CCNE1_RAT
ID CCNE1_RAT Reviewed; 411 AA.
AC P39949; O09138;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=G1/S-specific cyclin-E1;
GN Name=Ccne1; Synonyms=Ccne;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8336937;
RA Tamura K., Kanaoka Y., Jinno S., Nagata A., Ogiso Y., Shimizu K.,
RA Hayakawa T., Nojima H., Okayama H.;
RT "Cyclin G: a new mammalian cyclin with homology to fission yeast Cig1.";
RL Oncogene 8:2113-2118(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-222.
RX PubMed=8673024;
RA Hosokawa Y., Yang M., Kaneko S., Tanaka M., Nakashima K.;
RT "Synergistic gene expressions of cyclin E, cdk2, cdk5 and E2F-1 during the
RT prolactin-induced G1/S transition in rat Nb2 pre-T lymphoma cells.";
RL Biochem. Mol. Biol. Int. 37:393-399(1995).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC (start) transition.
CC -!- SUBUNIT: Interacts with CDK2 protein kinase to form a serine/threonine
CC kinase holoenzyme complex. The cyclin subunit imparts substrate
CC specificity to the complex. Found in a complex with CDK2, CABLES1 and
CC CCNA1. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts
CC directly with UHRF2; the interaction ubiquitinates CCNE1 and appears to
CC occur independently of CCNE1 phosphorylation. Interacts with INCA1 (By
CC similarity). {ECO:0000250|UniProtKB:P24864,
CC ECO:0000250|UniProtKB:Q61457}.
CC -!- INTERACTION:
CC P39949; Q6PEC4: Skp1; NbExp=2; IntAct=EBI-847441, EBI-919194;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24864}.
CC -!- PTM: Phosphorylation of both Thr-396 by GSK3 and Ser-400 by CDK2
CC creates a high affinity degron recognized by FBXW7, and accelerates
CC degradation via the ubiquitin proteasome pathway. Phosphorylation at
CC Thr-77 creates a low affinity degron also recognized by FBXW7 (By
CC similarity). {ECO:0000250|UniProtKB:P24864}.
CC -!- PTM: Ubiquitinated by UHRF2; appears to occur independently of
CC phosphorylation. {ECO:0000250|UniProtKB:P24864}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03116.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D14015; BAA03116.1; ALT_FRAME; mRNA.
DR EMBL; D63164; BAA09640.1; -; mRNA.
DR AlphaFoldDB; P39949; -.
DR SMR; P39949; -.
DR ComplexPortal; CPX-2083; Cyclin E1-CDK2 complex.
DR DIP; DIP-29865N; -.
DR IntAct; P39949; 1.
DR STRING; 10116.ENSRNOP00000020014; -.
DR PhosphoSitePlus; P39949; -.
DR PaxDb; P39949; -.
DR RGD; 2294; Ccne1.
DR eggNOG; KOG0655; Eukaryota.
DR InParanoid; P39949; -.
DR PhylomeDB; P39949; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-RNO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR Reactome; R-RNO-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-RNO-8849470; PTK6 Regulates Cell Cycle.
DR Reactome; R-RNO-9706019; RHOBTB3 ATPase cycle.
DR PRO; PR:P39949; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0097134; C:cyclin E1-CDK2 complex; ISO:RGD.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0001547; P:antral ovarian follicle growth; IEP:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031670; P:cellular response to nutrient; IEP:RGD.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; ISO:RGD.
DR GO; GO:0006270; P:DNA replication initiation; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:RGD.
DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0014074; P:response to purine-containing compound; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0000723; P:telomere maintenance; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR028858; Cyclin_E.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF71; PTHR10177:SF71; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..411
FT /note="G1/S-specific cyclin-E1"
FT /id="PRO_0000080451"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24864"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24864"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24864"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24864"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24864"
FT CONFLICT 221
FT /note="A -> T (in Ref. 2; BAA09640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 47482 MW; 24CA81652056C036 CRC64;
MPRERKERDS KDHTKMKEEG GSDLSVRSRK RKPNVPVFLQ DPDEEIAKID KTVKSQDSSQ
PWDDDSACVD PCSFIPTPNK EEDNELEYPK TAFQPRKIRP PRASPLPVLN WANREEVWRI
MLNKEKTYLR DEHFLQRHPL LQARMRAVLL DWLMEVCEVY KLHRETFYLA QDFFDRYMAS
QQNIIKTLLQ LIGISALFIA SKLEEIYPPK LHQFAYVTDG ACSGDEILTM ELMMMKALKW
RLSPLTIVSW LNVYVQVAYV NDTGEVLMPQ YPQQVFVQIA ELLDLCVLDV GCLEFPYGVL
AASALYHFSS LELMQKVSGY QWCDIEKCVK WMVPFAMVIR EMGSSKLKHF RGVPMEDSHN
IQTHTNSLDL LDKAQAKKAI LSEQNRISPP PSGVLTPPHS SKKQSSEQET E
