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P22579

- SIN3_YEAST

UniProt

P22579 - SIN3_YEAST

Protein

Transcriptional regulatory protein SIN3

Gene

SIN3

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 140 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SIN3 has also a RPD3 independent function required for normal longevity.18 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. transcription coactivator activity Source: SGD
    4. transcription corepressor activity Source: SGD

    GO - Biological processi

    1. double-strand break repair via nonhomologous end joining Source: SGD
    2. histone deacetylation Source: SGD
    3. negative regulation of chromatin silencing at rDNA Source: SGD
    4. negative regulation of chromatin silencing at silent mating-type cassette Source: SGD
    5. negative regulation of chromatin silencing at telomere Source: SGD
    6. negative regulation of transcription during meiosis Source: SGD
    7. negative regulation of transcription from RNA polymerase II promoter Source: SGD
    8. negative regulation of transcription from RNA polymerase I promoter Source: SGD
    9. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    10. positive regulation of transcription from RNA polymerase II promoter in response to heat stress Source: SGD
    11. regulation of DNA-dependent DNA replication initiation Source: SGD
    12. regulation of transcription involved in G2/M transition of mitotic cell cycle Source: SGD
    13. transcription, DNA-templated Source: UniProtKB-KW
    14. transfer RNA gene-mediated silencing Source: SGD

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Repressor

    Keywords - Biological processi

    Cell cycle, Cell division, Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33421-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional regulatory protein SIN3
    Gene namesi
    Name:SIN3
    Synonyms:CPE1, GAM2, RPD1, SDI1, SDS16, UME4
    Ordered Locus Names:YOL004W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL004w.
    SGDiS000005364. SIN3.

    Subcellular locationi

    GO - Cellular componenti

    1. Rpd3L complex Source: SGD
    2. Rpd3S complex Source: SGD
    3. Sin3-type complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15361536Transcriptional regulatory protein SIN3PRO_0000121544Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei137 – 1371Phosphoserine1 Publication
    Modified residuei303 – 3031Phosphothreonine1 Publication
    Modified residuei304 – 3041Phosphothreonine2 Publications
    Modified residuei316 – 3161Phosphoserine1 Publication
    Modified residuei1046 – 10461Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP22579.
    PaxDbiP22579.
    PeptideAtlasiP22579.

    Expressioni

    Gene expression databases

    GenevestigatoriP22579.

    Interactioni

    Subunit structurei

    Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1. Interacts with ESS1 and STB1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-17160,EBI-17160
    OPI1P219575EBI-17160,EBI-12555
    RPD3P3256111EBI-17160,EBI-15864

    Protein-protein interaction databases

    BioGridi34400. 534 interactions.
    DIPiDIP-597N.
    IntActiP22579. 84 interactions.
    MINTiMINT-422975.
    STRINGi4932.YOL004W.

    Structurei

    3D structure databases

    ProteinModelPortaliP22579.
    SMRiP22579. Positions 219-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini217 – 28771PAH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 47471PAH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini656 – 72772PAH 3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi480 – 51940Gln-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 PAH (paired amphipathic helix) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5602.
    GeneTreeiENSGT00390000007239.
    HOGENOMiHOG000248545.
    KOiK11644.
    OMAiREQKPIQ.
    OrthoDBiEOG7T4MTQ.

