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G1/S-specific cyclin-D1 (B-cell lymphoma 1 protein) (BCL-1) (BCL-1 oncogene) (PRAD1 oncogene)

 CCND1_HUMAN             Reviewed;         295 AA.
P24385; Q6LEF0;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
05-DEC-2018, entry version 207.
RecName: Full=G1/S-specific cyclin-D1;
AltName: Full=B-cell lymphoma 1 protein;
Short=BCL-1;
AltName: Full=BCL-1 oncogene;
AltName: Full=PRAD1 oncogene;
Name=CCND1; Synonyms=BCL1, PRAD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1826542; DOI=10.1038/350512a0;
Motokura T., Bloom T., Kim H.G., Jueppner H., Ruderman J.V.,
Kronenberg H.M., Arnold A.;
"A novel cyclin encoded by a bcl1-linked candidate oncogene.";
Nature 350:512-515(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1833066; DOI=10.1016/0092-8674(91)90042-W;
Lew D.J., Dulic V., Reed S.I.;
"Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
function in yeast.";
Cell 66:1197-1206(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1827756; DOI=10.1016/0092-8674(91)90100-D;
Xiong Y., Connolly T., Futcher B., Beach D.;
"Human D-type cyclin.";
Cell 65:691-699(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1833629; DOI=10.1128/MCB.11.10.4846;
Withers D.A., Harvey R.C., Faust J.B., Melnyk O., Carey K.,
Meeker T.C.;
"Characterization of a candidate bcl-1 gene.";
Mol. Cell. Biol. 11:4846-4853(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8204893;
Rimokh R., Berger F., Bastard C., Klein B., French M., Archimbaud E.,
Rouault J.-P., Santa Lucia B., Duret L., Vuillaume M.;
"Rearrangement of CCND1 (BCL1/PRAD1) 3' untranslated region in mantle-
cell lymphomas and t(11q13)-associated leukemias.";
Blood 83:3689-3696(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
TISSUE=Placenta;
PubMed=7687458; DOI=10.1002/gcc.2870070205;
Motokura T., Arnold A.;
"The PRAD1/cyclin D1 proto-oncogene: genomic organization, 5' DNA
sequence, and sequence of a tumor-specific rearrangement breakpoint.";
Genes Chromosomes Cancer 7:89-95(1993).
[10]
INTERACTION WITH CDK4 AND CDK6.
PubMed=8302605;
Bates S., Bonetta L., McAllan D., Parry D., Holder A., Dickson C.,
Peters G.;
"CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-
dependent kinases that associate with cyclin D1.";
Oncogene 9:71-79(1994).
[11]
INVOLVEMENT IN MULTIPLE MYELOMA.
PubMed=8695815;
Chesi M., Bergsagel P.L., Brents L.A., Smith C.M., Gerhard D.S.,
Kuehl W.M.;
"Dysregulation of cyclin D1 by translocation into an IgH gamma switch
region in two multiple myeloma cell lines.";
Blood 88:674-681(1996).
[12]
INTERACTION WITH CDK4 IN THE CCND1-CDK4-CDKN COMPLEX, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=9106657; DOI=10.1101/gad.11.7.847;
LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C.,
Chou H.S., Fattaey A., Harlow E.;
"New functional activities for the p21 family of CDK inhibitors.";
Genes Dev. 11:847-862(1997).
[13]
UBIQUITINATION, AND MUTAGENESIS OF THR-286 AND THR-288.
PubMed=10766840; DOI=10.1074/jbc.275.16.12074;
Germain D., Russell A., Thompson A., Hendley J.;
"Ubiquitination of free cyclin D1 is independent of phosphorylation on
threonine 286.";
J. Biol. Chem. 275:12074-12079(2000).
[14]
FUNCTION OF CCND1-CDK4 COMPLEX IN SMAD PHOSPHORYLATION.
PubMed=15241418; DOI=10.1038/nature02650;
Matsuura I., Denissova N.G., Wang G., He D., Long J., Liu F.;
"Cyclin-dependent kinases regulate the antiproliferative function of
Smads.";
Nature 430:226-231(2004).
[15]
FUNCTION, AND INTERACTION WITH INSM1.
PubMed=16569215; DOI=10.1042/BJ20051669;
Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.;
"INSM1 functions as a transcriptional repressor of the neuroD/beta2
gene through the recruitment of cyclin D1 and histone deacetylases.";
Biochem. J. 397:169-177(2006).
