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Protein Page:
ERCC2 (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
ERCC2 ATP-dependent 5'-3' DNA helicase, component of the core- TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. Might also have a role in aging process and could play a causative role in the generation of skin cancers. Belongs to the helicase family. RAD3/XPD subfamily. One of the six 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. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity. Interacts with Epstein-Barr virus EBNA2. Note: This description may include information from UniProtKB.
Protein type: Helicase; EC 3.6.1.-; EC 3.6.4.12
Chromosomal Location of Human Ortholog: 19q13.3
Cellular Component: nucleoplasm; holo TFIIH complex; cytoplasm; spindle; nucleus; cyclin-dependent protein kinase activating kinase holoenzyme complex
Molecular Function: ATP-dependent DNA helicase activity; RNA polymerase subunit kinase activity; protein C-terminus binding; DNA-dependent ATPase activity; protein binding; DNA binding; 4 iron, 4 sulfur cluster binding; metal ion binding; protein N-terminus binding; 5'-3' DNA helicase activity; ATP binding; protein kinase activity
Biological Process: transcription from RNA polymerase II promoter; extracellular matrix organization and biogenesis; erythrocyte maturation; viral reproduction; positive regulation of viral transcription; apoptosis; positive regulation of transcription, DNA-dependent; protein amino acid phosphorylation; embryonic cleavage; bone mineralization; post-embryonic development; chromosome segregation; mRNA capping; UV protection; transcription-coupled nucleotide-excision repair; nucleotide-excision repair, DNA damage removal; positive regulation of DNA binding; aging; ATP catabolic process; transcription initiation from RNA polymerase II promoter; in utero embryonic development; multicellular organism growth; transcription from RNA polymerase I promoter; hair cell differentiation; nucleotide-excision repair, DNA incision; RNA elongation from RNA polymerase I promoter; DNA repair; termination of RNA polymerase I transcription; hair follicle maturation; DNA duplex unwinding; cell proliferation; myelin formation in the central nervous system; nucleotide-excision repair; spinal cord development; 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 #:  P18074 (UniProtKB)
Alt. Names/Synonyms: Basic transcription factor 2 80 kDa subunit; BTF2 p80; COFS2; CXPD; DNA excision repair protein ERCC-2; DNA repair protein complementing XP-D cells; EM9; ERCC2; excision repair cross-complementing rodent repair deficiency, complementation group 2; MGC102762; MGC126218; MGC126219; TFIIH 80 kDa subunit; TFIIH basal transcription factor complex 80 kDa subunit; TFIIH basal transcription factor complex helicase subunit; TFIIH p80; TTD; xeroderma pigmentosum complementary group D; Xeroderma pigmentosum group D-complementing protein; XPD; XPDC
Gene Symbols: ERCC2
Molecular weight: 86,909 Da
Basal Isoelectric point: 6.72  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

ERCC2

Protein Structure Not Found.


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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 K35-ub LKRTLDAkGHGVLEM
0 1 K96-ub KLLNFYEkQEGEkLP
0 1 K101-ub YEkQEGEkLPFLGLA
0 3 T122-p LCIHPEVtPLRFGKD
0 2 Y175 VPLPAGIYNLDDLkA
0 1 K181-ub IYNLDDLkALGRRQG
0 1 T252-p DSMSVNLtRRTLDRC
0 1 K268-ub GNLETLQkTVLRIKE
0 1 S296-p VEGLREAsAARETDA
0 3 K507-ub DQVAISSkFETREDI
0 1 Y584-p TSVALEKyQEACENG
0 1 K603-ub LLSVARGkVSEGIDF
0 1 T653 IRENDFLTFDAMRHA
0 1 K682-ub GLMVFADkRFARGDK
0 1 K718-ub DEGVQVAkYFLRQMA
0 1 K751-ub LESEETLkRIEQIAQ
  mouse

 
K35 LKRTLDAKGHGVLEM
Q96 KLLSFYEQQEGEKLP
K101 YEQQEGEKLPFLGLA
T122 LCIHPEVTPLRFGKD
Y175-p MPLPAGIyNLDDLKA
K181 IyNLDDLKALGQRQG
T252 DSMSVNLTRRTLDRC
K268 SNLDTLQKTVLRIKE
S296 VEGLREASVARETDA
K507-ub DQVAISSkFETREDI
Y584 TSVALEKYQEACENG
K603 LLSVARGKVSEGIDF
T653-p IRENDFLtFDAMRHA
K682 GLMVFADKRFARADK
K718 DEGVQVAKYFLRQMA
Q751 LQSEETLQRIEQIAQ
  rat

 
K35 LKRTLDAKGHGVLEM
Q96 KLLSFYEQQEGEKLP
K101 YEQQEGEKLPFLGLA
T122 LCIHPEVTPLRFGKD
Y175 VPLPAGIYNLDDLKA
K181 IYNLDDLKALGQRQG
T252 DSMSVNLTRRTLDRC
K268 SNLDTLQKTVLRIKE
S296 VEGLREASAARETDA
K507 DQVAISSKFETREDI
Y584 TSVALEKYQEACENG
K603 LLSVARGKVSEGIDF
T653 IRENDFLTFDAMRHA
K682 GLMVFADKRFARADK
K718 DEGVQVAKYFLRQMA
Q751 LQSEETLQRIEQIAQ
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