CCNE1_HUMAN
ID CCNE1_HUMAN Reviewed; 410 AA.
AC P24864; A8K684; Q14091; Q8NFG1; Q92501; Q9UD21;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=G1/S-specific cyclin-E1;
GN Name=CCNE1; Synonyms=CCNE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=1833066; DOI=10.1016/0092-8674(91)90042-w;
RA Lew D.J., Dulic V., Reed S.I.;
RT "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
RT function in yeast.";
RL Cell 66:1197-1206(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=1833068; DOI=10.1016/0092-8674(91)90044-y;
RA Koff A., Cross F., Fisher A., Schumacher J., le Guellec K., Philippe M.,
RA Roberts J.M.;
RT "Human cyclin E, a new cyclin that interacts with two members of the CDC2
RT gene family.";
RL Cell 66:1217-1228(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E1L AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=7739542; DOI=10.1128/mcb.15.5.2612;
RA Ohtsubo M., Theodoras A.M., Schumacher J., Roberts J.M., Pagano M.;
RT "Human cyclin E, a nuclear protein essential for the G1-to-S phase
RT transition.";
RL Mol. Cell. Biol. 15:2612-2624(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E1L).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E1L).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RX PubMed=8649818;
RA Geng Y., Eaton E.N., Picon M., Roberts J.M., Lundberg A.S., Gifford A.,
RA Sardet C., Weinberg R.A.;
RT "Regulation of cyclin E transcription by E2Fs and retinoblastoma protein.";
RL Oncogene 12:1173-1180(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-370.
RX PubMed=8833152; DOI=10.1006/geno.1996.0112;
RA Li H., Lahti J.M., Valentine M., Saito M., Reed S.I., Look A.T., Kidd V.J.;
RT "Molecular cloning and chromosomal localization of the human cyclin C
RT (CCNC) and cyclin E (CCNE) genes: deletion of the CCNC gene in human
RT tumors.";
RL Genomics 32:253-259(1996).
RN [9]
RP ALTERNATIVE SPLICING.
RX PubMed=8207080; DOI=10.1242/jcs.107.2.581;
RA Sewing A., Roenicke V., Buerger C., Funk M., Mueller R.;
RT "Alternative splicing of human cyclin E.";
RL J. Cell Sci. 107:581-588(1994).
RN [10]
RP PHOSPHORYLATION AT THR-395.
RX PubMed=8861947; DOI=10.1002/j.1460-2075.1996.tb00793.x;
RA Won K.A., Reed S.I.;
RT "Activation of cyclin E/CDK2 is coupled to site-specific
RT autophosphorylation and ubiquitin-dependent degradation of cyclin E.";
RL EMBO J. 15:4182-4193(1996).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=9840943; DOI=10.1038/sj.onc.1202505;
RA Zariwala M., Liu J., Xiong Y.;
RT "Cyclin E2, a novel human G1 cyclin and activating partner of CDK2 and
RT CDK3, is induced by viral oncoproteins.";
RL Oncogene 17:2787-2798(1998).
RN [12]
RP PHOSPHORYLATION AT THR-77; SER-387; THR-395 AND SER-399.
RX PubMed=14536078; DOI=10.1016/s1097-2765(03)00287-9;
RA Welcker M., Singer J., Loeb K.R., Grim J., Bloecher A., Gurien-West M.,
RA Clurman B.E., Roberts J.M.;
RT "Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E
RT degradation.";
RL Mol. Cell 12:381-392(2003).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CDK2.
RX PubMed=15178429; DOI=10.1016/j.bbrc.2004.04.190;
RA Li Y., Mori T., Hata H., Homma Y., Kochi H.;
RT "NIRF induces G1 arrest and associates with Cdk2.";
RL Biochem. Biophys. Res. Commun. 319:464-468(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-387 AND THR-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP UBIQUITINATION, AND INTERACTION WITH UHRF2.
RX PubMed=21952639; DOI=10.4161/cc.10.19.17176;
RA Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.;
RT "NIRF constitutes a nodal point in the cell cycle network and is a
RT candidate tumor suppressor.";
RL Cell Cycle 10:3284-3299(2011).
RN [18]
RP INTERACTION WITH INCA1.
RX PubMed=21540187; DOI=10.1074/jbc.m110.203471;
RA Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S.,
RA Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G.,
RA Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.;
RT "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1
RT (INCA1) regulates proliferation and is repressed by oncogenic signaling.";
RL J. Biol. Chem. 286:28210-28222(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 96-378 IN COMPLEX WITH CDK2, AND
RP INTERACTION WITH CDK2.
RX PubMed=15660127; DOI=10.1038/sj.emboj.7600554;
RA Honda R., Lowe E.D., Dubinina E., Skamnaki V., Cook A., Brown N.R.,
RA Johnson L.N.;
RT "The structure of cyclin E1/CDK2: implications for CDK2 activation and
RT CDK2-independent roles.";
RL EMBO J. 24:452-463(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 73-80 IN COMPLEX WITH SKP1 AND
RP FBXW7, AND PHOSPHORYLATION AT THR-77; THR-395 AND SER-399.
