ERCC3_DROME - dbPTM
ERCC3_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERCC3_DROME
UniProt AC Q02870
Protein Name General transcription and DNA repair factor IIH helicase subunit XPB
Gene Name hay
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 798
Subcellular Localization Nucleus.
Protein Description ATP-dependent 3'-5' DNA helicase, 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. The ATPase activity of haywire/XPB/ERCC3, but not its helicase activity, is required for DNA opening. 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. The ATP-dependent helicase activity of haywire/XPB/ERCC3 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..
Protein Sequence MGPPKKSRKDRSGGDKFGKKRRAEDEAFTQLVDDNDSLDATESEGIPGAASKNAETNDEQINTDEYGAKDYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEYLKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEDFIQGTLDGKAITQFGTKLPPGATDKPTPDPAAAAGADGTTAVPEDITDFYEKIDKEEEDEDEANLKTVSFEVAQEKIEVIQKRCIEIEHPLLAEYDFRNDTNNPDINIDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGVSVEQWKQQFKMWSTADDSMICRFTSEAKDKPMGCGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLTATLLREDDKIADLNFLIGPKLYEANWLELQKKGYIARVQCAEVWCPMSPEFYREYLTTKTSKKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKMNKPFIYGPTSQNERIQILQNFKFNSKVNTIFVSKVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEYNAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYKVITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPGYRPSGSGGAVRRVGGLSSMSGGDDAIYYEHRKKNIGSVHPLFKKFRG
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
29PhosphorylationRAEDEAFTQLVDDND
HHHCHHHHHHCCCCC
28.2123607784
37PhosphorylationQLVDDNDSLDATESE
HHCCCCCCCCCCCCC
34.1122668510
41PhosphorylationDNDSLDATESEGIPG
CCCCCCCCCCCCCCC
39.4523607784
43PhosphorylationDSLDATESEGIPGAA
CCCCCCCCCCCCCCH
36.4523607784

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 ERCC3_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERCC3_DROME !!

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 ERCC3_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF2H1_DROMETfb1physical
23549790
PUF68_DROMEpUf68physical
20667914

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERCC3_DROME

loading...

Related Literatures of Post-Translational Modification

TOP