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P38811

- TRA1_YEAST

UniProt

P38811 - TRA1_YEAST

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Protein

Transcription-associated protein 1

Gene

TRA1

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

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 Curated

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-acetylserine1 Publication
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2622 – 3177556FATPROSITE-ProRule annotationAdd
BLAST
Domaini3414 – 3711298PI3K/PI4KAdd
BLAST
Domaini3712 – 374433FATCPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family. TRA1 subfamily.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00390000017961.
HOGENOMiHOG000160814.
InParanoidiP38811.
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_dom.
[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

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        10         20         30         40         50
MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA
60 70 80 90 100
VIPLLLNQLK EVPISYDAHS PEQKLRNSML DIFNRCLMNQ TFQPYAMEVL
110 120 130 140 150
EFLLSVLPKE NEENGILCMK VLTTLFKSFK SILQDKLDSF IRIIIQIYKN
160 170 180 190 200
TPNLINQTFY EAGKAEQGDL DSPKEPQADE LLDEFSKNDE EKDFPSKQSS
210 220 230 240 250
TEPRFENSTS SNGLRSSMFS FKILSECPIT MVTLYSSYKQ LTSTSLPEFT
260 270 280 290 300
PLIMNLLNIQ IKQQQEAREQ AESRGEHFTS ISTEIINRPA YCDFILAQIK
310 320 330 340 350
ATSFLAYVFI RGYAPEFLQD YVNFVPDLII RLLQDCPSEL SSARKELLHA
360 370 380 390 400
TRHILSTNYK KLFLPKLDYL FDERILIGNG FTMHETLRPL AYSTVADFIH
410 420 430 440 450
NIRSELQLSE IEKTIKIYTG YLLDESLALT VQIMSAKLLL NLVERILKLG
460 470 480 490 500
KENPQEAPRA KKLLMIIIDS YMNRFKTLNR QYDTIMKYYG RYETHKKEKA
510 520 530 540 550
EKLKNSIQDN DKESEEFMRK VLEPSDDDHL MPQPKKEDIN DSPDVEMTES
560 570 580 590 600
DKVVKNDVEM FDIKNYAPIL LLPTPTNDPI KDAFYLYRTL MSFLKTIIHD
610 620 630 640 650
LKVFNPPPNE YTVANPKLWA SVSRVFSYEE VIVFKDLFHE CIIGLKFFKD
660 670 680 690 700
HNEKLSPETT KKHFDISMPS LPVSATKDAR ELMDYLAFMF MQMDNATFNE
710 720 730 740 750
IIEQELPFVY ERMLEDSGLL HVAQSFLTSE ITSPNFAGIL LRFLKGKLKD
760 770 780 790 800
LGNVDFNTSN VLIRLFKLSF MSVNLFPNIN EVVLLPHLND LILNSLKYST
810 820 830 840 850
TAEEPLVYFY LIRTLFRSIG GGRFENLYRS IKPILQVLLQ SLNQMILTAR
860 870 880 890 900
LPHERELYVE LCITVPVRLS VLAPYLPFLM KPLVFALQQY PDLVSQGLRT
910 920 930 940 950
LELCIDNLTA EYFDPIIEPV IDDVSKALFN LLQPQPFNHA ISHNVVRILG
