GTF2I_HUMAN - dbPTM
GTF2I_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GTF2I_HUMAN
UniProt AC P78347
Protein Name General transcription factor II-I
Gene Name GTF2I
Organism Homo sapiens (Human).
Sequence Length 998
Subcellular Localization Cytoplasm . Nucleus . Colocalizes with BTK in the cytoplasm.
Protein Description 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 MAQVAMSTLPVEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRKDFQKDFVKYCVEEEEKAAEMHKMKSTTQANRMSVDAVEIETLRKTVEDYFCFCYGKALGKSTVVPVPYEKMLRDQSAVVVQGLPEGVAFKHPENYDLATLKWILENKAGISFIIKRPFLEPKKHVGGRVMVTDADRSILSPGGSCGPIKVKTEPTEDSGISLEMAAVTVKEESEDPDYYQYNIQAGPSETDDVDEKQPLSKPLQGSHHSSEGNEGTEMEVPAEDSTQHVPSETSEDPEVEVTIEDDDYSPPSKRPKANELPQPPVPEPANAGKRKVREFNFEKWNARITDLRKQVEELFERKYAQAIKAKGPVTIPYPLFQSHVEDLYVEGLPEGIPFRRPSTYGIPRLERILLAKERIRFVIKKHELLNSTREDLQLDKPASGVKEEWYARITKLRKMVDQLFCKKFAEALGSTEAKAVPYQKFEAHPNDLYVEGLPENIPFRSPSWYGIPRLEKIIQVGNRIKFVIKRPELLTHSTTEVTQPRTNTPVKEDWNVRITKLRKQVEEIFNLKFAQALGLTEAVKVPYPVFESNPEFLYVEGLPEGIPFRSPTWFGIPRLERIVRGSNKIKFVVKKPELVISYLPPGMASKINTKALQSPKRPRSPGSNSKVPEIEVTVEGPNNNNPQTSAVRTPTQTNGSNVPFKPRGREFSFEAWNAKITDLKQKVENLFNEKCGEALGLKQAVKVPFALFESFPEDFYVEGLPEGVPFRRPSTFGIPRLEKILRNKAKIKFIIKKPEMFETAIKESTSSKSPPRKINSSPNVNTTASGVEDLNIIQVTIPDDDNERLSKVEKARQLREQVNDLFSRKFGEAIGMGFPVKVPYRKITINPGCVVVDGMPPGVSFKAPSYLEISSMRRILDSAEFIKFTVIRPFPGLVINNQLVDQSESEGPVIQESAEPSQLEVPATEEIKETDGSSQIKQEPDPTW
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------MAQVAMSTL
------CCCCCCCCC
24.7022223895
7Phosphorylation-MAQVAMSTLPVEDE
-CCCCCCCCCCCCCC
19.6328355574
8PhosphorylationMAQVAMSTLPVEDEE
CCCCCCCCCCCCCCC
23.2325106551
16PhosphorylationLPVEDEESSESRMVV
CCCCCCCCCHHHHHH
37.0423401153
17PhosphorylationPVEDEESSESRMVVT
CCCCCCCCHHHHHHH
42.7629255136
19PhosphorylationEDEESSESRMVVTFL
CCCCCCHHHHHHHHH
27.8529255136
24PhosphorylationSESRMVVTFLMSALE
CHHHHHHHHHHHHHH
10.3123879269
35SumoylationSALESMCKELAKSKA
HHHHHHHHHHHHCCC
47.3128112733
70UbiquitinationRAFVNTRKDFQKDFV
CEEECCCHHHHHHHH
61.94-
74AcetylationNTRKDFQKDFVKYCV
CCCHHHHHHHHHHHH
53.8026051181
74UbiquitinationNTRKDFQKDFVKYCV
CCCHHHHHHHHHHHH
53.8021890473
74 (in isoform 1)Ubiquitination-53.8021890473
74 (in isoform 2)Ubiquitination-53.8021890473
74 (in isoform 3)Ubiquitination-53.8021890473
74 (in isoform 4)Ubiquitination-53.8021890473
74UbiquitinationNTRKDFQKDFVKYCV
CCCHHHHHHHHHHHH
53.8021890473
78AcetylationDFQKDFVKYCVEEEE
HHHHHHHHHHHHHHH
32.6926051181
78UbiquitinationDFQKDFVKYCVEEEE
HHHHHHHHHHHHHHH
32.69-
79PhosphorylationFQKDFVKYCVEEEEK
HHHHHHHHHHHHHHH
9.0928102081
80GlutathionylationQKDFVKYCVEEEEKA
HHHHHHHHHHHHHHH
2.2922555962
86SumoylationYCVEEEEKAAEMHKM
HHHHHHHHHHHHHHC
57.06-
86AcetylationYCVEEEEKAAEMHKM
HHHHHHHHHHHHHHC
57.0626051181
86SumoylationYCVEEEEKAAEMHKM
HHHHHHHHHHHHHHC
57.0628112733
92SumoylationEKAAEMHKMKSTTQA
HHHHHHHHCCCCHHH
46.8728112733
94SumoylationAAEMHKMKSTTQANR
HHHHHHCCCCHHHHC
49.83-
94SumoylationAAEMHKMKSTTQANR
HHHHHHCCCCHHHHC
49.8328112733
95PhosphorylationAEMHKMKSTTQANRM
HHHHHCCCCHHHHCC
32.9430243723
96PhosphorylationEMHKMKSTTQANRMS
HHHHCCCCHHHHCCC
19.8728450419
97PhosphorylationMHKMKSTTQANRMSV
