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Protein Page:
XPB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
XPB ATP-dependent 3'-5' DNA helicase, component of the core- TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage. One of the 6 subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. Interacts with PUF60. Interacts with ATF7IP. Interacts with Epstein-Barr virus EBNA2. Belongs to the helicase family. RAD25/XPB subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.12; Helicase; DNA repair, damage; Transcription factor
Chromosomal Location of Human Ortholog: 2q21
Cellular Component: holo TFIIH complex; nucleoplasm; nucleus
Molecular Function: 3'-5' DNA helicase activity; ATPase activity; DNA binding; DNA-dependent ATPase activity; helicase activity; protein binding; protein C-terminus binding; protein kinase activity; protein N-terminus binding; RNA polymerase subunit kinase activity; transcription factor binding
Biological Process: apoptosis; DNA repair; DNA topological change; hair cell differentiation; mRNA capping; nucleotide-excision repair; nucleotide-excision repair, DNA duplex unwinding; nucleotide-excision repair, DNA incision; nucleotide-excision repair, DNA incision, 3'-to lesion; nucleotide-excision repair, DNA incision, 5'-to lesion; nucleotide-excision repair, preincision complex assembly; nucleotide-excision repair, preincision complex stabilization; positive regulation of apoptosis; positive regulation of transcription from RNA polymerase II promoter; protein localization; response to oxidative stress; response to UV; RNA elongation from RNA polymerase I promoter; RNA elongation from RNA polymerase II promoter; termination of RNA polymerase I transcription; transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase I promoter; transcription initiation from RNA polymerase II promoter; transcription-coupled nucleotide-excision repair
Disease: Trichothiodystrophy 2, Photosensitive; Xeroderma Pigmentosum, Complementation Group B
Reference #:  P19447 (UniProtKB)
Alt. Names/Synonyms: Basic transcription factor 2 89 kDa subunit; BTF2; BTF2 p89; DNA excision repair protein ERCC-3; DNA repair protein complementing XP-B cells; ERCC3; excision repair cross-complementing rodent repair deficiency, complementation group 3 (xeroderma pigmentosum group B complementing); GTF2H; RAD25; TFIIH; TFIIH 89 kDa subunit; TFIIH basal transcription factor complex 89 kDa subunit; TFIIH basal transcription factor complex helicase XPB subunit; TFIIH p89; Xeroderma pigmentosum group B-complementing protein; xeroderma pigmentosum, complementation group B; XPB; XPBC
Gene Symbols: ERCC3
Molecular weight: 89,278 Da
Basal Isoelectric point: 6.83  Predict pI for various phosphorylation states
CST Pathways:  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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XPB

Protein Structure Not Found.
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Sites Implicated In
activity, inhibited: S751‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y19‑p KKSRKRHyEDEEDDE
0 2 P34 EDAPGNDPQEAVPSA
0 1 Y139‑p QTSDITEyLRKLSKT
0 1 K157‑ub DGIMQFIkLCTVSYG
0 1 S202‑p RECRLRNsEGEAtEL
0 1 T207‑p RNsEGEAtELITETF
0 3 K222‑ub TSKSAISkTAESSGG
0 1 T232‑p ESSGGPStSRVtDPQ
0 1 T236‑p GPStSRVtDPQGKsD
0 1 S242‑p VtDPQGKsDIPMDLF
0 1 Y319‑p PTAVLRPyQEKsLRK
0 1 S323‑p LRPyQEKsLRKMFGN
0 1 S404‑p KDKPIGCsVAISTYS
0 88 Y581‑p RLNKPYIyGPTSQGE
0 3 K601‑ub QNFKHNPkINTIFIS
0 1 R676 EMAYSTKRQRFLVDQ
0 2 S686‑p FLVDQGYsFKVITKL
0 1 K706‑ub EDLAFSTkEEQQQLL
0 1 T720‑p LQKVLAAtDLDAEEE
2 0 S751‑p FGTMSSMsGADDTVy
0 7 Y758‑p sGADDTVyMEYHSSR
  mouse

 
Y19 KKSKKRQYEEEEEDE
S34‑p DDIPGNEsQEAVPSA
Y139 QTSDITEYLRKLSKT
K157 DGIIQFIKLCTVSYG
A202 RECRLRNAEGEATEL
T207 RNAEGEATELITETF
K222 TSKSAISKTAAEGSG
T233 EGSGGPSTSQGVDAQ
V237 GPSTSQGVDAQATSD
S243 GVDAQATSDIPKDLF
Y320 PTAVLRPYQEKSLRK
S324 LRPYQEKSLRKMFGN
S405 KDKPIGCSVAISTYS
Y582‑p RLNKPYIyGPTSQGE
K602‑ub QNFKHNPkINTIFIS
R677‑m2 EMAYSTKrQRFLVDQ
S687 FLVDQGYSFKVITKL
K707 EELAFSTKEEQQQLL
T721 LQKVLAATDLDAEEE
S752 CGTMSSLSGADDTVY
Y759 SGADDTVYMEYHSSR
  rat

 
Y19 KKSKKRQYEEEEEDE
S34‑p DDAPGNEsQEAVPSA
Y139 QTSDITEYLRKLSKT
K157 DGIIQFIKLCTVSYG
A202 RECRLRNAEGEATEL
T207 RNAEGEATELITETF
K222 TSKSAISKTVEGSGG
T232 EGSGGASTSQGVDAQ
V236 GASTSQGVDAQAKSD
S242 GVDAQAKSDIPKDLF
Y319 PTAVLRPYQEKSLRK
S323 LRPYQEKSLRKMFGN
S404 KDKPIGCSIAISTYS
Y581 RLNKPYIYGPTSQGE
K601 QNFKHNPKINTIFIS
R676 EMAYSTKRQRFLVDQ
S686 FLVDQGYSFKVITKL
K706 EELAFSTKEEQQQLL
T720 LQKVLAATDLDAEEE
S751 FGTMSSLSGADDTVY
Y758 SGADDTVYMEYHSSR
  hamster

 
Y19 KKSKKRQYEEEEEDE
S34 DDTPGNDSQEAVPSA
Y139 QTSDITEYLKKLSKT
K157 DGIMQFIKLCTVSYG
A202 RECRLRNAEGEATEL
T207 RNAEGEATELITETF
K222 TSKSAISKTAEGSGG
T232 EGSGGPSTSQVVDPQ
V236 GPSTSQVVDPQAKSD
S242 VVDPQAKSDIPKDLF
Y319 PTAVLRPYQEKSLRK
S323 LRPYQEKSLRKMFGN
S404 KDKPIGCSIAISTYS
Y581 RLNKPYIYGPTSQGE
K601 QNFKHNPKINTIFIS
R676 EMAYSTKRQRFLVDQ
S686 FLVDQGYSFKVITKL
K706 EELAFSTKEEQQQLL
T720 LQKVLAATDLDAEEE
S751‑p FGTMSSMsGADDTVY
Y758 sGADDTVYMEYHSSR
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