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Q03957

- CTK1_YEAST

UniProt

Q03957 - CTK1_YEAST

Protein

CTD kinase subunit alpha

Gene

CTK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and through PTI1, pre-mRNA 3'-end processing. Participates in both positive and negative regulation of CTD phosphorylation. Required for DNA damage induced transcription, including the expression of the RNR genes, and reprogramming of gene expression upon amino acid starvation. Required for SET2 mediated H3K36 methylation. Also regulates H3K4 methylation. Controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and catalyzing phosphorylation of the CTD required to localize H3K4 chromatin modification specifically to the 5' ends of genes, thereby creating a boundary for H3K4 methylation that prevents a mark associated with transcriptional initiation from spreading into the bodies of genes. Involved in RNA polymerase I transcription. Involved in telomere maintenance. Acts together with SNF1 to induce GSY2 transcription in response to glucose limitation. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. Functions in translation elongation by enhancing decoding fidelity. Needed for translational accuracy by phosphorylating RPS2.12 Publications

    Catalytic activityi

    ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei212 – 2121ATPPROSITE-ProRule annotation
    Active sitei306 – 3061Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1979ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: SGD
    3. protein binding Source: IntAct
    4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB-KW
    2. mRNA 3'-end processing Source: SGD
    3. peptidyl-serine phosphorylation Source: SGD
    4. phosphorylation of RNA polymerase II C-terminal domain Source: SGD
    5. positive regulation of DNA-templated transcription, elongation Source: SGD
    6. positive regulation of transcription from RNA polymerase I promoter Source: SGD
    7. positive regulation of translational fidelity Source: SGD
    8. protein phosphorylation Source: SGD
    9. regulation of cell cycle Source: GOC
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    DNA damage, mRNA processing, Protein biosynthesis, Stress response, Transcription

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31916-MONOMER.
    BRENDAi2.7.11.22. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTD kinase subunit alpha (EC:2.7.11.23)
    Short name:
    CTDK-I subunit alpha
    Alternative name(s):
    CTD kinase 58 kDa subunit
    CTD kinase subunit 1
    Gene namesi
    Name:CTK1
    Ordered Locus Names:YKL139W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL139w.
    SGDiS000001622. CTK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: SGD
    3. nucleoplasm Source: SGD
    4. nucleus Source: SGD
    5. trimeric positive transcription elongation factor complex b Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Null mutants are viable, but grow more slowly than wild-type cells at 30 degrees Celsius. They are cold-sensitive, failing to grow at 12 degrees Celsius. They display flocculent growth in liquid media and they show abnormal cell morphologies, for example, a significant fraction of the cells are greatly enlarged. Deletion mutant has increased phosphorylation of 'Ser-5' of the CTD repeat during logarithmic growth. Deletion eliminates transient increase in CTD 'Ser-2' phosphorylation observed during diauxic shift. Deletion mutant is synthetically lethal when combined with deletion of DST1 or ELP genes. Deletion mutants are modestly sensitive to the uracil analog 6-azauracil (6AU), which inhibits elongation by depleting nucleotide pools. Deletion mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and UV irradiation. 'Ser-2' phosphorylation within the CTD repeats is not increased in deletion mutants upon treatment with DNA-damaging agents.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi324 – 3241D → N: Cold-sensitive. Sensitive to hydroxyurea and UV irradiation. Interferes with ATP-binding. 2 Publications
    Mutagenesisi338 – 3381T → A: Cold-sensitive. Abolishes kinase activity. Delayed growth at early stationary phase. Shows no increase in CTD Ser-2 phosphorylation in the transition from rapid growth to stationary phase. Has compromised transcriptional activation of two stationary-phase genes CTT1 and SPI1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 528528CTD kinase subunit alphaPRO_0000085906Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine; by autocatalysisBy similarity
    Modified residuei338 – 3381Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated on Thr-338 by CAK1. Phosphorylation is essential for the elevated CTD Ser-2 phosphorylation and required to activate transcription of stationary-phase genes during the diauxic shift.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03957.
    PaxDbiQ03957.
    PeptideAtlasiQ03957.

    Expressioni

    Gene expression databases

    GenevestigatoriQ03957.

