TF2H5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TF2H5_HUMAN
• UniProt AC: Q6ZYL4
• Protein Name: General transcription factor IIH subunit 5
• Gene Name: GTF2H5
• Organism: Homo sapiens (Human).
• Sequence Length: 71
• Subcellular Localization: Nucleus .
• Protein Description: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell..
• Protein Sequence: MVNVLKGVLIECDPAMKQFLLYLDESNALGKKFIIQDIDDTHVFVIAELVNVLQERVGELMDQNAFSLTQK

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
6	Ubiquitination	--MVNVLKGVLIECD --CCCCCCEEEEECC	42.57	23000965
31	Ubiquitination	DESNALGKKFIIQDI CCCCCCCCCEEEECC	45.41	22817900
32	Ubiquitination	ESNALGKKFIIQDID CCCCCCCCEEEECCC	39.74	22817900
41	Ubiquitination	IIQDIDDTHVFVIAE EEECCCCCCCHHHHH	19.05	21890473
42	Ubiquitination	IQDIDDTHVFVIAEL EECCCCCCCHHHHHH	20.29	22817900
61	Sulfoxidation	QERVGELMDQNAFSL HHHHHHHHHHCCCCC	4.30	21406390
69	Phosphorylation	DQNAFSLTQK----- HHCCCCCCCC-----	32.87	17525332

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TF2H5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TF2H5_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TF2H5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK7_HUMAN	CDK7	physical	15220921
ERCC3_HUMAN	ERCC3	physical	15220921
ERCC3_HUMAN	ERCC3	physical	16669699
CCNH_HUMAN	CCNH	physical	26496610
CDK7_HUMAN	CDK7	physical	26496610
ERCC2_HUMAN	ERCC2	physical	26496610
ERCC3_HUMAN	ERCC3	physical	26496610
ERCC5_HUMAN	ERCC5	physical	26496610
TF2H1_HUMAN	GTF2H1	physical	26496610
TF2H2_HUMAN	GTF2H2	physical	26496610
TF2H3_HUMAN	GTF2H3	physical	26496610
TF2H4_HUMAN	GTF2H4	physical	26496610
ITPR1_HUMAN	ITPR1	physical	26496610
MAT1_HUMAN	MNAT1	physical	26496610
NUP98_HUMAN	NUP98	physical	26496610
IPP2_HUMAN	PPP1R2	physical	26496610
BRE1B_HUMAN	RNF40	physical	26496610
SYHM_HUMAN	HARS2	physical	26496610
CDCA3_HUMAN	CDCA3	physical	26496610
TF2H1_HUMAN	GTF2H1	physical	28514442
TF2H4_HUMAN	GTF2H4	physical	28514442
TF2H2_HUMAN	GTF2H2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 616395: Trichothiodystrophy 3, photosensitive (TTD3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-69, AND MASSSPECTROMETRY.
PubMed: 17525332