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P38811 (TRA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription-associated protein 1
Alternative name(s):
p400 kDa component of SAGA
Gene names
Name:TRA1
Ordered Locus Names:YHR099W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length3744 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Subunit structure

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. Ref.3 Ref.4 Ref.5 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus Probable.

Domain

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

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.

Sequence similarities

Belongs to the PI3/PI4-kinase family. TRA1 subfamily.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 1 PI3K/PI4K domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 37443743Transcription-associated protein 1
PRO_0000088854

Regions

Domain2622 – 3177556FAT
Domain3414 – 3711298PI3K/PI4K
Domain3712 – 374433FATC

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.13
Modified residue1721Phosphoserine Ref.11 Ref.12
Modified residue5421Phosphoserine Ref.11 Ref.12

Experimental info

Mutagenesis2411L → 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.
Mutagenesis6041F → 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.
Mutagenesis27331W → 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.
Mutagenesis31451S → 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.
Mutagenesis32221L → 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.
Mutagenesis33021D → 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.

Sequences

Sequence LengthMass (Da)Tools
P38811 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: AE3588676F5D5777

FASTA3,744433,180
        10         20         30         40         50         60 
MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA VIPLLLNQLK 

        70         80         90        100        110        120 
EVPISYDAHS PEQKLRNSML DIFNRCLMNQ TFQPYAMEVL EFLLSVLPKE NEENGILCMK 

       130        140        150        160        170        180 
VLTTLFKSFK SILQDKLDSF IRIIIQIYKN TPNLINQTFY EAGKAEQGDL DSPKEPQADE 

       190        200        210        220        230        240 
LLDEFSKNDE EKDFPSKQSS TEPRFENSTS SNGLRSSMFS FKILSECPIT MVTLYSSYKQ 

       250        260        270        280        290        300 
LTSTSLPEFT PLIMNLLNIQ IKQQQEAREQ AESRGEHFTS ISTEIINRPA YCDFILAQIK 

       310        320        330        340        350        360 
ATSFLAYVFI RGYAPEFLQD YVNFVPDLII RLLQDCPSEL SSARKELLHA TRHILSTNYK 

       370        380        390        400        410        420 
KLFLPKLDYL FDERILIGNG FTMHETLRPL AYSTVADFIH NIRSELQLSE IEKTIKIYTG 

       430        440        450        460        470        480 
YLLDESLALT VQIMSAKLLL NLVERILKLG KENPQEAPRA KKLLMIIIDS YMNRFKTLNR 

       490        500        510        520        530        540 
QYDTIMKYYG RYETHKKEKA EKLKNSIQDN DKESEEFMRK VLEPSDDDHL MPQPKKEDIN 

       550        560        570        580        590        600 
DSPDVEMTES DKVVKNDVEM FDIKNYAPIL LLPTPTNDPI KDAFYLYRTL MSFLKTIIHD 

       610        620        630        640        650        660 
LKVFNPPPNE YTVANPKLWA SVSRVFSYEE VIVFKDLFHE CIIGLKFFKD HNEKLSPETT 

       670        680        690        700        710        720 
KKHFDISMPS LPVSATKDAR ELMDYLAFMF MQMDNATFNE IIEQELPFVY ERMLEDSGLL 

       730        740        750        760        770        780 
HVAQSFLTSE ITSPNFAGIL LRFLKGKLKD LGNVDFNTSN VLIRLFKLSF MSVNLFPNIN 

       790        800        810        820        830        840 
EVVLLPHLND LILNSLKYST TAEEPLVYFY LIRTLFRSIG GGRFENLYRS IKPILQVLLQ 

       850        860        870        880        890        900 
SLNQMILTAR LPHERELYVE LCITVPVRLS VLAPYLPFLM KPLVFALQQY PDLVSQGLRT 

       910        920        930        940        950        960 
LELCIDNLTA EYFDPIIEPV IDDVSKALFN LLQPQPFNHA ISHNVVRILG KLGGRNRQFL 

       970        980        990       1000       1010       1020 
KPPTDLTEKT ELDIDAIADF KINGMPEDVP LSVTPGIQSA LNILQSYKSD IHYRKSAYKY 

      1030       1040       1050       1060       1070       1080 
LTCVLLLMTK SSAEFPTNYT ELLKTAVNSI KLERIGIEKN FDLEPTVNKR DYSNQENLFL 

      1090       1100       1110       1120       1130       1140 
RLLESVFYAT SIKELKDDAM DLLNNLLDHF CLLQVNTTLL NKRNYNGTFN IDLKNPNFML 

      1150       1160       1170       1180       1190       1200 
DSSLILDAIP FALSYYIPEV REVGVLAYKR IYEKSCLIYG EELALSHSFI PELAKQFIHL 

      1210       1220       1230       1240       1250       1260 
CYDETYYNKR GGVLGIKVLI DNVKSSSVFL KKYQYNLANG LLFVLKDTQS EAPSAITDSA 

      1270       1280       1290       1300       1310       1320 
EKLLIDLLSI TFADVKEEDL GNKVLENTLT DIVCELSNAN PKVRNACQKS LHTISNLTGI 

      1330       1340       1350       1360       1370       1380 
PIVKLMDHSK QFLLSPIFAK PLRALPFTMQ IGNVDAITFC LSLPNTFLTF NEELFRLLQE 

      1390       1400       1410       1420       1430       1440 
SIVLADAEDE SLSTNIQKTT EYSTSEQLVQ LRIACIKLLA IALKNEEFAT AQQGNIRIRI 

      1450       1460       1470       1480       1490       1500 
LAVFFKTMLK TSPEIINTTY EALKGSLAEN SKLPKELLQN GLKPLLMNLS DHQKLTVPGL 

      1510       1520       1530       1540       1550       1560 
DALSKLLELL IAYFKVEIGR KLLDHLTAWC RVEVLDTLFG QDLAEQMPTK IIVSIINIFH 

      1570       1580       1590       1600       1610       1620 
LLPPQADMFL NDLLLKVMLL ERKLRLQLDS PFRTPLARYL NRFHNPVTEY FKKNMTLRQL 

      1630       1640       1650       1660       1670       1680 
VLFMCNIVQR PEAKELAEDF EKELDNFYDF YISNIPKNQV RVVSFFTNMV DLFNTMVITN 

      1690       1700       1710       1720       1730       1740 
GDEWLKKKGN MILKLKDMLN LTLKTIKENS FYIDHLQLNQ SIAKFQALYL RFTELSERDQ 

      1750       1760       1770       1780       1790       1800 
NPLLLDFIDF SFSNGIKASY SLKKFIFHNI IASSNKEKQN NFINDATLFV LSDKCLDARI 

      1810       1820       1830       1840       1850       1860 
FVLKNVINST LIYEVATSGS LKSYLVEDKK PKWLELLHNK IWKNSNAILA YDVLDHHDLF 

      1870       1880       1890       1900       1910       1920 
RFELLQLSAI FIKADPEIIA EIKKDIIKFC WNFIKLEDTL IKQSAYLVTS YFISKFDFPI 

      1930       1940       1950       1960       1970       1980 
KVVTQVFVAL LRSSHVEARY LVKQSLDVLT PVLHERMNAA GTPDTWINWV KRVMVENSSS 

      1990       2000       2010       2020       2030       2040 
QNNILYQFLI SHPDLFFNSR DLFISNIIHH MNKITFMSNS NSDSHTLAID LASLILYWEN 

      2050       2060       2070       2080       2090       2100 
KTLEITNVNN TKTDSDGDVV MSDSKSDINP VEADTTAIIV DANNNSPISL HLREACTAFL 

      2110       2120       2130       2140       2150       2160 
IRYVCASNHR AIETELGLRA INILSELISD KHWTNVNVKL VYFEKFLIFQ DLDSENILYY 

      2170       2180       2190       2200       2210       2220 
CMNALDVLYV FFKNKTKEWI MENLPTIQNL LEKCIKSDHH DVQEALQKVL QVIMKAIKAQ 

      2230       2240       2250       2260       2270       2280 
GVSVIIEEES PGKTFIQMLT SVITQDLQET SSVTAGVTLA WVLFMNFPDN IVPLLTPLMK 

      2290       2300       2310       2320       2330       2340 
TFSKLCKDHL SISQPKDAMA LEEARITTKL LEKVLYILSL KVSLLGDSRR PFLSTVALLI 

      2350       2360       2370       2380       2390       2400 
DHSMDQNFLR KIVNMSRSWI FNTEIFPTVK EKAAILTKML AFEIRGEPSL SKLFYEIVLK 

      2410       2420       2430       2440       2450       2460 
LFDQEHFNNT EITVRMEQPF LVGTRVEDIG IRKRFMTILD NSLERDIKER LYYVIRDQNW 

      2470       2480       2490       2500       2510       2520 
EFIADYPWLN QALQLLYGSF NREKELSLKN IYCLSPPSIL QEYLPENAEM VTEVNDLELS 

      2530       2540       2550       2560       2570       2580 
NFVKGHIASM QGLCRIISSD FIDSLIEIFY QDPKAIHRAW VTLFPQVYKS IPKNEKYGFV 

      2590       2600       2610       2620       2630       2640 
RSIITLLSKP YHTRQISSRT NVINMLLDSI SKIESLELPP HLVKYLAISY NAWYQSINIL 

      2650       2660       2670       2680       2690       2700 
ESIQSNTSID NTKIIEANED ALLELYVNLQ EEDMFYGLWR RRAKYTETNI GLSYEQIGLW 

      2710       2720       2730       2740       2750       2760 
DKAQQLYEVA QVKARSGALP YSQSEYALWE DNWIQCAEKL QHWDVLTELA KHEGFTDLLL 

      2770       2780       2790       2800       2810       2820 
ECGWRVADWN SDRDALEQSV KSVMDVPTPR RQMFKTFLAL QNFAESRKGD QEVRKLCDEG 

      2830       2840       2850       2860       2870       2880 
IQLSLIKWVS LPIRYTPAHK WLLHGFQQYM EFLEATQIYA NLHTTTVQNL DSKAQEIKRI 

      2890       2900       2910       2920       2930       2940 
LQAWRDRLPN TWDDVNMWND LVTWRQHAFQ VINNAYLPLI PALQQSNSNS NINTHAYRGY 

      2950       2960       2970       2980       2990       3000 
HEIAWVINRF AHVARKHNMP DVCISQLARI YTLPNIEIQE AFLKLREQAK CHYQNMNELT 

      3010       3020       3030       3040       3050       3060 
TGLDVISNTN LVYFGTVQKA EFFTLKGMFL SKLRAYEEAN QAFATAVQID LNLAKAWAQW 

      3070       3080       3090       3100       3110       3120 
GFFNDRRLSE EPNNISFASN AISCYLQAAG LYKNSKIREL LCRILWLISI DDASGMLTNA 

      3130       3140       3150       3160       3170       3180 
FDSFRGEIPV WYWITFIPQL LTSLSHKEAN MVRHILIRIA KSYPQALHFQ LRTTKEDFAV 

      3190       3200       3210       3220       3230       3240 
IQRQTMAVMG DKPDTNDRNG RRQPWEYLQE LNNILKTAYP LLALSLESLV AQINDRFKST 

      3250       3260       3270       3280       3290       3300 
TDEDLFRLIN VLLIDGTLNY NRLPFPRKNP KLPENTEKNL VKFSTTLLAP YIRPKFNADF 

      3310       3320       3330       3340       3350       3360 
IDNKPDYETY IKRLRYWRRR LENKLDRASK KENLEVLCPH LSNFHHQKFE DIEIPGQYLL 

      3370       3380       3390       3400       3410       3420 
NKDNNVHFIK IARFLPTVDF VRGTHSSYRR LMIRGHDGSV HSFAVQYPAV RHSRREERMF 

      3430       3440       3450       3460       3470       3480 
QLYRLFNKSL SKNVETRRRS IQFNLPIAIP LSPQVRIMND SVSFTTLHEI HNEFCKKKGF 

      3490       3500       3510       3520       3530       3540 
DPDDIQDFMA DKLNAAHDDA LPAPDMTILK VEIFNSIQTM FVPSNVLKDH FTSLFTQFED 

      3550       3560       3570       3580       3590       3600 
FWLFRKQFAS QYSSFVFMSY MMMINNRTPH KIHVDKTSGN VFTLEMLPSR FPYERVKPLL 

      3610       3620       3630       3640       3650       3660 
KNHDLSLPPD SPIFHNNEPV PFRLTPNIQS LIGDSALEGI FAVNLFTISR ALIEPDNELN 

      3670       3680       3690       3700       3710       3720 
TYLALFIRDE IISWFSNLHR PIIENPQLRE MVQTNVDLII RKVAQLGHLN STPTVTTQFI 

      3730       3740 
LDCIGSAVSP RNLARTDVNF MPWF 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes."
Saleh A., Schieltz D., Ting N., McMahon S.B., Litchfield D.W., Yates J.R. III, Lees-Miller S.P., Cole M.D., Brandl C.J.
J. Biol. Chem. 273:26559-26565(1998) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00060 Genomic DNA. Translation: AAB68923.1.
BK006934 Genomic DNA. Translation: DAA06793.1.
PIRS46715.
RefSeqNP_011967.1. NM_001179229.1.

3D structure databases

ProteinModelPortalP38811.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36532. 192 interactions.
DIPDIP-805N.
IntActP38811. 69 interactions.
MINTMINT-627837.
STRING4932.YHR099W.

Proteomic databases

PaxDbP38811.
PeptideAtlasP38811.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR099W; YHR099W; YHR099W.
GeneID856499.
KEGGsce:YHR099W.

Organism-specific databases

CYGDYHR099w.
SGDS000001141. TRA1.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00390000017961.
HOGENOMHOG000160814.
KOK08874.
OMAVDFMGAQ.
OrthoDBEOG7PCJR4.

Enzyme and pathway databases

BioCycYEAST:G3O-31144-MONOMER.

Gene expression databases

GenevestigatorP38811.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.10.10. 7 hits.
1.25.40.10. 2 hits.
InterProIPR011989. 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]
PfamPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 12 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982215.
PROP38811.

Entry information

Entry nameTRA1_YEAST
AccessionPrimary (citable) accession number: P38811
Secondary accession number(s): D3DL49
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families