T2FA_HUMAN - dbPTM
T2FA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T2FA_HUMAN
UniProt AC P35269
Protein Name General transcription factor IIF subunit 1
Gene Name GTF2F1
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization Nucleus.
Protein Description TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation..
Protein Sequence MAALGPSSQNVTEYVVRVPKNTTKKYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSEFNRKLREEARRKKYGIVLKEFRPEDQPWLLRVNGKSGRKFKGIKKGGVTENTSYYIFTQCPDGAFEAFPVHNWYNFTPLARHRTLTAEEAEEEWERRNKVLNHFSIMQQRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDLEMSSDASDASGEEGGRVPKAKKKAPLAKGGRKKKKKKGSDDEAFEDSDDGDFEGQEVDYMSDGSSSSQEEPESKAKAPQQEEGPKGVDEQSDSSEESEEEKPPEEDKEEEEEKKAPTPQEKKRRKDSSEESDSSEESDIDSEASSALFMAKKKTPPKRERKPSGGSSRGNSRPGTPSAEGGSTSSTLRAAASKLEQGKRVSEMPAAKRLRLDTGPQSLSGKSTPQPPSGKTTPNSGDVQVTEDAVRRYLTRKPMTTKDLLKKFQTKKTGLSSEQTVNVLAQILKRLNPERKMINDKMHFSLKE
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
2Acetylation------MAALGPSSQ
------CCCCCCCCC		16.0522223895
7Phosphorylation-MAALGPSSQNVTEY
-CCCCCCCCCCEEEE		42.6420068231
8PhosphorylationMAALGPSSQNVTEYV
CCCCCCCCCCEEEEE		28.9820068231
12PhosphorylationGPSSQNVTEYVVRVP
CCCCCCEEEEEEECC		29.1920068231
14PhosphorylationSSQNVTEYVVRVPKN
CCCCEEEEEEECCCC		8.5520068231
22PhosphorylationVVRVPKNTTKKYNIM
EEECCCCCCCEECEE		46.2327251275
23PhosphorylationVRVPKNTTKKYNIMA
EECCCCCCCEECEEE		34.6329396449
41PhosphorylationADKVNFATWNQARLE
CCCCCCHHHHHHHHH		22.3228555341
54UbiquitinationLERDLSNKKIYQEEE
HHHHHCCCCCCCCCC		36.8522817900
55UbiquitinationERDLSNKKIYQEEEM
HHHHCCCCCCCCCCC		51.3921906983
57PhosphorylationDLSNKKIYQEEEMPE
HHCCCCCCCCCCCCC		20.82-
62SulfoxidationKIYQEEEMPESGAGS
CCCCCCCCCCCCCCH		5.1621406390
65PhosphorylationQEEEMPESGAGSEFN
CCCCCCCCCCCHHHH		28.2425627689
83UbiquitinationREEARRKKYGIVLKE
HHHHHHHHCCEEEEE		47.0729967540
832-HydroxyisobutyrylationREEARRKKYGIVLKE
HHHHHHHHCCEEEEE		47.07-
89AcetylationKKYGIVLKEFRPEDQ
HHCCEEEEECCCCCC		43.8626051181
89UbiquitinationKKYGIVLKEFRPEDQ
HHCCEEEEECCCCCC		43.8621963094
154PhosphorylationTPLARHRTLTAEEAE
CCCCCCCCCCHHHHH		23.4923401153
156PhosphorylationLARHRTLTAEEAEEE
CCCCCCCCHHHHHHH		31.2627273156
169UbiquitinationEEWERRNKVLNHFSI
HHHHHHHHHHHHHHH		46.4123000965
175PhosphorylationNKVLNHFSIMQQRRL
HHHHHHHHHHHHHHC		15.0327080861
183UbiquitinationIMQQRRLKDQDQDED
HHHHHHCCCCCCCCC		52.0821906983
194UbiquitinationQDEDEEEKEKRGRRK
CCCCHHHHHHHHHHH		72.3424816145
217PhosphorylationLEDDLEMSSDASDAS
HHHHHCCCCCCCCCC		18.7223927012
218PhosphorylationEDDLEMSSDASDASG
HHHHCCCCCCCCCCC		35.5723927012
221PhosphorylationLEMSSDASDASGEEG
HCCCCCCCCCCCCCC		38.4120201521
224PhosphorylationSSDASDASGEEGGRV
CCCCCCCCCCCCCCC		52.2920201521
237UbiquitinationRVPKAKKKAPLAKGG
CCCHHHHCCCCCCCC		55.3024816145
253PhosphorylationKKKKKKGSDDEAFED
CCCCCCCCCCCCCCC		51.2525137130
261PhosphorylationDDEAFEDSDDGDFEG
CCCCCCCCCCCCCCC		30.3325137130
275PhosphorylationGQEVDYMSDGSSSSQ
CCEEEEECCCCCCCC		32.3725137130
278PhosphorylationVDYMSDGSSSSQEEP
EEEECCCCCCCCCCH		31.8525137130
279PhosphorylationDYMSDGSSSSQEEPE
EEECCCCCCCCCCHH		39.2725137130
280PhosphorylationYMSDGSSSSQEEPES
EECCCCCCCCCCHHH		37.4225137130
281PhosphorylationMSDGSSSSQEEPESK
ECCCCCCCCCCHHHH		43.4925137130
305PhosphorylationPKGVDEQSDSSEESE
CCCCCCCCCCCCCCC		37.1023927012
307PhosphorylationGVDEQSDSSEESEEE
CCCCCCCCCCCCCCC		44.9123927012
308PhosphorylationVDEQSDSSEESEEEK
CCCCCCCCCCCCCCC		50.8323927012
311PhosphorylationQSDSSEESEEEKPPE
CCCCCCCCCCCCCCH		46.3823927012
315AcetylationSEESEEEKPPEEDKE
CCCCCCCCCCHHHHH		69.977408151
328AcetylationKEEEEEKKAPTPQEK
HHHHHHHHCCCHHHH		63.987370183
331PhosphorylationEEEKKAPTPQEKKRR
HHHHHCCCHHHHHHH		42.3328176443
341PhosphorylationEKKRRKDSSEESDSS
HHHHHCCCCCCCCCC		42.5625022875
342PhosphorylationKKRRKDSSEESDSSE
HHHHCCCCCCCCCCC		56.3625022875
345PhosphorylationRKDSSEESDSSEESD
HCCCCCCCCCCCCHH		38.4525022875
347PhosphorylationDSSEESDSSEESDID
CCCCCCCCCCCHHHC		49.2625022875
348PhosphorylationSSEESDSSEESDIDS
CCCCCCCCCCHHHCH		50.8325022875
351PhosphorylationESDSSEESDIDSEAS
CCCCCCCHHHCHHHH		35.5025022875
355PhosphorylationSEESDIDSEASSALF
CCCHHHCHHHHHHHH		35.0822817900
358PhosphorylationSDIDSEASSALFMAK
HHHCHHHHHHHHHHC		16.4625022875
359PhosphorylationDIDSEASSALFMAKK
HHCHHHHHHHHHHCC		35.7220071362
368PhosphorylationLFMAKKKTPPKRERK
HHHHCCCCCCCCCCC		54.4230576142
377PhosphorylationPKRERKPSGGSSRGN
CCCCCCCCCCCCCCC		59.8427273156
380PhosphorylationERKPSGGSSRGNSRP
CCCCCCCCCCCCCCC		22.0127273156
381PhosphorylationRKPSGGSSRGNSRPG
CCCCCCCCCCCCCCC		47.7027273156
385PhosphorylationGGSSRGNSRPGTPSA
CCCCCCCCCCCCCCC		42.5519664994
389PhosphorylationRGNSRPGTPSAEGGS
CCCCCCCCCCCCCCC		19.4319664994
391PhosphorylationNSRPGTPSAEGGSTS
CCCCCCCCCCCCCCH		38.5029255136
396PhosphorylationTPSAEGGSTSSTLRA
CCCCCCCCCHHHHHH		35.6530266825
397PhosphorylationPSAEGGSTSSTLRAA
CCCCCCCCHHHHHHH		29.9430266825
398PhosphorylationSAEGGSTSSTLRAAA
CCCCCCCHHHHHHHH		24.0329255136
399PhosphorylationAEGGSTSSTLRAAAS
CCCCCCHHHHHHHHH		31.3929255136
400PhosphorylationEGGSTSSTLRAAASK
CCCCCHHHHHHHHHH		21.7429255136
407AcetylationTLRAAASKLEQGKRV
HHHHHHHHHHHCCCH		51.8519608861
412UbiquitinationASKLEQGKRVSEMPA
HHHHHHCCCHHCCCH		49.6924816145
412AcetylationASKLEQGKRVSEMPA
HHHHHHCCCHHCCCH		49.6930584513
415PhosphorylationLEQGKRVSEMPAAKR
HHHCCCHHCCCHHHH		32.0128555341
421AcetylationVSEMPAAKRLRLDTG
HHCCCHHHHCCCCCC		54.8125953088
427PhosphorylationAKRLRLDTGPQSLSG
HHHCCCCCCCCCCCC		56.1827273156
431PhosphorylationRLDTGPQSLSGKSTP
CCCCCCCCCCCCCCC		27.8629255136
433PhosphorylationDTGPQSLSGKSTPQP
CCCCCCCCCCCCCCC		49.8029255136
435AcetylationGPQSLSGKSTPQPPS
CCCCCCCCCCCCCCC		48.0225953088
436PhosphorylationPQSLSGKSTPQPPSG
CCCCCCCCCCCCCCC		49.1723927012
437PhosphorylationQSLSGKSTPQPPSGK
CCCCCCCCCCCCCCC		29.4523927012
442PhosphorylationKSTPQPPSGKTTPNS
CCCCCCCCCCCCCCC		60.6523927012
444AcetylationTPQPPSGKTTPNSGD
CCCCCCCCCCCCCCC		54.2725953088
444UbiquitinationTPQPPSGKTTPNSGD
CCCCCCCCCCCCCCC		54.2724816145
445PhosphorylationPQPPSGKTTPNSGDV
CCCCCCCCCCCCCCC		51.5223927012
446PhosphorylationQPPSGKTTPNSGDVQ
CCCCCCCCCCCCCCE		24.7823927012
449PhosphorylationSGKTTPNSGDVQVTE
CCCCCCCCCCCEECH		37.2630266825
455PhosphorylationNSGDVQVTEDAVRRY
CCCCCEECHHHHHHH		15.8523927012
466AcetylationVRRYLTRKPMTTKDL
HHHHHHCCCCCHHHH		33.6330584501
469PhosphorylationYLTRKPMTTKDLLKK
HHHCCCCCHHHHHHH		38.9429083192
470PhosphorylationLTRKPMTTKDLLKKF
HHCCCCCHHHHHHHH		19.1329083192
471AcetylationTRKPMTTKDLLKKFQ
HCCCCCHHHHHHHHC		36.8930584507
479PhosphorylationDLLKKFQTKKTGLSS
HHHHHHCCCCCCCCH		37.3323828894
