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Protein Page:
ERCC4 (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
ERCC4 Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link. Defects in ERCC4 are the cause of xeroderma pigmentosum complementation group F (XP-F); also known as xeroderma pigmentosum VI (XP6). XP-F is an autosomal recessive disease characterized by hypersensitivity of the skin to sunlight followed by high incidence of skin cancer and frequent neurologic abnormalities. Defects in ERCC4 are a cause of XFE progeroid syndrome (XFEPS). This syndrome is illustrated by one patient who presented with dwarfism, cachexia and microcephaly. Belongs to the XPF family. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.-.-; Deoxyribonuclease; DNA repair, damage
Chromosomal Location of Human Ortholog: 16p13.12
Cellular Component: chromosome, telomeric region; nuclear chromosome, telomeric region; nucleoplasm; nucleotide-excision repair complex; nucleus
Molecular Function: damaged DNA binding; endodeoxyribonuclease activity; protein binding; protein C-terminus binding; protein N-terminus binding; single-stranded DNA binding; single-stranded DNA specific endodeoxyribonuclease activity; structure-specific DNA binding
Biological Process: DNA repair; double-strand break repair via homologous recombination; 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; nucleotide-excision repair, preincision complex stabilization; resolution of meiotic joint molecules as recombinants; response to UV; telomere maintenance; transcription-coupled nucleotide-excision repair
Disease: Fanconi Anemia, Complementation Group Q; Tracheoesophageal Fistula With Or Without Esophageal Atresia; Xeroderma Pigmentosum, Complementation Group F; Xfe Progeroid Syndrome
Reference #:  Q92889 (UniProtKB)
Alt. Names/Synonyms: DNA excision repair protein ERCC-4; DNA repair endonuclease XPF; DNA repair protein complementing XP-F cells; ERCC11; ERCC4; excision repair cross-complementing rodent repair deficiency, complementation group 4; excision-repair, complementing defective, in Chinese hamster; RAD1; Xeroderma pigmentosum group F-complementing protein; xeroderma pigmentosum, complementation group F; XPF
Gene Symbols: ERCC4
Molecular weight: 104,486 Da
Basal Isoelectric point: 6.5  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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ERCC4

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



 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 Y191‑p NLFVRKLyLWPRFHV
0 5 K260‑ac SLENAIGkPFDKTIR
0 1 S283 QLGAKTKSLVQDLkI
0 1 K289‑ac KSLVQDLkILRTLLQ
0 1 I363 KISEKMEIKEGEETK
0 1 T385 NPKWEALTEVLKEIE
0 1 K452‑ub KAEEVWMkFRKEDSS
0 1 S465‑p SSKRIRKsHKRPKDP
0 1 K500‑ac TLTQMVGkPEELEEE
0 1 I518 EEGYRREISssPEsC
0 1 S519 EGYRREISssPEsCP
0 3 S520‑p GYRREISssPEsCPE
0 8 S521‑p YRREISssPEsCPEE
0 3 S524‑p EISssPEsCPEEIKH
0 1 E533 PEEIKHEEFDVNLSS
0 1 T660‑p NLDLVRGtAsADVST
0 1 S662‑p DLVRGtAsADVSTDt
0 1 T669‑p sADVSTDtRKAGGQE
0 1 T710‑p GIDIEPVtLEVGDYI
0 1 Y742‑p SLNNGRLySQCISMS
0 1 Y752‑p CISMSRYykRPVLLI
0 1 K753‑ub ISMSRYykRPVLLIE
0 1 S764 LLIEFDPSKPFSLTS
  mouse

 
Y191 NLFVRKLYLWPRFHV
K260 SLENALGKPFDKTIR
S283‑p QLGAKTKsLVQDLKI
K289 KsLVQDLKILRTLLQ
S363‑p KTSEKTSsPEVQETK
T385‑p NPKWEALtDVLKEIE
N452 KAEEVWVNVRKGDGP
S465 GPKRTTKSDKRPKAA
S501 TLTQVLGSAEEPPED
T519‑p EEDLCRQtsssPEGC
S520‑p EDLCRQtsssPEGCG
S521‑p DLCRQtsssPEGCGV
S522‑p LCRQtsssPEGCGVE
G525 QtsssPEGCGVEIKR
S534‑p GVEIKREsFDLNVSS
S661 NLDLARGSAALDAPT
A663 DLARGSAALDAPTDT
T670 ALDAPTDTRKAGGQE
T711 GIDIEPVTLEVGDYI
Y743 SLHSGRLYSQCLAMS
Y753 CLAMSRYYRRPVLLI
R754 LAMSRYYRRPVLLIE
S765‑p LLIEFDPsKPFSLAP
  rat

 
Y162 NLFMKKLYLWPRFHV
K231‑ac SLENALGkPFDKTIR
S254 QLGAKTKSLVQDLKI
K260 KSLVQDLKILRTLLQ
G334 KTSEKMAGPEEQETK
T356 NPKWEALTEVLKEIE
N423 KAEEVWVNFRKGDGP
S436 GPKRTMKSDKRPKDA
T472 TLTQVLGTAEEPPEE
T490 EEDLHKQTGSSPEVC
G491 EDLHKQTGSSPEVCG
S492 DLHKQTGSSPEVCGG
S493 LHKQTGSSPEVCGGE
V496 QTGSSPEVCGGEIQH
S505 GGEIQHESFDLNVSS
T632 NLDLARGTAAMDTPT
A634 DLARGTAAMDTPTDT
T641 AMDTPTDTRKAGGQE
T682 GIDIEPVTLEVGDYI
Y714 SLHSGRLYSQCLAMS
Y724 CLAMSRYYRRPVLLI
R725 LAMSRYYRRPVLLIE
S736 LLIEFDPSKPFSLAP
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