Search by BoMiProt ID - Bomi8116


Primary Information

BoMiProt ID Bomi8116
Protein Name Poly [ADP-ribose] polymerase 1/ADP-ribosyltransferase diphtheria toxin-like 1/DNA ADP-ribosyltransferase PARP1/NAD(+) ADP-ribosyltransferase 1/Poly[ADP-ribose] synthase 1/Protein poly-ADP-ribosyltransferase PARP1
Organism Bos taurus
Uniprot IdP18493
Milk FractionWhey
Ref Sequence Id NP_777176.1
Aminoacid Length 1016
Molecular Weight 113486
Fasta Sequence https://www.uniprot.org/uniprot/P18493.fasta
Gene Name PARP1/ADPRT
Gene Id 286764
Protein Existence Status reviewed

Secondary Information

Protein Function Poly(ADP-ribose) polymerase-1 (PARP-1) is a nuclear enzyme with a crucial role in the maintenance of genomic stability. In addition to the role of PARP-1 in DNA repair, multiple studies have also demonstrated its involvement in several inflammatory diseases, such as septic shock, asthma, atherosclerosis, and stroke, as well as in cancer. 
Biochemical Properties Poly(ADP-ribose)polymerase-1 (PARP-1) catalyzes the polymerization of ADP-ribose units from NAD+ modules on target proteins, resulting in the attachment of linear or branched polymers. There are six functional domains (A-F) of PARP-1 molecule is present in context of three classic domains, i.e., DNA binding (DBD), automodification (AD) and catalytic (CD) released by proteolytic enzymes.
Significance in milk PARP1 is activated during mastitis, which may prove to be a useful biomarker of mastitis.PARP1 is involved in several cellular processes including transcription, epigenetics, chromatin re-modelling as well as in the maintenance of genomic stability.
PTMs Acetylation,Phosphorylation and ADP-ribosylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P18493|PARP1_BOVIN Poly [ADP-ribose] polymerase 1 OS=Bos taurus OX=9913 GN=PARP1 PE=2 SV=2 MAESSDKLYRVEYAKSGRASCKKCKESIPKDSIRMAFMVES*41PMFDGKIPHWYHLSCFWKV GFSIWHPDVEVEGFSELRWDDQQTIKKMAETGGRTDVSGKGQDGVGSKTEKTLIDFGAGY AKSNRSTCKSCMEKIDKGQVRLSKKVVYPDKPQLGMVDCWYHPKCFVQKREELGFRPEFS*180 ATHLMGFS*188VLTAEDQETLKKQLPAIKGERKRKGDEVDGIDEVTKKKSKKEKDKEIKLEKA LKAQNDLIWNVKDELKKACSTNDLKELLIFNKQEVPS*277GES*280AILDRVADGMVFGALLPCEE CSGQLVFKGDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYFKKLKIKKQDRIF PPESSTPVGAAAPPSAASAPAAVHSGPPDKPLSNMKILTLGKLSQNKDEVKATIEKLGGK LTGTANKASLCISTKKEVDKLNKKMEEVKEANIRVVSEDFLQDISASTKSLQELLSTHLL SPWGAEVKVEPVEAVGPKGKSGAAPSKKSKGPVKEEGTNKSEKRMKLTLKGGAAVDPDSG LEHNAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGS NKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKHPKKFYPLEIDYGQDEEAVKKLTVN PGTKSKLPKPVQNLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQ ALSQGSSDSHILDLSNRFYTLIPHDFGMKKPPLLNNANSVQAKVEMLDNLLDIEVAYSLL RGGS*784DDSS*788KDPIDVNYEKLKTDIKVVDKDSEEAEIIRKYVKNTHATTHNAYDLEVVDIFK IEREGESQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFA DMVSKSANYCHTSQGDPIGLILLGEAALGNMYELKHARHISKLPKGKHSVKGLGKTTPDP SASITVDGVEVPLGTGISSGVNDTCLLYNEYIVYDIAQVHLKYLLKLKFNFKTSLW
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs PARP-1 is the most important member, exhibiting poly (ADP-rybosil)ation activity, is a protein postransductional modification essential to cellular processes, such as the regulation of DNA reparation, the maintenance of chromatin function and genomic stability, the regulation of transcription, cell cycle progression, and cell death.
Bibliography 1.García S, Conde C. The Role of Poly(ADP-ribose) Polymerase-1 in Rheumatoid Arthritis. Mediators Inflamm. 2015;2015:837250. doi: 10.1155/2015/837250. Epub 2015 Mar 3. PMID: 26339143; PMCID: PMC4539103. 2.Kiliańska ZM, Zołnierczyk J, Wesierska-Gadek J. Biologiczna aktywność polimerazy poli(ADP-rybozy)-1 [Biological activity of poly(ADP-ribose)polymerase-1]. Postepy Hig Med Dosw (Online). 2010 Jul 30;64:344-63. Polish. PMID: 20679690. 3. J. C. Ame, C. Spenlehauer, and G. de Murcia, “The PARP ´ superfamily,” BioEssays, vol. 26, no. 8, pp. 882–893, 2004. 4.V. Schreiber, F. Dantzer, J. C. Ame, and G. de Murcia, “Poly (ADP-ribose): novel functions for an old molecule,” Nature Reviews Molecular Cell Biology, vol. 7, no. 7, pp. 517–528, 2006. 5.B. C. Woodhouse and G. L. Dianov, “Poly ADP-ribose polymerase-1: an international molecule of mystery,” DNA Repair, vol. 7, no. 7, pp. 1077–1086, 2008. 6.De Matteis G, Reale A, Grandoni F, Meyer-Ficca ML, Scatà MC, Meyer RG, Buttazzoni L, Moioli B. Assessment of Poly(ADP-ribose) Polymerase1 (PARP1) expression and activity in cells purified from blood and milk of dairy cattle. Vet Immunol Immunopathol. 2018 Aug;202:102-108. doi: 10.1016/j.vetimm.2018.06.013. Epub 2018 Jun 30. PMID: 30078582.