CCND2_BOVIN
ID CCND2_BOVIN Reviewed; 289 AA.
AC Q0P5D3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=G1/S-specific cyclin-D2;
GN Name=CCND2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory component of the cyclin D2-CDK4 (DC) complex that
CC phosphorylates and inhibits members of the retinoblastoma (RB) protein
CC family including RB1 and regulates the cell-cycle during G(1)/S
CC transition. Phosphorylation of RB1 allows dissociation of the
CC transcription factor E2F from the RB/E2F complex and the subsequent
CC transcription of E2F target genes which are responsible for the
CC progression through the G(1) phase. Hypophosphorylates RB1 in early
CC G(1) phase. Cyclin D-CDK4 complexes are major integrators of various
CC mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P30279}.
CC -!- SUBUNIT: Interacts with either CDK4 or CDK6 protein kinase to form a
CC serine/threonine kinase holoenzyme complex. The cyclin subunit imparts
CC substrate specificity to the complex. {ECO:0000250|UniProtKB:P30279}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm
CC {ECO:0000250|UniProtKB:P30279}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate
CC at the nuclear membrane and are then translocated into the nucleus
CC through interaction with KIP/CIP family members.
CC {ECO:0000250|UniProtKB:P30279}.
CC -!- PTM: Phosphorylation at Thr-280 by MAP kinases is required for
CC ubiquitination and degradation by the DCX(AMBRA1) complex.
CC {ECO:0000250|UniProtKB:P24385}.
CC -!- PTM: Ubiquitinated by the DCX(AMBRA1) complex during the transition
CC from G1 to S cell phase, leading to its degradation: ubiquitination is
CC dependent on Thr-280 phosphorylation. The DCX(AMBRA1) complex
CC represents the major regulator of CCND2 stability during the G1/S
CC transition (By similarity). Polyubiquitinated by the SCF(FBXL2)
CC complex, leading to proteasomal degradation (By similarity).
CC {ECO:0000250|UniProtKB:P30279, ECO:0000250|UniProtKB:P30280}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000305}.
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DR EMBL; BC120199; AAI20200.1; -; mRNA.
DR RefSeq; NP_001069840.1; NM_001076372.1.
DR AlphaFoldDB; Q0P5D3; -.
DR SMR; Q0P5D3; -.
DR STRING; 9913.ENSBTAP00000022145; -.
DR PaxDb; Q0P5D3; -.
DR PRIDE; Q0P5D3; -.
DR Ensembl; ENSBTAT00000022145; ENSBTAP00000022145; ENSBTAG00000016649.
DR GeneID; 615414; -.
DR KEGG; bta:615414; -.
DR CTD; 894; -.
DR VEuPathDB; HostDB:ENSBTAG00000016649; -.
DR VGNC; VGNC:26963; CCND2.
DR eggNOG; KOG0656; Eukaryota.
DR GeneTree; ENSGT00940000155180; -.
DR HOGENOM; CLU_052190_0_0_1; -.
DR InParanoid; Q0P5D3; -.
DR OMA; CLEMDTN; -.
DR OrthoDB; 1234739at2759; -.
DR TreeFam; TF101004; -.
DR Reactome; R-BTA-69231; Cyclin D associated events in G1.
DR Reactome; R-BTA-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000016649; Expressed in cumulus cell and 107 other tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0097129; C:cyclin D2-CDK4 complex; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
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; IPR015451; Cyclin_D.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF66; PTHR10177:SF66; 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; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..289
FT /note="G1/S-specific cyclin-D2"
FT /id="PRO_0000282333"
FT DOMAIN 26..151
FT /note="Cyclin N-terminal"
FT REGION 264..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30279"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30280"
SQ SEQUENCE 289 AA; 32613 MW; 72FC14F57AD563EF CRC64;
MELLCGEVEP VRRAVPDANL LHDDRVLQNL LTIEERYLPQ CSYFKCVQKD IQPYMRRMVA
TWMLEVCEEQ KCEEEVFPLA INYLDRFLAG VPTPKTHLQL LGAVCMFLAS KLKETIPLTA
EKLCIYTDNS IKPQELLEWE LVVLGKLKWN LAAVTPHDFI EHILRKLPQP SEKLSLIRKH
AQTFIALCAT DFKFAMYPPS MIATGSVGAA ICGLQQDEDV SSLTGDALVD LLAKITNTDV
DCLKACQEQI EVVLLNSLQQ YRQDQGDGSK SEDELDQAST PTDVRDIDL
