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P24385 (CCND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G1/S-specific cyclin-D1
Alternative name(s):
B-cell lymphoma 1 protein
Short name=BCL-1
BCL-1 oncogene
PRAD1 oncogene
Gene names
Name:CCND1
Synonyms:BCL1, PRAD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory component of the cyclin D1-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 D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. Ref.12 Ref.14 Ref.15 Ref.16

Subunit structure

Interacts with FBXO4 By similarity. Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Component of the ternary complex CCND1/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity. Interacts directly with CDKN1B. Interacts with UHRF2; the interaction ubiquitinates CCND1 and appears to occur independently of phosphorylation. Can form similar complexes with either CDKN1A or CDKN2A. Interacts with USP2. Interacts (via cyclin N-terminal domain) with INSM1 (via N-terminal region); the interaction competes with the binding of CCND1 to CDK4 during cell cycle progression and inhibits CDK4 activity. Interacts with CDK4; the interaction is prevented with the binding of CCND1 to INSM1 during cell cycle progression. Ref.10 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20

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

Phosphorylation at Thr-286 by MAP kinases is required for ubiquitination and degradation following DNA damage. It probably plays an essential role for recognition by the FBXO31 component of SCF (SKP1-cullin-F-box) protein ligase complex.

Ubiquitinated, primarily as 'Lys-48'-linked polyubiquitination. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex containing FBXO4 and CRYAB. Following DNA damage it is ubiquitinated by some SCF (SKP1-cullin-F-box) protein ligase complex containing FBXO31. SCF-type ubiquitination is dependent on Thr-286 phosphorylation By similarity. Ubiquitinated also by UHRF2 apparently in a phosphorylation-independent manner. Ubiquitination leads to its degradation and G1 arrest. Deubiquitinated by USP2; leading to its stabilization. Ref.13 Ref.18 Ref.19 Ref.20

Involvement in disease

A chromosomal aberration involving CCND1 may be a cause of B-lymphocytic malignancy, particularly mantle-cell lymphoma (MCL). Translocation t(11;14)(q13;q32) with immunoglobulin gene regions. Activation of CCND1 may be oncogenic by directly altering progression through the cell cycle.

A chromosomal aberration involving CCND1 may be a cause of parathyroid adenomas. Translocation t(11;11)(q13;p15) with the parathyroid hormone (PTH) enhancer.

Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia.
Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving CCND1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus.

Sequence similarities

Belongs to the cyclin family. Cyclin D subfamily.

Contains 1 cyclin N-terminal domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
Transcription
Transcription regulation
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityChromosomal rearrangement
   DiseaseProto-oncogene
   Molecular functionCyclin
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from direct assay Ref.19. Source: UniProtKB

Leydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

Notch signaling pathway

Traceable author statement. Source: Reactome

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from direct assay Ref.19. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Inferred from electronic annotation. Source: Ensembl

fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

mitotic G1 DNA damage checkpoint

Inferred from direct assay Ref.19. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle arrest

Inferred from direct assay Ref.17. Source: UniProtKB

negative regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.15Ref.16. Source: UniProtKB

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of G2/M transition of mitotic cell cycle

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of cyclin-dependent protein kinase activity

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

positive regulation of mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

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

re-entry into mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

response to UV-A

Inferred from direct assay PubMed 18483258. Source: BHF-UCL

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 18291362. Source: UniProtKB

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to iron ion

Inferred from electronic annotation. Source: Ensembl

response to magnesium ion

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcyclin-dependent protein kinase holoenzyme complex

Inferred from direct assay PubMed 17420273PubMed 8114739. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred from direct assay. Source: LIFEdb

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11793365. Source: UniProtKB

tight junction

Inferred from electronic annotation. Source: Ensembl

transcriptional repressor complex

Inferred from direct assay Ref.15Ref.16. Source: UniProtKB

   Molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.19. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

proline-rich region binding

Inferred from direct assay Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19Ref.20. Source: UniProtKB

protein kinase activity

Inferred from electronic annotation. Source: Ensembl

protein kinase binding

Inferred from physical interaction Ref.17. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.15Ref.16. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.15Ref.17. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295G1/S-specific cyclin-D1
PRO_0000080430