HHHCCCCHHHHCCCC
32.5430243723
101MethylationKSTTQANRMSVDAVE
CCCHHHHCCCCCEEE
23.05-
102SulfoxidationSTTQANRMSVDAVEI
CCHHHHCCCCCEEEH
4.6121406390
103PhosphorylationTTQANRMSVDAVEIE
CHHHHCCCCCEEEHH
17.3819664994
111PhosphorylationVDAVEIETLRKTVED
CCEEEHHHHHHHHHH
37.2129978859
126AcetylationYFCFCYGKALGKSTV
HHHHHHHHHCCCCCE
17.6026051181
130SumoylationCYGKALGKSTVVPVP
HHHHHCCCCCEEECC
43.75-
1302-HydroxyisobutyrylationCYGKALGKSTVVPVP
HHHHHCCCCCEEECC
43.75-
130AcetylationCYGKALGKSTVVPVP
HHHHHCCCCCEEECC
43.75-
130SumoylationCYGKALGKSTVVPVP
HHHHHCCCCCEEECC
43.7528112733
130UbiquitinationCYGKALGKSTVVPVP
HHHHHCCCCCEEECC
43.75-
140SumoylationVVPVPYEKMLRDQSA
EEECCHHHHCCCCCE
37.07-
140AcetylationVVPVPYEKMLRDQSA
EEECCHHHHCCCCCE
37.0726051181
140SumoylationVVPVPYEKMLRDQSA
EEECCHHHHCCCCCE
37.0728112733
140UbiquitinationVVPVPYEKMLRDQSA
EEECCHHHHCCCCCE
37.0721890473
140 (in isoform 1)Ubiquitination-37.0721890473
140 (in isoform 2)Ubiquitination-37.0721890473
140 (in isoform 3)Ubiquitination-37.0721890473
140 (in isoform 4)Ubiquitination-37.0721890473
140UbiquitinationVVPVPYEKMLRDQSA
EEECCHHHHCCCCCE
37.0721890473
143MethylationVPYEKMLRDQSAVVV
CCHHHHCCCCCEEEE
36.10-
146PhosphorylationEKMLRDQSAVVVQGL
HHHCCCCCEEEECCC
27.5928387310
160AcetylationLPEGVAFKHPENYDL
CCCCCCCCCCCCCCH
48.8126051181
160UbiquitinationLPEGVAFKHPENYDL
CCCCCCCCCCCCCCH
48.8121890473
160 (in isoform 1)Ubiquitination-48.8121890473
160 (in isoform 2)Ubiquitination-48.8121890473
160 (in isoform 3)Ubiquitination-48.8121890473
160 (in isoform 4)Ubiquitination-48.8121890473
160UbiquitinationLPEGVAFKHPENYDL
CCCCCCCCCCCCCCH
48.8121890473
171AcetylationNYDLATLKWILENKA
CCCHHHHHHHHHCCC
28.0326051181
171UbiquitinationNYDLATLKWILENKA
CCCHHHHHHHHHCCC
28.03-
177SumoylationLKWILENKAGISFII
HHHHHHCCCCEEEEE
38.32-
181PhosphorylationLENKAGISFIIKRPF
HHCCCCEEEEEECCC
14.9627499020
185AcetylationAGISFIIKRPFLEPK
CCEEEEEECCCCCCC
49.5626051181
185SumoylationAGISFIIKRPFLEPK
CCEEEEEECCCCCCC
49.5628112733
1922-HydroxyisobutyrylationKRPFLEPKKHVGGRV
ECCCCCCCCCCCCEE
46.25-
200SulfoxidationKHVGGRVMVTDADRS
CCCCCEEEEECCCCC
2.3021406390
202PhosphorylationVGGRVMVTDADRSIL
CCCEEEEECCCCCCC
13.8422617229
206MethylationVMVTDADRSILSPGG
EEEECCCCCCCCCCC
27.58-
207PhosphorylationMVTDADRSILSPGGS
EEECCCCCCCCCCCC
28.5523927012
210PhosphorylationDADRSILSPGGSCGP
CCCCCCCCCCCCCCC
21.5919664994
214PhosphorylationSILSPGGSCGPIKVK
CCCCCCCCCCCEEEE
23.0923401153
215GlutathionylationILSPGGSCGPIKVKT
CCCCCCCCCCEEEEC
9.4522555962
219AcetylationGGSCGPIKVKTEPTE
CCCCCCEEEECCCCC
40.5925953088
219MethylationGGSCGPIKVKTEPTE
CCCCCCEEEECCCCC
40.5923583077
219SumoylationGGSCGPIKVKTEPTE
CCCCCCEEEECCCCC
40.5928112733
219UbiquitinationGGSCGPIKVKTEPTE
CCCCCCEEEECCCCC
40.59-
221SumoylationSCGPIKVKTEPTEDS
CCCCEEEECCCCCCC
42.01-
221SumoylationSCGPIKVKTEPTEDS
CCCCEEEECCCCCCC
42.0125114211
222PhosphorylationCGPIKVKTEPTEDSG
CCCEEEECCCCCCCC
50.6220873877
225PhosphorylationIKVKTEPTEDSGISL
EEEECCCCCCCCCEE
46.3120873877
228PhosphorylationKTEPTEDSGISLEMA
ECCCCCCCCCEEEEE
31.6220873877
231PhosphorylationPTEDSGISLEMAAVT
CCCCCCCEEEEEEEE
23.0820873877
