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Protein Page:
XPB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
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: Helicase; DNA repair, damage; EC 3.6.4.12; Transcription factor
Chromosomal Location of Human Ortholog: 2q21
Cellular Component: nucleoplasm; holo TFIIH complex; nucleolus; nucleus
Molecular Function: protein C-terminus binding; DNA-dependent ATPase activity; GTP binding; ATPase activity; dATP binding; 3'-5' DNA helicase activity; protein N-terminus binding; transcription factor binding; peptide binding; protein kinase activity; RNA polymerase subunit kinase activity; ATP-dependent DNA helicase activity; protein binding; DNA binding; damaged DNA binding; ATP binding
Biological Process: transcription from RNA polymerase II promoter; DNA topological change; viral reproduction; positive regulation of viral transcription; apoptosis; positive regulation of apoptosis; protein amino acid phosphorylation; protein localization; mRNA capping; UV protection; transcription-coupled nucleotide-excision repair; nucleotide-excision repair, DNA damage removal; response to UV; ATP catabolic process; transcription initiation from RNA polymerase II promoter; RNA elongation from RNA polymerase I promoter; transcription from RNA polymerase I promoter; nucleotide-excision repair, DNA incision; hair cell differentiation; DNA repair; termination of RNA polymerase I transcription; nucleotide-excision repair, DNA duplex unwinding; nucleotide-excision repair; RNA elongation from RNA polymerase II promoter; response to hypoxia; gene expression; positive regulation of transcription from RNA polymerase II promoter; response to oxidative stress; transcription initiation from RNA polymerase I promoter
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
Select Structure to View Below

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


 SS 

SS: 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.


 MS 

MS: 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 1 Y139-p QTSDITEyLRKLSKT
0 1 K157-ub DGIMQFIkLCTVSYG
0 1 S202-p RECRLRNsEGEAtEL
0 1 T207-p RNsEGEAtELITETF
0 2 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 T691 GYsFKVITKLAGMEE
0 1 K706-ub EDLAFSTkEEQQQLL
2 0 S751-p FGTMSSMsGADDTVy
0 6 Y758-p sGADDTVyMEYHSSR
  mouse

 
Y19 KKSKKRQYEEEEEDE
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-p FLVDQGYsFKVItKL
T692-p GYsFKVItKLAGMEE
K707 EELAFSTKEEQQQLL
S752 CGTMSSLSGADDTVY
Y759 SGADDTVYMEYHSSR
  rat

 
Y19 KKSKKRQYEEEEEDE
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
T691 GYSFKVITKLAGMEE
K706 EELAFSTKEEQQQLL
S751 FGTMSSLSGADDTVY
Y758 SGADDTVYMEYHSSR
  hamster

 
Y19 KKSKKRQYEEEEEDE
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
T691 GYSFKVITKLAGMEE
K706 EELAFSTKEEQQQLL
S751-p FGTMSSMsGADDTVY
Y758 sGADDTVYMEYHSSR
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