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P38811

- TRA1_YEAST

UniProt

P38811 - TRA1_YEAST

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Protein

Transcription-associated protein 1

Gene
TRA1, YHR099W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential component of histone acetyltransferase (HAT) complexes, which serves as a target for activators during recruitment of HAT complexes. Essential for vegetative growth. Functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.2 Publications

GO - Molecular functioni

  1. phosphotransferase activity, alcohol group as acceptor Source: InterPro
  2. protein binding Source: IntAct

GO - Biological processi

  1. DNA repair Source: SGD
  2. histone acetylation Source: SGD
  3. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-31144-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription-associated protein 1
Alternative name(s):
p400 kDa component of SAGA
Gene namesi
Name:TRA1
Ordered Locus Names:YHR099W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR099w.
SGDiS000001141. TRA1.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: SGD
  2. nucleus Source: SGD
  3. SAGA complex Source: SGD
  4. SLIK (SAGA-like) complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi241 – 2411L → S in TRA1-2; when associated with L-604; R-2733; P-3145; S-3222 and G-3302. Defects in its ability to interact with acidic activators.
Mutagenesisi604 – 6041F → L in TRA1-2; when associated with S-241; R-2733; P-3145; S-3222 and G-3302. Defects in its ability to interact with acidic activators.
Mutagenesisi2733 – 27331W → R in TRA1-2; when associated with S-241; L-604; P-3145; S-3222 and G-3302. Defects in its ability to interact with acidic activators.
Mutagenesisi3145 – 31451S → P in TRA1-2; when associated with S-241; L-604; R-2733; S-3222 and G-3302. Defects in its ability to interact with acidic activators.
Mutagenesisi3222 – 32221L → S in TRA1-2; when associated with S-241; L-604; R-2733; P-3145 and G-3302. Defects in its ability to interact with acidic activators.
Mutagenesisi3302 – 33021D → G in TRA1-2; when associated with S-241; L-604; R-2733; P-3145 and S-3222. Defects in its ability to interact with acidic activators.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 37443743Transcription-associated protein 1PRO_0000088854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei172 – 1721Phosphoserine2 Publications
Modified residuei542 – 5421Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP38811.
PaxDbiP38811.
PeptideAtlasiP38811.

Expressioni

Gene expression databases

GenevestigatoriP38811.

Interactioni

Subunit structurei

Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7,TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Also identified in the NuA4 complex with ESA1. Identified in the Ada.spt complex with ADA3 and SPT7.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADA2Q0233623EBI-24638,EBI-2186
ESA1Q0864910EBI-24638,EBI-6648
HFI1Q120608EBI-24638,EBI-8287
NGG1P324943EBI-24638,EBI-2192
SPT7P351779EBI-24638,EBI-17958
SWC4P532014EBI-24638,EBI-23061
YAF9P539304EBI-24638,EBI-28841

Protein-protein interaction databases

BioGridi36532. 192 interactions.
DIPiDIP-805N.
IntActiP38811. 69 interactions.
MINTiMINT-627837.
STRINGi4932.YHR099W.

Structurei

3D structure databases

ProteinModelPortaliP38811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2622 – 3177556FATAdd
BLAST
Domaini3414 – 3711298PI3K/PI4KAdd
BLAST
Domaini3712 – 374433FATCAdd
BLAST

Domaini

The C-terminal domain (2233-2836) is essential for its ability to interact with activators.

Sequence similaritiesi

Contains 1 FAT domain.
Contains 1 FATC domain.
Contains 1 PI3K/PI4K domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00390000017961.
HOGENOMiHOG000160814.
KOiK08874.
OMAiNCARYGR.
OrthoDBiEOG7PCJR4.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.10.10. 7 hits.
1.25.40.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 12 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P38811-1 [UniParc]FASTAAdd to Basket