RX PubMed=17434132; DOI=10.1016/j.molcel.2007.02.022;
RA Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.;
RT "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated
RT substrate recognition by SCF ubiquitin ligases.";
RL Mol. Cell 26:131-143(2007).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC (start) transition. {ECO:0000269|PubMed:7739542}.
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 (PubMed:15660127). Found in a complex with
CC CDK2, CABLES1 and CCNA1 (By similarity). Part of a complex consisting
CC of UHRF2, CDK2 and CCNE1 (PubMed:15178429). Interacts directly with
CC UHRF2; the interaction ubiquitinates CCNE1 and appears to occur
CC independently of CCNE1 phosphorylation (PubMed:21952639). Interacts
CC with INCA1 (PubMed:21540187). {ECO:0000250|UniProtKB:Q61457,
CC ECO:0000269|PubMed:15178429, ECO:0000269|PubMed:15660127,
CC ECO:0000269|PubMed:21540187, ECO:0000269|PubMed:21952639}.
CC -!- INTERACTION:
CC P24864; P38398: BRCA1; NbExp=2; IntAct=EBI-519526, EBI-349905;
CC P24864; P24941: CDK2; NbExp=20; IntAct=EBI-519526, EBI-375096;
CC P24864; P38936: CDKN1A; NbExp=9; IntAct=EBI-519526, EBI-375077;
CC P24864; P46527: CDKN1B; NbExp=8; IntAct=EBI-519526, EBI-519280;
CC P24864; Q08050: FOXM1; NbExp=2; IntAct=EBI-519526, EBI-866480;
CC P24864; A6NCL1: GMNC; NbExp=3; IntAct=EBI-519526, EBI-18587381;
CC P24864; Q96PU4: UHRF2; NbExp=4; IntAct=EBI-519526, EBI-625304;
CC P24864; Q5VK71: AKAP8; Xeno; NbExp=2; IntAct=EBI-519526, EBI-11601938;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7739542}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=E1L; Synonyms=E-L;
CC IsoId=P24864-1; Sequence=Displayed;
CC Name=E1S;
CC IsoId=P24864-2; Sequence=VSP_001253;
CC Name=3; Synonyms=E-S;
CC IsoId=P24864-3; Sequence=VSP_037381;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and placenta. Low levels
CC in bronchial epithelial cells. {ECO:0000269|PubMed:9840943}.
CC -!- PTM: Phosphorylation of both Thr-395 by GSK3 and Ser-399 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.
CC {ECO:0000269|PubMed:14536078, ECO:0000269|PubMed:17434132,
CC ECO:0000269|PubMed:21952639, ECO:0000269|PubMed:8861947}.
CC -!- PTM: Ubiquitinated by UHRF2; appears to occur independently of
CC phosphorylation. {ECO:0000269|PubMed:21952639}.
CC -!- MISCELLANEOUS: [Isoform E1S]: Lacks 49 residues within the cyclin box
CC and cannot complex with CDK2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccne1/";
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DR EMBL; M74093; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M73812; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291549; BAF84238.1; -; mRNA.
DR EMBL; AF518727; AAM54043.1; -; Genomic_DNA.
DR EMBL; BC035498; AAH35498.1; -; mRNA.
DR EMBL; X95406; CAA64687.1; -; Genomic_DNA.
DR EMBL; X95406; CAA64688.1; -; Genomic_DNA.
DR EMBL; AH003247; AAA83269.1; -; Genomic_DNA.
DR CCDS; CCDS12419.1; -. [P24864-1]
DR CCDS; CCDS46035.1; -. [P24864-3]
DR PIR; A40270; A40270.
DR RefSeq; NP_001229.1; NM_001238.3. [P24864-1]
DR RefSeq; NP_001309191.1; NM_001322262.1. [P24864-3]
DR PDB; 1W98; X-ray; 2.15 A; B=96-378.
DR PDB; 5L2W; X-ray; 2.80 A; B=96-378.
DR PDB; 7KJS; X-ray; 2.19 A; B=96-378.
DR PDBsum; 1W98; -.
DR PDBsum; 5L2W; -.
DR PDBsum; 7KJS; -.
DR AlphaFoldDB; P24864; -.
DR SMR; P24864; -.
DR BioGRID; 107338; 107.
DR ComplexPortal; CPX-2015; Cyclin E1-CDK2 complex.
DR CORUM; P24864; -.
DR DIP; DIP-149N; -.
DR IntAct; P24864; 26.
DR MINT; P24864; -.
DR STRING; 9606.ENSP00000262643; -.
DR BindingDB; P24864; -.
DR ChEMBL; CHEMBL3617; -.
DR iPTMnet; P24864; -.
DR PhosphoSitePlus; P24864; -.
DR BioMuta; CCNE1; -.
DR DMDM; 3041657; -.
DR EPD; P24864; -.
