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CDC28 · P00546

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Meet the protein

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

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

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

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

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

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
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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.
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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)
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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.
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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.
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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.
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    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.
    rights reuse state
    metadata_only
    source url
    https://rest.uniprot.org/uniprotkb/P00546.json
    source snapshot sha256
    756c9d3a748d52b3d222d898051e3becd0ca99a1d8d56acba5224314e57256e2
[1]
Evidence for this statement

Source annotation

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

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

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Sources and versions

An explanation grounded in the cited sources

  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
65b33cde9b0d1e94b6dd837851860c9f541969765c2ef4d677dd5c1a79301302
Source version
research-20260909.1
Updated
2026-09-09