T2FA_YEAST - dbPTM
T2FA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T2FA_YEAST
UniProt AC P41895
Protein Name Transcription initiation factor IIF subunit alpha
Gene Name TFG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 735
Subcellular Localization Nucleus.
Protein Description TFIIF is a general transcription initiation factor that binds to RNA polymerase II. Its functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation..
Protein Sequence MSRRNPPGSRNGGGPTNASPFIKRDRMRRNFLRMRMGQNGSNSSSPGVPNGDNSRGSLVKKDDPEYAEEREKMLLQIGVEADAGRSNVKVKDEDPNEYNEFPLRAIPKEDLENMRTHLLKFQSKKKINPVTDFHLPVRLHRKDTRNLQFQLTRAEIVQRQKEISEYKKKAEQERSTPNSGGMNKSGTVSLNNTVKDGSQTPTVDSVTKDNTANGVNSSIPTVTGSSVPPASPTTVSAVESNGLSNGSTSAANGLDGNASTANLANGRPLVTKLEDAGPAEDPTKVGMVKYDGKEVTNEPEFEEGTMDPLADVAPDGGGRAKRGNLRRKTRQLKVLDENAKKLRFEEFYPWVMEDFDGYNTWVGSYEAGNSDSYVLLSVEDDGSFTMIPADKVYKFTARNKYATLTIDEAEKRMDKKSGEVPRWLMKHLDNIGTTTTRYDRTRRKLKAVADQQAMDEDDRDDNSEVELDYDEEFADDEEAPIIDGNEQENKESEQRIKKEMLQANAMGLRDEEAPSENEEDELFGEKKIDEDGERIKKALQKTELAALYSSDENEINPYLSESDIENKENESPVKKEEDSDTLSKSKRSSPKKQQKKATNAHVHKEPTLRVKSIKNCVIILKGDKKILKSFPEGEWNPQTTKAVDSSNNASNTVPSPIKQEEGLNSTVAEREETPAPTITEKDIIEAIGDGKVNIKEFGKFIRRKYPGAENKKLMFAIVKKLCRKVGNDHMELKKE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
19PhosphorylationGGGPTNASPFIKRDR
CCCCCCCCHHHCHHH		23.5521440633
23AcetylationTNASPFIKRDRMRRN
CCCCHHHCHHHHHHH		48.9322865919
41PhosphorylationMRMGQNGSNSSSPGV
HHCCCCCCCCCCCCC		40.8822369663
43PhosphorylationMGQNGSNSSSPGVPN
CCCCCCCCCCCCCCC		33.6122369663
44PhosphorylationGQNGSNSSSPGVPNG
CCCCCCCCCCCCCCC		44.8122369663
45PhosphorylationQNGSNSSSPGVPNGD
CCCCCCCCCCCCCCC		26.0322369663
54PhosphorylationGVPNGDNSRGSLVKK
CCCCCCCCCCCCCCC		42.6422369663
57PhosphorylationNGDNSRGSLVKKDDP
CCCCCCCCCCCCCCH		28.9530377154
61AcetylationSRGSLVKKDDPEYAE
CCCCCCCCCCHHHHH		60.9425381059
120AcetylationNMRTHLLKFQSKKKI
HHHHHHHHHCCCCCC		47.9522865919
126UbiquitinationLKFQSKKKINPVTDF
HHHCCCCCCCCCCCC		51.9917644757
175PhosphorylationKKAEQERSTPNSGGM
HHHHHHCCCCCCCCC		47.6817287358
176PhosphorylationKAEQERSTPNSGGMN
HHHHHCCCCCCCCCC		32.4817287358
179PhosphorylationQERSTPNSGGMNKSG
HHCCCCCCCCCCCCC		37.6228889911
185PhosphorylationNSGGMNKSGTVSLNN
CCCCCCCCCEEEECC		34.3923749301
187PhosphorylationGGMNKSGTVSLNNTV
CCCCCCCEEEECCCC		17.6322369663
189PhosphorylationMNKSGTVSLNNTVKD
CCCCCEEEECCCCCC		25.8022369663
193PhosphorylationGTVSLNNTVKDGSQT
CEEEECCCCCCCCCC		28.0522369663
195AcetylationVSLNNTVKDGSQTPT
EEECCCCCCCCCCCC		55.0924489116
198PhosphorylationNNTVKDGSQTPTVDS
CCCCCCCCCCCCCCC		40.8022369663
200PhosphorylationTVKDGSQTPTVDSVT
CCCCCCCCCCCCCCC		23.7122369663
202PhosphorylationKDGSQTPTVDSVTKD
CCCCCCCCCCCCCCC		40.0924909858
205PhosphorylationSQTPTVDSVTKDNTA
CCCCCCCCCCCCCCC		27.6122369663
207PhosphorylationTPTVDSVTKDNTANG
CCCCCCCCCCCCCCC		36.3122369663
271PhosphorylationANGRPLVTKLEDAGP
CCCCCCEEEHHHCCC		37.2824909858
272AcetylationNGRPLVTKLEDAGPA
CCCCCEEEHHHCCCC		42.2624489116
284AcetylationGPAEDPTKVGMVKYD
CCCCCCCEEEEEEEC		42.0324489116
289AcetylationPTKVGMVKYDGKEVT
CCEEEEEEECCEECC		28.8225381059
296PhosphorylationKYDGKEVTNEPEFEE
EECCEECCCCCCCCC		34.6524961812
340UbiquitinationKVLDENAKKLRFEEF
HHHHHHHHHCCHHHH		65.0123749301
394UbiquitinationIPADKVYKFTARNKY
EECCCEEEEEECCCE		38.9523749301
411AcetylationLTIDEAEKRMDKKSG
EEHHHHHHHHHHCCC		61.1324489116
426UbiquitinationEVPRWLMKHLDNIGT
CHHHHHHHHHHHCCC		38.5517644757
426AcetylationEVPRWLMKHLDNIGT
CHHHHHHHHHHHCCC		38.5524489116
433PhosphorylationKHLDNIGTTTTRYDR
HHHHHCCCCCHHHHH		19.7119823750
434PhosphorylationHLDNIGTTTTRYDRT
HHHHCCCCCHHHHHH		22.4319823750
435PhosphorylationLDNIGTTTTRYDRTR
HHHCCCCCHHHHHHH		14.7619823750
436PhosphorylationDNIGTTTTRYDRTRR
HHCCCCCHHHHHHHH		25.7419823750
438PhosphorylationIGTTTTRYDRTRRKL
CCCCCHHHHHHHHHH		14.0019823750
441PhosphorylationTTTRYDRTRRKLKAV
CCHHHHHHHHHHHHH		31.7419823750
463PhosphorylationEDDRDDNSEVELDYD
CCCCCCCCCEECCCC		50.4428889911
515PhosphorylationLRDEEAPSENEEDEL
CCCCCCCCCCCCCHH		61.1622369663
542PhosphorylationIKKALQKTELAALYS
HHHHHHHHHHHHHHC		24.2221551504
548PhosphorylationKTELAALYSSDENEI
HHHHHHHHCCCCCCC		11.0319795423
549PhosphorylationTELAALYSSDENEIN
HHHHHHHCCCCCCCC		31.9619795423
550PhosphorylationELAALYSSDENEINP
HHHHHHCCCCCCCCC		35.0719795423
558PhosphorylationDENEINPYLSESDIE
CCCCCCCCCCHHHHC		20.5519795423
560PhosphorylationNEINPYLSESDIENK
CCCCCCCCHHHHCCC		29.2519795423
562PhosphorylationINPYLSESDIENKEN
CCCCCCHHHHCCCCC		40.2819795423
571PhosphorylationIENKENESPVKKEED
HCCCCCCCCCCHHHH		46.7222369663
579PhosphorylationPVKKEEDSDTLSKSK
CCCHHHHHHCCCHHH		35.4625521595
581PhosphorylationKKEEDSDTLSKSKRS
CHHHHHHCCCHHHCC		36.5619795423
583PhosphorylationEEDSDTLSKSKRSSP
HHHHHCCCHHHCCCH		36.6522369663
585PhosphorylationDSDTLSKSKRSSPKK
HHHCCCHHHCCCHHH		29.9024930733
604AcetylationATNAHVHKEPTLRVK
HHHCCCCCCCCCCCC		65.3922865919
628AcetylationKGDKKILKSFPEGEW
CCCHHHHHHCCCCCC		54.2322865919
645PhosphorylationQTTKAVDSSNNASNT
CCCCCCCCCCCCCCC		28.5028132839
646PhosphorylationTTKAVDSSNNASNTV
CCCCCCCCCCCCCCC		29.6428132839
650PhosphorylationVDSSNNASNTVPSPI
CCCCCCCCCCCCCCC		34.8522890988
652PhosphorylationSSNNASNTVPSPIKQ
CCCCCCCCCCCCCCC		31.1622890988
655PhosphorylationNASNTVPSPIKQEEG
CCCCCCCCCCCCCCC		34.6122369663
665PhosphorylationKQEEGLNSTVAEREE
CCCCCCCCCCCCCCC		29.3320377248
666PhosphorylationQEEGLNSTVAEREET
CCCCCCCCCCCCCCC		23.7422369663
673PhosphorylationTVAEREETPAPTITE
CCCCCCCCCCCCCCH		21.7222369663
677PhosphorylationREETPAPTITEKDII
CCCCCCCCCCHHHHH		42.5122369663
679PhosphorylationETPAPTITEKDIIEA
CCCCCCCCHHHHHHH		39.1922369663
699AcetylationVNIKEFGKFIRRKYP
CCHHHHHHHHHHHCC		42.8324489116
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of T2FA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T2FA_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of T2FA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_YEASTRPO21physical
14759368
RPB2_YEASTRPB2physical
14759368
T2FB_YEASTTFG2physical
14759368
TAF14_YEASTTAF14physical
14759368
RPB3_YEASTRPB3physical
14759368
T2FA_YEASTTFG1physical
14759368
RPB1_YEASTRPO21physical
12242279
SPT5_YEASTSPT5physical
12556496
RPB2_YEASTRPB2physical
12242279
T2FB_YEASTTFG2physical
12242279
TAF14_YEASTTAF14physical
12242279
MED17_YEASTSRB4physical
14749386
T2FB_YEASTTFG2physical
14749386
RPB3_YEASTRPB3physical
14749386
TAF14_YEASTTAF14physical
14749386
FCP1_YEASTFCP1physical
11003641
FCP1_YEASTFCP1physical
9405607
TAF14_YEASTTAF14physical
15896708
RPB1_YEASTRPO21physical
8657139
T2FB_YEASTTFG2physical
8657139
TAF14_YEASTTAF14physical
8657139
T2EA_YEASTTFA1physical
8657139
T2EB_YEASTTFA2physical
8657139
T2FB_YEASTTFG2genetic
15572698
RPB9_YEASTRPB9genetic
15572698
RPB1_YEASTRPO21genetic
16081422
HUR1_YEASTHUR1genetic
17314980
SAC3_YEASTSAC3genetic
17314980
VPS64_YEASTVPS64genetic
17314980
ATC6_YEASTSPF1genetic
17314980
SPT3_YEASTSPT3genetic
17314980
MED31_YEASTSOH1genetic
17314980
UBP6_YEASTUBP6genetic
17314980
UBP3_YEASTUBP3genetic
17314980
SWR1_YEASTSWR1genetic
17314980
VPS72_YEASTVPS72genetic
17314980
SIF2_YEASTSIF2genetic
17314980
BUD27_YEASTBUD27genetic
17314980
SRO9_YEASTSRO9genetic
17314980
SGF73_YEASTSGF73genetic
17314980
SEM1_YEASTSEM1genetic
17314980
HIR1_YEASTHIR1genetic
17314980
ISW1_YEASTISW1genetic
17314980
T2FB_YEASTTFG2physical
19818408
BAS1_YEASTBAS1genetic
20959818
RPB9_YEASTRPB9genetic
21288884
T2FB_YEASTTFG2physical
22095626
FCP1_YEASTFCP1physical
22095626
RPB1_YEASTRPO21physical
20033062
RPB2_YEASTRPB2physical
20033062
RPAB4_YEASTRPC10physical
23418395
RPB9_YEASTRPB9physical
23418395
RPB11_YEASTRPB11physical
23418395
RPB4_YEASTRPB4physical
23418395
RPB7_YEASTRPB7physical
23418395
RPAB5_YEASTRPB10physical
23418395
RPAB2_YEASTRPO26physical
23418395
RPB1_YEASTRPO21physical
23418395
RPB3_YEASTRPB3physical
23418395
RPAB1_YEASTRPB5physical
23418395
RPB2_YEASTRPB2physical
23418395
RPAB3_YEASTRPB8physical
23418395
T2FB_YEASTTFG2physical
23418395
TAF14_YEASTTAF14physical
23418395
SPT4_YEASTSPT4physical
23418395
SPT5_YEASTSPT5physical
23418395
GPN1_YEASTNPA3physical
23418395
RL37A_YEASTRPL37Agenetic
27708008
ECM7_YEASTECM7genetic
27708008
TOP1_YEASTTOP1genetic
27708008
LSM2_YEASTLSM2genetic
27708008
STU1_YEASTSTU1genetic
27708008
RPB1_YEASTRPO21genetic
27708008
RPB7_YEASTRPB7genetic
27708008
GPI19_YEASTGPI19genetic
27708008
TAF6_YEASTTAF6genetic
27708008
TIM16_YEASTPAM16genetic
27708008
KCY_YEASTURA6genetic
27708008
GPI12_YEASTGPI12genetic
27708008
NOP2_YEASTNOP2genetic
27708008
SEC12_YEASTSEC12genetic
27708008
MVD1_YEASTMVD1genetic
27708008
PROF_YEASTPFY1genetic
27708008
RPB2_YEASTRPB2genetic
27708008
PRS10_YEASTRPT4genetic
27708008
TF2B_YEASTSUA7genetic
27708008
BUR1_YEASTSGV1genetic
27708008
PRP4_YEASTPRP4genetic
27708008
PUR7_YEASTADE1genetic
27708008
URA7_YEASTURA7genetic
27708008
RXT2_YEASTRXT2genetic
27708008
ICS2_YEASTICS2genetic
27708008
SHG1_YEASTSHG1genetic
27708008
STE50_YEASTSTE50genetic
27708008
ATG15_YEASTATG15genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
VPS41_YEASTVPS41genetic
27708008
H2A1_YEASTHTA1genetic
27708008
PEX5_YEASTPEX5genetic
27708008
LSM6_YEASTLSM6genetic
27708008
URC2_YEASTURC2genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RTF1_YEASTRTF1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
INM1_YEASTINM1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
BFA1_YEASTBFA1genetic
27708008
UBL1_YEASTYUH1genetic
27708008
IXR1_YEASTIXR1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
BRE2_YEASTBRE2genetic
27708008
ERG3_YEASTERG3genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
ROM2_YEASTROM2genetic
27708008
ELP1_YEASTIKI3genetic
27708008
PYRC_YEASTURA4genetic
27708008
RS3A1_YEASTRPS1Agenetic
27708008
TSA1_YEASTTSA1genetic
27708008
VPS71_YEASTVPS71genetic
27708008
SCS7_YEASTSCS7genetic
27708008
PET8_YEASTPET8genetic
27708008
CPT1_YEASTCPT1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
SIN3_YEASTSIN3genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
ISU1_YEASTISU1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
OPY2_YEASTOPY2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of T2FA_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; THR-200; SER-515;SER-655 AND THR-673, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-515; SER-655AND THR-673, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-515 ANDSER-655, AND MASS SPECTROMETRY.

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