« Hide

MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA     50
VIPLLLNQLK EVPISYDAHS PEQKLRNSML DIFNRCLMNQ TFQPYAMEVL 100
EFLLSVLPKE NEENGILCMK VLTTLFKSFK SILQDKLDSF IRIIIQIYKN 150
TPNLINQTFY EAGKAEQGDL DSPKEPQADE LLDEFSKNDE EKDFPSKQSS 200
TEPRFENSTS SNGLRSSMFS FKILSECPIT MVTLYSSYKQ LTSTSLPEFT 250
PLIMNLLNIQ IKQQQEAREQ AESRGEHFTS ISTEIINRPA YCDFILAQIK 300
ATSFLAYVFI RGYAPEFLQD YVNFVPDLII RLLQDCPSEL SSARKELLHA 350
TRHILSTNYK KLFLPKLDYL FDERILIGNG FTMHETLRPL AYSTVADFIH 400
NIRSELQLSE IEKTIKIYTG YLLDESLALT VQIMSAKLLL NLVERILKLG 450
KENPQEAPRA KKLLMIIIDS YMNRFKTLNR QYDTIMKYYG RYETHKKEKA 500
EKLKNSIQDN DKESEEFMRK VLEPSDDDHL MPQPKKEDIN DSPDVEMTES 550
DKVVKNDVEM FDIKNYAPIL LLPTPTNDPI KDAFYLYRTL MSFLKTIIHD 600
LKVFNPPPNE YTVANPKLWA SVSRVFSYEE VIVFKDLFHE CIIGLKFFKD 650
HNEKLSPETT KKHFDISMPS LPVSATKDAR ELMDYLAFMF MQMDNATFNE 700
IIEQELPFVY ERMLEDSGLL HVAQSFLTSE ITSPNFAGIL LRFLKGKLKD 750
LGNVDFNTSN VLIRLFKLSF MSVNLFPNIN EVVLLPHLND LILNSLKYST 800
TAEEPLVYFY LIRTLFRSIG GGRFENLYRS IKPILQVLLQ SLNQMILTAR 850
LPHERELYVE LCITVPVRLS VLAPYLPFLM KPLVFALQQY PDLVSQGLRT 900
LELCIDNLTA EYFDPIIEPV IDDVSKALFN LLQPQPFNHA ISHNVVRILG 950
KLGGRNRQFL KPPTDLTEKT ELDIDAIADF KINGMPEDVP LSVTPGIQSA 1000
LNILQSYKSD IHYRKSAYKY LTCVLLLMTK SSAEFPTNYT ELLKTAVNSI 1050
KLERIGIEKN FDLEPTVNKR DYSNQENLFL RLLESVFYAT SIKELKDDAM 1100
DLLNNLLDHF CLLQVNTTLL NKRNYNGTFN IDLKNPNFML DSSLILDAIP 1150
FALSYYIPEV REVGVLAYKR IYEKSCLIYG EELALSHSFI PELAKQFIHL 1200
CYDETYYNKR GGVLGIKVLI DNVKSSSVFL KKYQYNLANG LLFVLKDTQS 1250
EAPSAITDSA EKLLIDLLSI TFADVKEEDL GNKVLENTLT DIVCELSNAN 1300
PKVRNACQKS LHTISNLTGI PIVKLMDHSK QFLLSPIFAK PLRALPFTMQ 1350
IGNVDAITFC LSLPNTFLTF NEELFRLLQE SIVLADAEDE SLSTNIQKTT 1400
EYSTSEQLVQ LRIACIKLLA IALKNEEFAT AQQGNIRIRI LAVFFKTMLK 1450
TSPEIINTTY EALKGSLAEN SKLPKELLQN GLKPLLMNLS DHQKLTVPGL 1500
DALSKLLELL IAYFKVEIGR KLLDHLTAWC RVEVLDTLFG QDLAEQMPTK 1550
IIVSIINIFH LLPPQADMFL NDLLLKVMLL ERKLRLQLDS PFRTPLARYL 1600
NRFHNPVTEY FKKNMTLRQL VLFMCNIVQR PEAKELAEDF EKELDNFYDF 1650
YISNIPKNQV RVVSFFTNMV DLFNTMVITN GDEWLKKKGN MILKLKDMLN 1700
LTLKTIKENS FYIDHLQLNQ SIAKFQALYL RFTELSERDQ NPLLLDFIDF 1750
SFSNGIKASY SLKKFIFHNI IASSNKEKQN NFINDATLFV LSDKCLDARI 1800
FVLKNVINST LIYEVATSGS LKSYLVEDKK PKWLELLHNK IWKNSNAILA 1850
YDVLDHHDLF RFELLQLSAI FIKADPEIIA EIKKDIIKFC WNFIKLEDTL 1900
IKQSAYLVTS YFISKFDFPI KVVTQVFVAL LRSSHVEARY LVKQSLDVLT 1950
PVLHERMNAA GTPDTWINWV KRVMVENSSS QNNILYQFLI SHPDLFFNSR 2000
