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P22579

- SIN3_YEAST

UniProt

P22579 - SIN3_YEAST

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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

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. transcription coactivator activity Source: SGD
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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
EAF3Q124329EBI-17160,EBI-6281
OPI1P219575EBI-17160,EBI-12555
RPD3P3256112EBI-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.
InParanoidiP22579.
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

        10         20         30         40         50
MSQVWHNSNS QSNDVATSND ATGSNERNEK EPSLQGNKPG FVQQQQRITL
60 70 80 90 100
PSLSALSTKE EDRRDSNGQQ ALTSHAAHIL GYPPPHSNAM PSIATDSALK
110 120 130 140 150
QPHEYHPRPK SSSSSPSINA SLMNAGPAPL PTVGAASFSL SRFDNPLPIK
160 170 180 190 200
APVHTEEPKS YNGLQEEEKA TQRPQDCKEV PAGVQPADAP DPSSNHADAN
210 220 230 240 250
DDNNNNENSH DEDADYRPLN VKDALSYLEQ VKFQFSSRPD IYNLFLDIMK
260 270 280 290 300
DFKSQAIDTP GVIERVSTLF RGYPILIQGF NTFLPQGYRI ECSSNPDDPI
310 320 330 340 350
RVTTPMGTTT VNNNISPSGR GTTDAQELGS FPESDGNGVQ QPSNVPMVPS
360 370 380 390 400
SVYQSEQNQD QQQSLPLLAT SSGLPSIQQP EMPAHRQIPQ SQSLVPQEDA
410 420 430 440 450
KKNVDVEFSQ AISYVNKIKT RFADQPDIYK HFLEILQTYQ REQKPINEVY
460 470 480 490 500
AQVTHLFQNA PDLLEDFKKF LPDSSASANQ QVQHAQQHAQ QQHEAQMHAQ
510 520 530 540 550
AQAQAQAQAQ VEQQKQQQQF LYPASGYYGH PSNRGIPQQN LPPIGSFSPP
560 570 580 590 600
TNGSTVHEAY QDQQHMQPPH FMPLPSIVQH GPNMVHQGIA NENPPLSDLR
610 620 630 640 650
TSLTEQYAPS SIQHQQQHPQ SISPIANTQY GDIPVRPEID LDPSIVPVVP
660 670 680 690 700
EPTEPIENNI SLNEEVTFFE KAKRYIGNKH LYTEFLKILN LYSQDILDLD
710 720 730 740 750
DLVEKVDFYL GSNKELFTWF KNFVGYQEKT KCIENIVHEK HRLDLDLCEA
760 770 780 790 800
FGPSYKRLPK SDTFMPCSGR DDMCWEVLND EWVGHPVWAS EDSGFIAHRK
810 820 830 840 850
NQYEETLFKI EEERHEYDFY IESNLRTIQC LETIVNKIEN MTENEKANFK
860 870 880 890 900
LPPGLGHTSM TIYKKVIRKV YDKERGFEII DALHEHPAVT APVVLKRLKQ
910 920 930 940 950
KDEEWRRAQR EWNKVWRELE QKVFFKSLDH LGLTFKQADK KLLTTKQLIS
960 970 980 990 1000
EISSIKVDQT NKKIHWLTPK PKSQLDFDFP DKNIFYDILC LADTFITHTT
1010 1020 1030 1040 1050
AYSNPDKERL KDLLKYFISL FFSISFEKIE ESLYSHKQNV SESSGSDDGS
1060 1070 1080 1090 1100
SIASRKRPYQ QEMSLLDILH RSRYQKLKRS NDEDGKVPQL SEPPEEEPNT
1110 1120 1130 1140 1150
IEEEELIDEE AKNPWLTGNL VEEANSQGII QNRSIFNLFA NTNIYIFFRH
1160 1170 1180 1190 1200
WTTIYERLLE IKQMNERVTK EINTRSTVTF AKDLDLLSSQ LSEMGLDFVG
1210 1220 1230 1240 1250
EDAYKQVLRL SRRLINGDLE HQWFEESLRQ AYNNKAFKLY TIDKVTQSLV
1260 1270 1280 1290 1300
KHAHTLMTDA KTAEIMALFV KDRNASTTSA KDQIIYRLQV RSHMSNTENM
1310 1320 1330 1340 1350
FRIEFDKRTL HVSIQYIALD DLTLKEPKAD EDKWKYYVTS YALPHPTEGI
1360 1370 1380 1390 1400
PHEKLKIPFL ERLIEFGQDI DGTEVDEEFS PEGISVSTLK IKIQPITYQL
1410 1420 1430 1440 1450
HIENGSYDVF TRKATNKYPT IANDNTQKGM VSQKKELISK FLDCAVGLRN
1460 1470 1480 1490 1500
NLDEAQKLSM QKKWENLKDS IAKTSAGNQG IESETEKGKI TKQEQSDNLD
1510 1520 1530
SSTASVLPAS ITTVPQDDNI ETTGNTESSD KGAKIQ
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.
InParanoidi P22579.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 141 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