[16]
FUNCTION, AND INTERACTION WITH INSM1.
PubMed=18417529; DOI=10.1677/JOE-08-0001;
Wang H.W., Muguira M., Liu W.D., Zhang T., Chen C., Aucoin R.,
Breslin M.B., Lan M.S.;
"Identification of an INSM1-binding site in the insulin promoter:
negative regulation of the insulin gene transcription.";
J. Endocrinol. 198:29-39(2008).
[17]
INTERACTION WITH INSM1 AND CDK4.
PubMed=19124461; DOI=10.1074/jbc.M808843200;
Zhang T., Liu W.D., Saunee N.A., Breslin M.B., Lan M.S.;
"Zinc finger transcription factor INSM1 interrupts cyclin D1 and CDK4
binding and induces cell cycle arrest.";
J. Biol. Chem. 284:5574-5581(2009).
[18]
INTERACTION WITH USP2, UBIQUITINATION, AND DEUBIQUITINATION BY USP2.
PubMed=19917254; DOI=10.1016/j.molcel.2009.10.018;
Shan J., Zhao W., Gu W.;
"Suppression of cancer cell growth by promoting cyclin D1
degradation.";
Mol. Cell 36:469-476(2009).
[19]
PHOSPHORYLATION AT THR-286, UBIQUITINATION, AND MUTAGENESIS OF
THR-286.
PubMed=19412162; DOI=10.1038/nature08011;
Santra M.K., Wajapeyee N., Green M.R.;
"F-box protein FBXO31 mediates cyclin D1 degradation to induce G1
arrest after DNA damage.";
Nature 459:722-725(2009).
[20]
UBIQUITINATION, AND INTERACTION WITH UHRF2.
PubMed=21952639; DOI=10.4161/cc.10.19.17176;
Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.;
"NIRF constitutes a nodal point in the cell cycle network and is a
candidate tumor suppressor.";
Cell Cycle 10:3284-3299(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-271 IN COMPLEX WITH WILD
TYPE AND MUTANTS ALA-172; PHE-172 AND ASP-172 CDK4.
PubMed=19237565; DOI=10.1073/pnas.0809645106;
Day P.J., Cleasby A., Tickle I.J., O'Reilly M., Coyle J.E.,
Holding F.P., McMenamin R.L., Yon J., Chopra R., Lengauer C.,
Jhoti H.;
"Crystal structure of human CDK4 in complex with a D-type cyclin.";
Proc. Natl. Acad. Sci. U.S.A. 106:4166-4170(2009).
-!- FUNCTION: Regulatory component of the cyclin D1-CDK4 (DC) complex
that phosphorylates and inhibits members of the retinoblastoma
(RB) protein family including RB1 and regulates the cell-cycle
during G(1)/S transition. Phosphorylation of RB1 allows
dissociation of the transcription factor E2F from the RB/E2F
complex and the subsequent transcription of E2F target genes which
are responsible for the progression through the G(1) phase.
Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4
complexes are major integrators of various mitogenenic and
antimitogenic signals. Also substrate for SMAD3, phosphorylating
SMAD3 in a cell-cycle-dependent manner and repressing its
transcriptional activity. Component of the ternary complex, cyclin
D1/CDK4/CDKN1B, required for nuclear translocation and activity of
the cyclin D-CDK4 complex. Exhibits transcriptional corepressor
activity with INSM1 on the NEUROD1 and INS promoters in a cell
cycle-independent manner. {ECO:0000269|PubMed:15241418,
ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:18417529,
ECO:0000269|PubMed:9106657}.
-!- SUBUNIT: Interacts with FBXO4 (By similarity). Interacts with
either CDK4 or CDK6 protein kinase to form a serine/threonine
kinase holoenzyme complex. The cyclin subunit imparts substrate
specificity to the complex. Component of the ternary complex
CCND1/CDK4/CDKN1B required for nuclear translocation and
modulation of CDK4-mediated kinase activity. Interacts directly
with CDKN1B. Interacts with UHRF2; the interaction ubiquitinates
CCND1 and appears to occur independently of phosphorylation. Can
form similar complexes with either CDKN1A or CDKN2A. Interacts
with USP2. Interacts (via cyclin N-terminal domain) with INSM1
(via N-terminal region); the interaction competes with the binding
of CCND1 to CDK4 during cell cycle progression and inhibits CDK4
activity. Interacts with CDK4; the interaction is prevented with
the binding of CCND1 to INSM1 during cell cycle progression.
{ECO:0000250, ECO:0000269|PubMed:16569215,
ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:19124461,
ECO:0000269|PubMed:19237565, ECO:0000269|PubMed:19917254,
ECO:0000269|PubMed:21952639, ECO:0000269|PubMed:8302605,
ECO:0000269|PubMed:9106657}.
-!- INTERACTION:
Q96TE0:-; NbExp=3; IntAct=EBI-375001, EBI-10201595;
P10275:AR; NbExp=4; IntAct=EBI-375001, EBI-608057;
P38398:BRCA1; NbExp=3; IntAct=EBI-375001, EBI-349905;
P30260:CDC27; NbExp=3; IntAct=EBI-375001, EBI-994813;
P24941:CDK2; NbExp=3; IntAct=EBI-375001, EBI-375096;
P11802:CDK4; NbExp=29; IntAct=EBI-375001, EBI-295644;
P30285:Cdk4 (xeno); NbExp=2; IntAct=EBI-375001, EBI-847225;
Q00534:CDK6; NbExp=4; IntAct=EBI-375001, EBI-295663;
P38936:CDKN1A; NbExp=15; IntAct=EBI-375001, EBI-375077;
P46527:CDKN1B; NbExp=3; IntAct=EBI-375001, EBI-519280;
Q5XUX0:FBXO31; NbExp=4; IntAct=EBI-375001, EBI-6162477;
O15379:HDAC3; NbExp=3; IntAct=EBI-375001, EBI-607682;
Q16656:NRF1; NbExp=2; IntAct=EBI-375001, EBI-2547810;
Q62796:Ralbp1 (xeno); NbExp=2; IntAct=EBI-375001, EBI-3956409;
Q96PU4:UHRF2; NbExp=4; IntAct=EBI-375001, EBI-625304;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9106657}.
Cytoplasm {ECO:0000269|PubMed:9106657}. Membrane
{ECO:0000269|PubMed:9106657}. Note=Cyclin D-CDK4 complexes
accumulate at the nuclear membrane and are then translocated to
the nucleus through interaction with KIP/CIP family members.
{ECO:0000250}.
-!- PTM: Phosphorylation at Thr-286 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.
{ECO:0000269|PubMed:19412162, ECO:0000269|PubMed:19917254}.
-!- PTM: Ubiquitinated, primarily as 'Lys-48'-linked
polyubiquitination. Ubiquitinated by a SCF (SKP1-CUL1-F-box
protein) ubiquitin-protein ligase complex containing FBXO4 and
CRYAB. Following DNA damage it is ubiquitinated by some SCF (SKP1-
cullin-F-box) protein ligase complex containing FBXO31. SCF-type
ubiquitination is dependent on Thr-286 phosphorylation (By
similarity). Ubiquitinated also by UHRF2 apparently in a
phosphorylation-independent manner. Ubiquitination leads to its
degradation and G1 arrest. Deubiquitinated by USP2; leading to its
stabilization. {ECO:0000250, ECO:0000269|PubMed:19412162,
ECO:0000269|PubMed:19917254}.
-!- DISEASE: Note=A chromosomal aberration involving CCND1 may be a
cause of B-lymphocytic malignancy, particularly mantle-cell
lymphoma (MCL). Translocation t(11;14)(q13;q32) with
immunoglobulin gene regions. Activation of CCND1 may be oncogenic
by directly altering progression through the cell cycle.
-!- DISEASE: Note=A chromosomal aberration involving CCND1 may be a
cause of parathyroid adenomas. Translocation t(11;11)(q13;p15)
with the parathyroid hormone (PTH) enhancer.
-!- DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of
plasma cells usually arising in the bone marrow and characterized
by diffuse involvement of the skeletal system, hyperglobulinemia,
Bence-Jones proteinuria and anemia. Complications of multiple
myeloma are bone pain, hypercalcemia, renal failure and spinal
cord compression. The aberrant antibodies that are produced lead
to impaired humoral immunity and patients have a high prevalence
of infection. Amyloidosis may develop in some patients. Multiple
myeloma is part of a spectrum of diseases ranging from monoclonal
gammopathy of unknown significance (MGUS) to plasma cell leukemia.
