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Protein

Mediator of RNA polymerase II transcription subunit 15

Gene

GAL11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. It has an important role in the negative regulation of Ty transcription.3 Publications

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD
  • RNA polymerase II transcription coactivator activity involved in preinitiation complex assembly Source: SGD
  • TFIIE-class transcription factor binding Source: SGD
  • TFIIH-class transcription factor binding Source: SGD
  • transcription factor activity, RNA polymerase II transcription factor recruiting Source: SGD
  • transcription factor activity, TFIIE-class binding Source: SGD

GO - Biological processi

  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of invasive growth in response to glucose limitation Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of establishment of protein localization to chromosome Source: SGD
  • RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-33462-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 15
Alternative name(s):
Autonomous replication regulatory protein 3
Basal expression activator protein 1
Defective silencing suppressor protein 4
Mediator complex subunit 15
Transcription regulatory protein GAL11
Ty insertion suppressor protein 13
Gene namesi
Name:GAL11
Synonyms:ABE1, MED15, RAR3, SDS4, SPT13
Ordered Locus Names:YOL051W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL051W.
SGDiS000005411. GAL11.

Subcellular locationi

GO - Cellular componenti

  • core mediator complex Source: SGD
  • mediator complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 10811080Mediator of RNA polymerase II transcription subunit 15PRO_0000096363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei736 – 7361PhosphoserineCombined sources
Modified residuei752 – 7521PhosphoserineCombined sources
Modified residuei783 – 7831PhosphoserineCombined sources
Modified residuei785 – 7851PhosphoserineCombined sources
Modified residuei789 – 7891PhosphoserineCombined sources
Modified residuei793 – 7931PhosphothreonineCombined sources
Modified residuei831 – 8311PhosphoserineCombined sources
Modified residuei1003 – 10031PhosphoserineCombined sources
Modified residuei1008 – 10081PhosphoserineCombined sources
Modified residuei1018 – 10181PhosphoserineCombined sources
Modified residuei1034 – 10341PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP19659.
PeptideAtlasiP19659.
PRIDEiP19659.

PTM databases

iPTMnetiP19659.

Interactioni

Subunit structurei

Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. GAL11/MED15 interacts directly with the activator GAL4.2 Publications

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD
  • TFIIE-class transcription factor binding Source: SGD
  • TFIIH-class transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi34353. 155 interactions.
DIPiDIP-2334N.
IntActiP19659. 16 interactions.
MINTiMINT-635654.

Structurei

Secondary structure

1
1081
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Helixi14 – 3522Combined sources
Helixi41 – 5818Combined sources
Helixi63 – 8927Combined sources
Helixi164 – 1707Combined sources
Helixi172 – 1743Combined sources
Helixi180 – 1834Combined sources
Helixi196 – 1994Combined sources
Helixi201 – 2044Combined sources
Helixi210 – 23223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K0NNMR-A6-90[»]
2LPBNMR-A158-238[»]
ProteinModelPortaliP19659.
SMRiP19659. Positions 6-90, 158-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19659.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati422 – 42321
Repeati424 – 42522
Repeati426 – 42723
Repeati428 – 42924
Repeati430 – 43125
Repeati432 – 43326
Repeati434 – 43527
Repeati436 – 43728
Repeati438 – 43929
Repeati440 – 441210
Repeati442 – 443211
Repeati444 – 445212; approximate
Repeati446 – 447213; approximate
Repeati448 – 449214
Repeati450 – 451215
Repeati452 – 453216
Repeati454 – 455217
Repeati456 – 457218
Repeati458 – 459219
Repeati460 – 461220
Repeati462 – 463221
Repeati464 – 465222
Repeati466 – 467223
Repeati468 – 469224
Repeati470 – 471225
Repeati472 – 473226
Repeati474 – 475227
Repeati476 – 477228
Repeati478 – 479229
Repeati480 – 481230

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni422 – 4816030 X 2 AA approximate tandem repeats of Q-AAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 15812Poly-GlnAdd
BLAST
Compositional biasi674 – 69623Poly-GlnAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 15 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000113522.
InParanoidiP19659.
KOiK15158.
OMAiITSSFKQ.
OrthoDBiEOG7MD514.