    Family and domain databases

    Gene3Di1.20.1160.11. 3 hits.
    InterProiIPR013194. HDAC_interact.
    IPR003822. PAH.
    [Graphical view]
    PfamiPF02671. PAH. 3 hits.
    PF08295. Sin3_corepress. 1 hit.
    [Graphical view]
    SMARTiSM00761. HDAC_interact. 1 hit.
    [Graphical view]
    SUPFAMiSSF47762. SSF47762. 3 hits.
    PROSITEiPS51477. PAH. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22579-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQVWHNSNS QSNDVATSND ATGSNERNEK EPSLQGNKPG FVQQQQRITL     50
    PSLSALSTKE EDRRDSNGQQ ALTSHAAHIL GYPPPHSNAM PSIATDSALK 100
    QPHEYHPRPK SSSSSPSINA SLMNAGPAPL PTVGAASFSL SRFDNPLPIK 150
    APVHTEEPKS YNGLQEEEKA TQRPQDCKEV PAGVQPADAP DPSSNHADAN 200
    DDNNNNENSH DEDADYRPLN VKDALSYLEQ VKFQFSSRPD IYNLFLDIMK 250
    DFKSQAIDTP GVIERVSTLF RGYPILIQGF NTFLPQGYRI ECSSNPDDPI 300
    RVTTPMGTTT VNNNISPSGR GTTDAQELGS FPESDGNGVQ QPSNVPMVPS 350
    SVYQSEQNQD QQQSLPLLAT SSGLPSIQQP EMPAHRQIPQ SQSLVPQEDA 400
    KKNVDVEFSQ AISYVNKIKT RFADQPDIYK HFLEILQTYQ REQKPINEVY 450
    AQVTHLFQNA PDLLEDFKKF LPDSSASANQ QVQHAQQHAQ QQHEAQMHAQ 500
    AQAQAQAQAQ VEQQKQQQQF LYPASGYYGH PSNRGIPQQN LPPIGSFSPP 550
    TNGSTVHEAY QDQQHMQPPH FMPLPSIVQH GPNMVHQGIA NENPPLSDLR 600
    TSLTEQYAPS SIQHQQQHPQ SISPIANTQY GDIPVRPEID LDPSIVPVVP 650
    EPTEPIENNI SLNEEVTFFE KAKRYIGNKH LYTEFLKILN LYSQDILDLD 700
    DLVEKVDFYL GSNKELFTWF KNFVGYQEKT KCIENIVHEK HRLDLDLCEA 750
    FGPSYKRLPK SDTFMPCSGR DDMCWEVLND EWVGHPVWAS EDSGFIAHRK 800
    NQYEETLFKI EEERHEYDFY IESNLRTIQC LETIVNKIEN MTENEKANFK 850
    LPPGLGHTSM TIYKKVIRKV YDKERGFEII DALHEHPAVT APVVLKRLKQ 900
    KDEEWRRAQR EWNKVWRELE QKVFFKSLDH LGLTFKQADK KLLTTKQLIS 950
    EISSIKVDQT NKKIHWLTPK PKSQLDFDFP DKNIFYDILC LADTFITHTT 1000
    AYSNPDKERL KDLLKYFISL FFSISFEKIE ESLYSHKQNV SESSGSDDGS 1050
    SIASRKRPYQ QEMSLLDILH RSRYQKLKRS NDEDGKVPQL SEPPEEEPNT 1100
    IEEEELIDEE AKNPWLTGNL VEEANSQGII QNRSIFNLFA NTNIYIFFRH 1150
    WTTIYERLLE IKQMNERVTK EINTRSTVTF AKDLDLLSSQ LSEMGLDFVG 1200
    EDAYKQVLRL SRRLINGDLE HQWFEESLRQ AYNNKAFKLY TIDKVTQSLV 1250
    KHAHTLMTDA KTAEIMALFV KDRNASTTSA KDQIIYRLQV RSHMSNTENM 1300
    FRIEFDKRTL HVSIQYIALD DLTLKEPKAD EDKWKYYVTS YALPHPTEGI 1350
    PHEKLKIPFL ERLIEFGQDI DGTEVDEEFS PEGISVSTLK IKIQPITYQL 1400
    HIENGSYDVF TRKATNKYPT IANDNTQKGM VSQKKELISK FLDCAVGLRN 1450
    NLDEAQKLSM QKKWENLKDS IAKTSAGNQG IESETEKGKI TKQEQSDNLD 1500
    SSTASVLPAS ITTVPQDDNI ETTGNTESSD KGAKIQ 1536
    Length:1,536
    Mass (Da):174,839
    Last modified:November 1, 1997 - v2
    Checksum:i0834726312B13878
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti510 – 5101Q → QAQ(PubMed:2233725)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36822 Genomic DNA. Translation: AAA34839.1.
    Z74746 Genomic DNA. Translation: CAA99003.1.
    BK006948 Genomic DNA. Translation: DAA10779.1.
    PIRiS66686. RGBYS3.
    RefSeqiNP_014639.1. NM_001183258.1.

    Genome annotation databases

    EnsemblFungiiYOL004W; YOL004W; YOL004W.
    GeneIDi854158.
    KEGGisce:YOL004W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36822 Genomic DNA. Translation: AAA34839.1 .
    Z74746 Genomic DNA. Translation: CAA99003.1 .
    BK006948 Genomic DNA. Translation: DAA10779.1 .
    PIRi S66686. RGBYS3.
    RefSeqi NP_014639.1. NM_001183258.1.

    3D structure databases

    ProteinModelPortali P22579.
    SMRi P22579. Positions 219-287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34400. 534 interactions.
    DIPi DIP-597N.
    IntActi P22579. 84 interactions.
    MINTi MINT-422975.
    STRINGi 4932.YOL004W.

    Proteomic databases

    MaxQBi P22579.
    PaxDbi P22579.
    PeptideAtlasi P22579.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL004W ; YOL004W ; YOL004W .
    GeneIDi 854158.
    KEGGi sce:YOL004W.

    Organism-specific databases

    CYGDi YOL004w.
    SGDi S000005364. SIN3.

    Phylogenomic databases

    eggNOGi COG5602.
    GeneTreei ENSGT00390000007239.
    HOGENOMi HOG000248545.
    KOi K11644.
    OMAi REQKPIQ.
    OrthoDBi EOG7T4MTQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33421-MONOMER.

    Miscellaneous databases

    NextBioi 975926.
    PROi P22579.

    Gene expression databases

    Genevestigatori P22579.