960 970 980 990 1000
KLGGRNRQFL KPPTDLTEKT ELDIDAIADF KINGMPEDVP LSVTPGIQSA
1010 1020 1030 1040 1050
LNILQSYKSD IHYRKSAYKY LTCVLLLMTK SSAEFPTNYT ELLKTAVNSI
1060 1070 1080 1090 1100
KLERIGIEKN FDLEPTVNKR DYSNQENLFL RLLESVFYAT SIKELKDDAM
1110 1120 1130 1140 1150
DLLNNLLDHF CLLQVNTTLL NKRNYNGTFN IDLKNPNFML DSSLILDAIP
1160 1170 1180 1190 1200
FALSYYIPEV REVGVLAYKR IYEKSCLIYG EELALSHSFI PELAKQFIHL
1210 1220 1230 1240 1250
CYDETYYNKR GGVLGIKVLI DNVKSSSVFL KKYQYNLANG LLFVLKDTQS
1260 1270 1280 1290 1300
EAPSAITDSA EKLLIDLLSI TFADVKEEDL GNKVLENTLT DIVCELSNAN
1310 1320 1330 1340 1350
PKVRNACQKS LHTISNLTGI PIVKLMDHSK QFLLSPIFAK PLRALPFTMQ
1360 1370 1380 1390 1400
IGNVDAITFC LSLPNTFLTF NEELFRLLQE SIVLADAEDE SLSTNIQKTT
1410 1420 1430 1440 1450
EYSTSEQLVQ LRIACIKLLA IALKNEEFAT AQQGNIRIRI LAVFFKTMLK
1460 1470 1480 1490 1500
TSPEIINTTY EALKGSLAEN SKLPKELLQN GLKPLLMNLS DHQKLTVPGL
1510 1520 1530 1540 1550
DALSKLLELL IAYFKVEIGR KLLDHLTAWC RVEVLDTLFG QDLAEQMPTK
1560 1570 1580 1590 1600
IIVSIINIFH LLPPQADMFL NDLLLKVMLL ERKLRLQLDS PFRTPLARYL
1610 1620 1630 1640 1650
NRFHNPVTEY FKKNMTLRQL VLFMCNIVQR PEAKELAEDF EKELDNFYDF
1660 1670 1680 1690 1700
YISNIPKNQV RVVSFFTNMV DLFNTMVITN GDEWLKKKGN MILKLKDMLN
1710 1720 1730 1740 1750
LTLKTIKENS FYIDHLQLNQ SIAKFQALYL RFTELSERDQ NPLLLDFIDF
1760 1770 1780 1790 1800
SFSNGIKASY SLKKFIFHNI IASSNKEKQN NFINDATLFV LSDKCLDARI
1810 1820 1830 1840 1850
FVLKNVINST LIYEVATSGS LKSYLVEDKK PKWLELLHNK IWKNSNAILA
1860 1870 1880 1890 1900
YDVLDHHDLF RFELLQLSAI FIKADPEIIA EIKKDIIKFC WNFIKLEDTL
1910 1920 1930 1940 1950
IKQSAYLVTS YFISKFDFPI KVVTQVFVAL LRSSHVEARY LVKQSLDVLT
1960 1970 1980 1990 2000
PVLHERMNAA GTPDTWINWV KRVMVENSSS QNNILYQFLI SHPDLFFNSR
2010 2020 2030 2040 2050
DLFISNIIHH MNKITFMSNS NSDSHTLAID LASLILYWEN KTLEITNVNN
2060 2070 2080 2090 2100
TKTDSDGDVV MSDSKSDINP VEADTTAIIV DANNNSPISL HLREACTAFL
2110 2120 2130 2140 2150
IRYVCASNHR AIETELGLRA INILSELISD KHWTNVNVKL VYFEKFLIFQ
2160 2170 2180 2190 2200
DLDSENILYY CMNALDVLYV FFKNKTKEWI MENLPTIQNL LEKCIKSDHH
2210 2220 2230 2240 2250
DVQEALQKVL QVIMKAIKAQ GVSVIIEEES PGKTFIQMLT SVITQDLQET
2260 2270 2280 2290 2300
SSVTAGVTLA WVLFMNFPDN IVPLLTPLMK TFSKLCKDHL SISQPKDAMA
2310 2320 2330 2340 2350
LEEARITTKL LEKVLYILSL KVSLLGDSRR PFLSTVALLI DHSMDQNFLR
2360 2370 2380 2390 2400
KIVNMSRSWI FNTEIFPTVK EKAAILTKML AFEIRGEPSL SKLFYEIVLK
2410 2420 2430 2440 2450
