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P39949 (CCNE1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G1/S-specific cyclin-E1
Gene names
Name:Ccne1
Synonyms:Ccne
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

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.

Subcellular location

Nucleus By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the cyclin family. Cyclin E subfamily.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentNucleus
   Molecular functionCyclin
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: InterPro

antral ovarian follicle growth

Inferred from expression pattern PubMed 17084963. Source: RGD

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to nutrient

Inferred from expression pattern PubMed 17979132. Source: RGD

liver development

Inferred from expression pattern PubMed 15809057. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 16273211. Source: RGD

positive regulation of cell differentiation

Inferred from direct assay PubMed 15642789. Source: RGD

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

response to corticosterone

Inferred from expression pattern PubMed 12807724. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 17483238. Source: RGD

response to drug

Inferred from expression pattern PubMed 16760380. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 16019103. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 16689928. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 17056119. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 17654247. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 15945272. Source: RGD

response to progesterone

Inferred from expression pattern PubMed 12810531. Source: RGD

response to purine-containing compound

Inferred from expression pattern PubMed 16759516. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 16273211. Source: RGD

response to vitamin E

Inferred from expression pattern PubMed 16298738. Source: RGD

   Cellular_componentcentrosome

Inferred from direct assay PubMed 15514162. Source: RGD

cytoplasm

Inferred from direct assay PubMed 10952244. Source: RGD

nucleus

Inferred from direct assay PubMed 14614307. Source: RGD

   Molecular_functionprotein complex binding

Inferred from physical interaction PubMed 10952244. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 15809057. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411G1/S-specific cyclin-E1
PRO_0000080451

Amino acid modifications

Modified residue771Phosphothreonine By similarity
Modified residue1041Phosphoserine By similarity
Modified residue3881Phosphoserine By similarity
Modified residue3961Phosphothreonine By similarity
Modified residue4001Phosphoserine By similarity

Experimental info

Sequence conflict2211A → T in BAA09640. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P39949 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 24CA81652056C036

FASTA41147,482
        10         20         30         40         50         60 
MPRERKERDS KDHTKMKEEG GSDLSVRSRK RKPNVPVFLQ DPDEEIAKID KTVKSQDSSQ 

        70         80         90        100        110        120 
PWDDDSACVD PCSFIPTPNK EEDNELEYPK TAFQPRKIRP PRASPLPVLN WANREEVWRI 

       130        140        150        160        170        180 
MLNKEKTYLR DEHFLQRHPL LQARMRAVLL DWLMEVCEVY KLHRETFYLA QDFFDRYMAS 

       190        200        210        220        230        240 
QQNIIKTLLQ LIGISALFIA SKLEEIYPPK LHQFAYVTDG ACSGDEILTM ELMMMKALKW 

       250        260        270        280        290        300 
RLSPLTIVSW LNVYVQVAYV NDTGEVLMPQ YPQQVFVQIA ELLDLCVLDV GCLEFPYGVL 

       310        320        330        340        350        360 
AASALYHFSS LELMQKVSGY QWCDIEKCVK WMVPFAMVIR EMGSSKLKHF RGVPMEDSHN 

       370        380        390        400        410 
IQTHTNSLDL LDKAQAKKAI LSEQNRISPP PSGVLTPPHS SKKQSSEQET E 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14015 mRNA. Translation: BAA03116.1. Frameshift.
D63164 mRNA. Translation: BAA09640.1.
UniGeneRn.15455.

3D structure databases

ProteinModelPortalP39949.
SMRP39949. Positions 104-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29865N.

Proteomic databases

PaxDbP39949.
PRIDEP39949.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD2294. Ccne1.

Phylogenomic databases

eggNOGCOG5024.
HOGENOMHOG000231743.
HOVERGENHBG050834.
InParanoidP39949.
PhylomeDBP39949.

Gene expression databases

GenevestigatorP39949.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR028858. Cyclin_E.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10177:SF71. PTHR10177:SF71. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP39949.

Entry information

Entry nameCCNE1_RAT
AccessionPrimary (citable) accession number: P39949
Secondary accession number(s): O09138
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families