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Q00534

- CDK6_HUMAN

UniProt

Q00534 - CDK6_HUMAN

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Protein

Cyclin-dependent kinase 6

Gene

CDK6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e.g. erythroid and hematopoietic cells). Essential for cell proliferation within the dentate gyrus of the hippocampus and the subventricular zone of the lateral ventricles. Required during thymocyte development. Promotes the production of newborn neurons, probably by modulating G1 length. Promotes, at least in astrocytes, changes in patterns of gene expression, changes in the actin cytoskeleton including loss of stress fibers, and enhanced motility during cell differentiation. Prevents myeloid differentiation by interfering with RUNX1 and reducing its transcription transactivation activity, but promotes proliferation of normal myeloid progenitors. Delays senescence. Promotes the proliferation of beta-cells in pancreatic islets of Langerhans.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by INK4 proteins (CDKN2C/p18-INK4c), aminopurvalanol, PD0332991, 4-(Pyrazol-4-yl)-pyrimidines and fisetin, a flavonol inhibitor. Activated by Thr-177 phosphorylation and Tyr-24 dephosphorylation (By similarity). Stimulated by cyclin from herpesvirus saimiri (V-cyclin/ECLF2). Rapidly down-regulated prior to cell differentiation (e.g. erythroid and osteoblast).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPPROSITE-ProRule annotation
Active sitei145 – 1451Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: BHF-UCL
  2. cyclin binding Source: BHF-UCL
  3. cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL

GO - Biological processi

  1. astrocyte development Source: UniProtKB
  2. cell cycle arrest Source: UniProtKB
  3. cell dedifferentiation Source: BHF-UCL
  4. cell division Source: UniProtKB-KW
  5. dentate gyrus development Source: UniProtKB
  6. G1/S transition of mitotic cell cycle Source: UniProtKB
  7. generation of neurons Source: UniProtKB
  8. gliogenesis Source: BHF-UCL
  9. hematopoietic stem cell differentiation Source: Ensembl
  10. lateral ventricle development Source: UniProtKB
  11. mitotic cell cycle Source: Reactome
  12. negative regulation of cell cycle Source: UniProtKB
  13. negative regulation of cell differentiation Source: UniProtKB
  14. negative regulation of cell proliferation Source: UniProtKB
  15. negative regulation of cellular senescence Source: UniProtKB
  16. negative regulation of epithelial cell proliferation Source: BHF-UCL
  17. negative regulation of myeloid cell differentiation Source: UniProtKB
  18. negative regulation of osteoblast differentiation Source: BHF-UCL
  19. Notch signaling pathway Source: Ensembl
  20. positive regulation of cell-matrix adhesion Source: BHF-UCL
  21. positive regulation of fibroblast proliferation Source: BHF-UCL
  22. positive regulation of gene expression Source: Ensembl
  23. protein phosphorylation Source: BHF-UCL
  24. regulation of cell motility Source: UniProtKB
  25. regulation of erythrocyte differentiation Source: BHF-UCL
  26. regulation of gene expression Source: BHF-UCL
  27. response to virus Source: UniProtKB
  28. T cell differentiation in thymus Source: Ensembl
  29. type B pancreatic cell development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_821. Cyclin D associated events in G1.
SignaLinkiQ00534.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 6 (EC:2.7.11.22)
Alternative name(s):
Cell division protein kinase 6
Serine/threonine-protein kinase PLSTIRE
Gene namesi
Name:CDK6
Synonyms:CDKN6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:1777. CDK6.

Subcellular locationi

Cytoplasm. Nucleus. Cell projectionruffle
Note: Localized to the ruffling edge of spreading fibroblasts. Kinase activity only in nucleus.

GO - Cellular componenti

  1. cyclin-dependent protein kinase holoenzyme complex Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. cytosol Source: Reactome
  4. nucleus Source: BHF-UCL
  5. ruffle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

MIMi612223. phenotype.
Orphaneti2512. Autosomal recessive primary microcephaly.
PharmGKBiPA103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Cyclin-dependent kinase 6PRO_0000085789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei13 – 131Phosphotyrosine1 Publication
Modified residuei24 – 241Phosphotyrosine2 Publications
Modified residuei49 – 491Phosphothreonine1 Publication
Modified residuei70 – 701Phosphothreonine1 Publication
Modified residuei177 – 1771Phosphothreonine1 Publication
Modified residuei264 – 2641N6-acetyllysine1 Publication
Modified residuei325 – 3251Phosphothreonine1 Publication

Post-translational modificationi

Thr-177 phosphorylation and Tyr-24 dephosphorylation promotes kinase activity.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ00534.
PaxDbiQ00534.
PeptideAtlasiQ00534.
PRIDEiQ00534.

PTM databases

PhosphoSiteiQ00534.

Expressioni

Tissue specificityi

Expressed ubiquitously. Accumulates in squamous cell carcinomas, proliferating hematopoietic progenitor cells, beta-cells of pancreatic islets of Langerhans, and neuroblastomas. Reduced levels in differentiating cells.2 Publications

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection. Induced by NANOG during S-phase entry.2 Publications

Gene expression databases

BgeeiQ00534.
CleanExiHS_CDK6.
ExpressionAtlasiQ00534. baseline and differential.
GenevestigatoriQ00534.

Organism-specific databases

HPAiCAB004363.
HPA002637.

Interactioni

Subunit structurei

Interaction with D-type G1 cyclins. Cyclin binding promotes enzyme activation by phosphorylation at Thr-177 (By similarity). Binds to RUNX1, CDKN2D, FBXO7 and CDKN2C/p18-INK4c. Forms a cytoplasmic complex with Hsp90/HSP90AB1 and CDC37. FBXO7-binding promotes D-type cyclin binding. Interacts with Kaposi's sarcoma herpesvirus (KSHV) V-cyclin and herpesvirus saimiri (V-cyclin/ECLF2); the CDK6/V-cyclin complex phosphorylates NPM1 and thus lead to viral reactivation by reducing viral LANA levels.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCND1P243852EBI-295663,EBI-375001
CCND3P302814EBI-295663,EBI-375013
CDC37Q165433EBI-295663,EBI-295634
CDKN2AP4277110EBI-295663,EBI-375053
CDKN2BP427723EBI-295663,EBI-711280
CDKN2CP427733EBI-295663,EBI-711290
CDKN2DP552732EBI-295663,EBI-745859
FOXM1Q08050-12EBI-295663,EBI-866499
HSP90AB1P082382EBI-295663,EBI-352572
RUNX1Q011965EBI-295663,EBI-925904

Protein-protein interaction databases

BioGridi107456. 111 interactions.
DIPiDIP-687N.
IntActiQ00534. 95 interactions.
MINTiMINT-232049.
STRINGi9606.ENSP00000265734.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Beta strandi13 – 2210
Beta strandi25 – 328
Turni33 – 375
Beta strandi39 – 4911
Helixi58 – 7013
Beta strandi79 – 879
Beta strandi89 – 9911
Beta strandi102 – 1043
Helixi105 – 1117
Turni113 – 1153
Helixi119 – 13820
Helixi148 – 1503
Beta strandi151 – 1533
Beta strandi159 – 1613
Helixi172 – 1765
Beta strandi180 – 1823
Helixi183 – 1853
Helixi188 – 1914
Helixi199 – 21416
Helixi224 – 23512
Helixi240 – 2423
Beta strandi245 – 2495
Helixi251 – 2533
Helixi262 – 2643
Beta strandi266 – 2683
Helixi271 – 28010
Turni285 – 2873
Helixi291 – 2955
Helixi298 – 3003

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BI7X-ray3.40A1-326[»]
1BI8X-ray2.80A/C1-326[»]
1BLXX-ray1.90A1-326[»]
1G3NX-ray2.90A/E1-326[»]
1JOWX-ray3.10B1-308[»]
1XO2X-ray2.90B1-308[»]
2EUFX-ray3.00B1-308[»]
2F2CX-ray2.80B1-308[»]
3NUPX-ray2.60A1-301[»]
3NUXX-ray2.70A1-301[»]
4AUAX-ray2.31A1-301[»]
4EZ5X-ray2.70A1-301[»]
4TTHX-ray2.90B1-326[»]
ProteinModelPortaliQ00534.
SMRiQ00534. Positions 5-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00534.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 300288Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119154.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ00534.
KOiK02091.
OMAiFHSKSPQ.
OrthoDBiEOG73JKVV.
PhylomeDBiQ00534.
TreeFamiTF101022.

Family and domain databases

InterProiIPR028788. CDK6.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24056:SF130. PTHR24056:SF130. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00534-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKDGLCRAD QQYECVAEIG EGAYGKVFKA RDLKNGGRFV ALKRVRVQTG
60 70 80 90 100
EEGMPLSTIR EVAVLRHLET FEHPNVVRLF DVCTVSRTDR ETKLTLVFEH
110 120 130 140 150
VDQDLTTYLD KVPEPGVPTE TIKDMMFQLL RGLDFLHSHR VVHRDLKPQN
160 170 180 190 200
ILVTSSGQIK LADFGLARIY SFQMALTSVV VTLWYRAPEV LLQSSYATPV
210 220 230 240 250
DLWSVGCIFA EMFRRKPLFR GSSDVDQLGK ILDVIGLPGE EDWPRDVALP
260 270 280 290 300
RQAFHSKSAQ PIEKFVTDID ELGKDLLLKC LTFNPAKRIS AYSALSHPYF
310 320
QDLERCKENL DSHLPPSQNT SELNTA
Length:326
Mass (Da):36,938
Last modified:April 1, 1993 - v1
Checksum:i571733EE6BE7FD4A
GO

Polymorphismi

Genetic variations in CDK6 may influence stature as a quantitative trait, contributing to the stature quantitative trait locus 11 (STQTL11) [MIMi:612223]. Adult height is an easily observable and highly heritable complex continuous trait. Because of this, it is a model trait for studying genetic influence on quantitative traits.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101D → N.1 Publication
Corresponds to variant rs35654944 [ dbSNP | Ensembl ].
VAR_041978
Natural varianti199 – 1991P → L in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041979

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66365 mRNA. Translation: CAA47008.1.
AY128534 Genomic DNA. Translation: AAM76970.1.
AK313491 mRNA. Translation: BAG36273.1.
AC000065 Genomic DNA. No translation available.
AC004128 Genomic DNA. No translation available.
AC004011 Genomic DNA. No translation available.
CH236949 Genomic DNA. Translation: EAL24146.1.
CH471091 Genomic DNA. Translation: EAW76827.1.
BC052264 mRNA. Translation: AAH52264.1.
CCDSiCCDS5628.1.
PIRiS23387.
RefSeqiNP_001138778.1. NM_001145306.1.
NP_001250.1. NM_001259.6.
XP_006715898.1. XM_006715835.1.
UniGeneiHs.119882.

Genome annotation databases

EnsembliENST00000265734; ENSP00000265734; ENSG00000105810.
ENST00000424848; ENSP00000397087; ENSG00000105810.
GeneIDi1021.
KEGGihsa:1021.
UCSCiuc010lez.3. human.

Polymorphism databases

DMDMi266423.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66365 mRNA. Translation: CAA47008.1 .
AY128534 Genomic DNA. Translation: AAM76970.1 .
AK313491 mRNA. Translation: BAG36273.1 .
AC000065 Genomic DNA. No translation available.
AC004128 Genomic DNA. No translation available.
AC004011 Genomic DNA. No translation available.
CH236949 Genomic DNA. Translation: EAL24146.1 .
CH471091 Genomic DNA. Translation: EAW76827.1 .
BC052264 mRNA. Translation: AAH52264.1 .
CCDSi CCDS5628.1.
PIRi S23387.
RefSeqi NP_001138778.1. NM_001145306.1.
NP_001250.1. NM_001259.6.
XP_006715898.1. XM_006715835.1.
UniGenei Hs.119882.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BI7 X-ray 3.40 A 1-326 [» ]
1BI8 X-ray 2.80 A/C 1-326 [» ]
1BLX X-ray 1.90 A 1-326 [» ]
1G3N X-ray 2.90 A/E 1-326 [» ]
1JOW X-ray 3.10 B 1-308 [» ]
1XO2 X-ray 2.90 B 1-308 [» ]
2EUF X-ray 3.00 B 1-308 [» ]
2F2C X-ray 2.80 B 1-308 [» ]
3NUP X-ray 2.60 A 1-301 [» ]
3NUX X-ray 2.70 A 1-301 [» ]
4AUA X-ray 2.31 A 1-301 [» ]
4EZ5 X-ray 2.70 A 1-301 [» ]
4TTH X-ray 2.90 B 1-326 [» ]
ProteinModelPortali Q00534.
SMRi Q00534. Positions 5-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107456. 111 interactions.
DIPi DIP-687N.
IntActi Q00534. 95 interactions.
MINTi MINT-232049.
STRINGi 9606.ENSP00000265734.