{ECO:0000269|PubMed:8695815}. Note=The gene represented in this
entry is involved in disease pathogenesis. A chromosomal
aberration involving CCND1 is found in multiple myeloma.
Translocation t(11;14)(q13;q32) with the IgH locus.
-!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCL1ID36.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ccnd1/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=CCND1";
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EMBL; X59798; CAA42470.1; -; mRNA.
EMBL; M74092; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M64349; AAA52136.1; -; mRNA.
EMBL; M73554; AAA58392.1; -; mRNA.
EMBL; Z23022; CAA80558.1; -; mRNA.
EMBL; BT019845; AAV38648.1; -; mRNA.
EMBL; AF511593; AAM34300.2; -; Genomic_DNA.
EMBL; BC000076; AAH00076.1; -; mRNA.
EMBL; BC001501; AAH01501.1; -; mRNA.
EMBL; BC014078; AAH14078.1; -; mRNA.
EMBL; BC023620; AAH23620.1; -; mRNA.
EMBL; BC025302; AAH25302.1; -; mRNA.
EMBL; L09054; AAA36481.1; -; Genomic_DNA.
CCDS; CCDS8191.1; -.
PIR; A38977; A38977.
RefSeq; NP_444284.1; NM_053056.2.
UniGene; Hs.523852; -.
PDB; 2W96; X-ray; 2.30 A; A=1-271.
PDB; 2W99; X-ray; 2.80 A; A=1-271.
PDB; 2W9F; X-ray; 2.85 A; A=1-271.
PDB; 2W9Z; X-ray; 2.45 A; A=16-271.
PDB; 5VZU; X-ray; 2.70 A; E/F=279-295.
PDBsum; 2W96; -.
PDBsum; 2W99; -.
PDBsum; 2W9F; -.
PDBsum; 2W9Z; -.
PDBsum; 5VZU; -.
ProteinModelPortal; P24385; -.
SMR; P24385; -.
BioGrid; 107067; 101.
ComplexPortal; CPX-2010; Cyclin D1-CDK4 complex.
ComplexPortal; CPX-2014; Cyclin D1-CDK6 complex.
CORUM; P24385; -.
DIP; DIP-123N; -.
IntAct; P24385; 63.
MINT; P24385; -.
STRING; 9606.ENSP00000227507; -.
BindingDB; P24385; -.
ChEMBL; CHEMBL3610; -.
DrugBank; DB01169; Arsenic trioxide.
iPTMnet; P24385; -.
PhosphoSitePlus; P24385; -.
BioMuta; CCND1; -.
DMDM; 116152; -.
EPD; P24385; -.
PaxDb; P24385; -.
PeptideAtlas; P24385; -.
PRIDE; P24385; -.
ProteomicsDB; 54198; -.
DNASU; 595; -.
Ensembl; ENST00000227507; ENSP00000227507; ENSG00000110092.
GeneID; 595; -.
KEGG; hsa:595; -.
CTD; 595; -.
DisGeNET; 595; -.
EuPathDB; HostDB:ENSG00000110092.3; -.
GeneCards; CCND1; -.
HGNC; HGNC:1582; CCND1.
HPA; CAB000024; -.
HPA; HPA027802; -.
MalaCards; CCND1; -.
MIM; 168461; gene.
MIM; 254500; phenotype.
neXtProt; NX_P24385; -.
OpenTargets; ENSG00000110092; -.
Orphanet; 67038; B-cell chronic lymphocytic leukemia.
Orphanet; 52416; Mantle cell lymphoma.
Orphanet; 29073; Multiple myeloma.
PharmGKB; PA75; -.
eggNOG; KOG0656; Eukaryota.
eggNOG; ENOG410XRKC; LUCA.
GeneTree; ENSGT00940000157816; -.
HOGENOM; HOG000008182; -.
HOVERGEN; HBG050837; -.
InParanoid; P24385; -.
KO; K04503; -.
OMA; YRTTHFL; -.
OrthoDB; EOG091G0URX; -.
PhylomeDB; P24385; -.
TreeFam; TF101004; -.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8849470; PTK6 Regulates Cell Cycle.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SignaLink; P24385; -.
SIGNOR; P24385; -.
ChiTaRS; CCND1; human.
EvolutionaryTrace; P24385; -.