238PhosphorylationSLEMAAVTVKEESED
EEEEEEEEEECCCCC
22.5721406692
240SumoylationEMAAVTVKEESEDPD
EEEEEEEECCCCCCC
46.53-
240SumoylationEMAAVTVKEESEDPD
EEEEEEEECCCCCCC
46.53-
248PhosphorylationEESEDPDYYQYNIQA
CCCCCCCCEEEEECC
9.6116738337
248 (in isoform 2)Phosphorylation-9.619012831
248 (in isoform 3)Phosphorylation-9.619012831
248 (in isoform 5)Phosphorylation-9.619012831
249PhosphorylationESEDPDYYQYNIQAG
CCCCCCCEEEEECCC
16.359837922
249 (in isoform 2)Phosphorylation-16.35-
249 (in isoform 3)Phosphorylation-16.35-
249 (in isoform 5)Phosphorylation-16.35-
251 (in isoform 2)Phosphorylation-9.71-
251 (in isoform 3)Phosphorylation-9.71-
251 (in isoform 5)Phosphorylation-9.71-
256 (in isoform 2)Phosphorylation-15.1924144214
259 (in isoform 2)Phosphorylation-60.4324144214
260 (in isoform 2)Phosphorylation-41.6624144214
266 (in isoform 2)Phosphorylation-53.4024144214
270PhosphorylationVDEKQPLSKPLQGSH
CCCCCCCCCCCCCCC
38.6224719451
276 (in isoform 4)Phosphorylation-12.6927732954
277 (in isoform 2)Phosphorylation-31.5028387310
278 (in isoform 2)Phosphorylation-34.4228387310
279 (in isoform 4)Phosphorylation-25.3527732954
280 (in isoform 4)Phosphorylation-45.2027732954
281 (in isoform 2)Phosphorylation-69.8828387310
286 (in isoform 4)Phosphorylation-26.4427732954
297 (in isoform 4)Phosphorylation-39.2627732954
298 (in isoform 4)Phosphorylation-33.2825159151
301 (in isoform 4)Phosphorylation-53.0327732954
312PhosphorylationEDPEVEVTIEDDDYS
CCCCEEEEEECCCCC
12.7326074081
312 (in isoform 2)Ubiquitination-12.7321890473
318PhosphorylationVTIEDDDYSPPSKRP
EEEECCCCCCCCCCC
30.0310373551
319PhosphorylationTIEDDDYSPPSKRPK
EEECCCCCCCCCCCC
37.0126074081
322PhosphorylationDDDYSPPSKRPKANE
CCCCCCCCCCCCCCC
44.6826074081
326SumoylationSPPSKRPKANELPQP
CCCCCCCCCCCCCCC
68.80-
326SumoylationSPPSKRPKANELPQP
CCCCCCCCCCCCCCC
68.8028112733
332 (in isoform 4)Ubiquitination-68.5021890473
333 (in isoform 3)Ubiquitination-29.8921890473
343SumoylationPEPANAGKRKVREFN
CCCCCCCCCCCCCCC
46.78-
343AcetylationPEPANAGKRKVREFN
CCCCCCCCCCCCCCC
46.7825953088
343MethylationPEPANAGKRKVREFN
CCCCCCCCCCCCCCC
46.78-
343SumoylationPEPANAGKRKVREFN
CCCCCCCCCCCCCCC
46.7828112733
353SumoylationVREFNFEKWNARITD
CCCCCHHHHHHHHHH
41.43-
353AcetylationVREFNFEKWNARITD
CCCCCHHHHHHHHHH
41.4326822725
353SumoylationVREFNFEKWNARITD
CCCCCHHHHHHHHHH
41.4328112733
353UbiquitinationVREFNFEKWNARITD
CCCCCHHHHHHHHHH
41.4321890473
353 (in isoform 1)Ubiquitination-41.4321890473
359PhosphorylationEKWNARITDLRKQVE
HHHHHHHHHHHHHHH
24.3523090842
363SumoylationARITDLRKQVEELFE
HHHHHHHHHHHHHHH
67.02-
363UbiquitinationARITDLRKQVEELFE
HHHHHHHHHHHHHHH
67.02-
372SumoylationVEELFERKYAQAIKA
HHHHHHHHHHHHHHH
37.43-
372SumoylationVEELFERKYAQAIKA
HHHHHHHHHHHHHHH
37.43-
372UbiquitinationVEELFERKYAQAIKA
HHHHHHHHHHHHHHH
37.43-
378SumoylationRKYAQAIKAKGPVTI
HHHHHHHHHCCCEEC
47.24-
378SumoylationRKYAQAIKAKGPVTI
HHHHHHHHHCCCEEC
47.24-
378UbiquitinationRKYAQAIKAKGPVTI
HHHHHHHHHCCCEEC
47.24-
380SumoylationYAQAIKAKGPVTIPY
HHHHHHHCCCEECCC
59.7628112733
380UbiquitinationYAQAIKAKGPVTIPY
HHHHHHHCCCEECCC
59.76-
392PhosphorylationIPYPLFQSHVEDLYV
