T2EA_HUMAN - dbPTM
T2EA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T2EA_HUMAN
UniProt AC P29083
Protein Name General transcription factor IIE subunit 1
Gene Name GTF2E1
Organism Homo sapiens (Human).
Sequence Length 439
Subcellular Localization Nucleus.
Protein Description Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase..
Protein Sequence MADPDVLTEVPAALKRLAKYVIRGFYGIEHALALDILIRNSCVKEEDMLELLKFDRKQLRSVLNNLKGDKFIKCRMRVETAADGKTTRHNYYFINYRTLVNVVKYKLDHMRRRIETDERDSTNRASFKCPVCSSTFTDLEANQLFDPMTGTFRCTFCHTEVEEDESAMPKKDARTLLARFNEQIEPIYALLRETEDVNLAYEILEPEPTEIPALKQSKDHAATTAGAASLAGGHHREAWATKGPSYEDLYTQNVVINMDDQEDLHRASLEGKSAKERPIWLRESTVQGAYGSEDMKEGGIDMDAFQEREEGHAGPDDNEEVMRALLIHEKKTSSAMAGSVGAAAPVTAANGSDSESETSESDDDSPPRPAAVAVHKREEDEEEDDEFEEVADDPIVMVAGRPFSYSEVSQRPELVAQMTPEEKEAYIAMGQRMFEDLFE
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------MADPDVLTE
------CCCHHHHHH		36.7222814378
8PhosphorylationMADPDVLTEVPAALK
CCCHHHHHHHHHHHH		34.4821406692
15UbiquitinationTEVPAALKRLAKYVI
HHHHHHHHHHHHHHH		40.4124816145
152-HydroxyisobutyrylationTEVPAALKRLAKYVI
HHHHHHHHHHHHHHH		40.41-
19AcetylationAALKRLAKYVIRGFY
HHHHHHHHHHHHHHC		44.6425953088
19MethylationAALKRLAKYVIRGFY
HHHHHHHHHHHHHHC		44.64-
44AcetylationLIRNSCVKEEDMLEL
HHHCCCCCHHHHHHH		60.7626051181
67AcetylationRSVLNNLKGDKFIKC
HHHHHHCCCCCEEEE		68.1619608861
67UbiquitinationRSVLNNLKGDKFIKC
HHHHHHCCCCCEEEE		68.1633845483
67MalonylationRSVLNNLKGDKFIKC
HHHHHHCCCCCEEEE		68.1626320211
70AcetylationLNNLKGDKFIKCRMR
HHHCCCCCEEEEEEE		58.6225953088
73UbiquitinationLKGDKFIKCRMRVET
CCCCCEEEEEEEEEE		20.9424816145
80PhosphorylationKCRMRVETAADGKTT
EEEEEEEECCCCCCE		25.04-
85AcetylationVETAADGKTTRHNYY
EEECCCCCCEECCEE		47.4719817303
85UbiquitinationVETAADGKTTRHNYY
EEECCCCCCEECCEE		47.4724816145
86PhosphorylationETAADGKTTRHNYYF
EECCCCCCEECCEEE		34.2929083192
87PhosphorylationTAADGKTTRHNYYFI
ECCCCCCEECCEEEE		33.1629083192
91PhosphorylationGKTTRHNYYFINYRT
CCCEECCEEEEEHHH		8.1420090780
92PhosphorylationKTTRHNYYFINYRTL
CCEECCEEEEEHHHH		11.8722817900
98PhosphorylationYYFINYRTLVNVVKY
EEEEEHHHHHHHHHH		25.3820068231
104UbiquitinationRTLVNVVKYKLDHMR
HHHHHHHHHHHHHHH		32.17-
105PhosphorylationTLVNVVKYKLDHMRR
HHHHHHHHHHHHHHH		12.7420068231
126PhosphorylationRDSTNRASFKCPVCS
CCCCCCCCCCCCCCC		23.2324719451
188PhosphorylationNEQIEPIYALLRETE
HHHHHHHHHHHHHCC		11.2521945579
201PhosphorylationTEDVNLAYEILEPEP
CCCCCHHHHHHCCCC		13.4828796482
218UbiquitinationIPALKQSKDHAATTA
CCCHHCCCCCHHHHH		51.5529967540
229PhosphorylationATTAGAASLAGGHHR
HHHHHHHHHHCCCCH		20.4428555341
245PhosphorylationAWATKGPSYEDLYTQ
HHCCCCCCHHHHHCC		50.2329978859
246PhosphorylationWATKGPSYEDLYTQN
HCCCCCCHHHHHCCC		19.3229978859
250PhosphorylationGPSYEDLYTQNVVIN
CCCHHHHHCCCEEEE		20.7129978859
251PhosphorylationPSYEDLYTQNVVINM
CCHHHHHCCCEEEEC		22.4427642862
268PhosphorylationQEDLHRASLEGKSAK
HHHHHHHHHCCCCCC		27.2325159151
272UbiquitinationHRASLEGKSAKERPI
HHHHHCCCCCCCCCC		37.5529967540
284PhosphorylationRPIWLRESTVQGAYG
CCCEEEECCCCCCCC		27.6922210691
285PhosphorylationPIWLRESTVQGAYGS
CCEEEECCCCCCCCC		16.4627251275
290PhosphorylationESTVQGAYGSEDMKE
ECCCCCCCCCHHHHH		28.1927732954
292PhosphorylationTVQGAYGSEDMKEGG
CCCCCCCCHHHHHCC		20.1121815630
296UbiquitinationAYGSEDMKEGGIDMD
CCCCHHHHHCCCCHH		66.5824816145
330AcetylationRALLIHEKKTSSAMA
HHHHHHCCCCCCCCC		47.3825953088
330UbiquitinationRALLIHEKKTSSAMA
HHHHHHCCCCCCCCC		47.3833845483
332PhosphorylationLLIHEKKTSSAMAGS
HHHHCCCCCCCCCCC		38.6926074081
333PhosphorylationLIHEKKTSSAMAGSV
HHHCCCCCCCCCCCC		25.6126074081
334PhosphorylationIHEKKTSSAMAGSVG
HHCCCCCCCCCCCCC		27.5626074081
339PhosphorylationTSSAMAGSVGAAAPV
CCCCCCCCCCCCCCE		14.0826074081
347PhosphorylationVGAAAPVTAANGSDS
CCCCCCEEECCCCCC		20.9926074081
352PhosphorylationPVTAANGSDSESETS
CEEECCCCCCCCCCC		37.4626074081
354PhosphorylationTAANGSDSESETSES
EECCCCCCCCCCCCC		44.7326074081
356PhosphorylationANGSDSESETSESDD
CCCCCCCCCCCCCCC		50.5626074081
358PhosphorylationGSDSESETSESDDDS
CCCCCCCCCCCCCCC		47.2621406692
359PhosphorylationSDSESETSESDDDSP
CCCCCCCCCCCCCCC		30.9322210691
361PhosphorylationSESETSESDDDSPPR
CCCCCCCCCCCCCCC		46.2121406692
365PhosphorylationTSESDDDSPPRPAAV
CCCCCCCCCCCCCEE		43.7421406692
419PhosphorylationPELVAQMTPEEKEAY
HHHHHCCCHHHHHHH		18.5725159151
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 T2EA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T2EA_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 T2EA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF2B_HUMANGTF2Bphysical
9159119
TBP_HUMANTBPphysical
9159119
TAF11_HUMANTAF11physical
9159119
TF2H4_HUMANGTF2H4physical
9159119
TF2AA_HUMANGTF2A1physical
11509574
SND1_HUMANSND1physical
7651391
RPB1_HUMANPOLR2Aphysical
7926747
T2FB_HUMANGTF2F2physical
7926747
T2FA_HUMANGTF2F1physical
7926747
TBP_HUMANTBPphysical
7926747
TAF1_HUMANTAF1physical
7926747
ERCC3_HUMANERCC3physical
7926747
T2EB_HUMANGTF2E2physical
7926747
TAF6_HUMANTAF6physical
7926747
T2EB_HUMANGTF2E2physical
9677423
T2EB_HUMANGTF2E2physical
11113176
T2EB_HUMANGTF2E2physical
17643375
NEMO_HUMANIKBKGphysical
20211142
MTG8R_HUMANCBFA2T2physical
20211142
TRI29_HUMANTRIM29physical
20211142
PHS2_HUMANPCBD2physical
20211142
TRI15_HUMANTRIM15physical
20211142
ZBTB9_HUMANZBTB9physical
20211142
ZSCA1_HUMANZSCAN1physical
20211142
A4_HUMANAPPphysical
21832049
T2EB_HUMANGTF2E2physical
22939629
T2EB_HUMANGTF2E2physical
16547462
TF2H1_HUMANGTF2H1physical
18354501
AASD1_HUMANAARSD1physical
22863883
GCP60_HUMANACBD3physical
22863883
U5S1_HUMANEFTUD2physical
22863883
SYHC_HUMANHARSphysical
22863883
NSUN2_HUMANNSUN2physical
22863883
OXR1_HUMANOXR1physical
22863883
RUSD2_HUMANRPUSD2physical
22863883
SYSC_HUMANSARSphysical
22863883
SH3G1_HUMANSH3GL1physical
22863883
SHLB2_HUMANSH3GLB2physical
22863883
SNF8_HUMANSNF8physical
22863883
TTC1_HUMANTTC1physical
22863883
XPO5_HUMANXPO5physical
22863883
APC5_HUMANANAPC5physical
26344197
MCAF1_HUMANATF7IPphysical
26344197
EF1G_HUMANEEF1Gphysical
26344197
T2EB_HUMANGTF2E2physical
26344197
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 T2EA_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, 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-67, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-268, AND MASSSPECTROMETRY.

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