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G1/S-specific cyclin-D1

 CCND1_XENLA             Reviewed;         291 AA.
P50755;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
08-MAY-2019, entry version 87.
RecName: Full=G1/S-specific cyclin-D1;
Name=ccnd1;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Cockerill M.J., Hunt T.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Essential for the control of the cell cycle at the G1/S
(start) transition. May play a role in transcriptional regulation
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with the cdk4 and cdk6 protein kinases to form
a serine/threonine kinase holoenzyme complex. The cyclin subunit
imparts substrate specificity to the complex (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q91727:cdk4; NbExp=2; IntAct=EBI-7270567, EBI-7270544;
-!- PTM: Phosphorylation at Thr-282 by MAP kinases is required for
ubiquitination and degradation following DNA damage. It probably
plays an essential role for recognition by the FBXO31 component of
SCF (SKP1-cullin-F-box) protein ligase complex (By similarity).
{ECO:0000250}.
-!- PTM: Following DNA damage it is ubiquitinated by some SCF (SKP1-
cullin-F-box) protein ligase complex containing fbxo31.
Ubiquitination leads to its degradation and G1 arrest (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
{ECO:0000305}.
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EMBL; X89475; CAA61664.1; -; mRNA.
PIR; S57922; S57922.
SMR; P50755; -.
IntAct; P50755; 1.
MINT; P50755; -.
GO; GO:0005634; C:nucleus; IEA:InterPro.
GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
CDD; cd00043; CYCLIN; 1.
InterPro; IPR039361; Cyclin.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR004367; Cyclin_C-dom.
InterPro; IPR015451; Cyclin_D.
InterPro; IPR006671; Cyclin_N.
PANTHER; PTHR10177; PTHR10177; 1.
PANTHER; PTHR10177:SF67; PTHR10177:SF67; 1.
Pfam; PF02984; Cyclin_C; 1.
Pfam; PF00134; Cyclin_N; 1.
PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
SMART; SM00385; CYCLIN; 1.
SMART; SM01332; Cyclin_C; 1.
SUPFAM; SSF47954; SSF47954; 2.
PROSITE; PS00292; CYCLINS; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Cyclin; Phosphoprotein; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 291 G1/S-specific cyclin-D1.
/FTId=PRO_0000080436.
MOD_RES 282 282 Phosphothreonine. {ECO:0000250}.
SEQUENCE 291 AA; 32953 MW; A4747C5BD1679087 CRC64;
MELLCCEVDT IGRAHLDRNL ITDRVLQTML KAEETSCPSM SYFKCVQKEI LPNMRKIVAT
WMLEVCEEQK CEEEVFPLAM NYLDRFLSVE PLRKSWLQLL GATCMFLASK MKETIPLTAE
KLCIYTDNSI RPDELLIMEL RVLNKLKWDL ASVTPHDFIE HFLNKMPLTE DTKQIIRKHA
QTFVALCATD VNFISNPPSM IAAGSVAAAV QGLNLGNADS VFSTQRLTLF LSQVIKCDPD
CLRACQEQIE SLLESSLRQA QQQHNASSDT KNMVDEVDIS CTPTDVRDVN I


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