    Family and domain databases

    Gene3Di 1.20.1160.11. 3 hits.
    InterProi IPR013194. HDAC_interact.
    IPR003822. PAH.
    [Graphical view ]
    Pfami PF02671. PAH. 3 hits.
    PF08295. Sin3_corepress. 1 hit.
    [Graphical view ]
    SMARTi SM00761. HDAC_interact. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47762. SSF47762. 3 hits.
    PROSITEi PS51477. PAH. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs."
      Wang H., Clark I., Nicholson P.R., Herskowitz I., Stillman D.J.
      Mol. Cell. Biol. 10:5927-5936(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: S288c / GRF88.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [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. "RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes."
      Vidal M., Strich R., Easton Esposito R., Gaber R.F.
      Mol. Cell. Biol. 11:6306-6316(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "The Saccharomyces cerevisiae GAM2/SIN3 protein plays a role in both activation and repression of transcription."
      Yoshimoto H., Ohmae M., Yamashita I.
      Mol. Gen. Genet. 233:327-330(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein."
      Wang H., Stillman D.J.
      Mol. Cell. Biol. 13:1805-1814(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Evidence that the transcriptional regulators SIN3 and RPD3, and a novel gene (SDS3) with similar functions, are involved in transcriptional silencing in S. cerevisiae."
      Vannier D., Balderes D., Shore D.
      Genetics 144:1343-1353(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators."
      Kasten M.M., Dorland S., Stillman D.J.
      Mol. Cell. Biol. 17:4852-4858(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE RPD3 COMPLEX.
    9. "Identification of the Saccharomyces cerevisiae genes STB1-STB5 encoding Sin3p binding proteins."
      Kasten M.M., Stillman D.J.
      Mol. Gen. Genet. 256:376-386(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STB1.
    10. "Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo."
      Kadosh D., Struhl K.
      Mol. Cell. Biol. 18:5121-5127(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RPD3 COMPLEX.
    11. "Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3."
      Rundlett S.E., Carmen A.A., Suka N., Turner B.M., Grunstein M.
      Nature 392:831-835(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae."
      Sun Z.-W., Hampsey M.
      Genetics 152:921-932(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RPD3 COMPLEX.
    13. "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase."
      Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.
      EMBO J. 19:3739-3749(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESS1.
    14. "Combinatorial regulation of phospholipid biosynthetic gene expression by the UME6, SIN3 and RPD3 genes."
      Elkhaimi M., Kaadige M.R., Kamath D., Jackson J.C., Biliran H. Jr., Lopes J.M.
      Nucleic Acids Res. 28:3160-3167(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Identification of the Sin3-binding site in Ume6 defines a two-step process for conversion of Ume6 from a transcriptional repressor to an activator in yeast."
      Washburn B.K., Easton Esposito R.
      Mol. Cell. Biol. 21:2057-2069(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UME6.
    16. "Opposite role of yeast ING family members in p53-dependent transcriptional activation."
      Nourani A., Howe L., Pray-Grant M.G., Workman J.L., Grant P.A., Cote J.
      J. Biol. Chem. 278:19171-19175(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RPD3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Loss of Sin3/Rpd3 histone deacetylase restores the DNA damage response in checkpoint-deficient strains of Saccharomyces cerevisiae."
      Scott K.L., Plon S.E.
      Mol. Cell. Biol. 23:4522-4531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RPD3 COMPLEX.
    18. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    19. "The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase."
      Schroeder M., Clark R., Liu C.Y., Kaufman R.J.
      EMBO J. 23:2281-2292(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RPD3 COMPLEX.
    20. "The Rpd3-Sin3 histone deacetylase regulates replication timing and enables intra-S origin control in Saccharomyces cerevisiae."
      Aparicio J.G., Viggiani C.J., Gibson D.G., Aparicio O.M.
      Mol. Cell. Biol. 24:4769-4780(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes."
      De Nadal E., Zapater M., Alepuz P.M., Sumoy L., Mas G., Posas F.
      Nature 427:370-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RPD3 COMPLEX.
    22. "Saccharomyces cerevisiae Sin3p facilitates DNA double-strand break repair."
      Jazayeri A., McAinsh A.D., Jackson S.P.
      Proc. Natl. Acad. Sci. U.S.A. 101:1644-1649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RPD3 COMPLEX.
    23. "Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex."
      Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J., Washburn M.P., Workman J.L.
      Biochim. Biophys. Acta 1731:77-87(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RPD3C(L) COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    24. Cited for: IDENTIFICATION IN THE RPD3C(L) AND RPD3C(S) COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RPD3C(S) COMPLEX.
    25. "Genes determining yeast replicative life span in a long-lived genetic background."
      Kaeberlein M., Kirkland K.T., Fields S., Kennedy B.K.
      Mech. Ageing Dev. 126:491-504(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    27. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303; THR-304; SER-316 AND SER-1046, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSIN3_YEAST
    AccessioniPrimary (citable) accession number: P22579
    Secondary accession number(s): D6W263, Q08049
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1660 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3