DR jPOST; P24864; -.
DR MassIVE; P24864; -.
DR MaxQB; P24864; -.
DR PaxDb; P24864; -.
DR PeptideAtlas; P24864; -.
DR PRIDE; P24864; -.
DR ProteomicsDB; 54236; -. [P24864-1]
DR ProteomicsDB; 54237; -. [P24864-2]
DR ProteomicsDB; 54238; -. [P24864-3]
DR Antibodypedia; 3286; 1212 antibodies from 48 providers.
DR DNASU; 898; -.
DR Ensembl; ENST00000262643.8; ENSP00000262643.3; ENSG00000105173.14. [P24864-1]
DR Ensembl; ENST00000444983.6; ENSP00000410179.2; ENSG00000105173.14. [P24864-3]
DR GeneID; 898; -.
DR KEGG; hsa:898; -.
DR MANE-Select; ENST00000262643.8; ENSP00000262643.3; NM_001238.4; NP_001229.1.
DR UCSC; uc002nsn.4; human. [P24864-1]
DR CTD; 898; -.
DR DisGeNET; 898; -.
DR GeneCards; CCNE1; -.
DR HGNC; HGNC:1589; CCNE1.
DR HPA; ENSG00000105173; Tissue enhanced (bone marrow, placenta).
DR MIM; 123837; gene.
DR neXtProt; NX_P24864; -.
DR OpenTargets; ENSG00000105173; -.
DR PharmGKB; PA96; -.
DR VEuPathDB; HostDB:ENSG00000105173; -.
DR eggNOG; KOG0655; Eukaryota.
DR GeneTree; ENSGT00940000156256; -.
DR InParanoid; P24864; -.
DR OMA; HRIQTHV; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; P24864; -.
DR TreeFam; TF101005; -.
DR PathwayCommons; P24864; -.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-HSA-8849470; PTK6 Regulates Cell Cycle.
DR Reactome; R-HSA-9661069; Defective binding of RB1 mutants to E2F1,(E2F2, E2F3).
DR Reactome; R-HSA-9706019; RHOBTB3 ATPase cycle.
DR SignaLink; P24864; -.
DR SIGNOR; P24864; -.
DR BioGRID-ORCS; 898; 64 hits in 1086 CRISPR screens.
DR ChiTaRS; CCNE1; human.
DR EvolutionaryTrace; P24864; -.
DR GeneWiki; Cyclin_E1; -.
DR GenomeRNAi; 898; -.
DR Pharos; P24864; Tchem.
DR PRO; PR:P24864; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P24864; protein.
DR Bgee; ENSG00000105173; Expressed in secondary oocyte and 135 other tissues.
DR ExpressionAtlas; P24864; baseline and differential.
DR Genevisible; P24864; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0097134; C:cyclin E1-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
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; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR CDD; cd00043; CYCLIN; 1.
DR DisProt; DP01120; -.
DR IDEAL; IID00603; -.
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 3D-structure; Alternative splicing; Cell cycle; Cell division; Cyclin;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..410
FT /note="G1/S-specific cyclin-E1"
FT /id="PRO_0000080449"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14536078,
FT ECO:0000269|PubMed:17434132"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14536078,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:14536078,
FT ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:8861947,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 399
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|PubMed:14536078,
FT ECO:0000269|PubMed:17434132"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1833066,
FT ECO:0000303|PubMed:1833068, ECO:0000303|PubMed:7739542"
FT /id="VSP_037381"
FT VAR_SEQ 154..196
FT /note="Missing (in isoform E1S)"
FT /evidence="ECO:0000305"
FT /id="VSP_001253"
FT CONFLICT 9
FT /note="D -> K (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:1W98"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1W98"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:1W98"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:1W98"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 272..287
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 321..341
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:1W98"
FT HELIX 366..370
FT /evidence="ECO:0007829|PDB:1W98"
SQ SEQUENCE 410 AA; 47077 MW; 424DF0B253B7047E CRC64;
MPRERRERDA KERDTMKEDG GAEFSARSRK RKANVTVFLQ DPDEEMAKID RTARDQCGSQ
PWDNNAVCAD PCSLIPTPDK EDDDRVYPNS TCKPRIIAPS RGSPLPVLSW ANREEVWKIM
LNKEKTYLRD QHFLEQHPLL QPKMRAILLD WLMEVCEVYK LHRETFYLAQ DFFDRYMATQ
ENVVKTLLQL IGISSLFIAA KLEEIYPPKL HQFAYVTDGA CSGDEILTME LMIMKALKWR
LSPLTIVSWL NVYMQVAYLN DLHEVLLPQY PQQIFIQIAE LLDLCVLDVD CLEFPYGILA
ASALYHFSSS ELMQKVSGYQ WCDIENCVKW MVPFAMVIRE TGSSKLKHFR GVADEDAHNI
QTHRDSLDLL DKARAKKAML SEQNRASPLP SGLLTPPQSG KKQSSGPEMA
