Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  General transcription factor II-I  

UniProtKB / Swiss-Prot ID :  GTF2I_HUMAN

Gene Name (Synonyms) : 
GTF2I, BAP135, WBSCR6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Note=Colocalizes with BTK in the cytoplasm. 

Protein Function :  Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C- FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. 

Protein Sequence MAQVAMSTLPVEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRK...
Predicted Secondary Structure CCCHHHHHCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCEEEEEEECCCEEEEEECCCEEEHHHHH...
Protein Variant
LocationDescription
174L -> V (in dbSNP:rs1057896). VAR_051026
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAQVAM
---CCCHHH
24.70UniProtKB
Link-
74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDFQKDFVK
HHHHHHHHH
53.80Phosphositeplus
Link-
95PhosphoserineHKMKSTTQA
HHHHHHHCC
32.94HPRD
Link-
103PhosphoserineANRMSVDAV
CCCCCCCHH
17.38HPRD
Link
103PhosphoserineANRMSVDAV
CCCCCCCHH
17.38PhosphoELM
Link
103PhosphoserineANRMSVDAV
CCCCCCCHH
17.38Phosphositeplus
Link
103PhosphoserineANRMSVDAV
CCCCCCCHH
17.38SysPTM
Link
103Phosphoserine.ANRMSVDAV
CCCCCCCHH
17.38UniProtKB
Link
111PhosphothreonineVEIETLRKT
HHHHHHHHH
37.21HPRD
Link
140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VPYEKMLRD
CCHHHHCCC
37.07Phosphositeplus
Link
202PhosphothreonineRVMVTDADR
EEEECHHHH
13.84HPRD
Link-
202PhosphothreonineRVMVTDADR
EEEECHHHH
13.84Phosphositeplus
Link-
207PhosphoserineDADRSILSP
HHHHCCCCC
28.55HPRD
Link-
207PhosphoserineDADRSILSP
HHHHCCCCC
28.55PhosphoELM
Link-
207PhosphoserineDADRSILSP
HHHHCCCCC
28.55Phosphositeplus
Link-
207PhosphoserineDADRSILSP
HHHHCCCCC
28.55SysPTM
Link-
207Phosphoserine.DADRSILSP
HHHHCCCCC
28.55UniProtKB
Link-
210PhosphoserineRSILSPGGS
HCCCCCCCC
21.59HPRD
Link-
210PhosphoserineRSILSPGGS
HCCCCCCCC
21.59PhosphoELM
Link-
210PhosphoserineRSILSPGGS
HCCCCCCCC
21.59Phosphositeplus
Link-
210PhosphoserineRSILSPGGS
HCCCCCCCC
21.59SysPTM
Link-
210Phosphoserine.RSILSPGGS
HCCCCCCCC
21.59UniProtKB
Link-
214PhosphoserineSPGGSCGPI
CCCCCCCCC
23.09Phosphositeplus
Link-
248PhosphotyrosineEDPDYYQYN
CCCCCCCCC
9.61Phosphositeplus
Link-
248Phosphotyrosine (BTK)EDPDYYQYN
CCCCCCCCC
9.61HPRD
Link-
248Phosphotyrosine (BTK)EDPDYYQYN
CCCCCCCCC
9.61PhosphoELM
Link-
248Phosphotyrosine (JAK2)EDPDYYQYN
CCCCCCCCC
9.61HPRD
Link-
248Phosphotyrosine (SRC)EDPDYYQYN
CCCCCCCCC
9.61HPRD
Link-
248Phosphotyrosine; by BTK.EDPDYYQYN
CCCCCCCCC
9.61UniProtKB
Link-
249PhosphotyrosineDPDYYQYNI
CCCCCCCCC
16.35Phosphositeplus
Link-
318PhosphotyrosineEDDDYSPPS
CCCCCCCCC
30.03PhosphoELM
Link-
353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FNFEKWNAR
HCCCCCCCH
41.43Phosphositeplus
Link-
392Phosphoserine (PRKG1)PLFQSHVED
HHHHCCHHH
23.36HPRD
Link-
398PhosphotyrosineVEDLYVEGL
HHHEEEEEC
14.58Phosphositeplus
Link-
398Phosphotyrosine (BTK)VEDLYVEGL
HHHEEEEEC
14.58HPRD
Link-
