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Protein

G1/S-specific cyclin-E1

Gene

Ccne1

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

Functioni

Essential for the control of the cell cycle at the G1/S (start) transition.

GO - Molecular functioni

  1. cyclin-dependent protein serine/threonine kinase regulator activity Source: MGI
  2. kinase activity Source: MGI
  3. protein kinase binding Source: MGI

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. DNA replication initiation Source: MGI
  3. G1/S transition of mitotic cell cycle Source: InterPro
  4. protein phosphorylation Source: MGI
  5. regulation of cell cycle Source: MGI
  6. regulation of protein kinase activity Source: GOC
  7. Wnt signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_198608. G1/S-Specific Transcription.
REACT_199110. G0 and Early G1.
REACT_206830. E2F mediated regulation of DNA replication.
REACT_219010. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_257943. p53-Dependent G1 DNA Damage Response.

Names & Taxonomyi

Protein namesi
Recommended name:
G1/S-specific cyclin-E1
Gene namesi
Name:Ccne1
Synonyms:Ccne
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:88316. Ccne1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cyclin-dependent protein kinase holoenzyme complex Source: MGI
  2. nucleoplasm Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408G1/S-specific cyclin-E1PRO_0000080450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphothreonineBy similarity
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei385 – 3851PhosphoserineBy similarity
Modified residuei393 – 3931PhosphothreonineBy similarity
Modified residuei397 – 3971PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation of both Thr-393 by GSK3 and Ser-397 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway. Phosphorylation at Thr-74 creates a low affinity degron also recognized by FBXW7 (By similarity).By similarity
Ubiquitinated by UHRF2; appears to occur independently of phosphorylation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ61457.

PTM databases

PhosphoSiteiQ61457.

Expressioni

Tissue specificityi

Found in adult spleen, and to a lesser extent in adult testis and brain.

Gene expression databases

BgeeiQ61457.
CleanExiMM_CCNE1.
ExpressionAtlasiQ61457. baseline and differential.
GenevestigatoriQ61457.

Interactioni

Subunit structurei

Interacts with a member of the CDK2/CDK protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts directly with UHRF2; the interaction ubiquitinates CCNE1 and appears to occur independently of CCNE1 phosphorylation (By similarity). Found in a complex with CDK2, CABLES1 and CCNA1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdk1P114402EBI-643090,EBI-846949
Cdk2P973773EBI-643090,EBI-847048

Protein-protein interaction databases

BioGridi198552. 11 interactions.
DIPiDIP-45868N.
IntActiQ61457. 3 interactions.
MINTiMINT-1706339.

Structurei

3D structure databases

ProteinModelPortaliQ61457.
SMRiQ61457. Positions 101-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin E subfamily.Curated

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000231743.
HOVERGENiHBG050834.
InParanoidiQ61457.
KOiK06626.
OMAiPFAMVIR.
OrthoDBiEOG7HB595.
PhylomeDBiQ61457.
TreeFamiTF101005.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
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]
PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRERDSTDH SNMKEEGGSD LSVRSRKRKA NVAVFLQDPD EEIAKIDKTV
60 70 80 90 100
KSEDSSQPWD DNSACVDPCS FIPTPNKEED NELEYPRTAF QPRKIRPPRA
110 120 130 140 150
SPLPVLNWGN REEVWRIMLN KEKTYLRDEH FLQRHPLLQA RMRAVLLDWL
160 170 180 190 200
MEVCEVYKLH RETFYLAQDF FDRYMASQHN IIKTLLQLIG ISALFIASKL
210 220 230 240 250
EEIYPPKLHQ FAYVTDGACS GDEILTMELM MMKALKWRLS PLTIVSWLNV
260 270 280 290 300
YVQVAYVNDT GEVLMPQYPQ QVFVQIAELL DLCVLDVGCL EFPYGVLAAS
310 320 330 340 350
ALYHFSSLEL MQKVSGYQWC DIEKCVKWMV PFAMVIREMG SSKLKHFRGV
360 370 380 390 400
PMEDSHNIQT HTNSLDLLDK AQAKKAILSE QNRISPPPSV VLTPPPSSKK