    Interactioni

    Subunit structurei

    CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts directly with the CTK2 and CTK3 subunits, this interaction is required for kinase activity. Interacts with RNA polymerase I. Interacts with SNF1, but only at low glucose concentrations. Interacts with translating ribosomes.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTK2P4696210EBI-5230,EBI-5236
    CTK3P469638EBI-5230,EBI-5241

    Protein-protein interaction databases

    BioGridi33997. 354 interactions.
    DIPiDIP-6631N.
    IntActiQ03957. 26 interactions.
    MINTiMINT-636105.
    STRINGi4932.YKL139W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03957.
    SMRiQ03957. Positions 183-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini183 – 469287Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 448Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi506 – 52823Asn/Asp-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114964.
    HOGENOMiHOG000233024.
    KOiK00916.
    OMAiYADNDLS.
    OrthoDBiEOG7K3TWD.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    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.

    Q03957-1 [UniParc]FASTAAdd to Basket

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    MSYNNGNTYS KSYSRNNKRP LFGKRSPNPQ SLARPPPPKR IRTDSGYQSN    50
    MDNISSHRVN SNDQPGHTKS RGNNNLSRYN DTSFQTSSRY QGSRYNNNNT 100
    SYENRPKSIK RDETKAEFLS HLPKGPKSVE KSRYNNSSNT SNDIKNGYHA 150
    SKYYNHKGQE GRSVIAKKVP VSVLTQQRST SVYLRIMQVG EGTYGKVYKA 200
    KNTNTEKLVA LKKLRLQGER EGFPITSIRE IKLLQSFDHP NVSTIKEIMV 250
    ESQKTVYMIF EYADNDLSGL LLNKEVQISH SQCKHLFKQL LLGMEYLHDN 300
    KILHRDVKGS NILIDNQGNL KITDFGLARK MNSRADYTNR VITLWYRPPE 350
    LLLGTTNYGT EVDMWGCGCL LVELFNKTAI FQGSNELEQI ESIFKIMGTP 400
    TINSWPTLYD MPWFFMIMPQ QTTKYVNNFS EKFKSVLPSS KCLQLAINLL 450
    CYDQTKRFSA TEALQSDYFK EEPKPEPLVL DGLVSCHEYE VKLARKQKRP 500
    NILSTNTNNK GNGNSNNNNN NNNDDDDK 528
    Length:528
    Mass (Da):60,501
    Last modified:October 1, 1993 - v1
    Checksum:i9862EB10FD476F6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69024 Genomic DNA. Translation: AAC41642.1.
    Z28139 Genomic DNA. Translation: CAA81980.1.
    BK006944 Genomic DNA. Translation: DAA09023.1.
    PIRiS32593.
    RefSeqiNP_012783.1. NM_001179705.1.

    Genome annotation databases

    EnsemblFungiiYKL139W; YKL139W; YKL139W.
    GeneIDi853718.
    KEGGisce:YKL139W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69024 Genomic DNA. Translation: AAC41642.1 .
    Z28139 Genomic DNA. Translation: CAA81980.1 .
    BK006944 Genomic DNA. Translation: DAA09023.1 .
    PIRi S32593.
    RefSeqi NP_012783.1. NM_001179705.1.

    3D structure databases

    ProteinModelPortali Q03957.
    SMRi Q03957. Positions 183-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33997. 354 interactions.
    DIPi DIP-6631N.
    IntActi Q03957. 26 interactions.
    MINTi MINT-636105.
    STRINGi 4932.YKL139W.

    Proteomic databases

    MaxQBi Q03957.
    PaxDbi Q03957.
    PeptideAtlasi Q03957.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL139W ; YKL139W ; YKL139W .
    GeneIDi 853718.
    KEGGi sce:YKL139W.

    Organism-specific databases

    CYGDi YKL139w.
    SGDi S000001622. CTK1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114964.
    HOGENOMi HOG000233024.
    KOi K00916.
    OMAi YADNDLS.
    OrthoDBi EOG7K3TWD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31916-MONOMER.
    BRENDAi 2.7.11.22. 984.

    Miscellaneous databases

    NextBioi 974737.
    PROi Q03957.

