Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
ERCC1 (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
ERCC1 a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA excision repair. Belongs to the ERCC1/RAD10/SWI10 family. Heterodimer composed of ERCC1 and XPF/ERRC4. Defects in ERCC1 are the cause of cerebro-oculo-facio-skeletal syndrome type 4, a degenerative autosomal recessive disorder of prenatal onset affecting the brain, eye and spinal cord. After birth, it leads to brain atrophy, hypoplasia of the corpus callosum, hypotonia, cataracts, microcornea, optic atrophy, progressive joint contractures and growth failure. Facial dysmorphism is a constant feature. Abnormalities of the skull, eyes, limbs, heart and kidney also occur. Low levels of this protein are associated with increased sensitivity to cisplatin. The overall survival of non-small cell lung cancer patients with single-nucleotide polymorphisms at codon 118 receiving platinum-based chemotherapy was significantly improved. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Chromosomal Location of Human Ortholog: 19q13.32
Cellular Component: cytoplasm; nuclear chromosome, telomeric region; nucleoplasm; nucleotide-excision repair complex; transcription factor TFIID complex
Molecular Function: damaged DNA binding; protein binding; protein C-terminus binding; protein domain specific binding; single-stranded DNA binding; single-stranded DNA specific endodeoxyribonuclease activity; structure-specific DNA binding
Biological Process: cell proliferation; DNA recombination; DNA repair; double-strand break repair; double-strand break repair via homologous recombination; embryonic organ development; isotype switching; male gonad development; mitotic recombination; multicellular organism growth; multicellular organismal aging; negative regulation of telomere maintenance; nucleotide-excision repair; nucleotide-excision repair, DNA incision; nucleotide-excision repair, DNA incision, 3'-to lesion; nucleotide-excision repair, DNA incision, 5'-to lesion; oogenesis; post-embryonic hemopoiesis; pyrimidine dimer repair via nucleotide-excision repair; replicative cell aging; response to nutrient; response to oxidative stress; response to sucrose stimulus; response to X-ray; spermatogenesis; syncytium formation; transcription-coupled nucleotide-excision repair; UV protection
Disease: Cerebrooculofacioskeletal Syndrome 4
Reference #:  P07992 (UniProtKB)
Alt. Names/Synonyms: COFS4; DNA excision repair protein ERCC-1; ERCC1; excision repair cross-complementing rodent repair deficiency, complementation group 1 (includes overlapping antisense sequence); UV20
Gene Symbols: ERCC1
Molecular weight: 32,562 Da
Basal Isoelectric point: 5.9  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ERCC1

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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

► Hide Isoforms
 
0 2 K37‑ac EVPPGVAkPLFRSTQ
0 1 K37 EVPPGVAKPLFRSTQ
0 2 S104‑p KSNSIIVsPRQRGNP
0 2 K162‑ub GRLQSLGkNFALRVL
0 1 K243‑ub TECLTTVkSVNKTDS
0 1 K247 TTVkSVNKTDSQTLL
0 1 S259 TLLTTFGSLEQLIAA
0 1 A265 GSLEQLIAASREDLA
0 1 S267 LEQLIAASREDLALC
0 1 K281‑ub CPGLGPQkARRLFDV
0 1 K295‑ac VLHEPFLkVP_____
0 2 K295‑ub VLHEPFLkVP_____
0 1 - gap
  ERCC1 iso3  
K37 EVPPGVAKPLFRSTQ
K37 EVPPGVAKPLFRSTQ
S104 KSNSIIVSPRQRGNP
K162 GRLQSLGKNFALRVL
K243 TECLTTVKSVNKTDS
K247 TTVKSVNKTDSQTLL
S259 TLLTTFGSLEQLIAA
A265 GSLEQLIAASREDLA
S267 LEQLIAASREDLALC
K281 CPGLGPQKVRALGKN
- gap
- gap
S307‑p KHNLRPQsFKVKKEP
  mouse

 
K37 EVPCAGVKPLFRSSR
K37‑ub EVPCAGVkPLFRSSR
S104 KSNSIIVSPRQRGNP
K162 ERLQSLGKNFALRVL
K243 TECLTTVKSVNkTDS
K247‑ub TTVKSVNkTDSQTLL
S259‑p TLLATFGsLEQLFtA
T265‑p GsLEQLFtAsREDLA
S267‑p LEQLFtAsREDLALC
K281 CPGLGPQKARRLFEV
K295 VLHEPFLKVPR____
K295 VLHEPFLKVPR____
- gap
  rat

 
K37‑ac EAPSSGAkPLFKSSR
K37 EAPSSGAKPLFKSSR
S104 KSSSIIVSPRQRGNP
K162 ERLQSLGKNFALRVL
K243 TECLTTVKSVNKTDS
K247 TTVKSVNKTDSQTLL
S259 TLLTTFGSLEQLITA
T265 GSLEQLITASREDLA
S267 LEQLITASREDLALC
K281 CPGLGPQKARRLFEV
K295 VLHEPFLKVPR____
K295 VLHEPFLKVPR____
- gap
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.