PARP8_HUMAN - dbPTM
PARP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARP8_HUMAN
UniProt AC Q8N3A8
Protein Name Poly [ADP-ribose] polymerase 8
Gene Name PARP8
Organism Homo sapiens (Human).
Sequence Length 854
Subcellular Localization
Protein Description
Protein Sequence MGMCSRQERIQKDIDVVIQKSRAEKDCLFADFRYSDSTFTFTYVGGPRSVSYSVHVSEDYPDNTYVSSSENDEDVLVTTEPIPVIFHRIATELRKTNDINCCLSIKSKLQKENGEESRQNSTVEEDSEGDNDSEEFYYGGQVNYDGELHKHPQLEADLSAVREIYGPHAVSLREYGAIDDVDIDLHIDVSFLDEEIAVAWEVIRTEPIIVRLHCSLTQYLNGPVPTVDVFQISTKERFGLGHQLKKIMQTFVTQQWKQSKEKSNCLHNKKLSEKKVKSPLHLFSTLRRSPSYPPPGCGKSKSKLKSEQDGISKTHKLLRRTCSSTVKTDDVCVTKSHRTFGRSLSSDPRAEQAMTAIKSHKLLNRPCPAAVKSEECLTLKSHRLLTRSCSGDPRCEHNTNLKPHKLLSRSYSSNLRMEELYGLKNHKLLSKSYSSAPKSSKTELFKEPNAEGRRLSLTSGLIGILTPSSSSSSQLAPNGAKCIPVRDRGFLVQTIEFAEQRIPVLNEYCVVCDEPHVFQNGPMLRPTVCERELCVFAFQTLGVMNEAADEIATGAQVVDLLVSMCRSALESPRKVVIFEPYPSVVDPNDPQMLAFNPRKKNYDRVMKALDSITSIREMTQAPYLEIKKQMDKQDPLAHPLLQWVISSNRSHIVKLPVNRQLKFMHTPHQFLLLSSPPAKESNFRAAKKLFGSTFAFHGSHIENWHSILRNGLVVASNTRLQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKVSAKDEPASSSKSSNTSQSQKKGQQSQFLQSRNLKCIALCEVITSSDLHKHGEIWVVPNTDHVCTRFFFVYEDGQVGDANINTQEGGIHKEILRVIGNQTATG
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
5Phosphorylation---MGMCSRQERIQK
---CCCCCHHHHHHH		28.2727135362
20UbiquitinationDIDVVIQKSRAEKDC
HHHHHHCCCHHHCCE		30.6821890473
20 (in isoform 2)Ubiquitination-30.6821890473
20 (in isoform 1)Ubiquitination-30.6821890473
96PhosphorylationIATELRKTNDINCCL
HHHHHHHCCCCCCCH		31.52-
104PhosphorylationNDINCCLSIKSKLQK
CCCCCCHHHHHHHHH		17.66-
106UbiquitinationINCCLSIKSKLQKEN
CCCCHHHHHHHHHHC		37.86-
245UbiquitinationFGLGHQLKKIMQTFV
CCCHHHHHHHHHHHH		33.41-
257AcetylationTFVTQQWKQSKEKSN
HHHHHHHHHHHHHHC		40.1124468223
278PhosphorylationLSEKKVKSPLHLFST
CCHHHCCCHHHHHHH		35.3628450419
284PhosphorylationKSPLHLFSTLRRSPS
CCHHHHHHHHCCCCC		32.6526074081
285PhosphorylationSPLHLFSTLRRSPSY
CHHHHHHHHCCCCCC		19.5626074081
289PhosphorylationLFSTLRRSPSYPPPG
HHHHHCCCCCCCCCC		16.2730108239
291PhosphorylationSTLRRSPSYPPPGCG
HHHCCCCCCCCCCCC		52.0628450419
292PhosphorylationTLRRSPSYPPPGCGK
HHCCCCCCCCCCCCC		24.1230108239
321PhosphorylationTHKLLRRTCSSTVKT
HHHHHHHHCCCCCCC		15.4229514088
323PhosphorylationKLLRRTCSSTVKTDD
HHHHHHCCCCCCCCC		28.5623401153
324PhosphorylationLLRRTCSSTVKTDDV
HHHHHCCCCCCCCCE		39.0929514088
325PhosphorylationLRRTCSSTVKTDDVC
HHHHCCCCCCCCCEE		15.1029514088
328PhosphorylationTCSSTVKTDDVCVTK
HCCCCCCCCCEEEEC		32.85-
332ADP-ribosylationTVKTDDVCVTKSHRT
CCCCCCEEEECCCCC		4.0725043379
335UbiquitinationTDDVCVTKSHRTFGR
CCCEEEECCCCCCCC		24.70-
343PhosphorylationSHRTFGRSLSSDPRA
CCCCCCCCCCCCHHH		32.7428450419
345PhosphorylationRTFGRSLSSDPRAEQ
CCCCCCCCCCHHHHH		33.6623401153
346PhosphorylationTFGRSLSSDPRAEQA
