PARP1_RAT - dbPTM
PARP1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARP1_RAT
UniProt AC P27008
Protein Name Poly [ADP-ribose] polymerase 1
Gene Name Parp1
Organism Rattus norvegicus (Rat).
Sequence Length 1014
Subcellular Localization Nucleus . Nucleus, nucleolus . Localizes at sites of DNA damage.
Protein Description 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. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. Mediates the poly(ADP-ribosyl)ation of histones in a HPF1-dependent manner. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming..
Protein Sequence MAEATERLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDTEVDGFSELRWDDQQKVKKTAEAGGVAGKGQHGGGGKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQMRLSKKMLDPEKPQLGMIDRWYHPTCFVKNRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAVKSEGKRKCDEVDGIDEVAKKKSKKGKDKESSKLEKALKAQNELVWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLKIKKQDRLFPPESSAPAPPAPPVSITSAPTAVNSSAPADKPLSNMKILTLGKLSQNKDEAKAMIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFLQDVSASAKSLQELLSAHSLSSWGAEVKVEPGEVVVPKGKSAAPSKKSKGAVKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLESDKESRYWIFRSWGRVGTVIGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLAVKPGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAVSQGSSESQILDLSNRFYTLIPHDFGMKKPPLLNNTDSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTAPDPSASITLDGVEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEATERLY
------CCHHHHHHH		26.83-
41PhosphorylationRMAIMVQSPMFDGKV
EEEEEECCCCCCCCC		13.61-
75PhosphorylationDTEVDGFSELRWDDQ
CCCCCCCHHCCCCCH		41.0530417516
97AcetylationEAGGVAGKGQHGGGG
HHCCCCCCCCCCCCC		45.73-
105AcetylationGQHGGGGKAEKTLGD
CCCCCCCCCHHHHHH		57.56-
131AcetylationTCKGCMEKIEKGQMR
CCHHHHHHHHHHHHH		29.31-
177PhosphorylationLGFRPEYSASQLKGF
CCCCCCCCHHHHCCC		21.56-
179PhosphorylationFRPEYSASQLKGFSL
CCCCCCHHHHCCCCC		30.06-
185PhosphorylationASQLKGFSLLSAEDK
HHHHCCCCCCCHHHH		36.75-
258PhosphorylationDELKKACSTNDLKEL
HHHHHHCCCCCHHHH		34.8022108457
275PhosphorylationFNQQQVPSGESAILD
ECCCCCCCCCCHHHH		57.23-
278PhosphorylationQQVPSGESAILDRVA
CCCCCCCCHHHHHHC		24.92-
388ADP-ribosylationVNSSAPADKPLSNMK
CCCCCCCCCCCCCCE		52.63-
408PolyADP-ribosyl glutamic acidKLSQNKDEAKAMIEK
HHCCCHHHHHHHHHH		54.39-
408ADP-ribosylationKLSQNKDEAKAMIEK
HHCCCHHHHHHHHHH		54.39-
414ADP-ribosylationDEAKAMIEKLGGKLT
HHHHHHHHHHCHHCC		29.19-
414PolyADP-ribosyl glutamic acidDEAKAMIEKLGGKLT
HHHHHHHHHHCHHCC		29.19-
436ADP-ribosylationLCISTKKEVEKMSKK
EEHCCHHHHHHHHHH		58.42-
436PolyADP-ribosyl glutamic acidLCISTKKEVEKMSKK
EEHCCHHHHHHHHHH		58.42-
438ADP-ribosylationISTKKEVEKMSKKME
HCCHHHHHHHHHHHH		44.10-
438PolyADP-ribosyl glutamic acidISTKKEVEKMSKKME
HCCHHHHHHHHHHHH		44.10-
445ADP-ribosylationEKMSKKMEEVKAANV
HHHHHHHHHHHHCCC		69.39-
445PolyADP-ribosyl glutamic acidEKMSKKMEEVKAANV
HHHHHHHHHHHHCCC		69.39-
446PolyADP-ribosyl glutamic acidKMSKKMEEVKAANVR
HHHHHHHHHHHCCCE		45.91-
446ADP-ribosylationKMSKKMEEVKAANVR
HHHHHHHHHHHCCCE		45.91-
457PolyADP-ribosyl glutamic acidANVRVVCEDFLQDVS
CCCEEEEHHHHHHHH		39.94-
457ADP-ribosylationANVRVVCEDFLQDVS
CCCEEEEHHHHHHHH		39.94-
485PolyADP-ribosyl glutamic acidSLSSWGAEVKVEPGE
CHHHCCCEEEEECCC		38.64-
485ADP-ribosylationSLSSWGAEVKVEPGE
CHHHCCCEEEEECCC		38.64-
489ADP-ribosylationWGAEVKVEPGEVVVP
CCCEEEEECCCEEEC		41.70-
489PolyADP-ribosyl glutamic acidWGAEVKVEPGEVVVP
CCCEEEEECCCEEEC		41.70-
492PolyADP-ribosyl glutamic acidEVKVEPGEVVVPKGK
EEEEECCCEEECCCC		42.74-
492ADP-ribosylationEVKVEPGEVVVPKGK
EEEEECCCEEECCCC		42.74-
500ADP-ribosylationVVVPKGKSAAPSKKS
EEECCCCCCCCCCCC		38.03-
504ADP-ribosylationKGKSAAPSKKSKGAV
CCCCCCCCCCCCCCC		48.25-
507ADP-ribosylationSAAPSKKSKGAVKEE
CCCCCCCCCCCCCCC		39.81-
513ADP-ribosylationKSKGAVKEEGVNKSE
CCCCCCCCCCCCHHH		54.08-
513PolyADP-ribosyl glutamic acidKSKGAVKEEGVNKSE
CCCCCCCCCCCCHHH		54.08-
514ADP-ribosylationSKGAVKEEGVNKSEK
CCCCCCCCCCCHHHH		63.82-
514PolyADP-ribosyl glutamic acidSKGAVKEEGVNKSEK
CCCCCCCCCCCHHHH		63.82-
519ADP-ribosylationKEEGVNKSEKRMKLT
CCCCCCHHHHHEEEE		43.05-
520ADP-ribosylationEEGVNKSEKRMKLTL
CCCCCHHHHHEEEEE		46.41-
520PolyADP-ribosyl glutamic acidEEGVNKSEKRMKLTL
CCCCCHHHHHEEEEE		46.41-
600AcetylationGTVIGSNKLEQMPSK
EEEECCCCHHCCCCH		55.91-
621AcetylationFMKLYEEKTGNAWHS
HHHHHHHHHCCCCCC		50.2022902405
782PhosphorylationYSLLRGGSDDSSKDP
HHHHHCCCCCCCCCC		40.8628432305
785PhosphorylationLRGGSDDSSKDPIDV
HHCCCCCCCCCCCCC		44.2525575281
786PhosphorylationRGGSDDSSKDPIDVN
HCCCCCCCCCCCCCC		48.3425575281
940AcetylationKHASHISKLPKGKHS
HCHHHHHCCCCCCCC		69.1122902405
949AcetylationPKGKHSVKGLGKTAP
CCCCCCCCCCCCCCC		51.9722902405
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PARP1_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARP1_RAT !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PARP1_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HES1_RATHes1physical
15607978
RAD50_RATRad50physical
15607978
NPM_RATNpm1physical
15607978
H33_RATH3f3bphysical
15607978
SRC_RATSrcphysical
15607978
KCC2A_RATCamk2aphysical
15607978
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PARP1_RAT

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Related Literatures of Post-Translational Modification

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