DLFISNIIHH MNKITFMSNS NSDSHTLAID LASLILYWEN KTLEITNVNN 2050
TKTDSDGDVV MSDSKSDINP VEADTTAIIV DANNNSPISL HLREACTAFL 2100
IRYVCASNHR AIETELGLRA INILSELISD KHWTNVNVKL VYFEKFLIFQ 2150
DLDSENILYY CMNALDVLYV FFKNKTKEWI MENLPTIQNL LEKCIKSDHH 2200
DVQEALQKVL QVIMKAIKAQ GVSVIIEEES PGKTFIQMLT SVITQDLQET 2250
SSVTAGVTLA WVLFMNFPDN IVPLLTPLMK TFSKLCKDHL SISQPKDAMA 2300
LEEARITTKL LEKVLYILSL KVSLLGDSRR PFLSTVALLI DHSMDQNFLR 2350
KIVNMSRSWI FNTEIFPTVK EKAAILTKML AFEIRGEPSL SKLFYEIVLK 2400
LFDQEHFNNT EITVRMEQPF LVGTRVEDIG IRKRFMTILD NSLERDIKER 2450
LYYVIRDQNW EFIADYPWLN QALQLLYGSF NREKELSLKN IYCLSPPSIL 2500
QEYLPENAEM VTEVNDLELS NFVKGHIASM QGLCRIISSD FIDSLIEIFY 2550
QDPKAIHRAW VTLFPQVYKS IPKNEKYGFV RSIITLLSKP YHTRQISSRT 2600
NVINMLLDSI SKIESLELPP HLVKYLAISY NAWYQSINIL ESIQSNTSID 2650
NTKIIEANED ALLELYVNLQ EEDMFYGLWR RRAKYTETNI GLSYEQIGLW 2700
DKAQQLYEVA QVKARSGALP YSQSEYALWE DNWIQCAEKL QHWDVLTELA 2750
KHEGFTDLLL ECGWRVADWN SDRDALEQSV KSVMDVPTPR RQMFKTFLAL 2800
QNFAESRKGD QEVRKLCDEG IQLSLIKWVS LPIRYTPAHK WLLHGFQQYM 2850
EFLEATQIYA NLHTTTVQNL DSKAQEIKRI LQAWRDRLPN TWDDVNMWND 2900
LVTWRQHAFQ VINNAYLPLI PALQQSNSNS NINTHAYRGY HEIAWVINRF 2950
AHVARKHNMP DVCISQLARI YTLPNIEIQE AFLKLREQAK CHYQNMNELT 3000
TGLDVISNTN LVYFGTVQKA EFFTLKGMFL SKLRAYEEAN QAFATAVQID 3050
LNLAKAWAQW GFFNDRRLSE EPNNISFASN AISCYLQAAG LYKNSKIREL 3100
LCRILWLISI DDASGMLTNA FDSFRGEIPV WYWITFIPQL LTSLSHKEAN 3150
MVRHILIRIA KSYPQALHFQ LRTTKEDFAV IQRQTMAVMG DKPDTNDRNG 3200
RRQPWEYLQE LNNILKTAYP LLALSLESLV AQINDRFKST TDEDLFRLIN 3250
VLLIDGTLNY NRLPFPRKNP KLPENTEKNL VKFSTTLLAP YIRPKFNADF 3300
IDNKPDYETY IKRLRYWRRR LENKLDRASK KENLEVLCPH LSNFHHQKFE 3350
DIEIPGQYLL NKDNNVHFIK IARFLPTVDF VRGTHSSYRR LMIRGHDGSV 3400
HSFAVQYPAV RHSRREERMF QLYRLFNKSL SKNVETRRRS IQFNLPIAIP 3450
LSPQVRIMND SVSFTTLHEI HNEFCKKKGF DPDDIQDFMA DKLNAAHDDA 3500
LPAPDMTILK VEIFNSIQTM FVPSNVLKDH FTSLFTQFED FWLFRKQFAS 3550
QYSSFVFMSY MMMINNRTPH KIHVDKTSGN VFTLEMLPSR FPYERVKPLL 3600
KNHDLSLPPD SPIFHNNEPV PFRLTPNIQS LIGDSALEGI FAVNLFTISR 3650
ALIEPDNELN TYLALFIRDE IISWFSNLHR PIIENPQLRE MVQTNVDLII 3700
RKVAQLGHLN STPTVTTQFI LDCIGSAVSP RNLARTDVNF MPWF 3744
Length:3,744
Mass (Da):433,180
Last modified:February 1, 1995 - v1
Checksum:iAE3588676F5D5777
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00060 Genomic DNA. Translation: AAB68923.1.
BK006934 Genomic DNA. Translation: DAA06793.1.
PIRiS46715.
RefSeqiNP_011967.1. NM_001179229.1.

