ID   CCND3_HUMAN             Reviewed;         292 AA.
AC   P30281; Q5T8J0; Q96F49;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   25-NOV-2008, entry version 91.
DE   RecName: Full=G1/S-specific cyclin-D3;
GN   Name=CCND3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-259.
RX   MEDLINE=92347851; 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
RT   human D-type cyclins.";
RL   Genomics 13:575-584(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93015922; PubMed=1383201;
RA   Motokura T., Keyomarsi K., Kronenberg H.M., Arnold A.;
RT   "Cloning and characterization of human cyclin D3, a cDNA closely
RT   related in 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.
RA   Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W.,
RA   Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA   Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT   "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT   of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22935763; 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-237.
RC   TISSUE=Placenta;
RX   MEDLINE=92347850; PubMed=1386335; DOI=10.1016/0888-7543(92)90126-D;
RA   Inaba T., Matsushime H., Valentine M., Roussel M.F., Sherr C.J.,
RA   Look A.T.;
RT   "Genomic organization, chromosomal localization, and independent
RT   expression of human cyclin D genes.";
RL   Genomics 13:565-574(1992).
RN   [7]
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   [8]
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
RT   3(eIF3k) as a new interaction partner of cyclin D3.";
RL   FEBS Lett. 573:139-146(2004).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition. Potentiates the transcriptional activity of
CC       ATF5.
CC   -!- SUBUNIT: Interacts with the CDK4 and CDK6 protein kinases to form
CC       a serine/threonine kinase holoenzyme complex. The cyclin subunit
CC       imparts substrate specificity to the complex. Interacts with ATF5.
CC       Interacts with EIF3K.
CC   -!- INTERACTION:
CC       P11802:CDK4; NbExp=3; IntAct=EBI-375013, EBI-295644;
CC       Q00534:CDK6; NbExp=1; IntAct=EBI-375013, EBI-295663;
CC       P38936:CDKN1A; NbExp=1; IntAct=EBI-375013, EBI-375077;
CC       Q7L590:MCM10; NbExp=1; IntAct=EBI-375013, EBI-374912;
CC       O94921:PFTK1; NbExp=4; IntAct=EBI-375013, EBI-1043945;
CC       P62140:PPP1CB; NbExp=1; IntAct=EBI-375013, EBI-352350;
CC       P36873-1:PPP1CC; NbExp=1; IntAct=EBI-375013, EBI-356289;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
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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; AL160163; CAI23491.1; -; 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   PIR; B42822; B42822.
DR   RefSeq; NP_001751.1; -.
DR   UniGene; Hs.534307; -.
DR   HSSP; Q01043; 1JOW.
DR   IntAct; P30281; -.
DR   PhosphoSite; P30281; -.
DR   Ensembl; ENSG00000112576; Homo sapiens.
DR   GeneID; 896; -.
DR   KEGG; hsa:896; -.
DR   H-InvDB; HIX0005877; -.
DR   HGNC; HGNC:1585; CCND3.
DR   HPA; CAB000116; -.
DR   MIM; 123834; gene.
DR   PharmGKB; PA26152; -.
DR   HOGENOM; P30281; -.
DR   HOVERGEN; P30281; -.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   LinkHub; P30281; -.
DR   NextBio; 3702; -.
DR   ArrayExpress; P30281; -.
DR   CleanEx; HS_CCND3; -.
DR   GermOnline; ENSG00000112576; Homo sapiens.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme ...; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045737; P:positive regulation of cyclin-dependent pro...; IDA:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein amino acid p...; IDA:UniProtKB.
DR   InterPro; IPR015451; CycD.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR014400; Cyclin_A_B_D_E.
DR   InterPro; IPR004367; Cyclin_C.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR013763; Cyclin_related.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   PANTHER; PTHR10177:SF12; CycD; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Cytoplasm; Nucleus; Polymorphism.
FT   CHAIN         1    292       G1/S-specific cyclin-D3.
FT                                /FTId=PRO_0000080442.
FT   VARIANT     134    134       P -> S (in dbSNP:rs3218089).
FT                                /FTId=VAR_020412.
FT   VARIANT     253    253       E -> D (in dbSNP:rs33966734).
FT                                /FTId=VAR_033726.
FT   VARIANT     259    259       S -> A (in dbSNP:rs1051130).
FT                                /FTId=VAR_014205.
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
//