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Protein Page:
NHEJ1 (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
NHEJ1 DNA repair protein involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. May serve as a bridge between XRCC4 and the other NHEJ factors located at DNA ends, or may participate in reconfiguration of the end bound NHEJ factors to allow XRCC4 access to the DNA termini. It may act in concert with XRCC6/XRCC5 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are noncomplementary or partially complementary. Interacts with XRCC4 and the XRCC4-LIG4 complex. Binds DNA in a length-dependent manner. Ubiquitously expressed. Belongs to the XLF family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Cellular Component: nucleus
Molecular Function: protein binding; DNA binding
Biological Process: central nervous system development; B cell differentiation; response to ionizing radiation; positive regulation of ligase activity; double-strand break repair via nonhomologous end joining; DNA recombination; T cell differentiation
Reference #:  Q9H9Q4 (UniProtKB)
Alt. Names/Synonyms: Cernunnos; FLJ12610; NHEJ1; Non-homologous end-joining factor 1; nonhomologous end-joining factor 1; Protein cernunnos; XLF; XRCC4-like factor
Gene Symbols: NHEJ1
Molecular weight: 33,337 Da
Basal Isoelectric point: 5.65  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

NHEJ1

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

 
1 0 S55-p QVDTSVVsQRAKELN
1 1 S132-p LASPSLVsQHLIRPL
0 2 Y167 KDLEIQDYQESGATL
0 1 I175 QESGATLIRDRLkTE
0 1 K180-ub TLIRDRLkTEPFEEN
1 1 S203-p EKLPEACsIGDGKPF
0 1 T222 QDLYMAVTtQEVQVG
1 0 T223-p DLYMAVTtQEVQVGQ
1 2 S245-p PHTSNSAsLQGIDsQ
1 1 S251-p AsLQGIDsQCVNQPE
0 1 S262-p NQPEQLVssAPtLsA
1 2 S263-p QPEQLVssAPtLsAP
1 2 T266-p QLVssAPtLsAPEKE
0 1 S268-p VssAPtLsAPEKEST
0 1 S287-p PLQRPQLskVKRKKP
0 1 K288-m3 LQRPQLskVKRKKPR
  mouse

 
S55 QVDTSVVSQRAKELN
S132 PASSSLVSQHLIHPL
Y167-p KDLEIQAyQESGAVL
S175-p QESGAVLsRSRLKTE
K180 VLsRSRLKTEPFEEN
A203 EKLPEACAVGDGKPF
T222-p QSLYVAVtKQQIQAR
K223 SLYVAVtKQQIQARQ
S245-p TQASSSTsPRGTDNQ
- gap
S258 NQPEEPVSLSSTLSE
L259 QPEEPVSLSSTLSEP
T262 EPVSLSSTLSEPEYE
S264 VSLSSTLSEPEYEPV
V283 PMHRARLVKSKRKKP
K284 MHRARLVKSKRKKPR
  rat

 
S55 QVDTLEVSQRAKELN
S137 PASSLLVSQHLICPL
Y172-p KDLEIQAyQESGAVL
S180 QESGAVLSRGRLKTE
K185 VLSRGRLKTEPFEEN
A208 EKLPEACAVGDGRPF
T227 QSLYVAVTKQQVQAR
K228 SLYVAVTKQQVQARQ
S250 PQTSSSTSPQGTDSQ
S256 TSPQGTDSQLQNQPE
S267 NQPEQQISPTPTLSE
P268 QPEQQISPTPTLSEP
T271 QQISPTPTLSEPECE
S273 ISPTPTLSEPECEPM
V292 PVHRAQLVKAKRKKP
K293 VHRAQLVKAKRKKPR
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