ERCC3_HUMAN - dbPTM
ERCC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERCC3_HUMAN
UniProt AC P19447
Protein Name General transcription and DNA repair factor IIH helicase subunit XPB
Gene Name ERCC3
Organism Homo sapiens (Human).
Sequence Length 782
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 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 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 MGKRDRADRDKKKSRKRHYEDEEDDEEDAPGNDPQEAVPSAAGKQVDESGTKVDEYGAKDYRLQMPLKDDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIMQFIKLCTVSYGKVKLVLKHNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATELITETFTSKSAISKTAESSGGPSTSRVTDPQGKSDIPMDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCIHLEYPLLAEYDFRNDSVNPDINIDLKPTAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTAACTVRKRCLVLGNSAVSVEQWKAQFKMWSTIDDSQICRFTSDAKDKPIGCSVAISTYSMLGHTTKRSWEAERVMEWLKTQEWGLMILDEVHTIPAKMFRRVLTIVQAHCKLGLTATLVREDDKIVDLNFLIGPKLYEANWMELQNNGYIAKVQCAEVWCPMSPEFYREYVAIKTKKRILLYTMNPNKFRACQFLIKFHERRNDKIIVFADNVFALKEYAIRLNKPYIYGPTSQGERMQILQNFKHNPKINTIFISKVGDTSFDLPEANVLIQISSHGGSRRQEAQRLGRVLRAKKGMVAEEYNAFFYSLVSQDTQEMAYSTKRQRFLVDQGYSFKVITKLAGMEEEDLAFSTKEEQQQLLQKVLAATDLDAEEEVVAGEFGSRSSQASRRFGTMSSMSGADDTVYMEYHSSRSKAPSKHVHPLFKRFRK
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
19PhosphorylationKKSRKRHYEDEEDDE
HHHHHHHCCCCCCCC		29.16-
44UbiquitinationAVPSAAGKQVDESGT
HCCCCCCCEECCCCC		42.28-
52UbiquitinationQVDESGTKVDEYGAK
EECCCCCCCCCCCCC		51.74-
59UbiquitinationKVDEYGAKDYRLQMP
CCCCCCCCCEEECCC		51.43-
139PhosphorylationQTSDITEYLRKLSKT
CCCCHHHHHHHHHHH		11.80-
144PhosphorylationTEYLRKLSKTGVPDG
HHHHHHHHHHCCCHH		31.0725404012
145UbiquitinationEYLRKLSKTGVPDGI
HHHHHHHHHCCCHHH		60.79-
146PhosphorylationYLRKLSKTGVPDGIM
HHHHHHHHCCCHHHH		39.7825404012
157UbiquitinationDGIMQFIKLCTVSYG
HHHHHHHHHHCCCCC		38.51-
171UbiquitinationGKVKLVLKHNRYFVE
CCEEEEEECCCEEHH		31.21-
202PhosphorylationRECRLRNSEGEATEL
HHHHCCCCCCCHHHH		40.3130266825
207PhosphorylationRNSEGEATELITETF
CCCCCCHHHHHEEEC		27.3329255136
217UbiquitinationITETFTSKSAISKTA
HEEECCCHHHHHCCH		40.63-
222UbiquitinationTSKSAISKTAESSGG
CCHHHHHCCHHHCCC		45.7121906983
223PhosphorylationSKSAISKTAESSGGP
CHHHHHCCHHHCCCC		28.9428102081
226PhosphorylationAISKTAESSGGPSTS
HHHCCHHHCCCCCCC		31.6428102081
227PhosphorylationISKTAESSGGPSTSR
HHCCHHHCCCCCCCC		39.0028102081
231PhosphorylationAESSGGPSTSRVTDP
HHHCCCCCCCCCCCC		42.1425159151
232PhosphorylationESSGGPSTSRVTDPQ
HHCCCCCCCCCCCCC		24.5625159151
233PhosphorylationSSGGPSTSRVTDPQG
HCCCCCCCCCCCCCC		29.1425159151
236PhosphorylationGPSTSRVTDPQGKSD
CCCCCCCCCCCCCCC		40.6325159151
242PhosphorylationVTDPQGKSDIPMDLF
CCCCCCCCCCCCCHH		47.82-
265PhosphorylationDEEEEEETQTVSFEV
CHHHHHHHCEEEHHH		32.5925841592
267PhosphorylationEEEEETQTVSFEVKQ
HHHHHHCEEEHHHHH		26.0725841592
269PhosphorylationEEETQTVSFEVKQEM
HHHHCEEEHHHHHHH		21.0525841592
311UbiquitinationPDINIDLKPTAVLRP
CCCCCCCCCCCCCCC		36.25-
311SumoylationPDINIDLKPTAVLRP
CCCCCCCCCCCCCCC		36.25-
319PhosphorylationPTAVLRPYQEKSLRK
CCCCCCCCCHHHHHH		23.9121406692
323PhosphorylationLRPYQEKSLRKMFGN
CCCCCHHHHHHHHCC		32.4321406692
335PhosphorylationFGNGRARSGVIVLPC
HCCCCCCCEEEEEEC		36.1127134283
370PhosphorylationVLGNSAVSVEQWKAQ
EECCCCEEHHHHHHH		21.4717081983
382PhosphorylationKAQFKMWSTIDDSQI
HHHHHECCCCCHHHH		16.4029396449
383PhosphorylationAQFKMWSTIDDSQIC
HHHHECCCCCHHHHE		16.9529396449
387PhosphorylationMWSTIDDSQICRFTS
ECCCCCHHHHEEEEC		20.0729396449
393PhosphorylationDSQICRFTSDAKDKP
HHHHEEEECCCCCCC		13.3229396449
394PhosphorylationSQICRFTSDAKDKPI
HHHEEEECCCCCCCC		32.6229396449
399AcetylationFTSDAKDKPIGCSVA
EECCCCCCCCCEEEE		37.5226051181
404PhosphorylationKDKPIGCSVAISTYS
CCCCCCEEEEEEEHH		14.90-
526UbiquitinationYREYVAIKTKKRILL
HHHHHHHCCCCEEEE		44.55-
577UbiquitinationEYAIRLNKPYIYGPT
HHHHHCCCCEEECCC		43.73-
581PhosphorylationRLNKPYIYGPTSQGE
HCCCCEEECCCCHHH		15.9423917254
597UbiquitinationMQILQNFKHNPKINT
HHHHHHHCCCCCCCE		50.45-
597MalonylationMQILQNFKHNPKINT
HHHHHHHCCCCCCCE		50.4526320211
597AcetylationMQILQNFKHNPKINT
HHHHHHHCCCCCCCE		50.4525953088
601UbiquitinationQNFKHNPKINTIFIS
HHHCCCCCCCEEEEE		54.6421890473
601UbiquitinationQNFKHNPKINTIFIS
HHHCCCCCCCEEEEE		54.6421890473
685PhosphorylationRFLVDQGYSFKVITK
HHEECCCCCEEEHHH		12.8023186163
686PhosphorylationFLVDQGYSFKVITKL
HEECCCCCEEEHHHH		25.978304337
696SulfoxidationVITKLAGMEEEDLAF
EHHHHCCCCHHHCCC		4.9521406390
706UbiquitinationEDLAFSTKEEQQQLL
HHCCCCCHHHHHHHH		59.0421890473
720PhosphorylationLQKVLAATDLDAEEE
HHHHHHCCCCCHHHH		31.3327174698
735PhosphorylationVVAGEFGSRSSQASR
HHHCCCCCCCHHHHH		34.0227174698
737PhosphorylationAGEFGSRSSQASRRF
HCCCCCCCHHHHHHH		28.6227174698
738PhosphorylationGEFGSRSSQASRRFG
CCCCCCCHHHHHHHC		28.7627174698
741PhosphorylationGSRSSQASRRFGTMS
CCCCHHHHHHHCCCH		19.1527174698
748PhosphorylationSRRFGTMSSMSGADD
HHHHCCCHHCCCCCC		23.7927642862
749PhosphorylationRRFGTMSSMSGADDT
HHHCCCHHCCCCCCE		13.2228348404
751PhosphorylationFGTMSSMSGADDTVY
HCCCHHCCCCCCEEE		32.5528796482
756PhosphorylationSMSGADDTVYMEYHS
HCCCCCCEEEEEECC		17.6828796482
758PhosphorylationSGADDTVYMEYHSSR
CCCCCEEEEEECCCC		6.0628796482
761PhosphorylationDDTVYMEYHSSRSKA
CCEEEEEECCCCCCC		7.1728796482
763PhosphorylationTVYMEYHSSRSKAPS
EEEEEECCCCCCCCH		26.9228796482
764PhosphorylationVYMEYHSSRSKAPSK
EEEEECCCCCCCCHH		27.5328796482
767AcetylationEYHSSRSKAPSKHVH
EECCCCCCCCHHCCC		64.3125953088
771UbiquitinationSRSKAPSKHVHPLFK
CCCCCCHHCCCHHHH		48.89-
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
90SPhosphorylationKinaseCDK7P50613
PSP
751SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERCC3_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 ERCC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERCC2_HUMANERCC2physical
15220921
TF2H4_HUMANGTF2H4physical
15220921
TF2H1_HUMANGTF2H1physical
15220921
TF2H2_HUMANGTF2H2physical
15220921
TF2H3_HUMANGTF2H3physical
15220921
CDK7_HUMANCDK7physical
15220921
TF2H5_HUMANGTF2H5physical
15220921
CCNH_HUMANCCNHphysical
15220921
MAT1_HUMANMNAT1physical
15220921
T2EA_HUMANGTF2E1physical
7926747
T2EB_HUMANGTF2E2physical
7926747
TF2H1_HUMANGTF2H1physical
9118947
TF2H2_HUMANGTF2H2physical
9118947
TF2H3_HUMANGTF2H3physical
9118947
TF2H4_HUMANGTF2H4physical
9118947
ERCC2_HUMANERCC2physical
9118947
PRS8_HUMANPSMC5physical
9173976
ERCC2_HUMANERCC2physical
8652557
CDK7_HUMANCDK7physical
17643375
TF2H1_HUMANGTF2H1physical
17643375
TF2H3_HUMANGTF2H3physical
17643375
TF2H2_HUMANGTF2H2physical
17643375
CCNH_HUMANCCNHphysical
17643375
ERCC5_HUMANERCC5physical
17643375
BCR_HUMANBCRphysical
17643375
GCN1_HUMANGCN1L1physical
17643375
MAT1_HUMANMNAT1physical
17643375
ZSCA1_HUMANZSCAN1physical
20211142
TF2H1_HUMANGTF2H1physical
8692842
CCNH_HUMANCCNHphysical
8692842
MAT1_HUMANMNAT1physical
8692842
TAT_HV1H2tatphysical
9334327
TF2H2_HUMANGTF2H2physical
8194529
TF2H3_HUMANGTF2H3physical
8194529
TF2H1_HUMANGTF2H1physical
22939629
TF2H3_HUMANGTF2H3physical
22939629
TF2H4_HUMANGTF2H4physical
22939629
SIX5_HUMANSIX5physical
22939629
P53_HUMANTP53physical
12379483
MMS19_HUMANMMS19physical
11071939
RAD52_HUMANRAD52physical
12372413
UVSSA_HUMANUVSSAphysical
22902626
ERCC2_HUMANERCC2physical
22678362
IMA4_HUMANKPNA3physical
21988832
CEP70_HUMANCEP70physical
25416956
BCR_HUMANBCRphysical
10403766
MCF2_HUMANMCF2physical
10403766
CDC42_HUMANCDC42physical
10403766
TF2H1_HUMANGTF2H1physical
10403766
TF2H1_HUMANGTF2H1physical
26344197
T2H2L_HUMANGTF2H2Cphysical
26344197
TF2H2_HUMANGTF2H2physical
26344197
TF2H3_HUMANGTF2H3physical
26344197
TF2H4_HUMANGTF2H4physical
26344197
GOGA2_HUMANGOLGA2physical
21516116
UBXN7_HUMANUBXN7physical
26389662
TF2H3_HUMANGTF2H3physical
28514442
TF2H5_HUMANGTF2H5physical
28514442
TF2H1_HUMANGTF2H1physical
28514442
ERCC5_HUMANERCC5physical
28514442
TF2H4_HUMANGTF2H4physical
28514442
CCNH_HUMANCCNHphysical
28514442
ZN143_HUMANZNF143physical
28514442
BCR_HUMANBCRphysical
28514442
TF2H2_HUMANGTF2H2physical
28514442
UBP7_HUMANUSP7physical
28514442
COX11_HUMANCOX11physical
28514442
CDK7_HUMANCDK7physical
28514442
MAT1_HUMANMNAT1physical
28514442
LRC41_HUMANLRRC41physical
28514442
ERCC2_HUMANERCC2physical
26340423
TF2H1_HUMANGTF2H1physical
26340423
TF2H4_HUMANGTF2H4physical
26340423
TF2H2_HUMANGTF2H2physical
26340423
CDK7_HUMANCDK7physical
26340423
CCNH_HUMANCCNHphysical
26340423
TF2H3_HUMANGTF2H3physical
26340423
MAT1_HUMANMNAT1physical
26340423
TF2H5_HUMANGTF2H5physical
26340423
SPTA1_HUMANSPTA1physical
16889989
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610651Xeroderma pigmentosum complementation group B (XP-B)
616390Trichothiodystrophy 2, photosensitive (TTD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERCC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASSSPECTROMETRY.

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