CCCCHHHHHHHHHHC
23.3612082086
398PhosphorylationQSHVEDLYVEGLPEG
HHHHHHHHCCCCCCC
14.5817360941
412PhosphorylationGIPFRRPSTYGIPRL
CCCCCCCHHCCCCHH
32.2323911959
413PhosphorylationIPFRRPSTYGIPRLE
CCCCCCHHCCCCHHH
28.5727794612
414PhosphorylationPFRRPSTYGIPRLER
CCCCCHHCCCCHHHH
19.8628857561
435SumoylationRIRFVIKKHELLNST
HHHHHHHHHHHHHCC
31.05-
435AcetylationRIRFVIKKHELLNST
HHHHHHHHHHHHHCC
31.0527452117
435SumoylationRIRFVIKKHELLNST
HHHHHHHHHHHHHCC
31.0528112733
435UbiquitinationRIRFVIKKHELLNST
HHHHHHHHHHHHHCC
31.05-
435 (in isoform 2)Ubiquitination-31.0521890473
442PhosphorylationKHELLNSTREDLQLD
HHHHHHCCCHHHCCC
36.6828555341
447 (in isoform 2)Ubiquitination-61.0021890473
450SumoylationREDLQLDKPASGVKE
CHHHCCCCCCCCCCH
51.59-
450AcetylationREDLQLDKPASGVKE
CHHHCCCCCCCCCCH
51.5923954790
450SumoylationREDLQLDKPASGVKE
CHHHCCCCCCCCCCH
51.5928112733
450UbiquitinationREDLQLDKPASGVKE
CHHHCCCCCCCCCCH
51.59-
453PhosphorylationLQLDKPASGVKEEWY
HCCCCCCCCCCHHHH
53.2825159151
453 (in isoform 2)Ubiquitination-53.2821890473
455 (in isoform 4)Ubiquitination-6.9921890473
456SumoylationDKPASGVKEEWYARI
CCCCCCCCHHHHHHH
54.14-
4562-HydroxyisobutyrylationDKPASGVKEEWYARI
CCCCCCCCHHHHHHH
54.14-
456AcetylationDKPASGVKEEWYARI
CCCCCCCCHHHHHHH
54.1426051181
456MethylationDKPASGVKEEWYARI
CCCCCCCCHHHHHHH
54.1424129315
456SumoylationDKPASGVKEEWYARI
CCCCCCCCHHHHHHH
54.1428112733
456UbiquitinationDKPASGVKEEWYARI
CCCCCCCCHHHHHHH
54.14-
456 (in isoform 3)Ubiquitination-54.1421890473
460PhosphorylationSGVKEEWYARITKLR
CCCCHHHHHHHHHHH
6.8417360941
467 (in isoform 4)Ubiquitination-26.9521890473
4682-HydroxyisobutyrylationARITKLRKMVDQLFC
HHHHHHHHHHHHHHH
54.43-
468AcetylationARITKLRKMVDQLFC
HHHHHHHHHHHHHHH
54.4326051181
468 (in isoform 3)Ubiquitination-54.4321890473
469SulfoxidationRITKLRKMVDQLFCK
HHHHHHHHHHHHHHH
3.0421406390
473 (in isoform 4)Ubiquitination-4.7521890473
474 (in isoform 3)Ubiquitination-4.8221890473
475S-nitrosocysteineKMVDQLFCKKFAEAL
HHHHHHHHHHHHHHH
6.78-
475S-nitrosylationKMVDQLFCKKFAEAL
HHHHHHHHHHHHHHH
6.7822178444
476UbiquitinationMVDQLFCKKFAEALG
HHHHHHHHHHHHHHC
43.5221906983
476 (in isoform 1)Ubiquitination-43.5221890473
477SumoylationVDQLFCKKFAEALGS
HHHHHHHHHHHHHCC
51.49-
477AcetylationVDQLFCKKFAEALGS
HHHHHHHHHHHHHCC
51.4925953088
477SumoylationVDQLFCKKFAEALGS
HHHHHHHHHHHHHCC
51.49-
477UbiquitinationVDQLFCKKFAEALGS
HHHHHHHHHHHHHCC
51.49-
488SumoylationALGSTEAKAVPYQKF
HHCCCCCCCCCHHHH
43.62-
488AcetylationALGSTEAKAVPYQKF
HHCCCCCCCCCHHHH
43.6226051181
488SumoylationALGSTEAKAVPYQKF
HHCCCCCCCCCHHHH
43.6228112733
488UbiquitinationALGSTEAKAVPYQKF
HHCCCCCCCCCHHHH
43.6221906983
488 (in isoform 1)Ubiquitination-43.6221890473
494SumoylationAKAVPYQKFEAHPND
CCCCCHHHHCCCCCC
39.05-
494AcetylationAKAVPYQKFEAHPND
CCCCCHHHHCCCCCC
39.0525953088
494SumoylationAKAVPYQKFEAHPND
CCCCCHHHHCCCCCC
39.0528112733
494UbiquitinationAKAVPYQKFEAHPND
CCCCCHHHHCCCCCC
39.0521890473
494 (in isoform 1)Ubiquitination-39.0521890473
498 (in isoform 2)Ubiquitination-17.9421890473
503PhosphorylationEAHPNDLYVEGLPEN
CCCCCCCEECCCCCC
10.1821082442
515PhosphorylationPENIPFRSPSWYGIP
