ERCC8_HUMAN - dbPTM
ERCC8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERCC8_HUMAN
UniProt AC Q13216
Protein Name DNA excision repair protein ERCC-8
Gene Name ERCC8
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Nucleus .
Protein Description Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes..
Protein Sequence MLGFLSARQTGLEDPLRLRRAESTRRVLGLELNKDRDVERIHGGGINTLDIEPVEGRYMLSGGSDGVIVLYDLENSSRQSYYTCKAVCSIGRDHPDVHRYSVETVQWYPHDTGMFTSSSFDKTLKVWDTNTLQTADVFNFEETVYSHHMSPVSTKHCLVAVGTRGPKVQLCDLKSGSCSHILQGHRQEILAVSWSPRYDYILATASADSRVKLWDVRRASGCLITLDQHNGKKSQAVESANTAHNGKVNGLCFTSDGLHLLTVGTDNRMRLWNSSNGENTLVNYGKVCNNSKKGLKFTVSCGCSSEFVFVPYGSTIAVYTVYSGEQITMLKGHYKTVDCCVFQSNFQELYSGSRDCNILAWVPSLYEPVPDDDETTTKSQLNPAFEDAWSSSDEEG
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
6Phosphorylation--MLGFLSARQTGLE
--CCCCCCCCCCCCC
21.1028355574
71PhosphorylationSDGVIVLYDLENSSR
CCEEEEEEECCCCCC
13.9522817900
77PhosphorylationLYDLENSSRQSYYTC
EEECCCCCCCEEEEE
46.0125332170
125UbiquitinationSSFDKTLKVWDTNTL
CCCCCCEEEEECCCC
46.65-
154PhosphorylationHHMSPVSTKHCLVAV
CCCCCCCCCCEEEEE
25.66-
167UbiquitinationAVGTRGPKVQLCDLK
EECCCCCCEEEEECC
45.50-
195PhosphorylationEILAVSWSPRYDYIL
EEEEEEECCCCCEEE
7.6224719451
212AcetylationASADSRVKLWDVRRA
CCCCCCEEHHHHHHC
42.6323749302
212MalonylationASADSRVKLWDVRRA
CCCCCCEEHHHHHHC
42.6326320211
212UbiquitinationASADSRVKLWDVRRA
CCCCCCEEHHHHHHC
42.63-
220PhosphorylationLWDVRRASGCLITLD
HHHHHHCCCCEEEEE
28.3829083192
225PhosphorylationRASGCLITLDQHNGK
HCCCCEEEEECCCCE
16.0129083192
233 (in isoform 1)Ubiquitination-49.5521906983
233UbiquitinationLDQHNGKKSQAVESA
EECCCCEEEHHHHHC
49.552190698
247UbiquitinationANTAHNGKVNGLCFT
CCCCCCCCCCEEEEE
37.53-
286UbiquitinationNTLVNYGKVCNNSKK
CCEEEEEECCCCCCC
33.00-
286AcetylationNTLVNYGKVCNNSKK
CCEEEEEECCCCCCC
33.0025953088
390PhosphorylationPAFEDAWSSSDEEG-
HHHHHHHCCCCCCC-
22.9920363803
391PhosphorylationAFEDAWSSSDEEG--
HHHHHHCCCCCCC--
30.9820363803
392PhosphorylationFEDAWSSSDEEG---
HHHHHCCCCCCC---
43.4520363803

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 ERCC8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERCC8_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 ERCC8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EP300_HUMANEP300physical
16916636
HMGN1_HUMANHMGN1physical
16916636
DDB1_HUMANDDB1physical
12732143
CUL4A_HUMANCUL4Aphysical
12732143
CSN1_HUMANGPS1physical
12732143
RBX1_HUMANRBX1physical
12732143
CSN2_HUMANCOPS2physical
12732143
CSN3_HUMANCOPS3physical
12732143
CSN4_HUMANCOPS4physical
12732143
CSN5_HUMANCOPS5physical
12732143
CSN6_HUMANCOPS6physical
12732143
CSN7A_HUMANCOPS7Aphysical
12732143
CSN8_HUMANCOPS8physical
12732143
DDB1_HUMANDDB1physical
22232169
P53_HUMANTP53physical
22032989
ERCC6_HUMANERCC6physical
22032989
OGG1_HUMANOGG1physical
20100872
SSBP_HUMANSSBP1physical
20100872
DDB1_HUMANDDB1physical
22902626
CUL4B_HUMANCUL4Bphysical
22902626
CUL4A_HUMANCUL4Aphysical
22902626
ZNF24_HUMANZNF24physical
22902626
ERCC6_HUMANERCC6physical
22902626
RUVB2_HUMANRUVBL2physical
22902626
UVSSA_HUMANUVSSAphysical
22902626
PCNA_HUMANPCNAphysical
22902626
H10_HUMANH1F0physical
22902626
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
ERCC6_HUMANERCC6physical
26826127
TERA_HUMANVCPphysical
26826127
CUL4A_HUMANCUL4Aphysical
26826127
DDB1_HUMANDDB1physical
26826127
UBXN7_HUMANUBXN7physical
26826127
ERCC6_HUMANERCC6physical
16751180
CUL4A_HUMANCUL4Aphysical
16751180
CSN5_HUMANCOPS5physical
16751180
CSN8_HUMANCOPS8physical
16751180
DDB1_HUMANDDB1physical
16751180
RBX1_HUMANRBX1physical
16751180
DDB1_HUMANDDB1physical
28416769

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
216400Cockayne syndrome A (CSA)
614621UV-sensitive syndrome 2 (UVSS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERCC8_HUMAN

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Related Literatures of Post-Translational Modification

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