{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P11802","secondaryAccessions":["B2R9A0","B4DNF9","O00576","Q6FG61"],"uniProtkbId":"CDK4_HUMAN","entryAudit":{"firstPublicDate":"1989-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","entryVersion":267,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7652577"}],"value":"Cyclin-dependent kinase 4"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19075005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9106657"}],"value":"2.7.11.22"}]},"alternativeNames":[{"fullName":{"value":"Cell division protein kinase 4"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1773"}],"value":"PSK-J3"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7652577"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1773"}],"value":"CDK4"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15241418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18827403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9003781"}],"value":"Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19075005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9106657"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19075005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9106657"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19487459"}],"value":"Both phosphorylation at Thr-172 and binding of a D-type cyclin are necessary for enzymatic activity. Full activation of the cyclin-D-CDK4 complex appears to require other factors such as recruitment of the substrate via a substrate recruitment motif, and/or formation of the CDKN1B ternary complex. Inhibited by INK4 family members. In resting cells, the non-tyrosine-phosphorylated form of CDKN1B prevents phosphorylation at Thr-172 and inactivation, while, in proliferating cells, tyrosine phosphorylation of CDKN1B allows phosphorylation of Thr-172 of CDK4 and subsequent activation"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P30285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10580009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15107404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15558030"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16782892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18827403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19075005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19124461"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20399237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27353360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29127155"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9106657"}],"value":"Component of the D-CDK4 complex, composed of CDK4 and some D-type G1 cyclin (CCND1, CCND2 or CCND3). Interacts directly in the complex with CCND1, CCND2 or CCND3. Interacts with SEI1 and ZNF655. Forms a ternary complex, cyclin D-CDK4-CDKN1B, involved in modulating CDK4 enzymatic activity. Interacts directly with CDKN1B (phosphorylated on 'Tyr-88' and 'Tyr-89'); the interaction allows assembly of the cyclin D-CDK4 complex, Thr-172 phosphorylation, nuclear translocation and enhances the cyclin D-CDK4 complex activity. CDK4 activity is either inhibited or enhanced depending on stoichiometry of complex. The non-tyrosine-phosphorylated form of CDKN1B prevents T-loop phosphorylation of CDK4 producing inactive CDK4. Interacts (unphosphorylated form) with CDK2. Also forms ternary complexes with CDKN1A or CDKN2A. Interacts directly with CDKN1A (via its N-terminal); the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation and promotes the cyclin D-dependent enzyme activity of CDK4. Interacts with CCND1; the interaction is prevented with the binding of CCND1 to INSM1 during cell cycle progression. Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Interacts with FNIP1 and FNIP2 (PubMed:27353360)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q9UH17","geneName":"APOBEC3B","intActId":"EBI-2967317"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P24385","geneName":"CCND1","intActId":"EBI-375001"},"numberOfExperiments":46,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P30279","geneName":"CCND2","intActId":"EBI-748789"},"numberOfExperiments":18,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P30281","geneName":"CCND3","intActId":"EBI-375013"},"numberOfExperiments":41,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q16543","geneName":"CDC37","intActId":"EBI-295634"},"numberOfExperiments":16,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P50613","geneName":"CDK7","intActId":"EBI-1245958"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P38936","geneName":"CDKN1A","intActId":"EBI-375077"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P46527","geneName":"CDKN1B","intActId":"EBI-519280"},"numberOfExperiments":13,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P49918","geneName":"CDKN1C","intActId":"EBI-519256"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P42771","geneName":"CDKN2A","intActId":"EBI-375053"},"numberOfExperiments":18,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P42772","geneName":"CDKN2B","intActId":"EBI-711280"},"numberOfExperiments":22,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P42773","geneName":"CDKN2C","intActId":"EBI-711290"},"numberOfExperiments":26,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P55273","geneName":"CDKN2D","intActId":"EBI-745859"},"numberOfExperiments":30,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q969H0","geneName":"FBXW7","intActId":"EBI-359574"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q9UJC3","geneName":"HOOK1","intActId":"EBI-746704"},"numberOfExperiments":14,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P08238","geneName":"HSP90AB1","intActId":"EBI-352572"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q9UKT9","geneName":"IKZF3","intActId":"EBI-747204"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q0VD86","geneName":"INCA1","intActId":"EBI-6509505"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P01106","geneName":"MYC","intActId":"EBI-447544"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q9ULD0","geneName":"OGDHL","intActId":"EBI-3940481"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"P28749","geneName":"RBL1","intActId":"EBI-971402"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q08999","geneName":"RBL2","intActId":"EBI-971439"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P11802","intActId":"EBI-295644"},"interactantTwo":{"uniProtKBAccession":"Q9BY78","geneName":"RNF26","intActId":"EBI-2129375"},"numberOfEx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Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18827403"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18827403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20399237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9106657"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18827403"}],"value":"Nucleus membrane","id":"SL-0182"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P11802-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P11802-2"],"sequenceIds":["VSP_056487"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16782892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19075005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19487459"}],"value":"Phosphorylation at Thr-172 is required for enzymatic activity. Phosphorylated, in vitro, at this site by CCNH-CDK7, but, in vivo, appears to be phosphorylated by a proline-directed kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation and consequent CDK4 enzyme activity, is dependent on the tyrosine phosphorylation state of CDKN1B. Thus, in proliferating cells, CDK4 within the complex is phosphorylated on Thr-172 in the T-loop. In resting cells, phosphorylation on Thr-172 is prevented by the non-tyrosine-phosphorylated form of CDKN1B"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Melanoma, cutaneous malignant 3","diseaseAccession":"DI-01460","acronym":"CMM3","description":"A malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but may also involve other sites.","diseaseCrossReference":{"database":"MIM","id":"609048"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7652577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8528263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9311594"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9425228"}]},"note":{"texts":[{"value":"Disease susceptibility is associated with variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Microcephaly 31, primary, autosomal recessive","diseaseAccession":"DI-07152","acronym":"MCPH31","description":"A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH31 is characterized by progressive small head circumference, poor overall postnatal growth and short stature. Learning disabilities or speech delay may be present.","diseaseCrossReference":{"database":"MIM","id":"621507"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40210435"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily"}],"commentType":"SIMILARITY"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/238/CDK4","ftp":false}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19413330"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Cyclin-dependent kinase 4","featureId":"PRO_0000085778"},{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}]},{"type":"Region","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"Required for binding D-type cyclins"},{"type":"Active site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylalanine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19413330"}]},{"type":"Modified residue","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16782892"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19237565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19487459"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19369195"}]},{"type":"Alternative sequence","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"in isoform 2","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14702039"}],"featureId":"VSP_056487","alternativeSequence":{}},{"type":"Natural variant","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"in CMM3; 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