CCCCCCCCCCCCCCC
24.5425159151
517PhosphorylationNIPFRSPSWYGIPRL
CCCCCCCCCCCCCHH
33.8925159151
518 (in isoform 4)Ubiquitination-9.9621890473
519PhosphorylationPFRSPSWYGIPRLEK
CCCCCCCCCCCHHHH
14.9822115753
519 (in isoform 3)Ubiquitination-14.9821890473
520 (in isoform 2)Ubiquitination-19.7121890473
526SumoylationYGIPRLEKIIQVGNR
CCCCHHHHHHHHCCE
50.10-
5262-HydroxyisobutyrylationYGIPRLEKIIQVGNR
CCCCHHHHHHHHCCE
50.10-
526AcetylationYGIPRLEKIIQVGNR
CCCCHHHHHHHHCCE
50.1026051181
526MalonylationYGIPRLEKIIQVGNR
CCCCHHHHHHHHCCE
50.1026320211
526SumoylationYGIPRLEKIIQVGNR
CCCCHHHHHHHHCCE
50.1028112733
526UbiquitinationYGIPRLEKIIQVGNR
CCCCHHHHHHHHCCE
50.10-
539UbiquitinationNRIKFVIKRPELLTH
CEEEEEEECHHHHCC
57.5121890473
539 (in isoform 1)Ubiquitination-57.5121890473
540 (in isoform 4)Ubiquitination-20.8521890473
541 (in isoform 3)Ubiquitination-31.4221890473
545PhosphorylationIKRPELLTHSTTEVT
EECHHHHCCCCCEEC
26.8023312004
547PhosphorylationRPELLTHSTTEVTQP
CHHHHCCCCCEECCC
31.6128857561
548PhosphorylationPELLTHSTTEVTQPR
HHHHCCCCCEECCCC
21.2628555341
549PhosphorylationELLTHSTTEVTQPRT
HHHCCCCCEECCCCC
31.3223312004
552PhosphorylationTHSTTEVTQPRTNTP
CCCCCEECCCCCCCC
26.9928555341
556PhosphorylationTEVTQPRTNTPVKED
CEECCCCCCCCCCCC
50.5622167270
558PhosphorylationVTQPRTNTPVKEDWN
ECCCCCCCCCCCCCH
28.9222167270
561SumoylationPRTNTPVKEDWNVRI
CCCCCCCCCCCHHHH
51.68-
561AcetylationPRTNTPVKEDWNVRI
CCCCCCCCCCCHHHH
51.6823954790
561SumoylationPRTNTPVKEDWNVRI
CCCCCCCCCCCHHHH
51.6828112733
561UbiquitinationPRTNTPVKEDWNVRI
CCCCCCCCCCCHHHH
51.6821890473
561 (in isoform 1)Ubiquitination-51.6821890473
573UbiquitinationVRITKLRKQVEEIFN
HHHHHHHHHHHHHHC
69.96-
620PhosphorylationPEGIPFRSPTWFGIP
CCCCCCCCCCCCCCC
27.3621815630
622PhosphorylationGIPFRSPTWFGIPRL
CCCCCCCCCCCCCHH
34.3728387310
636PhosphorylationLERIVRGSNKIKFVV
HHHHHCCCCCEEEEE
25.1220068231
640SumoylationVRGSNKIKFVVKKPE
HCCCCCEEEEEECCE
33.44-
640SumoylationVRGSNKIKFVVKKPE
HCCCCCEEEEEECCE
33.44-
645SumoylationKIKFVVKKPELVISY
CEEEEEECCEEEEEE
31.92-
645AcetylationKIKFVVKKPELVISY
CEEEEEECCEEEEEE
31.9226051181
645SumoylationKIKFVVKKPELVISY
CEEEEEECCEEEEEE
31.92-
651PhosphorylationKKPELVISYLPPGMA
ECCEEEEEECCCCCH
17.0926074081
652PhosphorylationKPELVISYLPPGMAS
CCEEEEEECCCCCHH
16.4726074081
659PhosphorylationYLPPGMASKINTKAL
ECCCCCHHHHCHHHC
25.7718669648
660AcetylationLPPGMASKINTKALQ
CCCCCHHHHCHHHCC
30.3625953088
660SumoylationLPPGMASKINTKALQ
CCCCCHHHHCHHHCC
30.3628112733
660UbiquitinationLPPGMASKINTKALQ
CCCCCHHHHCHHHCC
30.36-
663PhosphorylationGMASKINTKALQSPK
CCHHHHCHHHCCCCC
22.5926074081
664SumoylationMASKINTKALQSPKR
CHHHHCHHHCCCCCC
42.48-
664SumoylationMASKINTKALQSPKR
CHHHHCHHHCCCCCC
42.4828112733
664UbiquitinationMASKINTKALQSPKR
CHHHHCHHHCCCCCC
42.48-
668PhosphorylationINTKALQSPKRPRSP
HCHHHCCCCCCCCCC
32.9923401153
670SumoylationTKALQSPKRPRSPGS
HHHCCCCCCCCCCCC
79.0528112733
674PhosphorylationQSPKRPRSPGSNSKV
CCCCCCCCCCCCCCC
35.9710648599
677PhosphorylationKRPRSPGSNSKVPEI
CCCCCCCCCCCCCEE
41.1223927012
679PhosphorylationPRSPGSNSKVPEIEV
CCCCCCCCCCCEEEE
36.4123927012
680SumoylationRSPGSNSKVPEIEVT
CCCCCCCCCCEEEEE
67.0928112733
687PhosphorylationKVPEIEVTVEGPNNN
CCCEEEEEEECCCCC
10.4730266825
698PhosphorylationPNNNNPQTSAVRTPT
CCCCCCCCCCEECCC
21.6522167270
699PhosphorylationNNNNPQTSAVRTPTQ
CCCCCCCCCEECCCC
21.3722167270
703PhosphorylationPQTSAVRTPTQTNGS
CCCCCEECCCCCCCC
24.8822167270
705PhosphorylationTSAVRTPTQTNGSNV
CCCEECCCCCCCCCC
47.6222167270
707PhosphorylationAVRTPTQTNGSNVPF
CEECCCCCCCCCCCC
43.9828387310
710PhosphorylationTPTQTNGSNVPFKPR
CCCCCCCCCCCCCCC
36.4022167270
711 (in isoform 2)Ubiquitination-47.0521890473
715SumoylationNGSNVPFKPRGREFS
CCCCCCCCCCCCEEE
27.95-
715AcetylationNGSNVPFKPRGREFS
CCCCCCCCCCCCEEE
27.9525953088
715MethylationNGSNVPFKPRGREFS
CCCCCCCCCCCCEEE
27.95-
715SumoylationNGSNVPFKPRGREFS
CCCCCCCCCCCCEEE
27.9528112733
715UbiquitinationNGSNVPFKPRGREFS
CCCCCCCCCCCCEEE
27.95-
722PhosphorylationKPRGREFSFEAWNAK
CCCCCEEEHHHHHCH
19.8822617229
729AcetylationSFEAWNAKITDLKQK
EHHHHHCHHHHHHHH
42.8126051181
729UbiquitinationSFEAWNAKITDLKQK
EHHHHHCHHHHHHHH
42.81-
731 (in isoform 4)Ubiquitination-34.2721890473
732 (in isoform 3)Ubiquitination-56.1721890473
734SumoylationNAKITDLKQKVENLF
HCHHHHHHHHHHHHH
51.38-
734SumoylationNAKITDLKQKVENLF
HCHHHHHHHHHHHHH
51.38-
736SumoylationKITDLKQKVENLFNE
HHHHHHHHHHHHHHH
50.34-
736SumoylationKITDLKQKVENLFNE
HHHHHHHHHHHHHHH
50.34-
736UbiquitinationKITDLKQKVENLFNE
HHHHHHHHHHHHHHH
50.34-
744SumoylationVENLFNEKCGEALGL
HHHHHHHHHHHHHCH
48.95-
7442-HydroxyisobutyrylationVENLFNEKCGEALGL
HHHHHHHHHHHHHCH
48.95-
744SumoylationVENLFNEKCGEALGL
HHHHHHHHHHHHHCH
48.95-
744UbiquitinationVENLFNEKCGEALGL
HHHHHHHHHHHHHCH
48.95-
752SumoylationCGEALGLKQAVKVPF
HHHHHCHHHHCCCCH
34.12-
752SumoylationCGEALGLKQAVKVPF
HHHHHCHHHHCCCCH
34.12-
752UbiquitinationCGEALGLKQAVKVPF
HHHHHCHHHHCCCCH
34.1221906983
752 (in isoform 1)Ubiquitination-34.1221890473
756UbiquitinationLGLKQAVKVPFALFE
HCHHHHCCCCHHHHH
47.40-
764PhosphorylationVPFALFESFPEDFYV
CCHHHHHHCCCCCEE
38.4720068231
770PhosphorylationESFPEDFYVEGLPEG
HHCCCCCEECCCCCC
15.20-
784PhosphorylationGVPFRRPSTFGIPRL
CCCCCCCHHCCCCHH
34.2625159151
785O-linked_GlycosylationVPFRRPSTFGIPRLE
CCCCCCHHCCCCHHH
28.6723301498
785PhosphorylationVPFRRPSTFGIPRLE
CCCCCCHHCCCCHHH
28.6730266825
806UbiquitinationAKIKFIIKKPEMFET
CCEEEEECCHHHHHH
58.42-
807SumoylationKIKFIIKKPEMFETA
CEEEEECCHHHHHHH
35.48-
807SumoylationKIKFIIKKPEMFETA
CEEEEECCHHHHHHH
35.48-
807UbiquitinationKIKFIIKKPEMFETA
CEEEEECCHHHHHHH
35.48-
813PhosphorylationKKPEMFETAIKESTS
CCHHHHHHHHHHCCC
23.5524732914
816SumoylationEMFETAIKESTSSKS
HHHHHHHHHCCCCCC
43.05-
816SumoylationEMFETAIKESTSSKS
HHHHHHHHHCCCCCC
43.0528112733
818PhosphorylationFETAIKESTSSKSPP
HHHHHHHCCCCCCCC
28.7030266825
819PhosphorylationETAIKESTSSKSPPR
HHHHHHCCCCCCCCC
37.8030266825
820PhosphorylationTAIKESTSSKSPPRK
HHHHHCCCCCCCCCC
45.0830266825
821PhosphorylationAIKESTSSKSPPRKI
HHHHCCCCCCCCCCC
36.9223401153
823PhosphorylationKESTSSKSPPRKINS
HHCCCCCCCCCCCCC
41.9322167270
827SumoylationSSKSPPRKINSSPNV
CCCCCCCCCCCCCCC
52.6028112733
827UbiquitinationSSKSPPRKINSSPNV
CCCCCCCCCCCCCCC
52.60-
830PhosphorylationSPPRKINSSPNVNTT
CCCCCCCCCCCCCCC
51.1230278072
831PhosphorylationPPRKINSSPNVNTTA
CCCCCCCCCCCCCCC
18.9230278072
836PhosphorylationNSSPNVNTTASGVED
CCCCCCCCCCCCCCC
21.3230278072
837PhosphorylationSSPNVNTTASGVEDL
CCCCCCCCCCCCCCC
17.3921955146
838 (in isoform 2)Ubiquitination-11.4021890473
839PhosphorylationPNVNTTASGVEDLNI
CCCCCCCCCCCCCCE
41.0821955146
850PhosphorylationDLNIIQVTIPDDDNE
CCCEEEEECCCCCCH
15.4928176443
858 (in isoform 4)Ubiquitination-50.9821890473
859 (in isoform 3)Ubiquitination-4.7821890473
860PhosphorylationDDDNERLSKVEKARQ
CCCCHHHHHHHHHHH
40.6623090842
861SumoylationDDNERLSKVEKARQL
CCCHHHHHHHHHHHH
60.03-
861AcetylationDDNERLSKVEKARQL
CCCHHHHHHHHHHHH
60.0326051181
861SumoylationDDNERLSKVEKARQL
CCCHHHHHHHHHHHH
60.0328112733
864SumoylationERLSKVEKARQLREQ
HHHHHHHHHHHHHHH
52.4328112733
877PhosphorylationEQVNDLFSRKFGEAI
HHHHHHHHHHHHHHH
41.6920068231
879SumoylationVNDLFSRKFGEAIGM
HHHHHHHHHHHHHCC
57.43-
879SumoylationVNDLFSRKFGEAIGM
HHHHHHHHHHHHHCC
57.4328112733
879UbiquitinationVNDLFSRKFGEAIGM
HHHHHHHHHHHHHCC
57.4321890473
879 (in isoform 1)Ubiquitination-57.4321890473
891SumoylationIGMGFPVKVPYRKIT
HCCCCCEECCCCEEE
37.42-
891SumoylationIGMGFPVKVPYRKIT
HCCCCCEECCCCEEE
37.4228112733
891UbiquitinationIGMGFPVKVPYRKIT
HCCCCCEECCCCEEE
37.42-
894PhosphorylationGFPVKVPYRKITINP
CCCEECCCCEEEECC
27.7625884760
896SumoylationPVKVPYRKITINPGC
CEECCCCEEEECCCC
38.06-
896SumoylationPVKVPYRKITINPGC
CEECCCCEEEECCCC
38.06-
896UbiquitinationPVKVPYRKITINPGC
CEECCCCEEEECCCC
38.06-
919PhosphorylationGVSFKAPSYLEISSM
CCCCCCCCCEEHHHH
47.4020068231
920PhosphorylationVSFKAPSYLEISSMR
CCCCCCCCEEHHHHH
13.8017360941
924PhosphorylationAPSYLEISSMRRILD
CCCCEEHHHHHHHHH
14.5420068231
925PhosphorylationPSYLEISSMRRILDS
CCCEEHHHHHHHHHH
23.2120068231
926SulfoxidationSYLEISSMRRILDSA
CCEEHHHHHHHHHHH
2.3921406390
927MethylationYLEISSMRRILDSAE
CEEHHHHHHHHHHHH
25.16-
932PhosphorylationSMRRILDSAEFIKFT
HHHHHHHHHHEEEEE
26.6724667141
957PhosphorylationNNQLVDQSESEGPVI
CCEEECCCCCCCCCC
38.3328348404
959PhosphorylationQLVDQSESEGPVIQE
EEECCCCCCCCCCCC
53.7727251275
967PhosphorylationEGPVIQESAEPSQLE
CCCCCCCCCCHHHCC
22.8928348404
971PhosphorylationIQESAEPSQLEVPAT
CCCCCCHHHCCCCCC
38.6120873877
978PhosphorylationSQLEVPATEEIKETD
HHCCCCCCCCHHCCC
28.2520873877
982SumoylationVPATEEIKETDGSSQ
CCCCCCHHCCCCCCC
58.82-
984PhosphorylationATEEIKETDGSSQIK
CCCCHHCCCCCCCCC
40.4326714015
987PhosphorylationEIKETDGSSQIKQEP
CHHCCCCCCCCCCCC
23.1425159151
988PhosphorylationIKETDGSSQIKQEPD
HHCCCCCCCCCCCCC
41.2625159151
991SumoylationTDGSSQIKQEPDPTW
CCCCCCCCCCCCCCC
40.76-
991SumoylationTDGSSQIKQEPDPTW
CCCCCCCCCCCCCCC
40.7625114211
991UbiquitinationTDGSSQIKQEPDPTW
CCCCCCCCCCCCCCC
40.76-
997PhosphorylationIKQEPDPTW------
CCCCCCCCC------
0.0028985074

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
248YPhosphorylationKinaseBTKQ06187
PSP
248YPhosphorylationKinaseJAK2O60674
PSP
248YPhosphorylationKinaseBTKQ06187
Uniprot
248YPhosphorylationKinaseSRCP12931
PSP
248YPhosphorylationKinaseSRCP12931
PSP
249YPhosphorylationKinaseSRCP12931
PSP
357YPhosphorylationKinaseBTKQ06187
PSP
371SPhosphorylationKinasePRKG1Q13976
GPS
398YPhosphorylationKinaseBTKQ06187
Uniprot
412SPhosphorylationKinasePKG1Q13976
PSP
462YPhosphorylationKinaseBTKQ06187
PSP
503YPhosphorylationKinaseBTKQ06187
Uniprot
611YPhosphorylationKinaseSRCP12931
PSP
627SPhosphorylationKinaseMAPK3P27361
GPS
627SPhosphorylationKinaseMAPK1P28482
GPS
633SPhosphorylationKinaseMAPK3P27361
GPS
633SPhosphorylationKinaseMAPK1P28482
GPS
743SPhosphorylationKinasePRKG1Q13976
GPS
784SPhosphorylationKinasePKG1Q13976
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GTF2I_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 GTF2I_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
12493763
HDAC2_HUMANHDAC2physical
12493763
MYC_HUMANMYCphysical
8377829
KGP1_HUMANPRKG1physical
12082086
BTK_HUMANBTKphysical
10373551
BTK_HUMANBTKphysical
9012831
ATF6A_HUMANATF6physical
11287625
SRF_HUMANSRFphysical
9584171
STAT1_HUMANSTAT1physical
9584171
STAT3_HUMANSTAT3physical
9584171
PIAS2_MOUSEPias2physical
12193603
SIZ2_YEASTNFI1physical
12193603
USF1_HUMANUSF1physical
1961251
MK03_HUMANMAPK3physical
10648599
HDAC3_HUMANHDAC3physical
16943425
MK01_HUMANMAPK1physical
11313464
OBF1_HUMANPOU2AF1physical
21549311
HDAC3_HUMANHDAC3physical
21549311
BRCA1_HUMANBRCA1physical
21407215
LEG3_HUMANLGALS3physical
18662664
SLU7_HUMANSLU7physical
18662664
RSMN_HUMANSNRPNphysical
18662664
SRSF9_HUMANSRSF9physical
22939629
ODPA_HUMANPDHA1physical
22939629
HNRH1_HUMANHNRNPH1physical
22939629
M3K3_HUMANMAP3K3physical
21988832
MK12_HUMANMAPK12physical
21988832
TAB2_HUMANTAB2physical
21988832
PUR8_HUMANADSLphysical
22863883
PYRG2_HUMANCTPS2physical
22863883
PRPS2_HUMANPRPS2physical
22863883
RD23B_HUMANRAD23Bphysical
22863883
RL28_HUMANRPL28physical
22863883
PIAS2_HUMANPIAS2physical
24722188
ZMYM3_HUMANZMYM3physical
24722188
AP2B1_HUMANAP2B1physical
24722188
DPY30_HUMANDPY30physical
24722188
GCC1_HUMANGCC1physical
24722188
MTUS2_HUMANMTUS2physical
24722188
TRAF6_HUMANTRAF6physical
24722188
TCPB_HUMANCCT2physical
26344197
TCPG_HUMANCCT3physical
26344197
NF2IP_HUMANNFATC2IPphysical
26344197
TCPA_HUMANTCP1physical
26344197
TRM1L_HUMANTRMT1Lphysical
26344197
XRCC6_HUMANXRCC6physical
26344197
MDM2_HUMANMDM2physical
26656605
TULP3_HUMANTULP3physical
27173435
ZMYM2_HUMANZMYM2physical
26275350
ZMYM3_HUMANZMYM3physical
26275350

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 GTF2I_HUMAN

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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
"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.
"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.
"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.
"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 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.
"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.
"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.
"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.
"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.
"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.
"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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