QSSEQETE
Length:408
Mass (Da):46,986
Last modified:November 13, 2007 - v2
Checksum:i4916B5D7117ADA69
GO

Sequence cautioni

The sequence CAA53482.1 differs from that shown. Reason: Frameshift at position 401. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → Q in AAH84588 (PubMed:15489334).Curated
Sequence conflicti179 – 1791H → Q in CAA53482 (PubMed:8003041).Curated
Sequence conflicti179 – 1791H → Q in AAH62152 (PubMed:15489334).Curated
Sequence conflicti179 – 1791H → Q in AAH84588 (PubMed:15489334).Curated
Sequence conflicti290 – 2912LE → FR in AAH62152 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75888 mRNA. Translation: CAA53482.1. Frameshift.
BC062152 mRNA. Translation: AAH62152.1.
BC084588 mRNA. Translation: AAH84588.1.
BC106191 mRNA. Translation: AAI06192.1.
CCDSiCCDS39914.1.
PIRiJC2497.
RefSeqiNP_031659.2. NM_007633.2.
UniGeneiMm.16110.

Genome annotation databases

EnsembliENSMUST00000108023; ENSMUSP00000103658; ENSMUSG00000002068.
GeneIDi12447.
KEGGimmu:12447.
UCSCiuc009gkr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75888 mRNA. Translation: CAA53482.1. Frameshift.
BC062152 mRNA. Translation: AAH62152.1.
BC084588 mRNA. Translation: AAH84588.1.
BC106191 mRNA. Translation: AAI06192.1.
CCDSiCCDS39914.1.
PIRiJC2497.
RefSeqiNP_031659.2. NM_007633.2.
UniGeneiMm.16110.

3D structure databases

ProteinModelPortaliQ61457.
SMRiQ61457. Positions 101-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198552. 11 interactions.
DIPiDIP-45868N.
IntActiQ61457. 3 interactions.
MINTiMINT-1706339.

PTM databases

PhosphoSiteiQ61457.

Proteomic databases

PRIDEiQ61457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108023; ENSMUSP00000103658; ENSMUSG00000002068.
GeneIDi12447.
KEGGimmu:12447.
UCSCiuc009gkr.1. mouse.

Organism-specific databases

CTDi898.
MGIiMGI:88316. Ccne1.

Phylogenomic databases

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000231743.
HOVERGENiHBG050834.
InParanoidiQ61457.
KOiK06626.
OMAiPFAMVIR.
OrthoDBiEOG7HB595.
PhylomeDBiQ61457.
TreeFamiTF101005.

Enzyme and pathway databases

ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_198608. G1/S-Specific Transcription.
REACT_199110. G0 and Early G1.
REACT_206830. E2F mediated regulation of DNA replication.
REACT_219010. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_257943. p53-Dependent G1 DNA Damage Response.

Miscellaneous databases

ChiTaRSiCcne1. mouse.
NextBioi281272.
PROiQ61457.
SOURCEiSearch...

Gene expression databases

BgeeiQ61457.
CleanExiMM_CCNE1.
ExpressionAtlasiQ61457. baseline and differential.
GenevestigatoriQ61457.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
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]
PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/J.
  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].
    Tissue: Embryo and Limb.
  3. "Cables enhances cdk2 tyrosine 15 phosphorylation by Wee1, inhibits cell growth, and is lost in many human colon and squamous cancers."
    Wu C.-L., Kirley S.D., Xiao H., Chuang Y., Chung D.C., Zukerberg L.R.
    Cancer Res. 61:7325-7332(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CDK2; CCNA1 AND CABLES1.

Entry informationi

Entry nameiCCNE1_MOUSE
AccessioniPrimary (citable) accession number: Q61457
Secondary accession number(s): Q05BA1, Q05BA6, Q05BB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 13, 2007
Last modified: March 4, 2015
This is version 126 of the entry and version 2 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

External Data

Dasty 3

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 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.