LFDQEHFNNT EITVRMEQPF LVGTRVEDIG IRKRFMTILD NSLERDIKER
2460 2470 2480 2490 2500
LYYVIRDQNW EFIADYPWLN QALQLLYGSF NREKELSLKN IYCLSPPSIL
2510 2520 2530 2540 2550
QEYLPENAEM VTEVNDLELS NFVKGHIASM QGLCRIISSD FIDSLIEIFY
2560 2570 2580 2590 2600
QDPKAIHRAW VTLFPQVYKS IPKNEKYGFV RSIITLLSKP YHTRQISSRT
2610 2620 2630 2640 2650
NVINMLLDSI SKIESLELPP HLVKYLAISY NAWYQSINIL ESIQSNTSID
2660 2670 2680 2690 2700
NTKIIEANED ALLELYVNLQ EEDMFYGLWR RRAKYTETNI GLSYEQIGLW
2710 2720 2730 2740 2750
DKAQQLYEVA QVKARSGALP YSQSEYALWE DNWIQCAEKL QHWDVLTELA
2760 2770 2780 2790 2800
KHEGFTDLLL ECGWRVADWN SDRDALEQSV KSVMDVPTPR RQMFKTFLAL
2810 2820 2830 2840 2850
QNFAESRKGD QEVRKLCDEG IQLSLIKWVS LPIRYTPAHK WLLHGFQQYM
2860 2870 2880 2890 2900
EFLEATQIYA NLHTTTVQNL DSKAQEIKRI LQAWRDRLPN TWDDVNMWND
2910 2920 2930 2940 2950
LVTWRQHAFQ VINNAYLPLI PALQQSNSNS NINTHAYRGY HEIAWVINRF
2960 2970 2980 2990 3000
AHVARKHNMP DVCISQLARI YTLPNIEIQE AFLKLREQAK CHYQNMNELT
3010 3020 3030 3040 3050
TGLDVISNTN LVYFGTVQKA EFFTLKGMFL SKLRAYEEAN QAFATAVQID
3060 3070 3080 3090 3100
LNLAKAWAQW GFFNDRRLSE EPNNISFASN AISCYLQAAG LYKNSKIREL
3110 3120 3130 3140 3150
LCRILWLISI DDASGMLTNA FDSFRGEIPV WYWITFIPQL LTSLSHKEAN
3160 3170 3180 3190 3200
MVRHILIRIA KSYPQALHFQ LRTTKEDFAV IQRQTMAVMG DKPDTNDRNG
3210 3220 3230 3240 3250
RRQPWEYLQE LNNILKTAYP LLALSLESLV AQINDRFKST TDEDLFRLIN
3260 3270 3280 3290 3300
VLLIDGTLNY NRLPFPRKNP KLPENTEKNL VKFSTTLLAP YIRPKFNADF
3310 3320 3330 3340 3350
IDNKPDYETY IKRLRYWRRR LENKLDRASK KENLEVLCPH LSNFHHQKFE
3360 3370 3380 3390 3400
DIEIPGQYLL NKDNNVHFIK IARFLPTVDF VRGTHSSYRR LMIRGHDGSV
3410 3420 3430 3440 3450
HSFAVQYPAV RHSRREERMF QLYRLFNKSL SKNVETRRRS IQFNLPIAIP
3460 3470 3480 3490 3500
LSPQVRIMND SVSFTTLHEI HNEFCKKKGF DPDDIQDFMA DKLNAAHDDA
3510 3520 3530 3540 3550
LPAPDMTILK VEIFNSIQTM FVPSNVLKDH FTSLFTQFED FWLFRKQFAS
3560 3570 3580 3590 3600
QYSSFVFMSY MMMINNRTPH KIHVDKTSGN VFTLEMLPSR FPYERVKPLL
3610 3620 3630 3640 3650
KNHDLSLPPD SPIFHNNEPV PFRLTPNIQS LIGDSALEGI FAVNLFTISR
3660 3670 3680 3690 3700
ALIEPDNELN TYLALFIRDE IISWFSNLHR PIIENPQLRE MVQTNVDLII
3710 3720 3730 3740
RKVAQLGHLN STPTVTTQFI LDCIGSAVSP RNLARTDVNF MPWF
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.
InParanoidi P38811.
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_dom.
[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: October 29, 2014
This is version 137 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