CCNE2_MOUSE
ID CCNE2_MOUSE Reviewed; 404 AA.
AC Q9Z238; Q9QWU5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=G1/S-specific cyclin-E2;
GN Name=Ccne2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9858585; DOI=10.1128/mcb.19.1.612;
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 expressed
RT in human cancers.";
RL Mol. Cell. Biol. 19:612-622(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential for the control of the cell cycle at the late G1
CC and early S phase.
CC -!- SUBUNIT: Interacts with the CDK2 (in vivo) and CDK3 (in vitro) protein
CC kinases to form a serine/threonine kinase holoenzyme complex. The
CC cyclin subunit imparts substrate specificity to the complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest levels in adult testis, thymus and brain.
CC Lower levels in placenta, spleen and colon.
CC -!- PTM: Phosphorylation by CDK2 triggers its release from CDK2 and
CC degradation via the ubiquitin proteasome pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC {ECO:0000305}.
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DR EMBL; AF091432; AAC80527.1; -; mRNA.
DR EMBL; AF106691; AAD08817.1; -; mRNA.
DR CCDS; CCDS17965.1; -.
DR RefSeq; NP_001032211.1; NM_001037134.2.
DR RefSeq; NP_001269872.1; NM_001282943.1.
DR RefSeq; NP_033960.1; NM_009830.3.
DR RefSeq; XP_006537636.1; XM_006537573.3.
DR RefSeq; XP_006537637.1; XM_006537574.3.
DR RefSeq; XP_006537638.1; XM_006537575.3.
DR RefSeq; XP_011248215.1; XM_011249913.2.
DR AlphaFoldDB; Q9Z238; -.
DR SMR; Q9Z238; -.
DR ComplexPortal; CPX-2082; Cyclin E2-CDK2 complex.
DR STRING; 10090.ENSMUSP00000029866; -.
DR iPTMnet; Q9Z238; -.
DR PhosphoSitePlus; Q9Z238; -.
DR EPD; Q9Z238; -.
DR MaxQB; Q9Z238; -.
DR PaxDb; Q9Z238; -.
DR PRIDE; Q9Z238; -.
DR ProteomicsDB; 281337; -.
DR Antibodypedia; 3593; 372 antibodies from 38 providers.
DR DNASU; 12448; -.
DR Ensembl; ENSMUST00000108324; ENSMUSP00000103960; ENSMUSG00000028212.
DR Ensembl; ENSMUST00000170901; ENSMUSP00000130693; ENSMUSG00000028212.
DR GeneID; 12448; -.
DR KEGG; mmu:12448; -.
DR UCSC; uc008rzd.2; mouse.
DR CTD; 9134; -.
DR MGI; MGI:1329034; Ccne2.
DR VEuPathDB; HostDB:ENSMUSG00000028212; -.
DR eggNOG; KOG0655; Eukaryota.
DR GeneTree; ENSGT00940000156934; -.
DR HOGENOM; CLU_020695_8_0_1; -.
DR InParanoid; Q9Z238; -.
DR OMA; KRHQYEI; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q9Z238; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
DR BioGRID-ORCS; 12448; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q9Z238; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z238; protein.
DR Bgee; ENSMUSG00000028212; Expressed in spermatocyte and 254 other tissues.
DR ExpressionAtlas; Q9Z238; baseline and differential.
DR Genevisible; Q9Z238; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0097134; C:cyclin E1-CDK2 complex; IBA:GO_Central.
DR GO; GO:0097135; C:cyclin E2-CDK2 complex; IDA:MGI.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IGI:MGI.
DR GO; GO:0006270; P:DNA replication initiation; IMP:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IGI:MGI.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IDA: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; IGI:MGI.
DR GO; GO:0000723; P:telomere maintenance; IGI:MGI.
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:SF70; PTHR10177:SF70; 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.
FT CHAIN 1..404
FT /note="G1/S-specific cyclin-E2"
FT /id="PRO_0000080462"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O96020"
FT CONFLICT 6
FT /note="Missing (in Ref. 2; AAD08817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 46669 MW; 0612C4ACBEE47DAA CRC64;
MSRRSSRLQA KQHAQPNQPD SPQETQIIQA KKRKTAQDVK KRKEEITKKH QYEIRNCWPP
VLSGGISPCI IIETPHKEIG TSDFSRFTNY RFKNLFINPS PLPDLSWACS QEVWQNMLQK
ENRYVHDKHF QVLHSDLEPQ MRSILLDWLL EVCEVYTLHR ETFYLAQDFF DRFMLTQKDV
NKNMLQLIGI TSLFIASKLE EIYAPKLQEF AYVTDGACSE VDILKMELNI LKALKWELCP
VTVISWLNLF LQVDAVKDVP KVLLPQYSQE TFIQIAQLLD LCILAIDSLE FQYRILAAAA
LCHFTSIEVV KKASGLEWDD ISECVDWMVP FVSVVKSVSP VKLKTFKKIP MEDRHNIQTH
TNYLALLNEV NYVNIYRKGG QLSPVCNGGI MTPPKSTEKP PGKH
