ID   CCNE2_HUMAN             Reviewed;         404 AA.
AC   O96020; O95439;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 79.
DE   RecName: Full=G1/S-specific cyclin-E2;
GN   Name=CCNE2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   TISSUE=Fetal lung;
RX   MEDLINE=99077999; PubMed=9858585;
RA   Gudas J.M., Payton M., Thukral S., Chen E., Bass M., Robinson M.O.,
RA   Coats S.;
RT   "Cyclin E2, a novel G1 cyclin that binds Cdk2 and is aberrantly
RT   expressed in human cancers.";
RL   Mol. Cell. Biol. 19:612-622(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=B-cell;
RX   MEDLINE=99054662; PubMed=9840927; DOI=10.1038/sj.onc.1202477;
RA   Lauper N., Beck A.R.P., Cariou S., Richman L., Hofmann K., Reith W.,
RA   Slingerland J.M., Amati B.;
RT   "Cyclin E2: a novel CDK2 partner in the late G1 and S phases of the
RT   mammalian cell cycle.";
RL   Oncogene 17:2637-2643(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   THR-392.
RC   TISSUE=Keratinocyte;
RX   MEDLINE=99054678; 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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-387.
RG   NIEHS SNPs program;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-383 AND THR-392,
RP   AND MASS SPECTROMETRY.
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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
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).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the late
CC       G1 and early S phase.
CC   -!- SUBUNIT: Interacts with the CDK2 (in vivo) and CDK3 (in vitro)
CC       protein kinases to form a serine/threonine kinase holoenzyme
CC       complex. The cyclin subunit imparts substrate specificity to the
CC       complex.
CC   -!- INTERACTION:
CC       P24941:CDK2; NbExp=5; IntAct=EBI-375033, EBI-375096;
CC       P38936:CDKN1A; NbExp=1; IntAct=EBI-375033, EBI-375077;
CC       P46527:CDKN1B; NbExp=1; IntAct=EBI-375033, EBI-519280;
CC       Q9UBD5:ORC3L; NbExp=1; IntAct=EBI-375033, EBI-374916;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O96020-1; Sequence=Displayed;
CC       Name=Short; Synonyms=SV;
CC         IsoId=O96020-2; Sequence=VSP_001256;
CC   -!- TISSUE SPECIFICITY: According to PubMed:9858585: highest levels in
CC       adult testis, thymus and brain. Lower levels in placenta, spleen
CC       and colon. Consistently elevated levels in tumor-derived cells
CC       compared to non-transformed proliferating cells. According to
CC       PubMed:9840927: low levels in thymus, prostate, brain, skeletal
CC       muscle, and kidney. Elevated levels in lung. According to
CC       PubMed:9840943: highly expressed in testis, placenta, thymus and
CC       brain. In a lesser extent in small intestine and colon.
CC   -!- INDUCTION: Activated by papilloma viral oncoproteins E6 and E7
CC       which bind to and inactivate p53 and Rb, respectively.
CC   -!- PTM: Phosphorylation by CDK2 triggers its release from CDK2 and
CC       degradation via the ubiquitin proteasome pathway (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ccne2/";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF106690; AAD08816.1; -; mRNA.
DR   EMBL; AF112857; AAD08819.1; -; mRNA.
DR   EMBL; AF091433; AAC80528.1; -; mRNA.
DR   EMBL; AF102778; AAC78145.1; -; mRNA.
DR   EMBL; AY850195; AAV97813.1; -; Genomic_DNA.
DR   IPI; IPI00014085; -.
DR   IPI; IPI00219502; -.
DR   RefSeq; NP_477097.1; -.
DR   UniGene; Hs.567387; -.
DR   IntAct; O96020; 7.
DR   PhosphoSite; O96020; -.
DR   PRIDE; O96020; -.
DR   Ensembl; ENSG00000175305; Homo sapiens.
DR   GeneID; 9134; -.
DR   KEGG; hsa:9134; -.
DR   GeneCards; GC08M095961; -.
DR   H-InvDB; HIX0007656; -.
DR   HGNC; HGNC:1590; CCNE2.
DR   HPA; CAB007825; -.
DR   MIM; 603775; gene.
DR   PharmGKB; PA26155; -.
DR   HOGENOM; O96020; -.
DR   HOVERGEN; O96020; -.
DR   OMA; O96020; FIQIAQL.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   NextBio; 34249; -.
DR   ArrayExpress; O96020; -.
DR   Bgee; O96020; -.
DR   CleanEx; HS_CCNE2; -.
DR   GermOnline; ENSG00000175305; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000075; P:cell cycle checkpoint; TAS:ProtInc.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein kina...; TAS:ProtInc.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR014400; Cyclin_A_B_D_E.
DR   InterPro; IPR004367; Cyclin_C.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR013763; Cyclin_related.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Cyclin; Nucleus;
KW   Phosphoprotein; Polymorphism.
FT   CHAIN         1    404       G1/S-specific cyclin-E2.
FT                                /FTId=PRO_0000080461.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     392    392       Phosphothreonine.
FT   VAR_SEQ     167    211       Missing (in isoform Short).
FT                                /FTId=VSP_001256.
FT   VARIANT     387    387       N -> S (in dbSNP:rs28399585).
FT                                /FTId=VAR_021347.
FT   MUTAGEN     392    392       T->A: Increase of steady state level.
SQ   SEQUENCE   404 AA;  46757 MW;  D7DC9BEEF3FD62EC CRC64;
     MSRRSSRLQA KQQPQPSQTE SPQEAQIIQA KKRKTTQDVK KRREEVTKKH QYEIRNCWPP
     VLSGGISPCI IIETPHKEIG TSDFSRFTNY RFKNLFINPS PLPDLSWGCS KEVWLNMLKK
     ESRYVHDKHF EVLHSDLEPQ MRSILLDWLL EVCEVYTLHR ETFYLAQDFF DRFMLTQKDI
     NKNMLQLIGI TSLFIASKLE EIYAPKLQEF AYVTDGACSE EDILRMELII LKALKWELCP
     VTIISWLNLF LQVDALKDAP KVLLPQYSQE TFIQIAQLLD LCILAIDSLE FQYRILTAAA
     LCHFTSIEVV KKASGLEWDS ISECVDWMVP FVNVVKSTSP VKLKTFKKIP MEDRHNIQTH
     TNYLAMLEEV NYINTFRKGG QLSPVCNGGI MTPPKSTEKP PGKH
//