Family and domain databases

InterProiIPR003101. KIX_dom.
IPR008626. Mediator_Med15_fun.
[Graphical view]
PfamiPF16987. KIX_2. 1 hit.
PF05397. Med15_fungi. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19659-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAPVQDKD TLSNAERAKN VNGLLQVLMD INTLNGGSSD TADKIRIHAK
60 70 80 90 100
NFEAALFAKS SSKKEYMDSM NEKVAVMRNT YNTRKNAVTA AAANNNIKPV
110 120 130 140 150
EQHHINNLKN SGNSANNMNV NMNLNPQMFL NQQAQARQQV AQQLRNQQQQ
160 170 180 190 200
QQQQQQQQRR QLTPQQQQLV NQMKVAPIPK QLLQRIPNIP PNINTWQQVT
210 220 230 240 250
ALAQQKLLTP QDMEAAKEVY KIHQQLLFKA RLQQQQAQAQ AQANNNNNGL
260 270 280 290 300
PQNGNINNNI NIPQQQQMQP PNSSANNNPL QQQSSQNTVP NVLNQINQIF
310 320 330 340 350
SPEEQRSLLQ EAIETCKNFE KTQLGSTMTE PVKQSFIRKY INQKALRKIQ
360 370 380 390 400
ALRDVKNNNN ANNNGSNLQR AQNVPMNIIQ QQQQQNTNNN DTIATSATPN
410 420 430 440 450
AAAFSQQQNA SSKLYQMQQQ QQAQAQAQAQ AQAQAQAQAQ AQAAQAAQAQ
460 470 480 490 500
AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AHAQHQPSQQ PQQAQQQPNP
510 520 530 540 550
LHGLTPTAKD VEVIKQLSLD ASKTNLRLTD VTNSLSNEEK EKIKMKLKQG
560 570 580 590 600
QKLFVQVSNF APQVYIITKN ENFLKEVFQL RIFVKEILEK CAEGIFVVKL
610 620 630 640 650
DTVDRLIIKY QKYWESMRIQ ILRRQAILRQ QQQMANNNGN PGTTSTGNNN
660 670 680 690 700
NIATQQNMQQ SLQQMQHLQQ LKMQQQQQQQ QQQQQQQQQQ QQQQQQHIYP
710 720 730 740 750
SSTPGVANYS AMANAPGNNI PYMNHKNTSS MDFLNSMENT PKVPVSAAAT
760 770 780 790 800
PSLNKTINGK VNGRTKSNTI PVTSIPSTNK KLSISNAASQ QPTPRSASNT
810 820 830 840 850
AKSTPNTNPS PLKTQTKNGT PNPNNMKTVQ SPMGAQPSYN SAIIENAFRK
860 870 880 890 900
EELLLKDLEI RKLEISSRFK HRQEIFKDSP MDLFMSTLGD CLGIKDEEML
910 920 930 940 950
TSCTIPKAVV DHINGSGKRK PTKAAQRARD QDSIDISIKD NKLVMKSKFN
960 970 980 990 1000
KSNRSYSIAL SNVAAIFKGI GGNFKDLSTL VHSSSPSTSS NMDVGNPRKR
1010 1020 1030 1040 1050
KASVLEISPQ DSIASVLSPD SNIMSDSKKI KVDSPDDPFM TKSGATTSEK
1060 1070 1080
QEVTNEAPFL TSGTSSEQFN VWDWNNWTSA T
Length:1,081
Mass (Da):120,309
Last modified:November 1, 1997 - v3
Checksum:i275C78721B5415C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711N → T in AAA34622 (PubMed:3062377).Curated
Sequence conflicti302 – 3021P → Q in AAA34622 (PubMed:3062377).Curated
Sequence conflicti499 – 4991N → T in AAA34622 (PubMed:3062377).Curated
Sequence conflicti751 – 7511P → Q in AAA34622 (PubMed:3062377).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22481 Genomic DNA. Translation: AAA34622.1.
Z74793 Genomic DNA. Translation: CAA99056.1.
X91067 Genomic DNA. Translation: CAA62537.1.
BK006948 Genomic DNA. Translation: DAA10733.1.
PIRiS66736.
RefSeqiNP_014591.1. NM_001183305.1.

Genome annotation databases

EnsemblFungiiYOL051W; YOL051W; YOL051W.
GeneIDi854106.
KEGGisce:YOL051W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22481 Genomic DNA. Translation: AAA34622.1.
Z74793 Genomic DNA. Translation: CAA99056.1.
X91067 Genomic DNA. Translation: CAA62537.1.
BK006948 Genomic DNA. Translation: DAA10733.1.
PIRiS66736.
RefSeqiNP_014591.1. NM_001183305.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K0NNMR-A6-90[»]
2LPBNMR-A158-238[»]
ProteinModelPortaliP19659.
SMRiP19659. Positions 6-90, 158-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34353. 155 interactions.
DIPiDIP-2334N.
IntActiP19659. 16 interactions.
MINTiMINT-635654.

PTM databases

iPTMnetiP19659.

Proteomic databases

MaxQBiP19659.
PeptideAtlasiP19659.
PRIDEiP19659.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL051W; YOL051W; YOL051W.
GeneIDi854106.
KEGGisce:YOL051W.

Organism-specific databases

EuPathDBiFungiDB:YOL051W.
SGDiS000005411. GAL11.

Phylogenomic databases

HOGENOMiHOG000113522.
InParanoidiP19659.
KOiK15158.
OMAiITSSFKQ.
OrthoDBiEOG7MD514.

Enzyme and pathway databases

BioCyciYEAST:G3O-33462-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP19659.
PROiP19659.

Family and domain databases

InterProiIPR003101. KIX_dom.
IPR008626. Mediator_Med15_fun.
[Graphical view]
PfamiPF16987. KIX_2. 1 hit.
PF05397. Med15_fungi. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GAL11 protein, an auxiliary transcription activator for genes encoding galactose-metabolizing enzymes in Saccharomyces cerevisiae."
    Suzuki Y., Nogi Y., Abe A., Fukasawa T.
    Mol. Cell. Biol. 8:4991-4999(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Erratum
    Suzuki Y., Nogi Y., Abe A., Fukasawa T.
    Mol. Cell. Biol. 12:4806-4806(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
    Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
    Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-352.
    Strain: ATCC 90843 / S288c / FY73.
  6. "GAL11 (SPT13), a transcriptional regulator of diverse yeast genes, affects the phosphorylation state of GAL4, a highly specific transcriptional activator."
    Long R.M., Mylin L.M., Hopper J.E.
    Mol. Cell. Biol. 11:2311-2314(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II."
    Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D.
    Cell 77:599-608(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF MEDIATOR COMPLEX.
  8. "Evidence that Gal11 protein is a target of the Gal4 activation domain in the mediator."
    Jeong C.-J., Yang S.-H., Xie Y., Zhang L., Johnston S.A., Kodadek T.
    Biochemistry 40:9421-9427(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAL4.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. Cited for: NOMENCLATURE.
  12. Cited for: TOPOLOGY OF THE MEDIATOR COMPLEX.
  13. "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription in yeast extracts."
    Nair D., Kim Y., Myers L.C.
    J. Biol. Chem. 280:33739-33748(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
  14. "Mediator expression profiling epistasis reveals a signal transduction pathway with antagonistic submodules and highly specific downstream targets."
    van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P., van Leenen D., Holstege F.C.P.
    Mol. Cell 19:511-522(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  16. "Mediator as a general transcription factor."
    Takagi Y., Kornberg R.D.
    J. Biol. Chem. 281:80-89(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE MEDIATOR COMPLEX.
  17. "Genome-wide location of the coactivator mediator: binding without activation and transient Cdk8 interaction on DNA."
    Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G., van de Peppel J., Werner M., Holstege F.C.P.
    Mol. Cell 22:179-192(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "Activator-specific recruitment of Mediator in vivo."
    Fan X., Chou D.M., Struhl K.
    Nat. Struct. Mol. Biol. 13:117-120(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PROMOTER REGIONS.
  19. "Med19(Rox3) regulates intermodule interactions in the Saccharomyces cerevisiae mediator complex."
    Baidoobonso S.M., Guidi B.W., Myers L.C.
    J. Biol. Chem. 282:5551-5559(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  20. "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 SER-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  21. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-335; SER-736; SER-752; THR-793; SER-1003; SER-1018 AND SER-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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 SER-783; SER-785; SER-789; THR-793; SER-831; SER-1003; SER-1008; SER-1018 AND SER-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Structure of the yeast RNA polymerase II holoenzyme: mediator conformation and polymerase interaction."
    Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.
    Mol. Cell 10:409-415(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.

Entry informationi

Entry nameiMED15_YEAST
AccessioniPrimary (citable) accession number: P19659
Secondary accession number(s): D6W217, Q08221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.