Chemistry

BindingDBi Q00534.
ChEMBLi CHEMBL2508.
GuidetoPHARMACOLOGYi 1978.

PTM databases

PhosphoSitei Q00534.

Polymorphism databases

DMDMi 266423.

Proteomic databases

MaxQBi Q00534.
PaxDbi Q00534.
PeptideAtlasi Q00534.
PRIDEi Q00534.

Protocols and materials databases

DNASUi 1021.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265734 ; ENSP00000265734 ; ENSG00000105810 .
ENST00000424848 ; ENSP00000397087 ; ENSG00000105810 .
GeneIDi 1021.
KEGGi hsa:1021.
UCSCi uc010lez.3. human.

Organism-specific databases

CTDi 1021.
GeneCardsi GC07M092234.
GeneReviewsi CDK6.
HGNCi HGNC:1777. CDK6.
HPAi CAB004363.
HPA002637.
MIMi 603368. gene.
612223. phenotype.
neXtProti NX_Q00534.
Orphaneti 2512. Autosomal recessive primary microcephaly.
PharmGKBi PA103.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119154.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi Q00534.
KOi K02091.
OMAi FHSKSPQ.
OrthoDBi EOG73JKVV.
PhylomeDBi Q00534.
TreeFami TF101022.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 2681.
Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_821. Cyclin D associated events in G1.
SignaLinki Q00534.

Miscellaneous databases

ChiTaRSi CDK6. human.
EvolutionaryTracei Q00534.
GeneWikii Cyclin-dependent_kinase_6.
GenomeRNAii 1021.
NextBioi 4291.
PROi Q00534.
SOURCEi Search...

Gene expression databases

Bgeei Q00534.
CleanExi HS_CDK6.
ExpressionAtlasi Q00534. baseline and differential.
Genevestigatori Q00534.

Family and domain databases

InterProi IPR028788. CDK6.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24056:SF130. PTHR24056:SF130. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A family of human cdc2-related protein kinases."
    Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., Harlow E., Tsai L.-H.
    EMBO J. 11:2909-2917(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
    , 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].
    Tissue: Tongue.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. "Identification of G1 kinase activity for cdk6, a novel cyclin D partner."
    Meyerson M., Harlow E.
    Mol. Cell. Biol. 14:2077-2086(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PRB/RB1 KINASE, TISSUE SPECIFICITY, INTERACTION WITH D-TYPE CYCLINS.
  9. "Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells."
    Mahony D., Parry D.A., Lees E.
    Oncogene 16:603-611(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH D-TYPE CYCLINS; CDKN2D; HSP90AB1 AND CDC37.
  10. "CDK6 blocks differentiation: coupling cell proliferation to the block to differentiation in leukemic cells."
    Matushansky I., Radparvar F., Skoultchi A.I.
    Oncogene 22:4143-4149(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DIFFERENTIATION, ENZYME REGULATION.
  11. "Cyclin-dependent kinase 6 inhibits proliferation of human mammary epithelial cells."
    Lucas J.J., Domenico J., Gelfand E.W.
    Mol. Cancer Res. 2:105-114(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION.
  12. "Bone morphogenetic protein 2-induced osteoblast differentiation requires Smad-mediated down-regulation of Cdk6."
    Ogasawara T., Kawaguchi H., Jinno S., Hoshi K., Itaka K., Takato T., Nakamura K., Okayama H.
    Mol. Cell. Biol. 24:6560-6568(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DIFFERENTIATION.
  13. "Transforming activity of Fbxo7 is mediated specifically through regulation of cyclin D/cdk6."
    Laman H., Funes J.M., Ye H., Henderson S., Galinanes-Garcia L., Hara E., Knowles P., McDonald N., Boshoff C.
    EMBO J. 24:3104-3116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBXO7, SUBCELLULAR LOCATION.
  14. "Preferences for phosphorylation sites in the retinoblastoma protein of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro."
    Takaki T., Fukasawa K., Suzuki-Takahashi I., Semba K., Kitagawa M., Taya Y., Hirai H.
    J. Biochem. 137:381-386(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PRB/RB1 KINASE.
  15. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13 AND TYR-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Cdk6 blocks myeloid differentiation by interfering with Runx1 DNA binding and Runx1-C/EBPalpha interaction."
    Fujimoto T., Anderson K., Jacobsen S.E., Nishikawa S.I., Nerlov C.
    EMBO J. 26:2361-2370(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MYELOID DIFFERENTIATION, INTERACTION WITH RUNX1.
  18. "CDK4 and CDK6 delay senescence by kinase-dependent and p16INK4a-independent mechanisms."
    Ruas M., Gregory F., Jones R., Poolman R., Starborg M., Rowe J., Brookes S., Peters G.
    Mol. Cell. Biol. 27:4273-4282(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SENESCENCE.
  19. "A role for NANOG in G1 to S transition in human embryonic stem cells through direct binding of CDK6 and CDC25A."
    Zhang X., Neganova I., Przyborski S., Yang C., Cooke M., Atkinson S.P., Anyfantis G., Fenyk S., Keith W.N., Hoare S.F., Hughes O., Strachan T., Stojkovic M., Hinds P.W., Armstrong L., Lako M.
    J. Cell Biol. 184:67-82(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY NANOG.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24; THR-49; THR-70 AND THR-325, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Induction of human beta-cell proliferation and engraftment using a single G1/S regulatory molecule, cdk6."
    Fiaschi-Taesch N.M., Salim F., Kleinberger J., Troxell R., Cozar-Castellano I., Selk K., Cherok E., Takane K.K., Scott D.K., Stewart A.F.
    Diabetes 59:1926-1936(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BETA-CELL PROLIFERATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  24. Cited for: FUNCTION AS NPM1 KINASE, INTERACTION WITH KSHV V-CYCLIN.
  25. "Beyond the cell cycle: a new role for Cdk6 in differentiation."
    Grossel M.J., Hinds P.W.
    J. Cell. Biochem. 97:485-493(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON CELL DIFFERENTIATION.
  26. "Cell cycle, CDKs and cancer: a changing paradigm."
    Malumbres M., Barbacid M.
    Nat. Rev. Cancer 9:153-166(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON CELL CYCLE CONTROL, INHIBITORS, GENE FAMILY.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a."
    Russo A.A., Tong L., Lee J.O., Jeffrey P.D., Pavletich N.P.
    Nature 395:237-243(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEXES WITH INK4A AND INK4D.
  30. "Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors."
    Jeffrey P.D., Tong L., Pavletich N.P.
    Genes Dev. 14:3115-3125(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR CDKN2C/P18-INK4C.
  31. "Structural basis for CDK6 activation by a virus-encoded cyclin."
    Schulze-Gahmen U., Kim S.-H.
    Nat. Struct. Biol. 9:177-181(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-308 IN COMPLEX WITH HERPESVIRUS SAIMIRI V-CYCLIN/ECLF2, PHOSPHORYLATION AT THR-177.
  32. "Crystal structure of a human cyclin-dependent kinase 6 complex with a flavonol inhibitor, fisetin."
    Lu H., Chang D.J., Baratte B., Meijer L., Schulze-Gahmen U.
    J. Med. Chem. 48:737-743(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-308 IN COMPLEX WITH INHIBITOR.
  33. "Toward understanding the structural basis of cyclin-dependent kinase 6 specific inhibition."
    Lu H., Schulze-Gahmen U.
    J. Med. Chem. 49:3826-3831(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-308 IN COMPLEX WITH INHIBITORS AND V-CYCLIN.
  34. Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-301 IN COMPLEX WITH INHIBITORS.
  35. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-110 AND LEU-199.

Entry informationi

Entry nameiCDK6_HUMAN
AccessioniPrimary (citable) accession number: Q00534
Secondary accession number(s): A4D1G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Over-expressed in some leukemias and malignancies (including sarcoma, glioma, breast tumors, lymphoma and melanoma) as a consequence of nearby translocations.
Enhances beta-cells engraftment in pancreatic islets of Langerhans of diabetic patients.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3