SF71. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Whole embryoImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiB1WC54_RAT
AccessioniPrimary (citable) accession number: B1WC54
Entry historyi
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: July 6, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.