GTF2I_RAT - dbPTM
GTF2I_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GTF2I_RAT
UniProt AC Q5U2Y1
Protein Name General transcription factor II-I
Gene Name Gtf2i
Organism Rattus norvegicus (Rat).
Sequence Length 979
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 (By similarity). Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation (By similarity)..
Protein Sequence MAQVAMSALPAEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRKDFQKDFVKYCVEEEEKAAEMHKMKCTTQANRMSVDAVEIETLRKTVEDYFCFCYGKALGKSTVVPVPYEKMLRDQSAVAVQGLPEGVAFKHPEHYDLATLKWILENKAGISFIIKRPFLEPKKHLGGRVMAADADRPMLSPGGSCGPIKVKTEPTEDSGISLEMAAVTVKEESEDPDYYQYNIQGSHHSSEGNEGAEVEVPAEDSTQHVPSETSEDPEVEVTIEDDDYSPPTKRPKSSEPPPPPPVPEPTNAGKRKVREFNFEKWNARITDLRKQVEELFERKYAQAIKAKGPVTIPYPLFQSHVEDLYVEGLPEGIPFRRPSTYGIPRLERILLAKERIRFVIKKHELLNSTREDLQLDKPASGVKEEWYARITKLRKMVDQLFCKKFAEALGSTEAKAVPYQKFEAYPNDLYVEGLPENIPFRSPSWYGIPRLEKIIQVGNRIKFVIKRPELLTHSTTEVTQPRTNTPVKEDWNVRITKLRKQVEEIFNLKFAQALGLTEAVKVPYPVFESNPEFLYVEGLPEGIPFRSPTWFGIPRLERIVRGSNKIKFVVKKPELVVSYLPPGMASKINTKALQSPKRPRSPGSNSKVPEIEVTVEGPNNNSPQTSTVRTPTQTNGSNVPFKPRGREFSFEAWNAKITDLKQKVENLFNEKCGEALGLKQAVKVPFALFESFPEDFYVEGLPEGVPFRRPSTFGIPRLEKILRNKAKIKFIIKKPEMFETAIKESTSSKSPPRKTNSSPSVNTTASGVEDLNIIQVTIPDDDNERLSKVEKARQLREQVNDLFSRKFGEAIGMGFPVKVPYRKITINPGCVVVDGMPPGVSFKAPSYLEISSMRRILDSAEFIKFTVIRPFPGLVINNQLVDQNESEGPVIQESAEASQLEVPATEEIKETDGSSQIKQEPDPTW
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------MAQVAMSAL
------CCCHHHCCC
16.74-
16PhosphorylationLPAEDEESSESRMVV
CCCCCCCCCHHHHHH
37.0425575281
17PhosphorylationPAEDEESSESRMVVT
CCCCCCCCHHHHHHH
42.7625575281
19PhosphorylationEDEESSESRMVVTFL
CCCCCCHHHHHHHHH
27.8525575281
96PhosphorylationEMHKMKCTTQANRMS
HHHHCCCCCCHHHCC
19.2023984901
97PhosphorylationMHKMKCTTQANRMSV
HHHCCCCCCHHHCCC
34.8423984901
103PhosphorylationTTQANRMSVDAVEIE
CCCHHHCCCCEEEHH
17.3827097102
130AcetylationCYGKALGKSTVVPVP
HHHHHCCCCCEEECC
43.75-
210PhosphorylationDADRPMLSPGGSCGP
CCCCCCCCCCCCCCC
18.4227097102
214PhosphorylationPMLSPGGSCGPIKVK
CCCCCCCCCCCEEEE
23.0927097102
222 (in isoform 2)Phosphorylation-50.6223984901
225 (in isoform 2)Phosphorylation-46.3123984901
228 (in isoform 2)Phosphorylation-31.6223298284
233 (in isoform 2)Phosphorylation-21.7123298284
248PhosphorylationEESEDPDYYQYNIQG
ECCCCCCCEEEEEEC
9.61-
298PhosphorylationVTIEDDDYSPPTKRP
EEEECCCCCCCCCCC
30.03-
302PhosphorylationDDDYSPPTKRPKSSE
CCCCCCCCCCCCCCC
42.9728689409
307PhosphorylationPPTKRPKSSEPPPPP
CCCCCCCCCCCCCCC
42.4929779826
308PhosphorylationPTKRPKSSEPPPPPP
CCCCCCCCCCCCCCC
61.3227097102
334AcetylationVREFNFEKWNARITD
EEECCHHHHHHHHHH
41.43-
379PhosphorylationQSHVEDLYVEGLPEG
HHHHHHHHCCCCCCC
14.58-
393PhosphorylationGIPFRRPSTYGIPRL
CCCCCCCHHCCCCHH
32.2327097102
394PhosphorylationIPFRRPSTYGIPRLE
CCCCCCHHCCCCHHH
28.5728432305
395PhosphorylationPFRRPSTYGIPRLER
CCCCCHHCCCCHHHH
19.8628432305
431AcetylationREDLQLDKPASGVKE
CHHHCCCCCCCCCCH
51.5922902405
484PhosphorylationEAYPNDLYVEGLPEN
CCCCCCCEECCCCCC
10.18-
496PhosphorylationPENIPFRSPSWYGIP
CCCCCCCCCCCCCCC
24.5423984901
498PhosphorylationNIPFRSPSWYGIPRL
CCCCCCCCCCCCCHH
33.8923984901
500PhosphorylationPFRSPSWYGIPRLEK
CCCCCCCCCCCHHHH
14.9823984901
537PhosphorylationTEVTQPRTNTPVKED
CEECCCCCCCCCCCC
50.5628432305
539PhosphorylationVTQPRTNTPVKEDWN
ECCCCCCCCCCCCCH
28.9227097102
601PhosphorylationPEGIPFRSPTWFGIP
CCCCCCCCCCCCCCC
27.3627097102
649PhosphorylationINTKALQSPKRPRSP
HCHHHCCCCCCCCCC
32.9922108457
655PhosphorylationQSPKRPRSPGSNSKV
CCCCCCCCCCCCCCC
35.9725403869
658PhosphorylationKRPRSPGSNSKVPEI
CCCCCCCCCCCCCEE
41.1222673903
660PhosphorylationPRSPGSNSKVPEIEV
CCCCCCCCCCCEEEE
36.4125532521
668PhosphorylationKVPEIEVTVEGPNNN
CCCEEEEEEECCCCC
10.4723984901
676PhosphorylationVEGPNNNSPQTSTVR
EECCCCCCCCCCEEE
22.1027097102
679PhosphorylationPNNNSPQTSTVRTPT
CCCCCCCCCEEECCC
29.7427097102
680PhosphorylationNNNSPQTSTVRTPTQ
CCCCCCCCEEECCCC
21.4723984901
681PhosphorylationNNSPQTSTVRTPTQT
CCCCCCCEEECCCCC
19.8623984901
684PhosphorylationPQTSTVRTPTQTNGS
CCCCEEECCCCCCCC
26.7627097102
686PhosphorylationTSTVRTPTQTNGSNV
CCEEECCCCCCCCCC
47.6227097102
696AcetylationNGSNVPFKPRGREFS
CCCCCCCCCCCCEEE
27.95-
703PhosphorylationKPRGREFSFEAWNAK
CCCCCEEEHHHHHCH
19.8823984901
765PhosphorylationGVPFRRPSTFGIPRL
CCCCCCCHHCCCCHH
34.2627097102
766PhosphorylationVPFRRPSTFGIPRLE
CCCCCCHHCCCCHHH
28.6728432305
799PhosphorylationFETAIKESTSSKSPP
HHHHHHHCCCCCCCC
28.7028432305
800PhosphorylationETAIKESTSSKSPPR
HHHHHHCCCCCCCCC
37.8026437020
801PhosphorylationTAIKESTSSKSPPRK
HHHHHCCCCCCCCCC
45.0826437020
802PhosphorylationAIKESTSSKSPPRKT
HHHHCCCCCCCCCCC
36.9226437020
804PhosphorylationKESTSSKSPPRKTNS
HHCCCCCCCCCCCCC
41.9325403869
809PhosphorylationSKSPPRKTNSSPSVN
CCCCCCCCCCCCCCC
41.4323984901
811PhosphorylationSPPRKTNSSPSVNTT
CCCCCCCCCCCCCCC
49.1923984901
812PhosphorylationPPRKTNSSPSVNTTA
CCCCCCCCCCCCCCC
24.2223984901
814PhosphorylationRKTNSSPSVNTTASG
CCCCCCCCCCCCCCC
29.9123984901
817PhosphorylationNSSPSVNTTASGVED
CCCCCCCCCCCCCCC
22.9123984901
818PhosphorylationSSPSVNTTASGVEDL
CCCCCCCCCCCCCCC
17.3927097102
820PhosphorylationPSVNTTASGVEDLNI
CCCCCCCCCCCCCCE
41.0823984901
831PhosphorylationDLNIIQVTIPDDDNE
CCCEEEEECCCCCCH
15.4927097102

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
248YPhosphorylationKinaseBTK-Uniprot
379YPhosphorylationKinaseBTK-Uniprot
393SPhosphorylationKinasePRKG1-Uniprot
484YPhosphorylationKinaseBTK-Uniprot
765SPhosphorylationKinasePRKG1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GTF2I_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GTF2I_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GTF2I_RAT

loading...

Related Literatures of Post-Translational Modification

TOP