Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  General transcription factor IIH subunit 1  

UniProtKB / Swiss-Prot ID :  TF2H1_HUMAN

Gene Name (Synonyms) : 
GTF2H1, BTF2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. 

Protein Sequence MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLH...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHCCCCEEEEECCCEEECCCCCCCEEEEEEEECCEECCCCCCCCCEEEEEEEEE...
Protein Variant
LocationDescription
234R -> W (in dbSNP:rs4150603). VAR_014345
285S -> F (in dbSNP:rs4150636). VAR_014346
517L -> V (in dbSNP:rs4150665). VAR_014347
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATSSE
---CCCCHH
19.05UniProtKB
Link
93Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RDAVKDLLQ
HHHHHHHHH
44.36Phosphositeplus
Link
218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NMTEKEFWT
CCCCHHHHH
49.39Phosphositeplus
Link-
239PhosphoserineLNTGSKDLF
CCCCCHHHH
22.43Phosphositeplus
Link-
339PhosphoserineMDGNSGDAD
CCCCCCCCC
43.51HPRD
Link-
339Phosphoserine.MDGNSGDAD
CCCCCCCCC
43.51UniProtKB
Link-
368PhosphoserineGKNNSVKTI
CCCCCEEEE
34.09HPRD
Link-
368PhosphoserineGKNNSVKTI
CCCCCEEEE
34.09Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
XPA_HUMANphysical interactionMINT-14161MINT11259578
ERCC5_HUMANphysical interactionMINT-16122MINT11259578
ERCC4_HUMANphysical interactionMINT-15872MINT11259578
ERCC2_HUMANphysical interactionDIP:683EDIP8652557
TF2H2_HUMANphysical interactionDIP:687EDIP8652557
GCA14_HUMANphysical interactionEBI-732094
intact16169070
MCM2_HUMANin vitroHPRD:01807HPRD12392551
ERCC2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01807HPRD9130708
8652557
ESR1_HUMANin vitro
in vivo
HPRD:01807HPRD10949034
ERCC3_HUMANin vitro
in vivo
HPRD:01807HPRD9130708
8652557
9118947
8194528
ERCC4_HUMANin vitroHPRD:01807HPRD11259578
ERCC5_HUMANin vitro
in vivo
HPRD:01807HPRD8652557
11259578
PLCG1_HUMANin vitroHPRD:01807HPRD10467411
PRS7_HUMANin vitro
in vivo
HPRD:01807HPRD11118327
P85A_HUMANin vitroHPRD:01807HPRD10467411
T2EA_HUMANin vitroHPRD:01807HPRD11113176
T2EB_HUMANin vitroHPRD:01807HPRD12665589
E2F1_HUMANin vitro
in vivo
HPRD:01807HPRD10428966
TF2H1_HUMANin vitro
in vivo
HPRD:01807HPRD8652557
10777215
8194528
11259578
TF2H2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01807HPRD9130708
8652557
RRN3_HUMANENSP00000265963STRING
RPAB1_HUMANENSP00000265963STRING
RPAB2_HUMANENSP00000265963STRING
TAF9_HUMANENSP00000265963STRING
RPB3_HUMANENSP00000265963STRING
ERCC2_HUMANENSP00000265963STRING
RPB9_HUMANENSP00000265963STRING
RFA3_HUMANENSP00000265963STRING
TF2H3_HUMANENSP00000265963STRING
TBP_HUMANENSP00000265963STRING
T2FA_HUMANENSP00000265963STRING
TAF4_HUMANENSP00000265963STRING
RFA1_HUMANENSP00000265963STRING
CDK7_HUMANENSP00000265963STRING
CCNH_HUMANENSP00000265963STRING
DDB2_HUMANENSP00000265963STRING
TF2H4_HUMANENSP00000265963STRING
MAT1_HUMANENSP00000265963STRING
CCNT1_HUMANENSP00000265963STRING
MCES_HUMANENSP00000265963STRING
ELOB_HUMANENSP00000265963STRING
ELL_HUMANENSP00000265963STRING
RPA2_HUMANENSP00000265963STRING
RPA1_HUMANENSP00000265963STRING
TAF12_HUMANENSP00000265963STRING
CCNT2_HUMANENSP00000265963STRING
ERCC8_HUMANENSP00000265963STRING
T2AG_HUMANENSP00000265963STRING
TAF4B_HUMANENSP00000265963STRING
RPB4_HUMANENSP00000265963STRING
TF2H2_HUMANENSP00000265963STRING
TAF1_HUMANENSP00000265963STRING
SSRP1_HUMANENSP00000265963STRING
T2EA_HUMANENSP00000265963STRING
ELOC_HUMANENSP00000265963STRING
XPC_HUMANENSP00000265963STRING
ERCC3_HUMANENSP00000265963STRING
RPAB3_HUMANENSP00000265963STRING
TF2AA_HUMANENSP00000265963STRING
TAF10_HUMANENSP00000265963STRING
CTDP1_HUMANENSP00000265963STRING
DDB1_HUMANENSP00000265963STRING
RPB7_HUMANENSP00000265963STRING
RPAC2_HUMANENSP00000265963STRING
UBF1_HUMANENSP00000265963STRING
ERCC4_HUMANENSP00000265963STRING
TAF7_HUMANENSP00000265963STRING
RPB2_HUMANENSP00000265963STRING
RPB1_HUMANENSP00000265963STRING
RPAB5_HUMANENSP00000265963STRING
NCBP2_HUMANENSP00000265963STRING
NELFA_HUMANENSP00000265963STRING
TTF1_HUMANENSP00000265963STRING
NELFB_HUMANENSP00000265963STRING
NELFD_HUMANENSP00000265963STRING
RPAB4_HUMANENSP00000265963STRING
ERCC5_HUMANENSP00000265963STRING
T2EB_HUMANENSP00000265963STRING
PTRF_HUMANENSP00000265963STRING
RD23B_HUMANENSP00000265963STRING
XAB2_HUMANENSP00000265963STRING
T2FB_HUMANENSP00000265963STRING
TCEA1_HUMANENSP00000265963STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-339, AND MASS SPECTROMETRY.
Phosphorylation
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-339, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures