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P30281 (CCND3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G1/S-specific cyclin-D3
Gene names
Name:CCND3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G1/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 G1 phase. Hypophosphorylates RB1 in early G1 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 D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Ref.12

Subunit structure

Interacts with the CDK4 and CDK6 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Interacts with ATF5. Interacts with EIF3K. Component of the ternary complex cyclin D/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity. Can form similar complexes with either CDKN1A or CDKN2A. Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Nucleus. Cytoplasm. Membrane. Note: Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members By similarity. Ref.12

Post-translational modification

Polyubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation.

Sequence similarities

Belongs to the cyclin family. Cyclin D subfamily.

Contains 1 cyclin N-terminal domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionCyclin
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cyclin-dependent protein kinase activity

Inferred from direct assay PubMed 8114739. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 8114739. Source: BHF-UCL

signal transduction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcyclin-dependent protein kinase holoenzyme complex

Inferred from direct assay PubMed 8114739. Source: BHF-UCL

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 11896535PubMed 15232106PubMed 16189514PubMed 17517622PubMed 21516116PubMed 21988832PubMed 23602568Ref.11PubMed 9311810. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 8114739. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30281-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P30281-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P30281-3)

The sequence of this isoform differs from the canonical sequence as follows:
     67-138: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P30281-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292G1/S-specific cyclin-D3
PRO_0000080442

Regions

Domain27 – 152126Cyclin N-terminal

Amino acid modifications

Modified residue2791Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 196196Missing in isoform 4.
VSP_046266
Alternative sequence1 – 8181Missing in isoform 2.
VSP_042649
Alternative sequence67 – 13872Missing in isoform 3.
VSP_046267
Natural variant1341P → S.
Corresponds to variant rs3218089 [ dbSNP | Ensembl ].
VAR_020412
Natural variant2531E → D.
Corresponds to variant rs33966734 [ dbSNP | Ensembl ].
VAR_033726
Natural variant2591S → A. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs1051130 [ dbSNP | Ensembl ].
VAR_014205

Secondary structure

................................... 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 16E7B1604FEB0029

FASTA29232,520
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F88EA393BA1B96DB
Show »

FASTA21122,887
Isoform 3 [UniParc].

Checksum: 15BC01266FE6BF4B
Show »

FASTA22024,238
Isoform 4 [UniParc].

Checksum: 83F7CF9D0B743ED7
Show »

