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Protein Page:
PARP1 (mouse)
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
PARP1 Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with PARP3, APTX and SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423. Interacts (when poly-ADP- ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with EEF1A1, RNF4 and TXK. Note: This description may include information from UniProtKB.
Protein type: EC 2.4.2.30; Transferase; Nuclear envelope; DNA repair, damage; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; transcription factor complex; protein complex; cytoplasm; nucleolus; nuclear envelope; nucleus
Molecular Function: transferase activity; identical protein binding; protein binding; transferase activity, transferring glycosyl groups; enzyme binding; DNA binding; zinc ion binding; metal ion binding; protein N-terminus binding; transcription factor binding; NAD binding; NAD+ ADP-ribosyltransferase activity
Biological Process: transcription, DNA-dependent; DNA damage response, detection of DNA damage; DNA repair; protein autoprocessing; protein amino acid ADP-ribosylation; regulation of transcription, DNA-dependent; cellular response to insulin stimulus; base-excision repair; double-strand break repair; transforming growth factor beta receptor signaling pathway; positive regulation of transcription from RNA polymerase II promoter; regulation of growth rate; DNA metabolic process; response to DNA damage stimulus; telomere maintenance
Reference #:  P11103 (UniProtKB)
Alt. Names/Synonyms: 5830444G22Rik; ADP-ribosyltransferase (NAD+, poly (ADP-ribose) polymerase) 1; Adprp; Adprt; ADPRT 1; Adprt1; AI893648; C80510; msPARP; NAD(+) ADP-ribosyltransferase 1; PARP; PARP-1; Parp1; poly (ADP-ribose) polymerase family, member 1; poly (ADP-ribose) polymerase) 1; Poly [ADP-ribose] polymerase 1; Poly[ADP-ribose] synthase 1; poly[ADP-ribose] synthetase 1; PPOL; sPARP-1
Gene Symbols: Parp1
Molecular weight: 113,100 Da
Basal Isoelectric point: 9.05  Predict pI for various phosphorylation states
CST Pathways:  Death Receptor Signaling  |  NF-kB Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PARP1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  NURSA  |  UniProtKB  |  Entrez-Gene  |  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 

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.


