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P39949

- CCNE1_RAT

UniProt

P39949 - CCNE1_RAT

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Protein
G1/S-specific cyclin-E1
Gene
Ccne1, Ccne
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

  1. protein complex binding Source: RGD
  2. protein kinase binding Source: RGD
Complete GO annotation...

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: InterPro
  2. antral ovarian follicle growth Source: RGD
  3. cell division Source: UniProtKB-KW
  4. cellular response to nutrient Source: RGD
  5. liver development Source: RGD
  6. organ regeneration Source: RGD
  7. positive regulation of cell differentiation Source: RGD
  8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  9. response to corticosterone Source: RGD
  10. response to cytokine Source: RGD
  11. response to drug Source: RGD
  12. response to estradiol Source: RGD
  13. response to ethanol Source: RGD
  14. response to methylmercury Source: RGD
  15. response to organic cyclic compound Source: RGD
  16. response to organonitrogen compound Source: RGD
  17. response to progesterone Source: RGD
  18. response to purine-containing compound Source: RGD
  19. response to steroid hormone Source: RGD
  20. response to vitamin E Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
G1/S-specific cyclin-E1
Gene namesi
Name:Ccne1
Synonyms:Ccne
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2294. Ccne1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. centrosome Source: RGD
  2. cytoplasm Source: RGD
  3. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411G1/S-specific cyclin-E1
PRO_0000080451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphothreonine By similarity
Modified residuei104 – 1041Phosphoserine By similarity
Modified residuei388 – 3881Phosphoserine By similarity
Modified residuei396 – 3961Phosphothreonine By similarity
Modified residuei400 – 4001Phosphoserine By similarity

Post-translational modificationi

Phosphorylation of both Thr-396 by GSK3 and Ser-400 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway. Phosphorylation at Thr-77 creates a low affinity degron also recognized by FBXW7 By similarity.
Ubiquitinated by UHRF2; appears to occur independently of phosphorylation By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP39949.
PRIDEiP39949.

Expressioni

Gene expression databases

GenevestigatoriP39949.

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. Found in a complex with CDK2, CABLES1 and CCNA1. 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.

Protein-protein interaction databases

DIPiDIP-29865N.

Structurei

3D structure databases

ProteinModelPortaliP39949.
SMRiP39949. Positions 104-373.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5024.
HOGENOMiHOG000231743.
HOVERGENiHBG050834.
InParanoidiP39949.
PhylomeDBiP39949.

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.

P39949-1 [UniParc]FASTAAdd to Basket

« Hide

MPRERKERDS KDHTKMKEEG GSDLSVRSRK RKPNVPVFLQ DPDEEIAKID    50
KTVKSQDSSQ PWDDDSACVD PCSFIPTPNK EEDNELEYPK TAFQPRKIRP 100
PRASPLPVLN WANREEVWRI MLNKEKTYLR DEHFLQRHPL LQARMRAVLL 150
DWLMEVCEVY KLHRETFYLA QDFFDRYMAS QQNIIKTLLQ LIGISALFIA 200
SKLEEIYPPK LHQFAYVTDG ACSGDEILTM ELMMMKALKW RLSPLTIVSW 250
LNVYVQVAYV NDTGEVLMPQ YPQQVFVQIA ELLDLCVLDV GCLEFPYGVL 300
AASALYHFSS LELMQKVSGY QWCDIEKCVK WMVPFAMVIR EMGSSKLKHF 350
RGVPMEDSHN IQTHTNSLDL LDKAQAKKAI LSEQNRISPP PSGVLTPPHS 400
SKKQSSEQET E 411
Length:411
Mass (Da):47,482
Last modified:November 13, 2007 - v2
Checksum:i24CA81652056C036
GO

Sequence cautioni

The sequence BAA03116.1 differs from that shown. Reason: Frameshift at position 15.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211A → T in BAA09640. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14015 mRNA. Translation: BAA03116.1. Frameshift.
D63164 mRNA. Translation: BAA09640.1.
UniGeneiRn.15455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14015 mRNA. Translation: BAA03116.1 . Frameshift.
D63164 mRNA. Translation: BAA09640.1 .
UniGenei Rn.15455.

3D structure databases

ProteinModelPortali P39949.
SMRi P39949. Positions 104-373.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-29865N.

Proteomic databases

PaxDbi P39949.
PRIDEi P39949.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

RGDi 2294. Ccne1.

Phylogenomic databases

eggNOGi COG5024.
HOGENOMi HOG000231743.
HOVERGENi HBG050834.
InParanoidi P39949.
PhylomeDBi P39949.

Miscellaneous databases

PROi P39949.

Gene expression databases

Genevestigatori P39949.

Family and domain databases

Gene3Di 1.10.472.10. 2 hits.
InterProi IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR028858. Cyclin_E.
IPR006671. Cyclin_N.
[Graphical view ]
PANTHERi PTHR10177:SF71. PTHR10177:SF71. 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. 1 hit.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
PROSITEi PS00292. CYCLINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cyclin G: a new mammalian cyclin with homology to fission yeast Cig1."
    Tamura K., Kanaoka Y., Jinno S., Nagata A., Ogiso Y., Shimizu K., Hayakawa T., Nojima H., Okayama H.
    Oncogene 8:2113-2118(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Synergistic gene expressions of cyclin E, cdk2, cdk5 and E2F-1 during the prolactin-induced G1/S transition in rat Nb2 pre-T lymphoma cells."
    Hosokawa Y., Yang M., Kaneko S., Tanaka M., Nakashima K.
    Biochem. Mol. Biol. Int. 37:393-399(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-222.

Entry informationi

Entry nameiCCNE1_RAT
AccessioniPrimary (citable) accession number: P39949
Secondary accession number(s): O09138
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 103 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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