Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ERCC1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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
Cellular Component: nucleoplasm; nucleotide-excision repair complex; transcription factor TFIID complex; nuclear chromosome, telomeric region; cytoplasm; nucleolus; nucleus
Molecular Function: protein C-terminus binding; protein domain specific binding; protein binding; structure-specific DNA binding; single-stranded DNA specific endodeoxyribonuclease activity; TATA-binding protein binding; damaged DNA binding; single-stranded DNA binding
Biological Process: oogenesis; chromosome organization and biogenesis; germ cell development; DNA recombination; negative regulation of telomere maintenance; UV protection; post-embryonic hemopoiesis; transcription-coupled nucleotide-excision repair; double-strand break repair; nucleotide-excision repair, DNA damage removal; nucleotide-excision repair, DNA incision, 5'-to lesion; response to nutrient; response to X-ray; mitotic recombination; multicellular organism growth; male gonad development; isotype switching; pyrimidine dimer repair via nucleotide-excision repair; multicellular organismal aging; DNA repair; replicative cell aging; DNA catabolic process, endonucleolytic; syncytium formation; response to sucrose stimulus; nucleotide-excision repair, DNA incision, 3'-to lesion; cell proliferation; nucleotide-excision repair; embryonic organ development; spermatogenesis; response to oxidative stress
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


Protein Structure Not Found.

STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  RCSB PDB  |  Phospho3D  |  DISEASE  |  Source  |  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


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


0 1 K295-u VLHEPFLkVP_____


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.