    Gene expression databases

    Genevestigatori Q03957.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    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

    1. "CTD kinase large subunit is encoded by CTK1, a gene required for normal growth of Saccharomyces cerevisiae."
      Lee J.M., Greenleaf A.L.
      Gene Expr. 1:149-167(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent cyclin-cyclin-dependent kinase complex."
      Sterner D.E., Lee J.M., Hardin S.E., Greenleaf A.L.
      Mol. Cell. Biol. 15:5716-5724(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CTD KINASE ACTIVITY, SUBUNIT, DISRUPTION PHENOTYPE.
    5. "Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I."
      Lee J.M., Greenleaf A.L.
      J. Biol. Chem. 272:10990-10993(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RNA POLYMERASE II TRANSCRIPTION.
    6. "Yeast carboxyl-terminal domain kinase I positively and negatively regulates RNA polymerase II carboxyl-terminal domain phosphorylation."
      Patturajan M., Conrad N.K., Bregman D.B., Corden J.L.
      J. Biol. Chem. 274:27823-27828(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION REGULATION, DISRUPTION PHENOTYPE.
    7. "Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo."
      Jona G., Wittschieben B.O., Svejstrup J.Q., Gileadi O.
      Gene 267:31-36(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. "Activation of the cyclin-dependent kinase CTDK-I requires the heterodimerization of two unstable subunits."
      Hautbergue G., Goguel V.
      J. Biol. Chem. 276:8005-8013(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION, INTERACTION WITH CTK2 AND CTK3.
    9. "The RNA polymerase II CTD kinase CTDK-I affects pre-mRNA 3' cleavage/polyadenylation through the processing component Pti1p."
      Skaar D.A., Greenleaf A.L.
      Mol. Cell 10:1429-1439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MRNA END PROCESSING.
    10. "Budding yeast CTDK-I is required for DNA damage-induced transcription."
      Ostapenko D., Solomon M.J.
      Eukaryot. Cell 2:274-283(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-324, DISRUPTION PHENOTYPE.
    11. "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast."
      Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H., Strahl B.D.
      Genes Dev. 17:654-663(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN H3K36 METHYLATION.
    12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA polymerase II C-terminal domain repeats."
      Jones J.C., Phatnani H.P., Haystead T.A., MacDonald J.A., Alam S.M., Greenleaf A.L.
      J. Biol. Chem. 279:24957-24964(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CTDK-I COMPLEX IN PHOSPHORYLATION.
    15. Cited for: FUNCTION IN RNA POLYMERASE I TRANSCRIPTION, INTERACTION WITH RNA POLYMERASE I, SUBCELLULAR LOCATION.
    16. "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length."
      Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C., Krauskopf A., Kupiec M., McEachern M.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE MAINTENANCE.
    17. "Glucose deprivation mediates interaction between CTDK-I and Snf1 in Saccharomyces cerevisiae."
      Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.
      FEBS Lett. 579:5318-5324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RESPONSE TO GLUCOSE LIMITATION, INTERACTION WITH SNF1.
    18. "Phosphorylation by Cak1 regulates the C-terminal domain kinase Ctk1 in Saccharomyces cerevisiae."
      Ostapenko D., Solomon M.J.
      Mol. Cell. Biol. 25:3906-3913(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-338 BY CAK1, MUTAGENESIS OF ASP-324 AND THR-338.
    19. "CTD kinase I is required for the integrity of the rDNA tandem array."
      Grenetier S., Bouchoux C., Goguel V.
      Nucleic Acids Res. 34:4996-5006(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "The RNA polymerase II CTD kinase Ctk1 functions in translation elongation."
      Roether S., Straesser K.
      Genes Dev. 21:1409-1421(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSLATION, INTERACTION WITH RIBOSOMES.
    21. "The RNA polymerase II kinase Ctk1 regulates positioning of a 5' histone methylation boundary along genes."
      Xiao T., Shibata Y., Rao B., Laribee R.N., O'Rourke R., Buck M.J., Greenblatt J.F., Krogan N.J., Lieb J.D., Strahl B.D.
      Mol. Cell. Biol. 27:721-731(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN H3K4 METHYLATION.

    Entry informationi

    Entry nameiCTK1_YEAST
    AccessioniPrimary (citable) accession number: Q03957
    Secondary accession number(s): D6VX57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 125 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3