       mouse

► Hide Isoforms
 
0 1 S5 ___MAEASERLYRVQ
0 3 S41 RMAIMVQSPMFDGKV
0 3 K97 EAGGVAGKGQDGSGG
0 3 K105-a GQDGSGGkAEKTLGD
0 1 K108 GSGGkAEKTLGDFAA
0 8 K119 DFAAEYAKSNRSMCK
0 1 K131 MCKGCLEKIEKGQMR
0 2 K165 YHPTCFVKKRDELGF
1 2 S177 LGFRPEYSASQLKGF
0 4 S179 FRPEYSASQLKGFSL
0 1 S185 ASQLKGFSLLSAEDK
1 1 K203 KKQLPAIKNEGKRKG
0 1 K209 IKNEGKRKGDEVDGT
0 1 K221 DGTDEVAKKKSRKET
0 1 K239 SKLEKALKAQNELIW
0 3 K249 NELIWNIKDELKKAC
0 7 K253 WNIKDELKKACSTND
0 3 K262 ACSTNDLKELLIFNQ
0 36 Q269 KELLIFNQQQVPSGE
0 2 S274 FNQQQVPSGESAILD
0 1 S277 QQVPSGESAILDRVA
0 1 K320 GDVTAWTKCMVKTQN
0 1 K337 RKEWVTPKEFREISY
0 1 - gap
0 2 H368 SSAPITVHWPLSVTS
2 2 S372 ITVHWPLSVTSAPTA
2 1 - gap
0 1 K394 DKPLSNMKILTLGKL
0 2 K400 MKILTLGKLSQNKDE
0 6 K400 MKILTLGKLSQNKDE
0 2 K414 EAKAVIEKLGGKLTG
0 2 K425 KLTGSANKASLCISI
0 3 K433 ASLCISIKKEVEKMN
0 7 K447 NKKMEEVKEANIRVV
0 3 K467 QDVSASTKSLQDLLS
3 1 K486 SPWGAEVKAEPGEVV
1 0 K498 EVVAPRGKSAAPSKK
1 0 K504 GKSAAPSKKSKGCFK
1 0 K507 AAPSKKSKGCFKEEG
1 6 K507 AAPSKKSKGCFKEEG
0 3 K517 FKEEGVNKSEKRMKL
1 26 K520 EGVNKSEKRMKLTLK
1 0 K523 NKSEKRMKLTLKGGA
0 2 K527 KRMKLTLKGGAAVDP
0 13 K547-u HSAHVLEkGGKVFSA
0 1 K550 HVLEkGGKVFSATLG
0 5 K563-u LGLVDIVkGTNSYYK
0 2 K578-u LQLLEDDkESRYWIF
0 1 K599 GTVIGSNKLEQMPSK
0 1 K599 GTVIGSNKLEQMPSK
0 1 S605 NKLEQMPSKEEAVEQ
0 2 K620 FMKLYEEKTGNAWHS
0 1 K636 NFTKYPKKFYPLEID
0 1 K666 GTKSKLPKPVQELVG
0 5 K747 PHDFGMKKPPLLNNA
0 1 Y774 LLDIEVAYSLLRGGs
1 14 S781-p YSLLRGGsDDSSKDP
1 0 S784 LRGGsDDSSKDPIDV
1 1 S785 RGGsDDSSKDPIDVN
0 3 K786 GGsDDSSKDPIDVNY
0 5 K795 PIDVNYEKLKTDIKV
0 3 R851 SQRYKPFRQLHNRRL
0 6 K939 KHASHISKLPKGKHS
0 7 K948 PKGKHSVKGLGKTTP
0 2 K1009 LKLKFNFKTSLW___
  PARP1 iso3  
S5 ___MAEASERLYRVE
S41 RMTIMVQSPMFDGKV
K97 EAGGVAGKGQDGSGG
K105 GQDGSGGKAEKTLGD
K108 GSGGKAEKTLGDFLA
K119-u DFLAEYAkSNRSMCK
K131 MCKGCLEKIEKGQMR
K165 YHPTCFVKKRDELGF
S177 LGFRPEYSASQLKGF
S179 FRPEYSASQLKGFSL
S185 ASQLKGFSLLSAEDK
K203 KKQLPAIKNEGKRKG
K209 IKNEGKRKGDEVDGT
K221 DGTDEVAKKKSKKGK
K240 SKLEKALKAQNELIW
K250 NELIWNIKDELKKAC
K254 WNIKDELKKACSTND
K263 ACSTNDLKELLIFNQ
Q270 KELLIFNQQQVPSGE
S275 FNQQQVPSGESAILD
S278 QQVPSGESAILDRVA
K321 GDVTAWTKCMVKTQN
K338 RKEWVTPKGFREISY
- gap
- gap
S373 APLALPLSVTSAPTA
- gap
K395 DKPLSNMKILTLGKL
K401 MKILTLGKLSQNKDE
K401 MKILTLGKLSQNKDE
K415 EAKAVIEKLGGKLTG
K426 KLTGSANKASLCIST
K434 ASLCISTKKEVEKMS
K448 SKKMEEVKAANVRVV
K468-u QDVSASTkSLQELLS
K487 SSWGAEVKAEPGEVV
K499 EVVAPKGKSAAPSKK
K505 GKSAAPSKKSKGAVK
K508 AAPSKKSKGAVKEEG
K508 AAPSKKSKGAVKEEG
K518 VKEEGVNKSEkRMKL
K521-a EGVNKSEkRMKLTLK
K524 NKSEkRMKLTLKGGA
K528 kRMKLTLKGGAAVDP
K548 HSAHVLEKGGKVFSA
K551 HVLEKGGKVFSATLG
R564 LGLVDIVRGTNSYYK
K579 LQLLEDDKESRYWIF
K600 GTVIGSNKLEQMPSK
K600 GTVIGSNKLEQMPSK
S606 NKLEQMPSKEDAVEH
K621 FMKLYEEKTGNAWHS
K637 NFTKYPKKFYPLEID
K667 GTKSKLPKPVQELVG
K748 PHDFGMKKPPLLNNA
Y775 LLDIEVAYSLLRGGS
S782 YSLLRGGSDDSSKDP
S785 LRGGSDDSSKDPIDV
S786 RGGSDDSSKDPIDVN
K787 GGSDDSSKDPIDVNY
K796 PIDVNYEKLKTDIKV
R852 SQRYKPFRQLHNRRL
K940 KHASHISKLPKGKHS
K949 PKGKHSVKGLGKTTP
K1010 LKLKFNFKTSLW___
  human