398Phosphotyrosine (BTK)VEDLYVEGL
HHHEEEEEC
14.58PhosphoELM
Link-
398Phosphotyrosine; by BTK.VEDLYVEGL
HHHEEEEEC
14.58UniProtKB
Link-
412PhosphoserineFRRPSTYGI
CCCCCCCCH
32.23Phosphositeplus
Link-
412Phosphoserine (PRKG1)FRRPSTYGI
CCCCCCCCH
32.23HPRD
Link-
412Phosphoserine; by PKG/PRKG1.FRRPSTYGI
CCCCCCCCH
32.23UniProtKB
Link-
460PhosphotyrosineKEEWYARIT
HHHHHHHHH
6.84Phosphositeplus
Link-
475S-nitrosocysteineDQLFCKKFA
HHHHHHHHH
6.78dbSNO
Link-
476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QLFCKKFAE
HHHHHHHHH
43.52Phosphositeplus
Link-
488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)STEAKAVPY
CCCHHHCCH
43.62Phosphositeplus
Link-
494Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VPYQKFEAH
CCHHHHHCC
39.05Phosphositeplus
Link-
503PhosphotyrosinePNDLYVEGL
CCCEEEECC
10.18Phosphositeplus
Link-
503Phosphotyrosine (BTK)PNDLYVEGL
CCCEEEECC
10.18HPRD
Link-
503Phosphotyrosine (BTK)PNDLYVEGL
CCCEEEECC
10.18PhosphoELM
Link-
503Phosphotyrosine; by BTK.PNDLYVEGL
CCCEEEECC
10.18UniProtKB
Link-
515PhosphoserineIPFRSPSWY
CCCCCCCCC
24.54HPRD
Link-
515PhosphoserineIPFRSPSWY
CCCCCCCCC
24.54PhosphoELM
Link-
515PhosphoserineIPFRSPSWY
CCCCCCCCC
24.54Phosphositeplus
Link-
515Phosphoserine.IPFRSPSWY
CCCCCCCCC
24.54UniProtKB
Link-
517PhosphoserineFRSPSWYGI
CCCCCCCCC
33.89HPRD
Link-
517PhosphoserineFRSPSWYGI
CCCCCCCCC
33.89PhosphoELM
Link-
517PhosphoserineFRSPSWYGI
CCCCCCCCC
33.89Phosphositeplus
Link-
517PhosphoserineFRSPSWYGI
CCCCCCCCC
33.89SysPTM
Link-
517Phosphoserine.FRSPSWYGI
CCCCCCCCC
33.89UniProtKB
Link-
539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KFVIKRPEL
EEEEECCCE
57.51Phosphositeplus
Link-
556PhosphothreonineTQPRTNTPV
CCCCCCCCC
50.56HPRD
Link-
556PhosphothreonineTQPRTNTPV
CCCCCCCCC
50.56PhosphoELM
Link-
556PhosphothreonineTQPRTNTPV
CCCCCCCCC
50.56Phosphositeplus
Link-
558PhosphothreoninePRTNTPVKE
CCCCCCCHH
28.92HPRD
Link-
558PhosphothreoninePRTNTPVKE
CCCCCCCHH
28.92PhosphoELM
Link-
558PhosphothreoninePRTNTPVKE
CCCCCCCHH
28.92Phosphositeplus
Link-
558PhosphothreoninePRTNTPVKE
CCCCCCCHH
28.92SysPTM
Link-
558Phosphothreonine.PRTNTPVKE
CCCCCCCHH
28.92UniProtKB
Link-
561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NTPVKEDWN
CCCCHHHHH
51.68Phosphositeplus
Link-
636PhosphoserineIVRGSNKIK
HHHHHHEEE
25.12HPRD
Link-
652Phosphotyrosine (SRC)LVISYLPPG
HHHHHCCCC
16.47HPRD
Link-
659PhosphoserinePGMASKINT
CCHHHCCCH
25.77HPRD
Link-
668PhosphoserineKALQSPKRP
HHHCCCCCC
32.99HPRD
Link-
668PhosphoserineKALQSPKRP
HHHCCCCCC
32.99Phosphositeplus
Link-
668PhosphoserineKALQSPKRP
HHHCCCCCC
32.99SysPTM
Link-
668Phosphoserine.KALQSPKRP
HHHCCCCCC
32.99UniProtKB
Link-
674PhosphoserineKRPRSPGSN
CCCCCCCCC
35.97HPRD
Link-
674PhosphoserineKRPRSPGSN
CCCCCCCCC
35.97Phosphositeplus
Link-
674PhosphoserineKRPRSPGSN
CCCCCCCCC
35.97SysPTM
Link-
674Phosphoserine.KRPRSPGSN
CCCCCCCCC
35.97UniProtKB
Link-
677PhosphoserineRSPGSNSKV
CCCCCCCCC
41.12HPRD
Link-
677PhosphoserineRSPGSNSKV
CCCCCCCCC
41.12PhosphoELM
