ERCC2_ARATH - dbPTM
ERCC2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERCC2_ARATH
UniProt AC Q8W4M7
Protein Name General transcription and DNA repair factor IIH helicase subunit XPD
Gene Name XPD {ECO:0000303|PubMed:16623910}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 758
Subcellular Localization Nucleus .
Protein Description ATP-dependent 5'-3' 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 ATP-dependent helicase activity of XPD 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. 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. XPD acts by forming a bridge between CAK and the core-TFIIH complex (By similarity). Essential during plant growth. [PubMed: 12857822 May negatively regulate a common response program mediated by UV damage and heat stress, that leads to tissue death and reduced chloroplast function]
Protein Sequence MIFKIEDVTVYFPYDNIYPEQYEYMVELKRALDAKGHCLLEMPTGTGKTIALLSLITSYRLSRPDSPIKLVYCTRTVHEMEKTLGELKLLHDYQVRHLGTQAKILALGLSSRKNLCVNTKVLAAENRDSVDAACRKRTASWVRALSTENPNVELCDFFENYEKAAENALLPPGVYTLEDLRAFGKNRGWCPYFLARHMIQFANVIVYSYQYLLDPKVAGFISKELQKESVVVFDEAHNIDNVCIEALSVSVRRVTLEGANRNLNKIRQEIDRFKATDAGRLRAEYNRLVEGLALRGDLSGGDQWLANPALPHDILKEAVPGNIRRAEHFVHVLRRLLQYLGVRLDTENVEKESPVSFVSSLNSQAGIEQKTLKFCYDRLQSLMLTLEITDTDEFLPIQTVCDFATLVGTYARGFSIIIEPYDERMPHIPDPILQLSCHDASLAIKPVFDRFQSVVITSGTLSPIDLYPRLLNFTPVVSRSFKMSMTRDCICPMVLTRGSDQLPVSTKFDMRSDPGVVRNYGKLLVEMVSIVPDGVVCFFVSYSYMDGIIATWNETGILKEIMQQKLVFIETQDVVETTLALDNYRRACDCGRGAVFFSVARGKVAEGIDFDRHYGRLVVMYGVPFQYTLSKILRARLEYLHDTFQIKEGDFLTFDALRQAAQCVGRVIRSKADYGMMIFADKRYSRHDKRSKLPGWILSHLRDAHLNLSTDMAIHIAREFLRKMAQPYDKAGTMGRKTLLTQEDLEKMAETGVQDMAY
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
100PhosphorylationYQVRHLGTQAKILAL
HHHHHHHHHHHHHHH
31.5425368622
248PhosphorylationNVCIEALSVSVRRVT
HHHHHHHCEEEEEEE
21.2828011693
250PhosphorylationCIEALSVSVRRVTLE
HHHHHCEEEEEEECC
13.4128011693
353PhosphorylationTENVEKESPVSFVSS
CCCCCCCCCCCHHHH
41.4919880383
356PhosphorylationVEKESPVSFVSSLNS
CCCCCCCCHHHHHHC
24.2623111157
363PhosphorylationSFVSSLNSQAGIEQK
CHHHHHHCCCCCCHH
27.0523111157

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 ERCC2_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERCC2_ARATH !!

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 ERCC2_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFB1A_ARATHAT1G55750physical
20706207
CCH11_ARATHCYCH;1physical
20706207
PSMD6_ARATHAT4G24820physical
20706207

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERCC2_ARATH

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Related Literatures of Post-Translational Modification

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