ERCC2_HUMAN - dbPTM
ERCC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERCC2_HUMAN
UniProt AC P18074
Protein Name General transcription and DNA repair factor IIH helicase subunit XPD
Gene Name ERCC2
Organism Homo sapiens (Human).
Sequence Length 760
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, spindle .
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/ERCC2 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/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers..
Protein Sequence MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEITDLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLKRIEQIAQQL
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
2Acetylation------MKLNVDGLL
------CCCCCCEEE		49.0925953088
11PhosphorylationNVDGLLVYFPYDYIY
CCCEEEEEECCCCCC		9.9824043423
14PhosphorylationGLLVYFPYDYIYPEQ
EEEEEECCCCCCHHH		16.1024043423
16PhosphorylationLVYFPYDYIYPEQFS
EEEECCCCCCHHHHH		9.1224043423
18PhosphorylationYFPYDYIYPEQFSYM
EECCCCCCHHHHHHH		8.4224043423
23PhosphorylationYIYPEQFSYMRELKR
CCCHHHHHHHHHHHH		20.0824043423
24PhosphorylationIYPEQFSYMRELKRT
CCHHHHHHHHHHHHH		11.0724043423
29UbiquitinationFSYMRELKRTLDAKG
HHHHHHHHHHHCCCC		38.29-
35UbiquitinationLKRTLDAKGHGVLEM
HHHHHCCCCCCEEEC		51.6221906983
58UbiquitinationSLLALIMAYQRAYPL
HHHHHHHHHHHHCCC		7.1329967540
63PhosphorylationIMAYQRAYPLEVTKL
HHHHHHHCCCCHHHH		15.5630576142
69UbiquitinationAYPLEVTKLIYCSRT
HCCCCHHHHHEECCC		37.75-
72UbiquitinationLEVTKLIYCSRTVPE
CCHHHHHEECCCHHH		8.5333845483
77UbiquitinationLIYCSRTVPEIEKVI
HHEECCCHHHHHHHH		3.7829967540
82UbiquitinationRTVPEIEKVIEELRK
CCHHHHHHHHHHHHH		54.9229967540
87UbiquitinationIEKVIEELRKLLNFY
HHHHHHHHHHHHHHH		3.6727667366
89UbiquitinationKVIEELRKLLNFYEK
HHHHHHHHHHHHHHH		70.7029967540
96UbiquitinationKLLNFYEKQEGEKLP
HHHHHHHHHCCCCCC		42.1221906983
101UbiquitinationYEKQEGEKLPFLGLA
HHHHCCCCCCCHHHH		72.7721906983
102UbiquitinationEKQEGEKLPFLGLAL
HHHCCCCCCCHHHHH		2.9327667366
104UbiquitinationQEGEKLPFLGLALSS
HCCCCCCCHHHHHCC		14.1527667366
109UbiquitinationLPFLGLALSSRKNLC
CCCHHHHHCCCCCEE		6.0129967540
110PhosphorylationPFLGLALSSRKNLCI
CCHHHHHCCCCCEEE		23.6124719451
113UbiquitinationGLALSSRKNLCIHPE
HHHHCCCCCEEECCC		57.1129967540
122PhosphorylationLCIHPEVTPLRFGKD
EEECCCCCCCCCCCC		18.2325159151
128UbiquitinationVTPLRFGKDVDGKCH
CCCCCCCCCCCCCEE		52.4427667366
133UbiquitinationFGKDVDGKCHSLTAS
CCCCCCCCEEEEEHH		25.0629967540
140UbiquitinationKCHSLTASYVRAQYQ
CEEEEEHHHHHHHHC		20.9423503661
155UbiquitinationHDTSLPHCRFYEEFD
CCCCCCCCCCHHHHH		2.8023503661
157UbiquitinationTSLPHCRFYEEFDAH
CCCCCCCCHHHHHCC		12.5423503661
158PhosphorylationSLPHCRFYEEFDAHG
CCCCCCCHHHHHCCC		8.6627642862
181UbiquitinationIYNLDDLKALGRRQG
CCCHHHHHHHCCCCC		48.8621906983
199UbiquitinationYFLARYSILHANVVV
HHHHHHHHHHHCEEE		2.1229967540
223UbiquitinationKIADLVSKELARKAV
HHHHHHCHHHHHCCE		49.6329967540
227UbiquitinationLVSKELARKAVVVFD
HHCHHHHHCCEEEEE		39.8421890473
233UbiquitinationARKAVVVFDEAHNID
HHCCEEEEECCCCCC		4.8023000965
242UbiquitinationEAHNIDNVCIDSMSV
CCCCCCCEEEEHHCE		2.4123000965
244UbiquitinationHNIDNVCIDSMSVNL
CCCCCEEEEHHCEEC		3.7023000965
244UbiquitinationHNIDNVCIDSMSVNL
CCCCCEEEEHHCEEC		3.7021890473
248UbiquitinationNVCIDSMSVNLTRRT
CEEEEHHCEECHHHH		16.2923000965
250UbiquitinationCIDSMSVNLTRRTLD
EEEHHCEECHHHHHH		28.5223000965
252PhosphorylationDSMSVNLTRRTLDRC
EHHCEECHHHHHHHH		16.95-
268UbiquitinationGNLETLQKTVLRIKE
CCHHHHHHHHHHHHH		43.6523000965
269PhosphorylationNLETLQKTVLRIKET
CHHHHHHHHHHHHHC		16.2924719451
274UbiquitinationQKTVLRIKETDEQRL
HHHHHHHHHCHHHHH		48.4023000965
296PhosphorylationVEGLREASAARETDA
HHHHHHHHHHHHCCH		20.0821406692
466UbiquitinationGTLSPLDIYPKILDF
CCCCHHHCCHHHHCC		9.2721890473
481UbiquitinationHPVTMATFTMTLARV
CCCCHHCHHHHHHHH		2.9721890473
483UbiquitinationVTMATFTMTLARVCL
CCHHCHHHHHHHHHH		2.2421890473
507UbiquitinationDQVAISSKFETREDI
CCEEEECCCCCHHHH		40.1921906983
565UbiquitinationLENIQRNKLLFIETQ
HHHHHHCCEEEEEEC		49.08-
578PhosphorylationTQDGAETSVALEKYQ
ECCCCCCHHHHHHHH		9.2627251275
584PhosphorylationTSVALEKYQEACENG
CHHHHHHHHHHHHCC		11.38-
603UbiquitinationLLSVARGKVSEGIDF
EEEHHCCCCCCCCCH		36.7121890473
630UbiquitinationVPYVYTQSRILKARL
CCCEECHHHHHHHHH		17.3122505724
645UbiquitinationEYLRDQFQIRENDFL
HHHHHHHCCCCCCCC		28.3522505724
671UbiquitinationVGRAIRGKTDYGLMV
HHHHHCCCCCCEEEE		28.5122505724
682UbiquitinationGLMVFADKRFARGDK
EEEEEECCHHCCCCC		46.0821906983
702PhosphorylationRWIQEHLTDANLNLT
HHHHHHHCCCCCCCC		34.6729888752
710UbiquitinationDANLNLTVDEGVQVA
CCCCCCCCCHHHHHH		7.7023503661
718UbiquitinationDEGVQVAKYFLRQMA
CHHHHHHHHHHHHHC		37.36-
725UbiquitinationKYFLRQMAQPFHRED
HHHHHHHCCCCCCHH		12.9323503661
751UbiquitinationLESEETLKRIEQIAQ
HCCHHHHHHHHHHHH		59.7721906983
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERCC2_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 ERCC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERCC3_HUMANERCC3physical
8152490
TF2H1_HUMANGTF2H1physical
8152490
TF2H2_HUMANGTF2H2physical
9771713
ERCC3_HUMANERCC3physical
8652557
MAT1_HUMANMNAT1physical
10801852
ERCC3_HUMANERCC3physical
22939629
MAT1_HUMANMNAT1physical
22939629
MMS19_HUMANMMS19physical
11071939
TF2H1_HUMANGTF2H1physical
11071939
RAD52_HUMANRAD52physical
12372413
MMS19_HUMANMMS19physical
22678362
PYRG1_HUMANCTPS1physical
26344197
SPTA1_HUMANSPTA1physical
16889989
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
278730Xeroderma pigmentosum complementation group D (XP-D)
601675Trichothiodystrophy 1, photosensitive (TTD1)
610756Cerebro-oculo-facio-skeletal syndrome 2 (COFS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERCC2_HUMAN

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Related Literatures of Post-Translational Modification

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