CCND1_CHICK
ID CCND1_CHICK Reviewed; 292 AA.
AC P55169;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=G1/S-specific cyclin-D1;
GN Name=CCND1;
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 [MRNA].
RA Li H., Lahti J.M., Kidd V.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory component of the cyclin D1-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:P24385}.
CC -!- SUBUNIT: Interacts with the CDK4 and CDK6 protein kinases to form a
CC serine/threonine kinase holoenzyme complex (By similarity). The cyclin
CC subunit imparts substrate specificity to the complex (By similarity).
CC {ECO:0000250|UniProtKB:P24385}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24385}. Cytoplasm
CC {ECO:0000250|UniProtKB:P24385}.
CC -!- PTM: Phosphorylation at Thr-283 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. The DCX(AMBRA1)
CC complex represents the major regulator of CCND1 stability during the
CC G1/S transition. {ECO:0000250|UniProtKB:P24385}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000305}.
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DR EMBL; U40844; AAA83271.1; -; mRNA.
DR RefSeq; NP_990712.1; NM_205381.1.
DR AlphaFoldDB; P55169; -.
DR SMR; P55169; -.
DR STRING; 9031.ENSGALP00000012203; -.
DR PaxDb; P55169; -.
DR GeneID; 396341; -.
DR KEGG; gga:396341; -.
DR CTD; 595; -.
DR VEuPathDB; HostDB:geneid_396341; -.
DR eggNOG; KOG0656; Eukaryota.
DR InParanoid; P55169; -.
DR OrthoDB; 1234739at2759; -.
DR PhylomeDB; P55169; -.
DR PRO; PR:P55169; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0070141; P:response to UV-A; ISS:UniProtKB.
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:SF67; PTHR10177:SF67; 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; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..292
FT /note="G1/S-specific cyclin-D1"
FT /id="PRO_0000080434"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24385"
SQ SEQUENCE 292 AA; 33264 MW; 7B543029DB45A67D CRC64;
MEHQLQCCEV ETIRRAYLDA NLLNDRVLQT MLKAEETCSP SVSYFKCVQK EILPYMRKIV
ATWMLEVCEE QKCEEEVFPL AMNYLDRFLS FEPLKKSRLQ LLGATCMFVA SKMKETIPLT
AEKLCIYTDN SIRPDELLQM ELLLVNKLKW NLAAMTPHDF IEHFLTKMPL AEDTKQIIRK
HAQTFVALCA TDVKFISNPP SMIAAGSVVA AVQGLHLGNT NTFLSYQCLT HFLSQVIKCD
PDCLRACQEQ IESLLESSLR QAQQHNVSSE TKTVEDEADL SCTPTDVRDV NI