Regions

Domain28 – 152125Cyclin N-terminal
Compositional bias272 – 2809Poly-Glu

Amino acid modifications

Modified residue2861Phosphothreonine Ref.19
Cross-link269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis2861T → A: Reduces ubiquitination and subsequent degradation by the proteasome; when associated with A-288. Abolishes ubiquitination and subsequent degradation following DNA damage. Ref.13 Ref.19
Mutagenesis2881T → A: Reduces ubiquitination and subsequent degradation by the proteasome; when associated with A-286. Ref.13
Sequence conflict1301N → G in AAA52136. Ref.3
Sequence conflict168 – 1692MP → IA in M74092. Ref.2
Sequence conflict1881L → S in AAA52136. Ref.3

Secondary structure

...................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24385 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 3CC00C9905F58D3A

FASTA29533,729
        10         20         30         40         50         60 
MEHQLLCCEV ETIRRAYPDA NLLNDRVLRA MLKAEETCAP SVSYFKCVQK EVLPSMRKIV 

        70         80         90        100        110        120 
ATWMLEVCEE QKCEEEVFPL AMNYLDRFLS LEPVKKSRLQ LLGATCMFVA SKMKETIPLT 

       130        140        150        160        170        180 
AEKLCIYTDN SIRPEELLQM ELLLVNKLKW NLAAMTPHDF IEHFLSKMPE AEENKQIIRK 

       190        200        210        220        230        240 
HAQTFVALCA TDVKFISNPP SMVAAGSVVA AVQGLNLRSP NNFLSYYRLT RFLSRVIKCD 

       250        260        270        280        290 
PDCLRACQEQ IEALLESSLR QAQQNMDPKA AEEEEEEEEE VDLACTPTDV RDVDI 

« Hide

References

« Hide 'large scale' references
[1]"A novel cyclin encoded by a bcl1-linked candidate oncogene."
Motokura T., Bloom T., Kim H.G., Jueppner H., Ruderman J.V., Kronenberg H.M., Arnold A.
Nature 350:512-515(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast."
Lew D.J., Dulic V., Reed S.I.
Cell 66:1197-1206(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Human D-type cyclin."
Xiong Y., Connolly T., Futcher B., Beach D.
Cell 65:691-699(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Characterization of a candidate bcl-1 gene."
Withers D.A., Harvey R.C., Faust J.B., Melnyk O., Carey K., Meeker T.C.
Mol. Cell. Biol. 11:4846-4853(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Rearrangement of CCND1 (BCL1/PRAD1) 3' untranslated region in mantle-cell lymphomas and t(11q13)-associated leukemias."
Rimokh R., Berger F., Bastard C., Klein B., French M., Archimbaud E., Rouault J.-P., Santa Lucia B., Duret L., Vuillaume M.
Blood 83:3689-3696(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]NIEHS SNPs program
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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].
Tissue: Brain and Placenta.
[9]"The PRAD1/cyclin D1 proto-oncogene: genomic organization, 5' DNA sequence, and sequence of a tumor-specific rearrangement breakpoint."
Motokura T., Arnold A.
Genes Chromosomes Cancer 7:89-95(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
Tissue: Placenta.
[10]"CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1."
Bates S., Bonetta L., McAllan D., Parry D., Holder A., Dickson C., Peters G.
Oncogene 9:71-79(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK4 AND CDK6.
[11]"Dysregulation of cyclin D1 by translocation into an IgH gamma switch region in two multiple myeloma cell lines."
Chesi M., Bergsagel P.L., Brents L.A., Smith C.M., Gerhard D.S., Kuehl W.M.
Blood 88:674-681(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MULTIPLE MYELOMA.
[12]"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 IN THE CCND1-CDK4-CDKN COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
[13]"Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286."
Germain D., Russell A., Thompson A., Hendley J.
J. Biol. Chem. 275:12074-12079(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, MUTAGENESIS OF THR-286 AND THR-288.
[14]"Cyclin-dependent kinases regulate the antiproliferative function of Smads."
Matsuura I., Denissova N.G., Wang G., He D., Long J., Liu F.
Nature 430:226-231(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF CCND1-CDK4 COMPLEX IN SMAD PHOSPHORYLATION.
[15]"INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases."
Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.
Biochem. J. 397:169-177(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH INSM1.
[16]"Identification of an INSM1-binding site in the insulin promoter: negative regulation of the insulin gene transcription."
Wang H.W., Muguira M., Liu W.D., Zhang T., Chen C., Aucoin R., Breslin M.B., Lan M.S.
J. Endocrinol. 198:29-39(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH INSM1.
[17]"Zinc finger transcription factor INSM1 interrupts cyclin D1 and CDK4 binding and induces cell cycle arrest."
Zhang T., Liu W.D., Saunee N.A., Breslin M.B., Lan M.S.
J. Biol. Chem. 284:5574-5581(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSM1 AND CDK4.
[18]"Suppression of cancer cell growth by promoting cyclin D1 degradation."
Shan J., Zhao W., Gu W.
Mol. Cell 36:469-476(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP2, UBIQUITINATION, DEUBIQUITINATION BY USP2.
[19]"F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage."
Santra M.K., Wajapeyee N., Green M.R.
Nature 459:722-725(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-286, UBIQUITINATION, MUTAGENESIS OF THR-286.
[20]"NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH UHRF2.
[21]"Crystal structure of human CDK4 in complex with a D-type cyclin."
Day P.J., Cleasby A., Tickle I.J., O'Reilly M., Coyle J.E., Holding F.P., McMenamin R.L., Yon J., Chopra R., Lengauer C., Jhoti H.
Proc. Natl. Acad. Sci. U.S.A. 106:4166-4170(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-271 IN COMPLEX WITH WILD TYPE AND MUTANTS ALA-172; PHE-172 AND ASP-172 CDK4.
+Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59798 mRNA. Translation: CAA42470.1.
M74092 mRNA. No translation available.
M64349 mRNA. Translation: AAA52136.1.
M73554 mRNA. Translation: AAA58392.1.
Z23022 mRNA. Translation: CAA80558.1.
BT019845 mRNA. Translation: AAV38648.1.
AF511593 Genomic DNA. Translation: AAM34300.2.
BC000076 mRNA. Translation: AAH00076.1.
BC001501 mRNA. Translation: AAH01501.1.
BC014078 mRNA. Translation: AAH14078.1.
BC023620 mRNA. Translation: AAH23620.1.
BC025302 mRNA. Translation: AAH25302.1.
L09054 Genomic DNA. Translation: AAA36481.1.
CCDSCCDS8191.1.
PIRA38977.
RefSeqNP_444284.1. NM_053056.2.
UniGeneHs.523852.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W96X-ray2.30A1-271[»]
2W99X-ray2.80A1-271[»]
2W9FX-ray2.85A1-271[»]
2W9ZX-ray2.45A16-271[»]
ProteinModelPortalP24385.
SMRP24385. Positions 22-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107067. 78 interactions.
DIPDIP-123N.
IntActP24385. 27 interactions.
MINTMINT-135422.
STRING9606.ENSP00000227507.

