CCND3_HUMAN
ID CCND3_HUMAN Reviewed; 292 AA.
AC P30281; B2RD63; B3KQ22; E9PAS4; E9PB36; Q5T8J0; Q6FG62; Q96F49;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=G1/S-specific cyclin-D3 {ECO:0000303|PubMed:1386336};
GN Name=CCND3 {ECO:0000303|PubMed:1386336, ECO:0000312|HGNC:HGNC:1585};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-259.
RX PubMed=1386336; DOI=10.1016/0888-7543(92)90127-e;
RA Xiong Y., Menninger J., Beach D., Ward D.C.;
RT "Molecular cloning and chromosomal mapping of CCND genes encoding human D-
RT type cyclins.";
RL Genomics 13:575-584(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1383201; DOI=10.1016/s0021-9258(19)88717-3;
RA Motokura T., Keyomarsi K., Kronenberg H.M., Arnold A.;
RT "Cloning and characterization of human cyclin D3, a cDNA closely related in
RT sequence to the PRAD1/cyclin D1 proto-oncogene.";
RL J. Biol. Chem. 267:20412-20415(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-259.
RG NIEHS SNPs program;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-259.
RC TISSUE=Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND VARIANT
RP ALA-259.
RC TISSUE=Synovium, Thymus, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-259.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-259.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-237.
RC TISSUE=Placenta;
RX PubMed=1386335; DOI=10.1016/0888-7543(92)90126-d;
RA Inaba T., Matsushime H., Valentine M., Roussel M.F., Sherr C.J., Look A.T.;
RT "Genomic organization, chromosomal localization, and independent expression
RT of human cyclin D genes.";
RL Genomics 13:565-574(1992).
RN [11]
RP FUNCTION, AND INTERACTION WITH CDK6.
RX PubMed=8114739; DOI=10.1128/mcb.14.3.2077-2086.1994;
RA Meyerson M., Harlow E.;
RT "Identification of G1 kinase activity for cdk6, a novel cyclin D partner.";
RL Mol. Cell. Biol. 14:2077-2086(1994).
RN [12]
RP INTERACTION WITH CDK4 AND CDKN1A.
RX PubMed=9106657; DOI=10.1101/gad.11.7.847;
RA LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C.,
RA Chou H.S., Fattaey A., Harlow E.;
RT "New functional activities for the p21 family of CDK inhibitors.";
RL Genes Dev. 11:847-862(1997).
RN [13]
RP INTERACTION WITH ATF5, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15358120; DOI=10.1016/j.bbrc.2004.07.053;
RA Liu W., Sun M., Jiang J., Shen X., Sun Q., Liu W., Shen H., Gu J.;
RT "Cyclin D3 interacts with human activating transcription factor 5 and
RT potentiates its transcription activity.";
RL Biochem. Biophys. Res. Commun. 321:954-960(2004).
RN [14]
RP INTERACTION WITH EIF3K.
RX PubMed=15327989; DOI=10.1016/j.febslet.2004.07.071;
RA Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J.;
RT "Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k)
RT as a new interaction partner of cyclin D3.";
RL FEBS Lett. 573:139-146(2004).
RN [15]
RP INTERACTION WITH CDK4; CDKN2A AND CDKN1B.
RX PubMed=16782892; DOI=10.1128/mcb.02006-05;
RA Bockstaele L., Kooken H., Libert F., Paternot S., Dumont J.E.,
RA de Launoit Y., Roger P.P., Coulonval K.;
RT "Regulated activating Thr172 phosphorylation of cyclin-dependent kinase
RT 4(CDK4): its relationship with cyclins and CDK 'inhibitors'.";
RL Mol. Cell. Biol. 26:5070-5085(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP UBIQUITINATION BY SCF(FBXL2).
RX PubMed=22020328; DOI=10.1038/onc.2011.432;
RA Chen B.B., Glasser J.R., Coon T.A., Mallampalli R.K.;
RT "F-box protein FBXL2 exerts human lung tumor suppressor-like activity by
RT ubiquitin-mediated degradation of cyclin D3 resulting in cell cycle
RT arrest.";
RL Oncogene 31:2566-2579(2012).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP UBIQUITINATION.
RX PubMed=33854235; DOI=10.1038/s41586-021-03445-y;
RA Simoneschi D., Rona G., Zhou N., Jeong Y.T., Jiang S., Milletti G.,
RA Arbini A.A., O'Sullivan A., Wang A.A., Nithikasem S., Keegan S., Siu Y.,
RA Cianfanelli V., Maiani E., Nazio F., Cecconi F., Boccalatte F., Fenyoe D.,
RA Jones D.R., Busino L., Pagano M.;
RT "CRL4AMBRA1 is a master regulator of D-type cyclins.";
RL Nature 592:789-793(2021).
RN [22]
RP UBIQUITINATION.
RX PubMed=33854239; DOI=10.1038/s41586-021-03474-7;
RA Chaikovsky A.C., Li C., Jeng E.E., Loebell S., Lee M.C., Murray C.W.,
RA Cheng R., Demeter J., Swaney D.L., Chen S.H., Newton B.W., Johnson J.R.,
RA Drainas A.P., Shue Y.T., Seoane J.A., Srinivasan P., He A., Yoshida A.,
RA Hipkins S.Q., McCrea E., Poltorack C.D., Krogan N.J., Diehl J.A., Kong C.,
RA Jackson P.K., Curtis C., Petrov D.A., Bassik M.C., Winslow M.M., Sage J.;
RT "The AMBRA1 E3 ligase adaptor regulates the stability of cyclin D.";
RL Nature 592:794-798(2021).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CDK4.
RX PubMed=19237555; DOI=10.1073/pnas.0809674106;
RA Takaki T., Echalier A., Brown N.R., Hunt T., Endicott J.A., Noble M.E.;
RT "The structure of CDK4/cyclin D3 has implications for models of CDK
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4171-4176(2009).
CC -!- FUNCTION: Regulatory component of the cyclin D3-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 (PubMed:8114739). Phosphorylation of RB1 allows dissociation
CC of the transcription factor E2F from the RB/E2F complex and the
CC subsequent transcription of E2F target genes which are responsible for
CC the progression through the G(1) phase (PubMed:8114739).
CC Hypophosphorylates RB1 in early G(1) phase (PubMed:8114739). Cyclin D-
CC CDK4 complexes are major integrators of various mitogenenic and
CC antimitogenic signals (PubMed:8114739). Component of the ternary
CC complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and
CC activity of the cyclin D-CDK4 complex (PubMed:16782892). Shows
CC transcriptional coactivator activity with ATF5 independently of CDK4
CC (PubMed:15358120). {ECO:0000269|PubMed:15358120,
CC ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:8114739}.
CC -!- SUBUNIT: Interacts with the CDK4 and CDK6 protein kinases to form a
CC serine/threonine kinase holoenzyme complex (PubMed:9106657,
CC PubMed:19237555, PubMed:8114739). The cyclin subunit imparts substrate
CC specificity to the complex (PubMed:8114739). Interacts with ATF5
CC (PubMed:15358120). Interacts with EIF3K (PubMed:15327989). Component of
CC the ternary complex cyclin D/CDK4/CDKN1B required for nuclear
CC translocation and modulation of CDK4-mediated kinase activity
CC (PubMed:16782892). Can form similar complexes with either CDKN1A or
CC CDKN2A (PubMed:9106657, PubMed:16782892). {ECO:0000269|PubMed:15327989,
CC ECO:0000269|PubMed:15358120, ECO:0000269|PubMed:16782892,
CC ECO:0000269|PubMed:19237555, ECO:0000269|PubMed:8114739,
CC ECO:0000269|PubMed:9106657}.
CC -!- INTERACTION:
CC P30281; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-375013, EBI-725606;
CC P30281; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-375013, EBI-10961312;
CC P30281; O94921: CDK14; NbExp=5; IntAct=EBI-375013, EBI-1043945;
CC P30281; Q00536-3: CDK16; NbExp=3; IntAct=EBI-375013, EBI-12401765;
CC P30281; Q07002: CDK18; NbExp=3; IntAct=EBI-375013, EBI-746238;
CC P30281; Q00526: CDK3; NbExp=5; IntAct=EBI-375013, EBI-1245761;
CC P30281; P11802: CDK4; NbExp=35; IntAct=EBI-375013, EBI-295644;
CC P30281; Q00535: CDK5; NbExp=8; IntAct=EBI-375013, EBI-1041567;
CC P30281; Q00534: CDK6; NbExp=28; IntAct=EBI-375013, EBI-295663;
CC P30281; P38936: CDKN1A; NbExp=24; IntAct=EBI-375013, EBI-375077;
CC P30281; P55273: CDKN2D; NbExp=3; IntAct=EBI-375013, EBI-745859;
CC P30281; P29373: CRABP2; NbExp=3; IntAct=EBI-375013, EBI-10204806;
CC P30281; O14964: HGS; NbExp=3; IntAct=EBI-375013, EBI-740220;
CC P30281; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-375013, EBI-14069005;
CC P30281; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-375013, EBI-743811;
CC P30281; Q9BT43: POLR3GL; NbExp=9; IntAct=EBI-375013, EBI-2855862;
CC P30281; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-375013, EBI-1105213;
CC P30281; Q5VK71: AKAP8; Xeno; NbExp=6; IntAct=EBI-375013, EBI-11601938;
CC P30281; P08393: ICP0; Xeno; NbExp=3; IntAct=EBI-375013, EBI-6148881;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15358120}. Cytoplasm
CC {ECO:0000269|PubMed:15358120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P30281-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30281-2; Sequence=VSP_042649;
CC Name=3;
CC IsoId=P30281-3; Sequence=VSP_046267;
CC Name=4;
CC IsoId=P30281-4; Sequence=VSP_046266;
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: ubiquitination is
CC dependent on Thr-283 phosphorylation (PubMed:33854235,
CC PubMed:33854239). The DCX(AMBRA1) complex represents the major
CC regulator of CCND3 stability during the G1/S transition
CC (PubMed:33854235, PubMed:33854239). Polyubiquitinated by the SCF(FBXL2)
CC complex, leading to proteasomal degradation (PubMed:22020328).
