Reviewed, UniProtKB/Swiss-Prot P38811 (TRA1_YEAST)

Names and origin

Protein names

Recommended name:
    Transcription-associated protein 1
Alternative name(s):
    p400 kDa component of SAGA

Gene names

Name:	TRA1
Ordered Locus Names:	YHR099W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	3744 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.5 Ref.6
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.
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Molecular function	Activator Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: SGD histone acetylation Ref.2 Inferred from direct assay. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from physical interaction. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ASTRA complex Inferred from direct assay. Source: SGD NuA4 histone acetyltransferase complex Ref.4 Inferred from physical interaction. Source: SGD SAGA complex Ref.2 Inferred from direct assay. Source: SGD SLIK (SAGA-like) complex Ref.7 Inferred from physical interaction. Source: SGD
Molecular function	phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro protein binding Ref.3 Ref.4 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADA2	Q02336	1	EBI-24638,EBI-2186
ESA1	Q08649	2	EBI-24638,EBI-6648
NGG1	P32494	1	EBI-24638,EBI-2192
SPT7	P35177	1	EBI-24638,EBI-17958
SWC4	P53201	1	EBI-24638,EBI-23061
YAF9	P53930	1	EBI-24638,EBI-28841

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3744	3744	Transcription-associated protein 1		PRO_0000088854
Regions
	Domain	2622 – 3177	556	FAT
	Domain	3414 – 3711	298	PI3K/PI4K
	Domain	3712 – 3744	33	FATC
Amino acid modifications
	Modified residue	172	1	Phosphoserine Ref.10 Ref.11
	Modified residue	542	1	Phosphoserine Ref.11
	Modified residue	1466	1	Phosphoserine Ref.10
	Modified residue	2788	1	Phosphothreonine Ref.11
Experimental info
	Mutagenesis	241	1	L → 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.
	Mutagenesis	604	1	F → 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.
	Mutagenesis	2733	1	W → 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.
	Mutagenesis	3145	1	S → 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.
	Mutagenesis	3222	1	L → 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.
	Mutagenesis	3302	1	D → 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		Length	Mass (Da)
	P38811-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: AE3588676F5D5777	FASTA	3,744	433,180
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"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: 9885573] [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.
[3]	"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: 9756893] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH ADA3 AND SPT7.
[4]	"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: 10487762] [Abstract] Cited for: IDENTIFICATION IN A NUA4 COMPLEX WITH ESA1.
[5]	"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: 10026213] [Abstract] Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
[6]	"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: 11423663] [Abstract] Cited for: FUNCTION, MUTANT TRA1-2.
[7]	"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: 12446794] [Abstract] Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[8]	"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: 12186975] [Abstract] Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
[9]	"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: 15647753] [Abstract] Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-1466, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-542 AND THR-2788, MASS SPECTROMETRY.
[12]	"Molecular architecture of the S. cerevisiae SAGA complex." Wu P.Y., Ruhlmann C., Winston F., Schultz P. Mol. Cell 15:199-208(2004) [PubMed: 15260971] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00060 Genomic DNA. Translation: AAB68923.1.
PIR	S46715.
RefSeq	NP_011967.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:805N.
IntAct	P38811. 49 interactions.
Proteomic databases
PeptideAtlas	P38811.
PRIDE	P38811.
Genome annotation databases
Ensembl	YHR099W. Saccharomyces cerevisiae. [Contig view]
GeneID	856499.
GenomeReviews	Gene locus YHR099W in contig U00093_GR.
KEGG	sce:YHR099W.
NMPDR	fig|4932.3.peg.3128.
Organism-specific databases
CYGD	YHR099w.
SGD	S000001141. TRA1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38811.
OMA	P38811. PSVIISH.
Gene expression databases
ArrayExpress	P38811.
GermOnline	YHR099W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003152. FATC. IPR000403. PI3/4_kinase_cat. IPR018936. PI3/4_kinase_CS. IPR003151. PIK-rel_kinase_FAT. IPR014009. PIK_FAT. [Graphical view]
Gene3D	G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
Pfam	PF02259. FAT. 1 hit. PF02260. FATC. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS00915. PI3_4_KINASE_1. False negative. PS00916. PI3_4_KINASE_2. False negative. PS50290. PI3_4_KINASE_3. False negative. PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982215.

Entry information

Entry name

TRA1_YEAST

Accession

Primary (citable) accession number: P38811

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)