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Protein Page:
ATRIP (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

Overview
ATRIP is required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein. Heterodimerizes with ATR. The heterodimer binds replication protein A (RPA), a protein complex that subsequently is recruited to single stranded DNA (ssDNA). Its EEXXXDDL motif is required for the interaction with catalytic subunit of DNA-PK and its recruitment to sites of DNA damage. e for this protein is either identical to or adjacent to that of ATRIP. Some of the mRNAs that encode ATRIP also encode TREX1 in another reading frame. Three alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; Cell cycle regulation; DNA binding protein
Cellular Component: nucleoplasm; microtubule cytoskeleton; nucleolus; nucleus
Molecular Function: protein binding
Biological Process: DNA damage checkpoint; DNA repair; DNA replication
Reference #:  Q8WXE1 (UniProtKB)
Alt. Names/Synonyms: AGS1; ATM and Rad3-related-interacting protein; ATR interacting protein; ATR-interacting protein; ATRIP; DKFZp762J2115; FLJ12343; MGC20625; MGC21482; MGC26740
Gene Symbols: ATRIP
Molecular weight: 85,838 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

ATRIP

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S224‑p, S239‑p
intracellular localization: S68‑p, S72‑p

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

► Hide Isoforms
 
0 1 S13 APGSKRRSEPPAPRP
0 3 K32-a GTGHPPSkRARGFsA
0 1 S38-p SkRARGFsAAAAPDP
1 0 S68-p EELDTLAsQALsQCP
1 0 S72-p TLAsQALsQCPAAAR
0 1 K96-u RLLDGMSkNPSGKNR
0 14 N97 LLDGMSkNPSGKNRE
0 1 N102 SkNPSGKNRETVPIK
0 1 A212 KLQTSERANKLAAPS
1 16 S224-p APSVSHVsPRKNPSV
1 17 S239-p VIKPEACsPQFGKTS
0 7 S518-p RSLVHRLsDGDMtSA
0 1 T523-p RLsDGDMtSALRGVA
0 2 Y636-p GCLLLLLyMYITSRP
5161 : Phospho-ATRIP (Ser224) Antibody
  ATRIP iso2  
S13 APGSKRRSEPPAPRP
K32 GTGHPPSKRARGFSA
S38 SKRARGFSAAAAPDP
S68 EELDTLASQALSQCP
S72 TLASQALSQCPAAAR
K96 RLLDGMSKNPSGKNR
N97 LLDGMSKNPSGKNRE
N102 SKNPSGKNRETVPIK
A212 KLQTSERANKLAAPS
S224 APSVSHVSPRKNPSV
S239 VIKPEACSPQFGKTS
S518 RSLVHRLSDGDMTSA
T523 RLSDGDMTSALRGVA
Y636 GCLLLLLYMYITSRP
  mouse

 
S14-p PNSHRKQsGGLEPFP
K33 SIENPPSKRARSFSE
S39 SKRARSFSETTVPDP
S69 EELDILASQALSQCP
S73 ILASQALSQCPVAPR
N96 RRLDGLPNsPIRKsR
S97-p RLDGLPNsPIRKsRE
S102-p PNsPIRKsREDIPVK
T212-p KSQSNGRtNKPAAPS
S224-p APSVSHVsPRKGSSV
S239-p VLKSEACsPHVGKTT
- gap
T518 VQTCADTTSASREDA
Y631 GCLLLRLYMYITSRP
5161 : Phospho-ATRIP (Ser224) Antibody
  rat

 
S14 PNSHRKQSGGLEPFL
K33 SIENPPSKRARSFSE
S39 SKRARSFSETTVPDP
S69 EELDILASQALSQCP
S73 ILASQALSQCPVAPP
N96 RRLDGLPNsPIRKNR
S97-p RLDGLPNsPIRKNRE
N102 PNsPIRKNREDIPVK
T212 KLQSNERTNKLTIPS
S224 IPSVSQVSPRKGSSV
S239 VVKSEACSPHVGKTT
- gap
- gap
Y630 GCLLLRLYMYITSRP
5161 : Phospho-ATRIP (Ser224) Antibody
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