TF2B_HUMAN - dbPTM
TF2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF2B_HUMAN
UniProt AC Q00403
Protein Name Transcription initiation factor IIB
Gene Name GTF2B
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Nucleus.
Protein Description General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II..
Protein Sequence MASTSRLDALPRVTCPNHPDAILVEDYRAGDMICPECGLVVGDRVIDVGSEWRTFSNDKATKDPSRVGDSQNPLLSDGDLSTMIGKGTGAASFDEFGNSKYQNRRTMSSSDRAMMNAFKEITTMADRINLPRNIVDRTNNLFKQVYEQKSLKGRANDAIASACLYIACRQEGVPRTFKEICAVSRISKKEIGRCFKLILKALETSVDLITTGDFMSRFCSNLCLPKQVQMAATHIARKAVELDLVPGRSPISVAAAAIYMASQASAEKRTQKEIGDIAGVADVTIRQSYRLIYPRAPDLFPTDFKFDTPVDKLPQL
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
3Phosphorylation-----MASTSRLDAL
-----CCCCCCCCCC
26.1423186163
4Phosphorylation----MASTSRLDALP
----CCCCCCCCCCC
14.3423186163
5Phosphorylation---MASTSRLDALPR
---CCCCCCCCCCCC
28.4923186163
27PhosphorylationDAILVEDYRAGDMIC
CEEEECCCCCCCEEC
6.7221214269
32SulfoxidationEDYRAGDMICPECGL
CCCCCCCEECCCCCC
3.1221406390
55UbiquitinationVGSEWRTFSNDKATK
CCCCCEECCCCCCCC
4.8822817900
59UbiquitinationWRTFSNDKATKDPSR
CEECCCCCCCCCHHH
63.3129967540
65PhosphorylationDKATKDPSRVGDSQN
CCCCCCHHHCCCCCC
50.1323090842
69UbiquitinationKDPSRVGDSQNPLLS
CCHHHCCCCCCCCCC
44.1621890473
70PhosphorylationDPSRVGDSQNPLLSD
CHHHCCCCCCCCCCC
26.4021712546
76PhosphorylationDSQNPLLSDGDLSTM
CCCCCCCCCCCHHHH
47.4325159151
81PhosphorylationLLSDGDLSTMIGKGT
CCCCCCHHHHCCCCC
22.2228464451
82PhosphorylationLSDGDLSTMIGKGTG
CCCCCHHHHCCCCCC
21.8029116813
83SulfoxidationSDGDLSTMIGKGTGA
CCCCHHHHCCCCCCC
3.2321406390
86UbiquitinationDLSTMIGKGTGAASF
CHHHHCCCCCCCCCH
42.2321906983
88UbiquitinationSTMIGKGTGAASFDE
HHHCCCCCCCCCHHH
27.4223000965
88PhosphorylationSTMIGKGTGAASFDE
HHHCCCCCCCCCHHH
27.4227251275
92PhosphorylationGKGTGAASFDEFGNS
CCCCCCCCHHHCCCC
32.4725159151
100UbiquitinationFDEFGNSKYQNRRTM
HHHCCCCHHCCCCCC
55.6523000965
100AcetylationFDEFGNSKYQNRRTM
HHHCCCCHHCCCCCC
55.6525953088
109PhosphorylationQNRRTMSSSDRAMMN
CCCCCCCHHHHHHHH
25.9922210691
110PhosphorylationNRRTMSSSDRAMMNA
CCCCCCHHHHHHHHH
24.6522210691
112UbiquitinationRTMSSSDRAMMNAFK
CCCCHHHHHHHHHHH
26.7421890473
119UbiquitinationRAMMNAFKEITTMAD
HHHHHHHHHHHHHHH
45.8823000965
123PhosphorylationNAFKEITTMADRINL
HHHHHHHHHHHHCCC
18.94-
127MethylationEITTMADRINLPRNI
HHHHHHHHCCCCHHH
15.34-
143UbiquitinationDRTNNLFKQVYEQKS
HHHHHHHHHHHHHHC
41.8621906983
147UbiquitinationNLFKQVYEQKSLKGR
HHHHHHHHHHCCCCC
53.3123000965
149UbiquitinationFKQVYEQKSLKGRAN
HHHHHHHHCCCCCHH
45.9033845483
178UbiquitinationEGVPRTFKEICAVSR
CCCCCCHHHHHHHHC
45.6223000965
178AcetylationEGVPRTFKEICAVSR
CCCCCCHHHHHHHHC
45.6225953088
196AcetylationKEIGRCFKLILKALE
HHHHHHHHHHHHHHH
37.9425953088
238UbiquitinationAATHIARKAVELDLV
HHHHHHHHHHHCCCC
48.0012931194
238AcetylationAATHIARKAVELDLV
HHHHHHHHHHHCCCC
48.0012931194
249PhosphorylationLDLVPGRSPISVAAA
CCCCCCCCHHHHHHH
32.2825159151
252PhosphorylationVPGRSPISVAAAAIY
CCCCCHHHHHHHHHH
14.7525627689
270PhosphorylationQASAEKRTQKEIGDI
HHHHHHHHHHHHHHH
55.87-
272UbiquitinationSAEKRTQKEIGDIAG
HHHHHHHHHHHHHHC
51.16-
274UbiquitinationEKRTQKEIGDIAGVA
HHHHHHHHHHHHCCC
8.4922817900
281UbiquitinationIGDIAGVADVTIRQS
HHHHHCCCCEEEEEE
12.4924816145
284PhosphorylationIAGVADVTIRQSYRL
HHCCCCEEEEEEEEE
15.81-
293PhosphorylationRQSYRLIYPRAPDLF
EEEEEEECCCCCCCC
7.4022817900
305UbiquitinationDLFPTDFKFDTPVDK
CCCCCCCCCCCCHHH
45.1822817900
312UbiquitinationKFDTPVDKLPQL---
CCCCCHHHCCCC---
63.4021906983

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 TF2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
238KAcetylation

12931194

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 TF2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_HUMANTBPphysical
9159119
TAF11_HUMANTAF11physical
9159119
TF2H4_HUMANGTF2H4physical
9159119
JUN_HUMANJUNphysical
7848298
T2FB_HUMANGTF2F2physical
8662660
T2FA_HUMANGTF2F1physical
8662660
REL_HUMANRELphysical
8413269
RPC1_HUMANPOLR3Aphysical
11416169
PKP2_HUMANPKP2physical
11416169
STF1_HUMANNR5A1physical
10478848
T2EB_HUMANGTF2E2physical
11113176
KLF5_HUMANKLF5physical
9089417
RPB1_HUMANPOLR2Aphysical
17643375
CTDP1_HUMANCTDP1physical
17643375
RPAB3_HUMANPOLR2Hphysical
17643375
VP16_HHV11UL48physical
15081896
NCOR1_HUMANNCOR1physical
9611234
TAF9_HUMANTAF9physical
9611234
TBP_HUMANTBPphysical
17994014
NXF1_HUMANNXF1physical
7707528
TBP_HUMANTBPphysical
10619841
TBP_HUMANTBPphysical
7671313
RPAB1_HUMANPOLR2Ephysical
9054408
TBP_HUMANTBPphysical
9054408
THA_HUMANTHRAphysical
7609079
SRA1_HUMANSRA1physical
20398657
TF65_HUMANRELAphysical
15013781
S22A2_HUMANSLC22A2physical
21988832
HMGCL_HUMANHMGCLphysical
21988832
JAK3_HUMANJAK3physical
21988832
TNIP1_HUMANTNIP1physical
25416956
NC2A_HUMANDRAP1physical
25416956
ILEU_HUMANSERPINB1physical
26186194
CYTS_HUMANCST4physical
26186194
CYTN_HUMANCST1physical
26186194
CYTT_HUMANCST2physical
26186194
PIGR_HUMANPIGRphysical
26186194
ZG16B_HUMANZG16Bphysical
26186194
MUC7_HUMANMUC7physical
26186194
PRP1_HUMANPRB1physical
26186194
OXSM_HUMANOXSMphysical
26186194
ALKB2_HUMANALKBH2physical
26344197
T2FB_HUMANGTF2F2physical
26344197
NP1L1_HUMANNAP1L1physical
26344197
NSUN2_HUMANNSUN2physical
26344197
PRP18_HUMANPRPF18physical
26344197
RFC5_HUMANRFC5physical
26344197
CYTT_HUMANCST2physical
28514442
CYTN_HUMANCST1physical
28514442
PIGR_HUMANPIGRphysical
28514442
CYTS_HUMANCST4physical
28514442
PRP1_HUMANPRB1physical
28514442
ILEU_HUMANSERPINB1physical
28514442
ZG16B_HUMANZG16Bphysical
28514442
OXSM_HUMANOXSMphysical
28514442
IGJ_HUMANIGJphysical
28514442
MUC7_HUMANMUC7physical
28514442

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 TF2B_HUMAN

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Related Literatures of Post-Translational Modification
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-76, 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-76, AND MASSSPECTROMETRY.

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