Link-
677PhosphoserineRSPGSNSKV
CCCCCCCCC
41.12Phosphositeplus
Link-
679PhosphoserinePGSNSKVPE
CCCCCCCCE
36.41HPRD
Link-
679PhosphoserinePGSNSKVPE
CCCCCCCCE
36.41HPRD
Link-
679PhosphoserinePGSNSKVPE
CCCCCCCCE
36.41PhosphoELM
Link-
679PhosphoserinePGSNSKVPE
CCCCCCCCE
36.41SysPTM
Link-
679Phosphoserine.PGSNSKVPE
CCCCCCCCE
36.41UniProtKB
Link-
687PhosphothreonineEIEVTVEGP
EEEEEECCC
10.47HPRD
Link-
687PhosphothreonineEIEVTVEGP
EEEEEECCC
10.47PhosphoELM
Link-
687PhosphothreonineEIEVTVEGP
EEEEEECCC
10.47SysPTM
Link-
687Phosphothreonine.EIEVTVEGP
EEEEEECCC
10.47UniProtKB
Link-
698PhosphothreonineNNPQTSAVR
CCCCCCCCC
21.65HPRD
Link-
698PhosphothreonineNNPQTSAVR
CCCCCCCCC
21.65PhosphoELM
Link-
699PhosphoserineNPQTSAVRT
CCCCCCCCC
21.37HPRD
Link-
699PhosphoserineNPQTSAVRT
CCCCCCCCC
21.37PhosphoELM
Link-
699PhosphoserineNPQTSAVRT
CCCCCCCCC
21.37Phosphositeplus
Link-
705PhosphothreonineVRTPTQTNG
CCCCCCCCC
47.62Phosphositeplus
Link-
710PhosphoserineQTNGSNVPF
CCCCCCCCC
36.40HPRD
Link-
722PhosphoserineGREFSFEAW
CCCCCCCCC
19.88Phosphositeplus
Link-
752Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ALGLKQAVK
HHCCCCHHH
34.12Phosphositeplus
Link-
764Phosphoserine (PRKG1)ALFESFPED
HHHHCCCCC
38.47HPRD
Link-
784PhosphoserineFRRPSTFGI
CCCCCCCCH
34.26Phosphositeplus
Link-
784Phosphoserine (PRKG1)FRRPSTFGI
CCCCCCCCH
34.26HPRD
Link-
784Phosphoserine; by PKG/PRKG1.FRRPSTFGI
CCCCCCCCH
34.26UniProtKB
Link-
785PhosphothreonineRRPSTFGIP
CCCCCCCHH
28.67Phosphositeplus
Link-
818PhosphoserineAIKESTSSK
HHHHCCCCC
28.70HPRD
Link-
823PhosphoserineTSSKSPPRK
CCCCCCCCC
41.93HPRD
Link-
823PhosphoserineTSSKSPPRK
CCCCCCCCC
41.93Phosphositeplus
Link-
823PhosphoserineTSSKSPPRK
CCCCCCCCC
41.93SysPTM
Link-
823Phosphoserine.TSSKSPPRK
CCCCCCCCC
41.93UniProtKB
Link-
830PhosphoserineRKINSSPNV
CCCCCCCCC
51.12HPRD
Link-
830PhosphoserineRKINSSPNV
CCCCCCCCC
51.12PhosphoELM
Link-
830PhosphoserineRKINSSPNV
CCCCCCCCC
51.12Phosphositeplus
Link-
831PhosphoserineKINSSPNVN
CCCCCCCCC
18.92HPRD
Link-
831PhosphoserineKINSSPNVN
CCCCCCCCC
18.92PhosphoELM
Link-
831PhosphoserineKINSSPNVN
CCCCCCCCC
18.92Phosphositeplus
Link-
836PhosphothreoninePNVNTTASG
CCCCCCCCC
21.32Phosphositeplus
Link-
837PhosphothreonineNVNTTASGV
CCCCCCCCH
17.39HPRD
Link-
837PhosphothreonineNVNTTASGV
CCCCCCCCH
17.39Phosphositeplus
Link-
839PhosphoserineNTTASGVED
CCCCCCHHH
41.08HPRD
Link-
839PhosphoserineNTTASGVED
CCCCCCHHH
41.08PhosphoELM
Link-
839PhosphoserineNTTASGVED
CCCCCCHHH
41.08Phosphositeplus
Link-
850PhosphothreonineIIQVTIPDD
CCCCCCCCC
15.49HPRD
Link-
850PhosphothreonineIIQVTIPDD
CCCCCCCCC
15.49PhosphoELM
Link-
877PhosphoserineNDLFSRKFG
HHHHHHHHH
41.69HPRD
Link-
879Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFSRKFGEA
HHHHHHHHH
57.43Phosphositeplus
Link-
920PhosphotyrosineKAPSYLEIS
CCCCCCCHH
13.80HPRD
Link-
920PhosphotyrosineKAPSYLEIS
CCCCCCCHH
13.80Phosphositeplus
Link-
925PhosphoserineLEISSMRRI
CCHHHHHHH
23.21HPRD
Link-
925PhosphoserineLEISSMRRI
CCHHHHHHH