482PhosphorylationKKFQTKKTGLSSEQT
HHHCCCCCCCCHHHH		44.9320068231
485PhosphorylationQTKKTGLSSEQTVNV
CCCCCCCCHHHHHHH		32.9220068231
486PhosphorylationTKKTGLSSEQTVNVL
CCCCCCCHHHHHHHH		38.4720068231
489PhosphorylationTGLSSEQTVNVLAQI
CCCCHHHHHHHHHHH		15.2520068231
510UbiquitinationERKMINDKMHFSLKE
HHHHCCCCCCCCCCC		29.7730230243
516UbiquitinationDKMHFSLKE------
CCCCCCCCC------		61.2430230243
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
385SPhosphorylationKinaseGTF2F1P35269
PSP
389TPhosphorylationKinaseGTF2F1P35269
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T2FA_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF2B_HUMANGTF2Bphysical
9159119
TBP_HUMANTBPphysical
9159119
TAF11_HUMANTAF11physical
9159119
T2EA_HUMANGTF2E1physical
9159119
TF2H4_HUMANGTF2H4physical
9159119
FEZ1_HUMANFEZ1physical
16169070
PTN_HUMANPTNphysical
16169070
TF2AA_HUMANGTF2A1physical
11509574
CTDP1_HUMANCTDP1physical
9765293
T2EB_HUMANGTF2E2physical
9677423
T2EB_HUMANGTF2E2physical
11113176
SRF_HUMANSRFphysical
8106390
HNRPU_HUMANHNRNPUphysical
10490622
RPB1_HUMANPOLR2Aphysical
17643375
RPB2_HUMANPOLR2Bphysical
17643375
IMA1_HUMANKPNA2physical
17643375
RFC2_HUMANRFC2physical
17643375
TRI27_HUMANTRIM27physical
20211142
PARP1_HUMANPARP1physical
16204234
RPB1_HUMANPOLR2Aphysical
12591939
HNRPU_HUMANHNRNPUphysical
15711563
RPB1_HUMANPOLR2Aphysical
15711563
TAT_HV1H2tatphysical
9121429
RPB1_HUMANPOLR2Aphysical
9121429
T2EA_HUMANGTF2E1physical
9121429
ERCC2_HUMANERCC2physical
9121429
TF2H1_HUMANGTF2H1physical
9121429
CDK8_HUMANCDK8physical
9121429
CCNC_HUMANCCNCphysical
9121429
TF2B_HUMANGTF2Bphysical
16878124
SAP_HUMANPSAPphysical
22863883
TRUA_HUMANPUS1physical
22863883
ABL1_HUMANABL1physical
7533294
T2FB_HUMANGTF2F2physical
26344197
HIRP3_HUMANHIRIP3physical
26344197
SRRM1_HUMANSRRM1physical
26344197
CTDP1_HUMANCTDP1physical
12732728
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of T2FA_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389;SER-391; SER-431; SER-436; SER-442 AND THR-445, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;SER-224; SER-385; THR-389 AND SER-433, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389;SER-391; SER-431; SER-436; SER-442 AND THR-445, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385 AND THR-389, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; THR-389 ANDSER-433, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;SER-224; SER-305; SER-307; SER-308; SER-311; SER-342; SER-345;SER-347; SER-348; SER-351 AND SER-355, AND MASS SPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221AND SER-224, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218 ANDSER-221, AND MASS SPECTROMETRY.
"Kinase activity and phosphorylation of the largest subunit of TFIIFtranscription factor.";
Rossignol M., Keriel A., Staub A., Egly J.-M.;
J. Biol. Chem. 274:22387-22392(1999).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, AND MUTAGENESIS OFSER-385 AND THR-389.
"TAFII250 is a bipartite protein kinase that phosphorylates the basetranscription factor RAP74.";
Dikstein R., Ruppert S., Tjian R.;
Cell 84:781-790(1996).
Cited for: PHOSPHORYLATION AT SERINE RESIDUES.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory