CCND2_CHICK
ID CCND2_CHICK Reviewed; 291 AA.
AC P49706;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=G1/S-specific cyclin-D2;
GN Name=CCND2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8566807; DOI=10.1016/0378-1119(95)00598-6;
RA Li H., Grenet J., Kidd V.J.;
RT "Structure and gene expression of avian cyclin D2.";
RL Gene 167:341-342(1995).
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 the CDK4 and CDK6 protein kinases 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-282 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-282 phosphorylation. The DCX(AMBRA1) complex
CC represents the major regulator of CCND2 stability during the G1/S
CC transition. {ECO:0000250|UniProtKB:P30280}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000305}.
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DR EMBL; U28980; AAA96955.1; -; Genomic_DNA.
DR PIR; JC4579; JC4579.
DR RefSeq; NP_989544.1; NM_204213.1.
DR RefSeq; XP_015147604.1; XM_015292118.1.
DR AlphaFoldDB; P49706; -.
DR SMR; P49706; -.
DR STRING; 9031.ENSGALP00000027885; -.
DR PaxDb; P49706; -.
DR Ensembl; ENSGALT00000027938; ENSGALP00000027885; ENSGALG00000017283.
DR Ensembl; ENSGALT00000083605; ENSGALP00000059783; ENSGALG00000017283.
DR GeneID; 374047; -.
DR KEGG; gga:374047; -.
DR CTD; 894; -.
DR VEuPathDB; HostDB:geneid_374047; -.
DR eggNOG; KOG0656; Eukaryota.
DR GeneTree; ENSGT00940000155180; -.
DR HOGENOM; CLU_052190_0_0_1; -.
DR InParanoid; P49706; -.
DR OMA; CLEMDTN; -.
DR OrthoDB; 1234739at2759; -.
DR PhylomeDB; P49706; -.
DR Reactome; R-GGA-69231; Cyclin D associated events in G1.
DR Reactome; R-GGA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-GGA-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR PRO; PR:P49706; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017283; Expressed in spleen and 12 other tissues.
DR ExpressionAtlas; P49706; baseline and differential.
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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell cycle; Cell division; Cyclin; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..291
FT /note="G1/S-specific cyclin-D2"
FT /id="PRO_0000080440"
FT REGION 264..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30280"
SQ SEQUENCE 291 AA; 33164 MW; 43A7E646AEAF3109 CRC64;
MELLCCEVDP MRRALPDPNL LYDDRVLHNL LTIEERYLPQ CSYFKCVQKD IQPFMRRMVA
TWMLEVCEEQ KCEEEVFPLA MNYLDRFLAV VPTRKCHLQL LGAVCMFLAS KLKETIPLTA
EKLCIYTDNS IKPQELLEWE LVVLGKLKWN LAAVTPHDFI EHILRKLPLP KDKLVLIRKH
AQTFIALCAT DFNFAMYPPS MIATGSVGAA ICGLQLDDGD RSLSGDSLTD FLAKITSTDV
DCLKACQEQI ESVLVSNLRQ VRQQQQQSNP SKTIEELDQA STPTDVRDIN L