Genome annotation databases

EnsemblFungiiYHR099W; YHR099W; YHR099W.
GeneIDi856499.
KEGGisce:YHR099W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00060 Genomic DNA. Translation: AAB68923.1 .
BK006934 Genomic DNA. Translation: DAA06793.1 .
PIRi S46715.
RefSeqi NP_011967.1. NM_001179229.1.

3D structure databases

ProteinModelPortali P38811.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36532. 192 interactions.
DIPi DIP-805N.
IntActi P38811. 69 interactions.
MINTi MINT-627837.
STRINGi 4932.YHR099W.

Proteomic databases

MaxQBi P38811.
PaxDbi P38811.
PeptideAtlasi P38811.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHR099W ; YHR099W ; YHR099W .
GeneIDi 856499.
KEGGi sce:YHR099W.

Organism-specific databases

CYGDi YHR099w.
SGDi S000001141. TRA1.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00390000017961.
HOGENOMi HOG000160814.
KOi K08874.
OMAi NCARYGR.
OrthoDBi EOG7PCJR4.

Enzyme and pathway databases

BioCyci YEAST:G3O-31144-MONOMER.

Miscellaneous databases

NextBioi 982215.
PROi P38811.

Gene expression databases

Genevestigatori P38811.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.10.10. 7 hits.
1.25.40.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical.
[Graphical view ]
Pfami PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 12 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The ATM-related cofactor Tra1 is a component of the purified SAGA complex."
    Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.
    Mol. Cell 2:863-867(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 149-164; 353-360; 438-445; 603-614; 751-760; 1060-1070; 1124-1134; 1311-1324; 1399-1412; 1451-1464; 1643-1658; 2197-2208; 2389-2399; 2401-2425; 2536-2550; 2601-2612; 2703-2713; 2797-2807; 3239-3247; 3440-3456; 3479-3492 AND 3681-3689, IDENTIFICATION IN A SAGA COMPLEX WITH SPT2; SPT7; SPT8; SPT20; HFI1; ADA2; ADA3 AND GCN5.
  4. Cited for: IDENTIFICATION IN A COMPLEX WITH ADA3 AND SPT7.
  5. "NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p."
    Allard S., Utley R.T., Savard J., Clarke A.S., Grant P.A., Brandl C.J., Pillus L., Workman J.L., Cote J.
    EMBO J. 18:5108-5119(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A NUA4 COMPLEX WITH ESA1.
  6. "Expanded lysine acetylation specificity of Gcn5 in native complexes."
    Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.
    J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
  7. "Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit."
    Brown C.E., Howe L., Sousa K., Alley S.C., Carrozza M.J., Tan S., Workman J.L.
    Science 292:2333-2337(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTANT TRA1-2.
  8. "The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway."
    Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L., Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.
    Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
  9. "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription."
    Sterner D.E., Belotserkovskaya R., Berger S.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
  10. "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation."
    Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.
    Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
  11. "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-172 AND SER-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-172 AND SER-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "Molecular architecture of the S. cerevisiae SAGA complex."
    Wu P.Y., Ruhlmann C., Winston F., Schultz P.
    Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.

Entry informationi

Entry nameiTRA1_YEAST
AccessioniPrimary (citable) accession number: P38811
Secondary accession number(s): D3DL49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Although strongly related to the PI3/PI4-kinase family, it lacks the typical motifs that constitute the catalytic site of PI3/PI4-kinase proteins, suggesting that it may lack such activity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

Similar proteinsi