FASTA969,736

References

« Hide 'large scale' references
[1]"Molecular cloning and chromosomal mapping of CCND genes encoding human D-type cyclins."
Xiong Y., Menninger J., Beach D., Ward D.C.
Genomics 13:575-584(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-259.
[2]"Cloning and characterization of human cyclin D3, a cDNA closely related in sequence to the PRAD1/cyclin D1 proto-oncogene."
Motokura T., Keyomarsi K., Kronenberg H.M., Arnold A.
J. Biol. Chem. 267:20412-20415(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]NIEHS SNPs program
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-259.
[4]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ALA-259.
Tissue: Cervix carcinoma.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), VARIANT ALA-259.
Tissue: Synovium, Thymus and Umbilical cord blood.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-259.
[7]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-259.
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[10]"Genomic organization, chromosomal localization, and independent expression of human cyclin D genes."
Inaba T., Matsushime H., Valentine M., Roussel M.F., Sherr C.J., Look A.T.
Genomics 13:565-574(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-237.
Tissue: Placenta.
[11]"New functional activities for the p21 family of CDK inhibitors."
LaBaer J., Garrett M.D., Stevenson L.F., Slingerland J.M., Sandhu C., Chou H.S., Fattaey A., Harlow E.
Genes Dev. 11:847-862(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK4 AND CDKN1A.
[12]"Cyclin D3 interacts with human activating transcription factor 5 and potentiates its transcription activity."
Liu W., Sun M., Jiang J., Shen X., Sun Q., Liu W., Shen H., Gu J.
Biochem. Biophys. Res. Commun. 321:954-960(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF5, FUNCTION, SUBCELLULAR LOCATION.
[13]"Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k) as a new interaction partner of cyclin D3."
Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J.
FEBS Lett. 573:139-146(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3K.
[14]"Regulated activating Thr172 phosphorylation of cyclin-dependent kinase 4(CDK4): its relationship with cyclins and CDK 'inhibitors'."
Bockstaele L., Kooken H., Libert F., Paternot S., Dumont J.E., de Launoit Y., Roger P.P., Coulonval K.
Mol. Cell. Biol. 26:5070-5085(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK4; CDKN2A AND CDKN1B.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"F-box protein FBXL2 exerts human lung tumor suppressor-like activity by ubiquitin-mediated degradation of cyclin D3 resulting in cell cycle arrest."
Chen B.B., Glasser J.R., Coon T.A., Mallampalli R.K.
Oncogene 31:2566-2579(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY SCF(FBXL2).
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"The structure of CDK4/cyclin D3 has implications for models of CDK activation."
Takaki T., Echalier A., Brown N.R., Hunt T., Endicott J.A., Noble M.E.
Proc. Natl. Acad. Sci. U.S.A. 106:4171-4176(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CDK4.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90814 mRNA. Translation: AAA51927.1.
M92287 mRNA. Translation: AAA52137.1.
AF517525 Genomic DNA. Translation: AAM51826.1.
BX400719 mRNA. No translation available.
AK057206 mRNA. Translation: BAG51884.1.
AK097856 mRNA. No translation available.
AK315421 mRNA. Translation: BAG37810.1.
CR542246 mRNA. Translation: CAG47042.1.
AL160163 Genomic DNA. Translation: CAI23491.1.
AL513008 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX04071.1.
BC011616 mRNA. Translation: AAH11616.1.
M88087 expand/collapse EMBL AC list , M88084, M88085, M88086 Genomic DNA. Translation: AAA51929.1.
CCDSCCDS47425.1. [P30281-3]
CCDS47426.1. [P30281-2]
CCDS47427.1. [P30281-4]
CCDS4863.1. [P30281-1]
PIRB42822.
RefSeqNP_001129489.1. NM_001136017.3. [P30281-2]
NP_001129597.1. NM_001136125.2. [P30281-3]
NP_001129598.1. NM_001136126.2. [P30281-4]
NP_001274356.1. NM_001287427.1.
NP_001274363.1. NM_001287434.1. [P30281-4]
NP_001751.1. NM_001760.4. [P30281-1]
UniGeneHs.534307.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3G33X-ray3.00B/D1-292[»]
ProteinModelPortalP30281.
SMRP30281. Positions 23-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107336. 40 interactions.
DIPDIP-31734N.
IntActP30281. 25 interactions.
MINTMINT-1201666.
STRING9606.ENSP00000362082.

Chemistry

BindingDBP30281.
ChEMBLCHEMBL2422.

PTM databases

PhosphoSiteP30281.

Polymorphism databases

DMDM20981685.

Proteomic databases

MaxQBP30281.
PaxDbP30281.
PRIDEP30281.

Protocols and materials databases

DNASU896.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372988; ENSP00000362079; ENSG00000112576. [P30281-2]
ENST00000372991; ENSP00000362082; ENSG00000112576. [P30281-1]
ENST00000414200; ENSP00000397545; ENSG00000112576. [P30281-3]
ENST00000415497; ENSP00000401595; ENSG00000112576. [P30281-4]
ENST00000511642; ENSP00000426212; ENSG00000112576. [P30281-2]
GeneID896.
KEGGhsa:896.
UCSCuc003orn.3. human. [P30281-1]

Organism-specific databases

CTD896.
GeneCardsGC06M041949.
HGNCHGNC:1585. CCND3.
HPACAB000116.
MIM123834. gene.
neXtProtNX_P30281.
PharmGKBPA26152.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5024.
HOGENOMHOG000008182.
HOVERGENHBG050837.
InParanoidP30281.
KOK10152.
OMAISGETEC.
OrthoDBEOG7J447H.
PhylomeDBP30281.
TreeFamTF101004.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
SignaLinkP30281.

Gene expression databases

ArrayExpressP30281.
BgeeP30281.
CleanExHS_CCND3.
GenevestigatorP30281.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR015451. Cyclin_D.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10177:SF65. PTHR10177:SF65. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCCND3. human.
EvolutionaryTraceP30281.
GeneWikiCyclin_D3.
GenomeRNAi896.
NextBio3702.
PROP30281.
SOURCESearch...

Entry information

Entry nameCCND3_HUMAN
AccessionPrimary (citable) accession number: P30281
Secondary accession number(s): B2RD63 expand/collapse secondary AC list , B3KQ22, E9PAS4, E9PB36, Q5T8J0, Q6FG62, Q96F49
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 15, 2002
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM