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CDC28 · P00546

In brief

CDC28 is UniProt protein record P00546 for Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (NCBI 559292). The retained sequence contains 298 amino acids. [1]

Evidence for this statement

Source annotation

Where to check this statement

uniprot-P00546
Captured UniProt JSON: primaryAccession, organism, sequence and FUNCTION comments
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Meet the protein

CDC28 is a cyclin-dependent protein kinase involved in controlling the yeast cell cycle. Entry P00546 includes information about the G1-to-S transition, when DNA copying begins, and phosphorylation of protein targets. Its organism is the specific Saccharomyces cerevisiae strain S288c; preserve that identity when comparing it with other yeasts.

[1]
Evidence for this statement

Editorial synthesis

Where to check this statement

uniprot-P00546
Captured UniProt JSON: primaryAccession, organism, sequence and FUNCTION comments

The functional statements in this entry have different evidential bases. UniProt marks some, including the contribution of a bound cyclin to target selection, as inferred by similarity; others cite experimental publications. Read the evidence code for the particular annotation. The status of the whole entry does not mean every statement was measured directly in the selected strain.

[1]
Evidence for this statement

Editorial synthesis

Where to check this statement

uniprot-P00546
Captured UniProt JSON: primaryAccession, organism, sequence and FUNCTION comments

A kinase coordinates cell-cycle transitions

CDC28 connects cell-cycle control with phosphorylation of protein targets. A bound cyclin contributes to target selection in the retained annotation, while particular target statements cite their own studies. For example, the entry describes phosphorylation of YTA7 during S phase in connection with histone transcription. A meaningful comparison asks which target, phase and evidential basis are being compared. The sequence of one CDC28 protein does not by itself show which cyclin is bound or the timing of activity in a particular cell.

[1]
Evidence for this statement

EcoGenesis

Where to check this statement

uniprot-P00546
Retained UniProt JSON: comments[commentType=FUNCTION], selected accession and entry version as recorded in evidence

Teaching diagram

Evidence for this statement

EcoGenesis

    Original teaching diagram of the relationship described in the retained FUNCTION annotation; no measured rate, geometry or experimental result is shown.
    1. CDC28 and cyclin

      Partner-dependent target selection

    2. Protein targets

      Phosphorylation

    3. Cell-cycle transition

      Read with phase and conditions

    • CDC28 and cyclin → Protein targets: connects with
    • Protein targets → Cell-cycle transition: connects with

    What is known about function

    Function and evidence from UniProt

    Inspect structured data
    Source text
    Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). Required to drive the G1-S transition (PubMed:2664468). More than 200 substrates have been identified (PubMed:14574415). Substrate specificity is in part regulated by the bound cyclin protein (By similarity). Phosphorylates YTA7 during S-phase to promote transcription of histones (PubMed:22156209). May phosphorylate CNN1, to contribute to the enrichment of CNN1 on anaphase kinetochores (PubMed:22561345)
    Source language
    en
    evidence codes
    • evidenceCode
      ECO:0000250
      Source
      UniProtKB
      id
      P04551
    • evidenceCode
      ECO:0000269
      Source
      PubMed
      id
      14574415
    • evidenceCode
      ECO:0000269
      Source
      PubMed
      id
      22156209
    • evidenceCode
      ECO:0000269
      Source
      PubMed
      id
      22561345
    • evidenceCode
      ECO:0000269
      Source
      PubMed
      id
      2664468
    [1]
    Evidence for this statement

    Source annotation

    Where to check this statement

    uniprot-P00546
    Captured UniProt JSON: comments[commentType=FUNCTION] and attached evidence codes

    Evidence codes qualify the annotation. This record is not a measurement of an illustrated specimen.

    Sequence and version

    P00546

    Inspect structured data
    accession
    P00546
    name
    Cyclin-dependent kinase 1
    length
    298
    entry version
    248
    sequence version
    1
    Sequence
    MSGELANYKRLEKVGEGTYGVVYKALDLRPGQGQRVVALKKIRLESEDEGVPSTAIREIS
LLKELKDDNIVRLYDIVHSDAHKLYLVFEFLDLDLKRYMEGIPKDQPLGADIVKKFMMQL
CKGIAYCHSHRILHRDLKPQNLLINKDGNLKLGDFGLARAFGVPLRAYTHEIVTLWYRAP
EVLLGGKQYSTGVDTWSIGCIFAEMCNRKPIFSGDSEIDQIFKIFRVLGTPNEAIWPDIV
YLPDFKPSFPQWRRKDLSQVVPSLDPRGIDLLDKLLAYDPINRISARRAAIHPYFQES
    [1]
    Evidence for this statement

    Source annotation

    Where to check this statement

    uniprot-P00546
    Captured UniProt JSON: sequence.value, sequence.length, sequenceVersion and entryVersion

    Genes and domains

    Cross-references supplied by UniProt

    Inspect structured data
    gene symbols
    • CDC28
    gene crossreferences
    • database
      EnsemblFungi
      id
      YBR160W_mRNA
      properties
      • key
        ProteinId
        value
        YBR160W
      • key
        GeneId
        value
        YBR160W
    • database
      GeneID
      id
      852457
      properties
      • key
        Description
        value
        -
    interpro domains
    • Provider
      interpro
      accession
      IPR050108
      name
      CDK
    • Provider
      interpro
      accession
      IPR011009
      name
      Kinase-like_dom_sf
    • Provider
      interpro
      accession
      IPR000719
      name
      Prot_kinase_dom
    • Provider
      interpro
      accession
      IPR017441
      name
      Protein_kinase_ATP_BS
    • Provider
      interpro
      accession
      IPR008271
      name
      Ser/Thr_kinase_AS
    [1]
    Evidence for this statement

    Source annotation

    Where to check this statement

    uniprot-P00546
    Captured UniProt JSON: genes, features and cross-references

    GO function annotations

    A sample with evidence codes

    Inspect structured data

    Shown / materialized / in provider response: 12 / 147 / 150

    GO
    GOEvidencePublication or ruleAssigned by
    GO:0000993
    RNA polymerase II complex binding
    Molecular Function    		ECO:0000314
    enables    		PMID:22689984SGD
    20130807
    GO:0004672
    protein kinase activity
    Molecular Function    		ECO:0000256
    enables    		GO_REF:0000002InterPro
    20260727
    GO:0004672
    protein kinase activity
    Molecular Function    		ECO:0007005
    enables    		PMID:16319894SGD
    20181119
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:12050115SGD
    20200716
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:16096060SGD
    20191106
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:17460120UniProt
    20230925
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:21498574SGD
    20191106
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000315
    enables    		PMID:21841787SGD
    20191106
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:22156209UniProt
    20210707
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:22521784SGD
    20191106
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000315
    enables    		PMID:22521784SGD
    20191106
    GO:0004674
    protein serine/threonine kinase activity
    Molecular Function    		ECO:0000314
    enables    		PMID:22563681SGD
    20191106
    [2] [3]
    Evidence for this statement

    Source annotation

    Where to check this statement

    quickgo-P00546-1
    Captured QuickGO annotation results: GO ID, qualifier, evidenceCode, reference, assignedBy and date; limited returned pages
    quickgo-P00546-2
    Captured QuickGO annotation results: GO ID, qualifier, evidenceCode, reference, assignedBy and date; limited returned pages

    These are source annotations, not independent proof of a causal mechanism. The complete captured responses are available as originals.

    Research cited by the protein record

    Bibliographic records

    Inspect structured data
    • Source
      uniprot
      id
      P00546-citation-6361575
      title
      Primary structure homology between the product of yeast cell division control gene CDC28 and vertebrate oncogenes.
      pmid
      6361575
      doi
      10.1038/307183a0
      year
      1984
      authors
      • Lorincz A.T.
      • Reed S.I.
      journal
      Nature
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-7597849
      title
      Sequence analysis of a 5.6 kb fragment of chromosome II from Saccharomyces cerevisiae reveals two new open reading frames next to CDC28.
      pmid
      7597849
      doi
      10.1002/yea.320110508
      year
      1995
      authors
      • Baur S.
      • Becker J.
      • Li Z.
      • Niegemann E.
      • Wehner E.
      • Wolter R.
      • Brendel M.
      journal
      Yeast
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-7813418
      title
      Complete DNA sequence of yeast chromosome II.
      pmid
      7813418
      doi
      10.1002/j.1460-2075.1994.tb06923.x
      year
      1994
      authors
      • Feldmann H.
      • Aigle M.
      • Aljinovic G.
      • Andre B.
      • Baclet M.C.
      • Barthe C.
      • Baur A.
      • Becam A.-M.
      • Biteau N.
      • Boles E.
      • Brandt T.
      • Brendel M.
      • Brueckner M.
      • Bussereau F.
      • Christiansen C.
      • Contreras R.
      • Crouzet M.
      • Cziepluch C.
      • Demolis N.
      • Delaveau T.
      • Doignon F.
      • Domdey H.
      • Duesterhus S.
      • Dubois E.
      • Dujon B.
      • El Bakkoury M.
      • Entian K.-D.
      • Feuermann M.
      • Fiers W.
      • Fobo G.M.
      • Fritz C.
      • Gassenhuber J.
      • Glansdorff N.
      • Goffeau A.
      • Grivell L.A.
      • de Haan M.
      • Hein C.
      • Herbert C.J.
      • Hollenberg C.P.
      • Holmstroem K.
      • Jacq C.
      • Jacquet M.
      • Jauniaux J.-C.
      • Jonniaux J.-L.
      • Kallesoee T.
      • Kiesau P.
      • Kirchrath L.
      • Koetter P.
      • Korol S.
      • Liebl S.
      • Logghe M.
      • Lohan A.J.E.
      • Louis E.J.
      • Li Z.Y.
      • Maat M.J.
      • Mallet L.
      • Mannhaupt G.
      • Messenguy F.
      • Miosga T.
      • Molemans F.
      • Mueller S.
      • Nasr F.
      • Obermaier B.
      • Perea J.
      • Pierard A.
      • Piravandi E.
      • Pohl F.M.
      • Pohl T.M.
      • Potier S.
      • Proft M.
      • Purnelle B.
      • Ramezani Rad M.
      • Rieger M.
      • Rose M.
      • Schaaff-Gerstenschlaeger I.
      • Scherens B.
      • Schwarzlose C.
      • Skala J.
      • Slonimski P.P.
      • Smits P.H.M.
      • Souciet J.-L.
      • Steensma H.Y.
      • Stucka R.
      • Urrestarazu L.A.
      • van der Aart Q.J.M.
      • Van Dyck L.
      • Vassarotti A.
      • Vetter I.
      • Vierendeels F.
      • Vissers S.
      • Wagner G.
      • de Wergifosse P.
      • Wolfe K.H.
      • Zagulski M.
      • Zimmermann F.K.
      • Mewes H.-W.
      • Kleine K.
      journal
      EMBO J.
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-24374639
      title
      The reference genome sequence of Saccharomyces cerevisiae: Then and now.
      pmid
      24374639
      doi
      10.1534/g3.113.008995
      year
      2014
      authors
      • Engel S.R.
      • Dietrich F.S.
      • Fisk D.G.
      • Binkley G.
      • Balakrishnan R.
      • Costanzo M.C.
      • Dwight S.S.
      • Hitz B.C.
      • Karra K.
      • Nash R.S.
      • Weng S.
      • Wong E.D.
      • Lloyd P.
      • Skrzypek M.S.
      • Miyasato S.R.
      • Simison M.
      • Cherry J.M.
      journal
      G3 (Bethesda)
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-14562106
      title
      Global analysis of protein expression in yeast.
      pmid
      14562106
      doi
      10.1038/nature02046
      year
      2003
      authors
      • Ghaemmaghami S.
      • Huh W.-K.
      • Bower K.
      • Howson R.W.
      • Belle A.
      • Dephoure N.
      • O'Shea E.K.
      • Weissman J.S.
      journal
      Nature
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-2664468
      title
      The Saccharomyces cerevisiae CKS1 gene, a homolog of the Schizosaccharomyces pombe suc1+ gene, encodes a subunit of the Cdc28 protein kinase complex.
      pmid
      2664468
      doi
      10.1128/mcb.9.5.2034-2041.1989
      year
      1989
      authors
      • Hadwiger J.A.
      • Wittenberg C.
      • Mendenhall M.D.
      • Reed S.I.
      journal
      Mol. Cell. Biol.
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-14574415
      title
      Targets of the cyclin-dependent kinase Cdk1.
      pmid
      14574415
      doi
      10.1038/nature02062
      year
      2003
      authors
      • Ubersax J.A.
      • Woodbury E.L.
      • Quang P.N.
      • Paraz M.
      • Blethrow J.D.
      • Shah K.
      • Shokat K.M.
      • Morgan D.O.
      journal
      Nature
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-15665377
      title
      Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.
      pmid
      15665377
      doi
      10.1074/mcp.m400219-mcp200
      year
      2005
      authors
      • Gruhler A.
      • Olsen J.V.
      • Mohammed S.
      • Mortensen P.
      • Faergeman N.J.
      • Mann M.
      • Jensen O.N.
      journal
      Mol. Cell. Proteomics
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-17330950
      title
      Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.
      pmid
      17330950
      doi
      10.1021/pr060559j
      year
      2007
      authors
      • Li X.
      • Gerber S.A.
      • Rudner A.D.
      • Beausoleil S.A.
      • Haas W.
      • Villen J.
      • Elias J.E.
      • Gygi S.P.
      journal
      J. Proteome Res.
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-19779198
      title
      Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.
      pmid
      19779198
      doi
      10.1126/science.1172867
      year
      2009
      authors
      • Holt L.J.
      • Tuch B.B.
      • Villen J.
      • Johnson A.D.
      • Gygi S.P.
      • Morgan D.O.
      journal
      Science
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-22156209
      title
      Restriction of histone gene transcription to S phase by phosphorylation of a chromatin boundary protein.
      pmid
      22156209
      doi
      10.1101/gad.173427.111
      year
      2011
      authors
      • Kurat C.F.
      • Lambert J.P.
      • van Dyk D.
      • Tsui K.
      • van Bakel H.
      • Kaluarachchi S.
      • Friesen H.
      • Kainth P.
      • Nislow C.
      • Figeys D.
      • Fillingham J.
      • Andrews B.J.
      journal
      Genes Dev.
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    • Source
      uniprot
      id
      P00546-citation-22814378
      title
      N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
      pmid
      22814378
      doi
      10.1073/pnas.1210303109
      year
      2012
      authors
      • 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.
      journal
      Proc. Natl. Acad. Sci. U.S.A.
      Reuse status
      metadata_only
      Source URL
      https://rest.uniprot.org/uniprotkb/P00546.json
      Source snapshot SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
    [1]
    Evidence for this statement

    Source annotation

    Where to check this statement

    uniprot-P00546
    Captured UniProt JSON: references and citation cross-references

    Only metadata is shown. Article text has a separate reuse decision.

    How to read these records

    Organism in the UniProt record

    Saccharomyces cerevisiae (strain ATCC 204508 / S288c) · NCBI 559292Scientific profile →

    Your research question

    Save the article to return to your question and this source version.

    Plan a test

    This is your research plan. Completing these fields does not confirm a hypothesis.

    Ask about this material

    Sources and versions

    Editorial draft · human review pending

    1. UniProt Consortium · P00546

      2026-09-09T03:19:40.513463+00:00 · CC-BY-4.0

      Provenance and original
      Source version
      entry 248; sequence 1
      Original SHA-256
      756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
      Processing
      Unmodified provider response; selected fields are projected into the document.
      Version details
      Native entry and sequence versions retained.

      View original JSON · Download original

    2. Gene Ontology Consortium / QuickGO · UniProtKB:P00546

      2026-09-09T03:19:42.173834+00:00 · CC-BY-4.0

      Provenance and original
      Original SHA-256
      229c2003f0d30fc3b13f848e278fa539b51940f83fbdba2214ae5d1d074f17a8
      Processing
      Unmodified provider response; selected fields are projected into the document.
      Version details
      No native GO release was supplied; exact response hash and retrieval time are retained.

      View original JSON · Download original

    3. Gene Ontology Consortium / QuickGO · UniProtKB:P00546

      2026-09-09T03:19:43.425341+00:00 · CC-BY-4.0

      Provenance and original
      Original SHA-256
      61d1cb9baedf35f7e46c90404b1233f7cc2b88bcf35d6ee3bde2aedf19502253
      Processing
      Unmodified provider response; selected fields are projected into the document.
      Version details
      No native GO release was supplied; exact response hash and retrieval time are retained.

      View original JSON · Download original

    Inspect structured data
    Content version
    1150ebd366b5806ecd1904fbf1c5f9c93e6c654d14e0d401f6094bf24f248ccc
    Source version
    research-20260909.1
    Updated
    2026-10-01