CPLM-005299

Genbank Nucleotide ID

G1/S-specific cyclin-D1

Protein Synonyms/Alias

B-cell lymphoma 1 protein; BCL-1; BCL-1 oncogene; PRAD1 oncogene

Homo sapiens (Human)

Position	Peptide	Type	References
33	RVLRAMLKAEETCAP	sumoylation	[1]
33	RVLRAMLKAEETCAP	ubiquitination	[2]
46	APSVSYFKCVQKEVL	ubiquitination	[3]
50	SYFKCVQKEVLPSMR	ubiquitination	[3]
95	FLSLEPVKKSRLQLL	ubiquitination	[4, 5, 6]
112	TCMFVASKMKETIPL	ubiquitination	[5, 6]
114	MFVASKMKETIPLTA	ubiquitination	[4]
149	LLLVNKLKWNLAAMT	ubiquitination	[5]
167	FIEHFLSKMPEAEEN	ubiquitination	[4]
175	MPEAEENKQIIRKHA	ubiquitination	[4, 5, 6]
180	ENKQIIRKHAQTFVA	ubiquitination	[5]
238	RFLSRVIKCDPDCLR	ubiquitination	[3, 4, 5]

[1] SUMO-modified nuclear cyclin D1 bypasses Ras-induced senescence.
Wang XD, Lapi E, Sullivan A, Ratnayaka I, Goldin R, Hay R, Lu X.
Cell Death Differ. 2011 Feb;18(2):304-14. [PMID: 20798689]
[2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]

Functional Description

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.

DOMAIN 28 152 Cyclin N-terminal.
MOD_RES 286 286 Phosphothreonine.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Cell cycle; Cell division; Chromosomal rearrangement; Complete proteome; Cyclin; Cytoplasm; DNA damage; Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:BHF-UCL.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0005923; C:tight junction; IEA:Compara.
GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:Compara.
GO:0004672; F:protein kinase activity; IEA:Compara.
GO:0060070; P:canonical Wnt receptor signaling pathway; IEA:Compara.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Compara.
GO:0045444; P:fat cell differentiation; IEA:Compara.
GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
GO:0007595; P:lactation; IEA:Compara.
GO:0033327; P:Leydig cell differentiation; IEA:Compara.
GO:0001889; P:liver development; IEA:Compara.
GO:0060749; P:mammary gland alveolus development; IEA:Compara.
GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Compara.
GO:0031571; P:mitotic G1 DNA damage checkpoint; IDA:UniProtKB.
GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Compara.
GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IEA:Compara.
GO:0031100; P:organ regeneration; IEA:Compara.
GO:0045737; P:positive regulation of cyclin-dependent protein kinase activity; IDA:BHF-UCL.
GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Compara.
GO:0000320; P:re-entry into mitotic cell cycle; IEA:Compara.
GO:0051592; P:response to calcium ion; IEA:Compara.
GO:0051412; P:response to corticosterone stimulus; IEA:Compara.
GO:0042493; P:response to drug; IEP:UniProtKB.
GO:0043627; P:response to estrogen stimulus; IEA:Compara.
GO:0045471; P:response to ethanol; IEA:Compara.
GO:0010039; P:response to iron ion; IEA:Compara.
GO:0032026; P:response to magnesium ion; IEA:Compara.
GO:0010243; P:response to organic nitrogen; IEA:Compara.
GO:0070141; P:response to UV-A; IDA:BHF-UCL.
GO:0033197; P:response to vitamin E; IEA:Compara.
GO:0010165; P:response to X-ray; IEA:Compara.

IPR013763; Cyclin-like.
IPR014400; Cyclin_A/B/D/E.
IPR004367; Cyclin_C-dom.
IPR006671; Cyclin_N.

PF02984; Cyclin_C
PF00134; Cyclin_N