CC {ECO:0000269|PubMed:22020328, ECO:0000269|PubMed:33854235,
CC ECO:0000269|PubMed:33854239}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccnd3/";
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DR EMBL; M90814; AAA51927.1; -; mRNA.
DR EMBL; M92287; AAA52137.1; -; mRNA.
DR EMBL; AF517525; AAM51826.1; -; Genomic_DNA.
DR EMBL; BX400719; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK057206; BAG51884.1; -; mRNA.
DR EMBL; AK097856; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK315421; BAG37810.1; -; mRNA.
DR EMBL; CR542246; CAG47042.1; -; mRNA.
DR EMBL; AL160163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04071.1; -; Genomic_DNA.
DR EMBL; BC011616; AAH11616.1; -; mRNA.
DR EMBL; M88087; AAA51929.1; -; Genomic_DNA.
DR EMBL; M88084; AAA51929.1; JOINED; Genomic_DNA.
DR EMBL; M88085; AAA51929.1; JOINED; Genomic_DNA.
DR EMBL; M88086; AAA51929.1; JOINED; Genomic_DNA.
DR CCDS; CCDS47425.1; -. [P30281-3]
DR CCDS; CCDS47426.1; -. [P30281-2]
DR CCDS; CCDS47427.1; -. [P30281-4]
DR CCDS; CCDS4863.1; -. [P30281-1]
DR PIR; B42822; B42822.
DR RefSeq; NP_001129489.1; NM_001136017.3. [P30281-2]
DR RefSeq; NP_001129597.1; NM_001136125.2. [P30281-3]
DR RefSeq; NP_001129598.1; NM_001136126.2. [P30281-4]
DR RefSeq; NP_001274356.1; NM_001287427.1.
DR RefSeq; NP_001274363.1; NM_001287434.1. [P30281-4]
DR RefSeq; NP_001751.1; NM_001760.4. [P30281-1]
DR PDB; 3G33; X-ray; 3.00 A; B/D=1-292.
DR PDBsum; 3G33; -.
DR AlphaFoldDB; P30281; -.
DR SMR; P30281; -.
DR BioGRID; 107336; 91.
DR ComplexPortal; CPX-2012; Cyclin D3-CDK4 complex.
DR ComplexPortal; CPX-2013; Cyclin D3-CDK6 complex.
DR CORUM; P30281; -.
DR DIP; DIP-31734N; -.
DR IntAct; P30281; 53.
DR MINT; P30281; -.
DR STRING; 9606.ENSP00000362082; -.
DR BindingDB; P30281; -.
DR ChEMBL; CHEMBL2422; -.
DR iPTMnet; P30281; -.
DR PhosphoSitePlus; P30281; -.
DR BioMuta; CCND3; -.
DR DMDM; 20981685; -.
DR EPD; P30281; -.
DR jPOST; P30281; -.
DR MassIVE; P30281; -.
DR MaxQB; P30281; -.
DR PaxDb; P30281; -.
DR PeptideAtlas; P30281; -.
DR PRIDE; P30281; -.
DR ProteomicsDB; 19071; -.
DR ProteomicsDB; 19134; -.
DR ProteomicsDB; 54648; -. [P30281-1]
DR ProteomicsDB; 54649; -. [P30281-2]
DR Antibodypedia; 3521; 844 antibodies from 43 providers.
DR DNASU; 896; -.
DR Ensembl; ENST00000372988.8; ENSP00000362079.4; ENSG00000112576.13. [P30281-2]
DR Ensembl; ENST00000372991.9; ENSP00000362082.5; ENSG00000112576.13. [P30281-1]
DR Ensembl; ENST00000414200.6; ENSP00000397545.2; ENSG00000112576.13. [P30281-3]
DR Ensembl; ENST00000415497.6; ENSP00000401595.2; ENSG00000112576.13. [P30281-4]
DR Ensembl; ENST00000511642.5; ENSP00000426212.1; ENSG00000112576.13. [P30281-2]
DR Ensembl; ENST00000616010.4; ENSP00000484424.1; ENSG00000112576.13. [P30281-4]
DR GeneID; 896; -.
DR KEGG; hsa:896; -.
DR MANE-Select; ENST00000372991.9; ENSP00000362082.5; NM_001760.5; NP_001751.1.
DR UCSC; uc003orn.4; human. [P30281-1]
DR CTD; 896; -.
DR DisGeNET; 896; -.
DR GeneCards; CCND3; -.
DR HGNC; HGNC:1585; CCND3.
DR HPA; ENSG00000112576; Tissue enhanced (lymphoid).
DR MIM; 123834; gene.
DR neXtProt; NX_P30281; -.
DR OpenTargets; ENSG00000112576; -.
DR PharmGKB; PA26152; -.
DR VEuPathDB; HostDB:ENSG00000112576; -.
DR eggNOG; KOG0656; Eukaryota.
DR GeneTree; ENSGT00940000160743; -.
DR HOGENOM; CLU_052190_0_0_1; -.
DR InParanoid; P30281; -.
DR OMA; QLLDWEI; -.
DR OrthoDB; 1234739at2759; -.
DR PhylomeDB; P30281; -.
DR TreeFam; TF101004; -.
DR PathwayCommons; P30281; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-9661069; Defective binding of RB1 mutants to E2F1,(E2F2, E2F3).
DR Reactome; R-HSA-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR SignaLink; P30281; -.
DR SIGNOR; P30281; -.
DR BioGRID-ORCS; 896; 90 hits in 1095 CRISPR screens.
DR ChiTaRS; CCND3; human.
DR EvolutionaryTrace; P30281; -.
DR GeneWiki; Cyclin_D3; -.
DR GenomeRNAi; 896; -.
DR Pharos; P30281; Tchem.
DR PRO; PR:P30281; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P30281; protein.
DR Bgee; ENSG00000112576; Expressed in granulocyte and 203 other tissues.
DR ExpressionAtlas; P30281; baseline and differential.
DR Genevisible; P30281; HS.
DR GO; GO:0097130; C:cyclin D3-CDK4 complex; IPI:ComplexPortal.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR CDD; cd00043; CYCLIN; 1.
DR DisProt; DP01447; -.
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:SF65; PTHR10177:SF65; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cyclin;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..292
FT /note="G1/S-specific cyclin-D3"
FT /id="PRO_0000080442"
FT DOMAIN 27..152
FT /note="Cyclin N-terminal"
FT REGION 254..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30282"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24385"
FT VAR_SEQ 1..196
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046266"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042649"
FT VAR_SEQ 67..138
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046267"
FT VARIANT 134
FT /note="P -> S (in dbSNP:rs3218089)"
FT /id="VAR_020412"
FT VARIANT 253
FT /note="E -> D (in dbSNP:rs33966734)"
FT /id="VAR_033726"
FT VARIANT 259
FT /note="S -> A (in dbSNP:rs1051130)"
FT /evidence="ECO:0000269|PubMed:1386336,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.6, ECO:0000269|Ref.8"
FT /id="VAR_014205"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3G33"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3G33"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:3G33"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:3G33"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:3G33"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:3G33"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:3G33"
SQ SEQUENCE 292 AA; 32520 MW; 16E7B1604FEB0029 CRC64;
MELLCCEGTR HAPRAGPDPR LLGDQRVLQS LLRLEERYVP RASYFQCVQR EIKPHMRKML
AYWMLEVCEE QRCEEEVFPL AMNYLDRYLS CVPTRKAQLQ LLGAVCMLLA SKLRETTPLT
IEKLCIYTDH AVSPRQLRDW EVLVLGKLKW DLAAVIAHDF LAFILHRLSL PRDRQALVKK
HAQTFLALCA TDYTFAMYPP SMIATGSIGA AVQGLGACSM SGDELTELLA GITGTEVDCL
RACQEQIEAA LRESLREASQ TSSSPAPKAP RGSSSQGPSQ TSTPTDVTAI HL