Chemistry

BindingDBP24385.
ChEMBLCHEMBL3610.
DrugBankDB01169. Arsenic trioxide.

PTM databases

PhosphoSiteP24385.

Polymorphism databases

DMDM116152.

Proteomic databases

MaxQBP24385.
PaxDbP24385.
PRIDEP24385.

Protocols and materials databases

DNASU595.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227507; ENSP00000227507; ENSG00000110092.
GeneID595.
KEGGhsa:595.
UCSCuc001opa.3. human.

Organism-specific databases

CTD595.
GeneCardsGC11P069455.
HGNCHGNC:1582. CCND1.
HPACAB000024.
HPA027801.
MIM168461. gene.
254500. phenotype.
neXtProtNX_P24385.
Orphanet67038. B-cell chronic lymphocytic leukemia.
52416. Mantle cell lymphoma.
29073. Multiple myeloma.
PharmGKBPA75.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5024.
HOGENOMHOG000008182.
HOVERGENHBG050837.
InParanoidP24385.
KOK04503.
OMAMKETVPL.
OrthoDBEOG7J447H.
PhylomeDBP24385.
TreeFamTF101004.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
SignaLinkP24385.

Gene expression databases

ArrayExpressP24385.
BgeeP24385.
CleanExHS_CCND1.
GenevestigatorP24385.

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:SF67. PTHR10177:SF67. 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

ChiTaRSCCND1. human.
EvolutionaryTraceP24385.
GeneWikiCyclin_D1.
GenomeRNAi595.
NextBio2419.
PROP24385.
SOURCESearch...

Entry information

Entry nameCCND1_HUMAN
AccessionPrimary (citable) accession number: P24385
Secondary accession number(s): Q6LEF0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: July 9, 2014
This is version 161 of the entry and version 1 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 chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM