T2FB_HUMAN - dbPTM
T2FB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID T2FB_HUMAN
UniProt AC P13984
Protein Name General transcription factor IIF subunit 2
Gene Name GTF2F2
Organism Homo sapiens (Human).
Sequence Length 249
Subcellular Localization Nucleus .
Protein Description TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity..
Protein Sequence MAERGELDLTGAKQNTGVWLVKVPKYLSQQWAKASGRGEVGKLRIAKTQGRTEVSFTLNEDLANIHDIGGKPASVSAPREHPFVLQSVGGQTLTVFTESSSDKLSLEGIVVQRAECRPAASENYMRLKRLQIEESSKPVRLSQQLDKVVTTNYKPVANHQYNIEYERKKKEDGKRARADKQHVLDMLFSAFEKHQYYNLKDLVDITKQPVVYLKEILKEIGVQNVKGIHKNTWELKPEYRHYQGEEKSD
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------MAERGELDL
------CCCCCCCCC		18.3919413330
10PhosphorylationERGELDLTGAKQNTG
CCCCCCCCCCCCCCC		34.46-
13UbiquitinationELDLTGAKQNTGVWL
CCCCCCCCCCCCEEE		45.4821890473
22UbiquitinationNTGVWLVKVPKYLSQ
CCCEEEEECHHHHHH		51.1219608861
22AcetylationNTGVWLVKVPKYLSQ
CCCEEEEECHHHHHH		51.1219608861
25SumoylationVWLVKVPKYLSQQWA
EEEEECHHHHHHHHH		62.91-
25UbiquitinationVWLVKVPKYLSQQWA
EEEEECHHHHHHHHH		62.91-
25AcetylationVWLVKVPKYLSQQWA
EEEEECHHHHHHHHH		62.9125953088
25SumoylationVWLVKVPKYLSQQWA
EEEEECHHHHHHHHH		62.91-
33UbiquitinationYLSQQWAKASGRGEV
HHHHHHHHHCCCCCC		39.8819608861
33AcetylationYLSQQWAKASGRGEV
HHHHHHHHHCCCCCC		39.8819608861
33MethylationYLSQQWAKASGRGEV
HHHHHHHHHCCCCCC		39.8819608861
35PhosphorylationSQQWAKASGRGEVGK
HHHHHHHCCCCCCCE		28.46-
37MethylationQWAKASGRGEVGKLR
HHHHHCCCCCCCEEE		35.29-
42AcetylationSGRGEVGKLRIAKTQ
CCCCCCCEEEEEECC		39.5023749302
71AcetylationNIHDIGGKPASVSAP
CHHHCCCEECCCCCC		32.0023749302
71UbiquitinationNIHDIGGKPASVSAP
CHHHCCCEECCCCCC		32.0021890473
74PhosphorylationDIGGKPASVSAPREH
HCCCEECCCCCCCCC		25.7322210691
76PhosphorylationGGKPASVSAPREHPF
CCEECCCCCCCCCCE		30.0220068231
87PhosphorylationEHPFVLQSVGGQTLT
CCCEEEEECCCEEEE		20.69-
124PhosphorylationRPAASENYMRLKRLQ
CCCCCHHHHHHEECC		4.6025884760
135PhosphorylationKRLQIEESSKPVRLS
EECCCCCCCCCCCHH		30.7629083192
136PhosphorylationRLQIEESSKPVRLSQ
ECCCCCCCCCCCHHH		44.2325159151
137AcetylationLQIEESSKPVRLSQQ
CCCCCCCCCCCHHHH		57.7319608861
137UbiquitinationLQIEESSKPVRLSQQ
CCCCCCCCCCCHHHH		57.7321906983
142PhosphorylationSSKPVRLSQQLDKVV
CCCCCCHHHHHCCEE		12.8117525332
147UbiquitinationRLSQQLDKVVTTNYK
CHHHHHCCEEECCCC		47.3921890473
150PhosphorylationQQLDKVVTTNYKPVA
HHHCCEEECCCCCCC		16.5928152594
151PhosphorylationQLDKVVTTNYKPVAN
HHCCEEECCCCCCCC		25.5828152594
153PhosphorylationDKVVTTNYKPVANHQ
CCEEECCCCCCCCCC		17.9928152594
154UbiquitinationKVVTTNYKPVANHQY
CEEECCCCCCCCCCC		34.7821890473
154AcetylationKVVTTNYKPVANHQY
CEEECCCCCCCCCCC		34.7823954790
154MalonylationKVVTTNYKPVANHQY
CEEECCCCCCCCCCC		34.7826320211
161PhosphorylationKPVANHQYNIEYERK
CCCCCCCCCEEEEEC		15.5728152594
165PhosphorylationNHQYNIEYERKKKED
CCCCCEEEEECHHHC		19.7628152594
1802-HydroxyisobutyrylationGKRARADKQHVLDML
CHHHHHHHHHHHHHH		41.12-
189PhosphorylationHVLDMLFSAFEKHQY
HHHHHHHHHHHHHCC		28.2524719451
193AcetylationMLFSAFEKHQYYNLK
HHHHHHHHHCCCCHH		29.5621466224
196PhosphorylationSAFEKHQYYNLKDLV
HHHHHHCCCCHHHHH		8.2728064214
197PhosphorylationAFEKHQYYNLKDLVD
HHHHHCCCCHHHHHH		13.8828102081
200UbiquitinationKHQYYNLKDLVDITK
HHCCCCHHHHHHCCC		45.4321890473
2072-HydroxyisobutyrylationKDLVDITKQPVVYLK
HHHHHCCCCCCHHHH		53.60-
218UbiquitinationVYLKEILKEIGVQNV
HHHHHHHHHHCCCCC		53.61-
226UbiquitinationEIGVQNVKGIHKNTW
HHCCCCCCCCCCCCE		60.75-
236UbiquitinationHKNTWELKPEYRHYQ
CCCCEEECCHHCCCC		25.04-
236SumoylationHKNTWELKPEYRHYQ
CCCCEEECCHHCCCC		25.04-
236SumoylationHKNTWELKPEYRHYQ
CCCCEEECCHHCCCC		25.04-
239PhosphorylationTWELKPEYRHYQGEE
CEEECCHHCCCCCCC		15.9526074081
242PhosphorylationLKPEYRHYQGEEKSD
ECCHHCCCCCCCCCC		14.8226074081
248PhosphorylationHYQGEEKSD------
CCCCCCCCC------		52.4028176443
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 T2FB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of T2FB_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 T2FB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HTSF1_HUMANHTATSF1physical
10454543
RPAB1_HUMANPOLR2Ephysical
11278533
T2EB_HUMANGTF2E2physical
11113176
RPB1_HUMANPOLR2Aphysical
17643375
RPB2_HUMANPOLR2Bphysical
17643375
RPB7_HUMANPOLR2Gphysical
17643375
RPAB3_HUMANPOLR2Hphysical
17643375
CTDP1_HUMANCTDP1physical
17643375
BAG6_HUMANBAG6physical
17643375
MED29_HUMANMED29physical
17643375
T2FA_HUMANGTF2F1physical
7827505
TAF10_HUMANTAF10physical
10373431
TAF5_HUMANTAF5physical
10373431
TAF4_HUMANTAF4physical
10373431
TF2B_HUMANGTF2Bphysical
16878124
HMGA1_HUMANHMGA1physical
18850631
RL27A_HUMANRPL27Aphysical
20195357
TC1D2_HUMANTCTEX1D2physical
20195357
U5S1_HUMANEFTUD2physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
GLYC_HUMANSHMT1physical
22863883
SRRT_HUMANSRRTphysical
26344197
SPT4H_HUMANSUPT4H1physical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
KLF5_HUMANKLF5physical
9089417
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 T2FB_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-22; LYS-33 AND LYS-137, ANDMASS 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-142, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASSSPECTROMETRY.

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