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 27-MAR-2024, entry version 222. 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=38; IntAct=EBI-375013, EBI-295644; CC P30281; Q00535: CDK5; NbExp=10; IntAct=EBI-375013, EBI-1041567; CC P30281; Q00534: CDK6; NbExp=30; IntAct=EBI-375013, EBI-295663; CC P30281; P38936: CDKN1A; NbExp=26; IntAct=EBI-375013, EBI-375077; CC P30281; P46527: CDKN1B; NbExp=6; IntAct=EBI-375013, EBI-519280; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7SJ3; X-ray; 2.51 A; B=1-259. DR PDBsum; 3G33; -. DR PDBsum; 7SJ3; -. DR AlphaFoldDB; P30281; -. DR SMR; P30281; -. DR BioGRID; 107336; 96. 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; 54. 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 CPTAC; CPTAC-2808; -. DR CPTAC; CPTAC-2809; -. DR EPD; P30281; -. DR jPOST; P30281; -. DR MassIVE; P30281; -. DR MaxQB; P30281; -. DR PaxDb; 9606-ENSP00000362082; -. DR PeptideAtlas; P30281; -. DR ProteomicsDB; 19071; -. DR ProteomicsDB; 19134; -. DR ProteomicsDB; 54648; -. [P30281-1] DR ProteomicsDB; 54649; -. [P30281-2] DR Pumba; P30281; -. DR Antibodypedia; 3521; 938 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 AGR; HGNC:1585; -. 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; SYFHCVQ; -. DR OrthoDB; 1077601at2759; -. 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; 94 hits in 1180 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 205 other cell types or tissues. DR ExpressionAtlas; P30281; baseline and differential. 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:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IDA:UniProt. 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; IDA:UniProt. 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: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:0007165; P:signal transduction; IEA:Ensembl. DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl. DR CDD; cd20575; CYCLIN_CCND3_rpt1; 1. DR CDD; cd20578; CYCLIN_CCND3_rpt2; 1. DR DisProt; DP01447; -. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR InterPro; IPR039361; Cyclin. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR004367; Cyclin_C-dom. DR InterPro; IPR006671; Cyclin_N. DR InterPro; IPR048258; Cyclins_cyclin-box. DR PANTHER; PTHR10177; CYCLINS; 1. DR PANTHER; PTHR10177:SF65; G1_S-SPECIFIC CYCLIN-D3; 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; Cyclin-like; 2. DR PROSITE; PS00292; CYCLINS; 1. DR Genevisible; P30281; HS. 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 19..22 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 25..35 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:7SJ3" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:3G33" FT HELIX 54..70 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 77..89 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 99..114 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 121..127 FT /evidence="ECO:0007829|PDB:7SJ3" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:3G33" FT HELIX 134..147 FT /evidence="ECO:0007829|PDB:7SJ3" FT TURN 148..150 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 158..166 FT /evidence="ECO:0007829|PDB:7SJ3" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 175..191 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 200..215 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 222..233 FT /evidence="ECO:0007829|PDB:7SJ3" FT HELIX 237..252 FT /evidence="ECO:0007829|PDB:7SJ3" 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 //