ID   CCNE1_XENLA             Reviewed;         408 AA.
AC   P50756; Q6DD61;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=G1/S-specific cyclin-E1;
GN   Name=cyce1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Couturier A., Philippe M.;
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8799808; DOI=10.1242/jcs.109.6.1173;
RA   Chevalier S., Couturier A., Chartrain I., le Guellec R., Beckhelling C.,
RA   le Guellec K., Philippe M., Ford C.C.;
RT   "Xenopus cyclin E, a nuclear phosphoprotein, accumulates when oocytes gain
RT   the ability to initiate DNA replication.";
RL   J. Cell Sci. 109:1173-1184(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:P24864}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24864}.
CC   -!- PTM: Phosphorylation by CDK2 triggers its release from CDK2 and
CC       degradation via the ubiquitin proteasome pathway.
CC       {ECO:0000250|UniProtKB:P24864}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z13966; CAA78370.1; -; mRNA.
DR   EMBL; L43512; AAA99294.1; -; mRNA.
DR   EMBL; BC077766; AAH77766.1; -; mRNA.
DR   RefSeq; NP_001081445.1; NM_001087976.1.
DR   RefSeq; XP_018112011.1; XM_018256522.1.
DR   RefSeq; XP_018112012.1; XM_018256523.1.
DR   RefSeq; XP_018112013.1; XM_018256524.1.
DR   AlphaFoldDB; P50756; -.
DR   SMR; P50756; -.
DR   BioGRID; 99179; 2.
DR   GeneID; 397840; -.
DR   KEGG; xla:397840; -.
DR   CTD; 397840; -.
DR   Xenbase; XB-GENE-17330407; ccne1.L.
DR   OMA; HRIQTHV; -.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 397840; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..408
FT                   /note="G1/S-specific cyclin-E1"
FT                   /id="PRO_0000080454"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
SQ   SEQUENCE   408 AA;  47141 MW;  34B54657288A00F6 CRC64;
     MPVISNPAVE KSTKDEGTAS CSVRSRKRKA DVAIFLQDPD ETLDSLEMTK KKQYQDRGPW
     SNEMTCKSPH KLIPTPEKEE HEPNPTNYSH FASLRFSPVS VSPLPRLGWA NQDDVWRNML
     NKDRIYLRDK NFFQKHPQLQ PNMRAILLDW LMEVCEVYKL HRETFYLAQD FFDRFMATQK
     NVIKSRLQLI GITSLFIAAK LEEIYPPKLH QFSFITDGAC TEDEITRMEL IIMKDLGWCL
     SPMTIVSWFN VFLQVAYIRE LQQFLRPQFP QEIYIQIVQL LDLCVLDICC LEYPYGVLAA
     SAMYHFSCPE LVEKVSGFKV TELQGCIKWL VPFAMAIKEG GKSKLNFFKG VDIEDAHNIQ
     THSGCLELME KVYINQALLE EQNRTSPIPT GVLTPPQSNK KQKSDRAD