 
S5-p ___MAESsDKLYRVE
S41-p RMAIMVQsPMFDGKV
K97-a EAGGVTGkGQDGIGS
K105-a GQDGIGSkAEkTLGD
K108-u GIGSkAEkTLGDFAA
K119-u DFAAEYAkSNRSTCK
K131-a TCKGCMEkIEKGQVR
K165-u YHPGCFVkNREELGF
S177-p LGFRPEYsAsQLKGF
S179-p FRPEYsAsQLKGFsL
S185-p AsQLKGFsLLATEDK
K203-s KKQLPGVkSEGKRkG
K209-u VkSEGKRkGDEVDGV
K221-u DGVDEVAkKKSKKEK
K239-u SKLEKALkAQNDLIW
K249-a NDLIWNIkDELkKVC
K253-a WNIkDELkKVCSTND
K262-u VCSTNDLkELLIFNk
K269-u kELLIFNkQQVPsGE
S274-p FNkQQVPsGEsAILD
S277-p QQVPsGEsAILDRVA
K320-u GDVTAWTkCMVKTQT
K337-u RKEWVTPkEFREISY
S364-p FPPETSAsVAAtPPP
T368-p TSAsVAAtPPPstAS
S372-p VAAtPPPstASAPAA
T373-p AAtPPPstASAPAAV
K394-u DKPLSNMkILTLGkL
K400-a MkILTLGkLSRNKDE
K400-u MkILTLGkLSRNKDE
K414-u EVKAMIEkLGGKLTG
K425-u KLTGTANkASLCIST
K433-a ASLCISTkKEVEKMN
K447-u NKKMEEVkEANIRVV
K467 QDVSASTKSLQELFL
K486-s SPWGAEVkAEPVEVV
K498-a EVVAPRGkSGAALSk
K505-a kSGAALSkKSkGQVK
K508-a AALSkKSkGQVKEEG
K508-m1 AALSkKSkGQVKEEG
K518-a VKEEGINkSEkRMkL
K521-a EGINkSEkRMkLTLk
K524-a NkSEkRMkLTLkGGA
K528-u kRMkLTLkGGAAVDP
K548-u HSAHVLEkGGkVFSA
K551-u HVLEkGGkVFSATLG
K564-u LGLVDIVkGTNSYYK
K579-u LQLLEDDkENRYWIF
K600-a GTVIGSNkLEQMPsK
K600-u GTVIGSNkLEQMPsK
S606-p NkLEQMPsKEDAIEH
K621-a FMKLYEEkTGNAWHS
K637-u NFTKYPKkFYPLEID
K667-u GTKSKLPkPVQDLIK
K748-u PHDFGMKkPPLLNNA
Y775-p LLDIEVAySLLRGGs
S782-p ySLLRGGsDDsskDP
S785-p LRGGsDDsskDPIDV
S786-p RGGsDDsskDPIDVN
K787-u GGsDDsskDPIDVNY
K796-u PIDVNYEkLKTDIKV
K852-u CQRYKPFkQLHNRRL
K940-u KHASHISkLPKGKHS
K949-u PKGKHSVkGLGKTTP
K1010-u LKLKFNFkTSLW___
  rat

 
T5 ___MAEATERLYRVE
S41 RMAIMVQSPMFDGKV
K97 EAGGVAGKGQHGGGG
K105 GQHGGGGKAEKTLGD
K108 GGGGKAEKTLGDFAA
K119 DFAAEYAKSNRSTCK
K131 TCKGCMEKIEKGQMR
K165 YHPTCFVKNRDELGF
S177 LGFRPEYSASQLKGF
S179 FRPEYSASQLKGFSL
S185 ASQLKGFSLLSAEDK
K203 KKQLPAVKSEGKRKC
K209 VKSEGKRKCDEVDGI
K221 DGIDEVAKKKSKKGK
K240 SKLEKALKAQNELVW
K250 NELVWNIKDELKKAC
K254 WNIKDELKKACSTND
K263 ACSTNDLKELLIFNQ
Q270 KELLIFNQQQVPSGE
S275 FNQQQVPSGESAILD
S278 QQVPSGESAILDRVA
K321 GDVTAWTKCMVKTQN
K338 RKEWVTPKEFREISY
- gap
- gap
S373 APPAPPVSITSAPTA
- gap
K395 DKPLSNMKILTLGKL
K401 MKILTLGKLSQNKDE
K401 MKILTLGKLSQNKDE
K415 EAKAMIEKLGGKLTG
K426 KLTGSANKASLCIST
K434 ASLCISTKKEVEKMS
K448 SKKMEEVKAANVRVV
K468 QDVSASAKSLQELLS
K487 SSWGAEVKVEPGEVV
K499 EVVVPKGKSAAPSKK
K505 GKSAAPSKKSKGAVK
K508 AAPSKKSKGAVKEEG
K508 AAPSKKSKGAVKEEG
K518 VKEEGVNKSEKRMKL
K521 EGVNKSEKRMKLTLK
K524 NKSEKRMKLTLKGGA
K528 KRMKLTLKGGAAVDP
K548 HSAHVLEKGGKVFSA
K551 HVLEKGGKVFSATLG
K564 LGLVDIVKGTNSYYK
K579 LQLLESDKESRYWIF
K600 GTVIGSNKLEQMPSK
K600 GTVIGSNKLEQMPSK
S606 NKLEQMPSKEDAVEH
K621 FMKLYEEKTGNAWHS
K637 NFTKYPKKFYPLEID
K667 GTKSKLPKPVQELVG
K748 PHDFGMKKPPLLNNT
Y775 LLDIEVAYSLLRGGS
S782 YSLLRGGSDDSSKDP
S785 LRGGSDDSSKDPIDV
S786 RGGSDDSSKDPIDVN
K787 GGSDDSSKDPIDVNY
K796 PIDVNYEKLKTDIKV
R852 SQRYKPFRQLHNRRL
K940 KHASHISKLPKGKHS
K949 PKGKHSVKGLGKTAP
K1010 LKLKFNFKTSLW___
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