23.21Phosphositeplus
Link-
991Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)SSQIKQEPD
CHHHCCCCC
40.76Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NFKB2_HUMANphysical interactionMINT-47918MINT14743216
NFKB2_HUMANphysical interactionMINT-48759MINT14743216
HDAC3_HUMANphysical interaction
physical interaction
physical interaction
DIP:40209EDIP12393887
12393887
12393887
NFKB2_HUMANphysical interactionDIP:44847EDIP14743216
BTK_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
phosphorylation
EBI-625147
EBI-625110
EBI-627
intact9012831
9012831
9012831
9012831
9012831
STAT3_HUMANin vitro
in vivo
HPRD:03399HPRD9584171
PRRX1_HUMANin vitro
in vivo
HPRD:03399HPRD9334314
TYY1_HUMANin vitro
in vivo
HPRD:03399HPRD11287625
USF1_HUMANin vitro
in vivo
HPRD:03399HPRD9384587
1961251
MYC_HUMANin vitroHPRD:03399HPRD8377829
STAT1_HUMANin vitro
in vivo
HPRD:03399HPRD9584171
SRF_HUMANin vitro
in vivo
HPRD:03399HPRD12082086
9584171
9334314
GTF2I_HUMANyeast 2-hybridHPRD:03399HPRD15231747
SMAD2_HUMANin vivoHPRD:03399HPRD16055724
TYY1_HUMANENSP00000322542STRING
SRF_HUMANENSP00000322542STRING
SRF_HUMANENSP00000322542STRING
HDAC3_HUMANENSP00000322542STRING
FOS_HUMANENSP00000322542STRING
ZMYM3_HUMANENSP00000322542STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-210 AND SER-679, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"cGMP-dependent protein kinase I beta physically and functionallyinteracts with the transcriptional regulator TFII-I.";
Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S.,Pilz R.B.;
J. Biol. Chem. 277:32003-32014(2002).
Cited for: PHOSPHORYLATION AT SER-412 AND SER-784 BY PRKG1, AND INTERACTION WITHPRKG1.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-668 ANDSER-674, 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-679; THR-687 ANDSER-823, AND MASS SPECTROMETRY.
"Induction of immunoglobulin heavy-chain transcription through thetranscription factor Bright requires TFII-I.";
Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L.,Webb C.F.;
Mol. Cell. Biol. 26:4758-4768(2006).
Cited for: INTERACTION WITH ARID3A AND BTK, PHOSPHORYLATION AT TYR-248, ANDFUNCTION.
"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-210, AND MASSSPECTROMETRY.
"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 THR-558, AND MASSSPECTROMETRY.
"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-515, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-207; SER-210AND THR-558, 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-210 AND SER-679, AND MASS SPECTROMETRY.
"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-103 AND THR-558, ANDMASS SPECTROMETRY.
"Identification of phosphorylation sites for Bruton's tyrosine kinasewithin the transcriptional regulator BAP/TFII-I.";
Egloff A.M., Desiderio S.;
J. Biol. Chem. 276:27806-27815(2001).
Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK,FUNCTION, AND MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures