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UniProtKB/Swiss-Prot entry P30281


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCND3_HUMAN
Primary accession number P30281
Secondary accession numbers Q5T8J0 Q96F49
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on May 15, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 89)
Name and origin of the protein
Protein name G1/S-specific cyclin-D3
Synonyms None
Gene name
Name: CCND3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-259.
DOI=10.1016/0888-7543(92)90127-E; PubMed=1386336 [NCBI, ExPASy, EBI, Israel, Japan]
Xiong Y., Menninger J., Beach D., Ward D.C.;
"Molecular cloning and chromosomal mapping of CCND genes encoding human D-type cyclins.";
Genomics 13:575-584(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1383201 [NCBI, ExPASy, EBI, Israel, Japan]
Motokura T., Keyomarsi K., Kronenberg H.M., Arnold A.;
"Cloning and characterization of human cyclin D3, a cDNA closely related in sequence to the PRAD1/cyclin D1 proto-oncogene.";
J. Biol. Chem. 267:20412-20415(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-259.
Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-237.
TISSUE=Placenta;
DOI=10.1016/0888-7543(92)90126-D; PubMed=1386335 [NCBI, ExPASy, EBI, Israel, Japan]
Inaba T., Matsushime H., Valentine M., Roussel M.F., Sherr C.J., Look A.T.;
"Genomic organization, chromosomal localization, and independent expression of human cyclin D genes.";
Genomics 13:565-574(1992).
[7]
INTERACTION WITH ATF5, FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.bbrc.2004.07.053; PubMed=15358120 [NCBI, ExPASy, EBI, Israel, Japan]
Liu W., Sun M., Jiang J., Shen X., Sun Q., Liu W., Shen H., Gu J.;
"Cyclin D3 interacts with human activating transcription factor 5 and potentiates its transcription activity.";
Biochem. Biophys. Res. Commun. 321:954-960(2004).
[8]
INTERACTION WITH EIF3K.
DOI=10.1016/j.febslet.2004.07.071; PubMed=15327989 [NCBI, ExPASy, EBI, Israel, Japan]
Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J.;
"Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k) as a new interaction partner of cyclin D3.";
FEBS Lett. 573:139-146(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M90814; AAA51927.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M92287; AAA52137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF517525; AAM51826.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL160163; CAI23491.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011616; AAH11616.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88087; AAA51929.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88084; AAA51929.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88085; AAA51929.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88086; AAA51929.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B42822; B42822.
RefSeq NP_001751.1; -.
UniGene Hs.534307
3D structure databases
HSSP Q01043; 1JOW. [HSSP ENTRY / PDB]
ModBase P30281.
Protein-protein interaction databases
IntAct P30281; -.
PTM databases
PhosphoSite P30281; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
Polymorphism databases
NIEHS-SNPs CCND3.
Organism-specific databases
H-InvDB HIX0005877; -.
HGNC HGNC:1585; CCND3.
GenAtlas CCND3.
HPA CAB000116; -.
MIM 123834; gene. [NCBI / EBI]
PharmGKB PA26152; -.
GeneCards P30281.
Gene expression databases
ArrayExpress P30281; -.
CleanEx HS_CCND3; -.
GermOnline ENSG00000112576; Homo sapiens.
Ontologies
GO
GO:0000307; Cellular component: cyclin-dependent protein kinase holoenzyme complex (inferred from direct assay from UniProtKB).
GO:0019901; Molecular function: protein kinase binding (inferred from physical interaction from UniProtKB).
GO:0045737; Biological process: positive regulation of cyclin-dependent protein kinase activity (inferred from direct assay from UniProtKB).
GO:0001934; Biological process: positive regulation of protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR015451; CycD.
IPR006670; Cyclin.
IPR014400; Cyclin_A_B_D_E.
IPR004367; Cyclin_C.
IPR006671; Cyclin_N.
IPR013763; Cyclin_related.
Graphical view of domain structure.
Gene3D G3DSA:1.10.472.10; Cyclin_related; 1.
PANTHER PTHR10177:SF12; CycD; 1.
Pfam PF02984; Cyclin_C; 1.
PF00134; Cyclin_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001771; Cyclin_A_B_D_E; 1.
SMART SM00385; CYCLIN; 1.
SMART graphical view of domain structure.
PROSITE PS00292; CYCLINS; 1.
BLOCKS P30281.
Genome annotation databases
Ensembl ENSG00000112576; Homo sapiens. [Contig view]
GeneID 896; -.
KEGG hsa:896; -.
Phylogenomic databases
HOGENOM P30281; -.
HOVERGEN P30281; -.
Other
LinkHub P30281; -.
SOURCE CCND3; Homo sapiens.
ProtoNet P30281.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell cycle; Cell division; Cyclin; Cytoplasm; Nucleus; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   292  292     G1/S-specific cyclin-D3. PRO_0000080442
VARIANT   134   134  1     P -> S (in dbSNP:rs3218089 [NCBI]). VAR_020412 
VARIANT   253   253  1     E -> D (in dbSNP:rs33966734 [NCBI]). VAR_033726 
VARIANT   259   259  1     S -> A (in dbSNP:rs1051130 [NCBI]). VAR_014205 
Sequence information
Length: 292 AA [This is the length of the unprocessed precursor] Molecular weight: 32520 Da [This is the MW of the unprocessed precursor] CRC64: 16E7B1604FEB0029 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELLCCEGTR HAPRAGPDPR LLGDQRVLQS LLRLEERYVP RASYFQCVQR EIKPHMRKML 

        70         80         90        100        110        120 
AYWMLEVCEE QRCEEEVFPL AMNYLDRYLS CVPTRKAQLQ LLGAVCMLLA SKLRETTPLT 

       130        140        150        160        170        180 
IEKLCIYTDH AVSPRQLRDW EVLVLGKLKW DLAAVIAHDF LAFILHRLSL PRDRQALVKK 

       190        200        210        220        230        240 
HAQTFLALCA TDYTFAMYPP SMIATGSIGA AVQGLGACSM SGDELTELLA GITGTEVDCL 

       250        260        270        280        290 
RACQEQIEAA LRESLREASQ TSSSPAPKAP RGSSSQGPSQ TSTPTDVTAI HL 

P30281 in FASTA format

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View entry in raw text format (no links)
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