GeneWiki; Cyclin_D1; -.
GenomeRNAi; 595; -.
PRO; PR:P24385; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110092; Expressed in 219 organ(s), highest expression level in endometrium epithelium.
CleanEx; HS_CCND1; -.
ExpressionAtlas; P24385; baseline and differential.
Genevisible; P24385; HS.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; EXP:Reactome.
GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0000320; P:re-entry into mitotic cell cycle; IEA:Ensembl.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0007088; P:regulation of mitotic nuclear division; IBA:GO_Central.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0044321; P:response to leptin; IDA:UniProtKB.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0070141; P:response to UV-A; IDA:BHF-UCL.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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;
3D-structure; Cell cycle; Cell division; Chromosomal rearrangement;
Complete proteome; Cyclin; Cytoplasm; DNA damage; Isopeptide bond;
Membrane; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 295 G1/S-specific cyclin-D1.
/FTId=PRO_0000080430.
DOMAIN 28 152 Cyclin N-terminal.
COMPBIAS 272 280 Poly-Glu.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19412162}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P25322}.
MUTAGEN 286 286 T->A: Reduces ubiquitination and
subsequent degradation by the proteasome;
when associated with A-288. Abolishes
ubiquitination and subsequent degradation
following DNA damage.
{ECO:0000269|PubMed:10766840,
ECO:0000269|PubMed:19412162}.
MUTAGEN 288 288 T->A: Reduces ubiquitination and
subsequent degradation by the proteasome;
when associated with A-286.
{ECO:0000269|PubMed:10766840}.
CONFLICT 130 130 N -> G (in Ref. 3; AAA52136).
{ECO:0000305}.
CONFLICT 168 169 MP -> IA (in Ref. 2; M74092).
{ECO:0000305}.
CONFLICT 188 188 L -> S (in Ref. 3; AAA52136).
{ECO:0000305}.
STRAND 9 11 {ECO:0000244|PDB:2W96}.
HELIX 26 37 {ECO:0000244|PDB:2W96}.
HELIX 44 47 {ECO:0000244|PDB:2W96}.
HELIX 54 70 {ECO:0000244|PDB:2W96}.
HELIX 77 89 {ECO:0000244|PDB:2W96}.
TURN 96 98 {ECO:0000244|PDB:2W96}.
HELIX 99 114 {ECO:0000244|PDB:2W96}.
HELIX 121 127 {ECO:0000244|PDB:2W96}.
TURN 128 130 {ECO:0000244|PDB:2W96}.
HELIX 134 147 {ECO:0000244|PDB:2W96}.
TURN 148 150 {ECO:0000244|PDB:2W96}.
HELIX 157 166 {ECO:0000244|PDB:2W96}.
HELIX 172 190 {ECO:0000244|PDB:2W96}.
HELIX 194 197 {ECO:0000244|PDB:2W96}.
HELIX 200 218 {ECO:0000244|PDB:2W96}.
TURN 220 222 {ECO:0000244|PDB:2W9Z}.
HELIX 224 226 {ECO:0000244|PDB:2W96}.
HELIX 229 237 {ECO:0000244|PDB:2W96}.
HELIX 241 255 {ECO:0000244|PDB:2W96}.
TURN 256 260 {ECO:0000244|PDB:2W96}.
STRAND 261 263 {ECO:0000244|PDB:2W96}.
HELIX 288 290 {ECO:0000244|PDB:5VZU}.
HELIX 292 294 {ECO:0000244|PDB:5VZU}.
SEQUENCE 295 AA; 33729 MW; 3CC00C9905F58D3A CRC64;
MEHQLLCCEV ETIRRAYPDA NLLNDRVLRA MLKAEETCAP SVSYFKCVQK EVLPSMRKIV
ATWMLEVCEE QKCEEEVFPL AMNYLDRFLS LEPVKKSRLQ LLGATCMFVA SKMKETIPLT
AEKLCIYTDN SIRPEELLQM ELLLVNKLKW NLAAMTPHDF IEHFLSKMPE AEENKQIIRK
HAQTFVALCA TDVKFISNPP SMVAAGSVVA AVQGLNLRSP NNFLSYYRLT RFLSRVIKCD
PDCLRACQEQ IEALLESSLR QAQQNMDPKA AEEEEEEEEE VDLACTPTDV RDVDI


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