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P38811

- TRA1_YEAST

UniProt

P38811 - TRA1_YEAST

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
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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

    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.
    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

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    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

    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 1, 2014
    This is version 136 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