CCCCCCCCCHHHHHH		57.8528450419
355PhosphorylationPRAEQAMTAIKSHKL
HHHHHHHHHHHHHHH		28.3927486199
358UbiquitinationEQAMTAIKSHKLLNR
HHHHHHHHHHHHHCC		44.00-
367ADP-ribosylationHKLLNRPCPAAVKSE
HHHHCCCCCCCCCCH		3.0225043379
372SumoylationRPCPAAVKSEECLTL
CCCCCCCCCHHHEEE		47.63-
372AcetylationRPCPAAVKSEECLTL
CCCCCCCCCHHHEEE		47.6320167786
372SumoylationRPCPAAVKSEECLTL
CCCCCCCCCHHHEEE		47.63-
376ADP-ribosylationAAVKSEECLTLKSHR
CCCCCHHHEEECCCE		2.8625043379
380AcetylationSEECLTLKSHRLLTR
CHHHEEECCCEECHH		38.6920167786
388PhosphorylationSHRLLTRSCSGDPRC
CCEECHHCCCCCCCC		13.85-
390PhosphorylationRLLTRSCSGDPRCEH
EECHHCCCCCCCCCC		47.6923898821
395ADP-ribosylationSCSGDPRCEHNTNLK
CCCCCCCCCCCCCCC		8.3125043379
405AcetylationNTNLKPHKLLSRSYS
CCCCCHHHHHCCCCC		60.7020167786
410PhosphorylationPHKLLSRSYSSNLRM
HHHHHCCCCCCCCCH		26.4528450419
411PhosphorylationHKLLSRSYSSNLRME
HHHHCCCCCCCCCHH		18.2730001349
412PhosphorylationKLLSRSYSSNLRMEE
HHHCCCCCCCCCHHH		17.6328450419
413PhosphorylationLLSRSYSSNLRMEEL
HHCCCCCCCCCHHHH		31.4828450419
424UbiquitinationMEELYGLKNHKLLSK
HHHHHCCHHCHHCCC		53.28-
427UbiquitinationLYGLKNHKLLSKSYS
HHCCHHCHHCCCCCC		61.59-
431UbiquitinationKNHKLLSKSYSSAPK
HHCHHCCCCCCCCCC		54.07-
434PhosphorylationKLLSKSYSSAPKSSK
HHCCCCCCCCCCCCC		27.4125072903
435PhosphorylationLLSKSYSSAPKSSKT
HCCCCCCCCCCCCCC		40.1224719451
441UbiquitinationSSAPKSSKTELFKEP
CCCCCCCCCCHHCCC		53.78-
456PhosphorylationNAEGRRLSLTSGLIG
CCCCCCEEECCCEEE		27.9928450419
458PhosphorylationEGRRLSLTSGLIGIL
CCCCEEECCCEEEEE		19.8528450419
459PhosphorylationGRRLSLTSGLIGILT
CCCEEECCCEEEEEC		36.5728450419
466PhosphorylationSGLIGILTPSSSSSS
CCEEEEECCCCCCCC		21.1428450419
560 (in isoform 2)Phosphorylation-3.2529116813
569 (in isoform 2)Phosphorylation-7.6429116813
571 (in isoform 2)Phosphorylation-30.7529116813
607UbiquitinationKNYDRVMKALDSITS
CCHHHHHHHHHHCHH		42.83-
614PhosphorylationKALDSITSIREMTQA
HHHHHCHHHHHHHCC		20.2729116813
654UbiquitinationSNRSHIVKLPVNRQL
CCCCEEEEEECCCCE		46.61-
706PhosphorylationSHIENWHSILRNGLV
HHHHCHHHHHHCCEE		18.22-
753PhosphorylationMNKKQKVSAKDEPAS
CCCCCCCCCCCCCCC		36.3122964224
760PhosphorylationSAKDEPASSSKSSNT
CCCCCCCCCCCCCCC		45.9517525332
767PhosphorylationSSSKSSNTSQSQKKG
CCCCCCCCHHHHHHH		30.0517525332
770PhosphorylationKSSNTSQSQKKGQQS
CCCCCHHHHHHHHHH		43.6717525332
777PhosphorylationSQKKGQQSQFLQSRN
HHHHHHHHHHHHHCC		18.2724719451
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 PARP8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARP8_HUMAN !!
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 PARP8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PARP8_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PARP8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760; THR-767 ANDSER-770, AND MASS SPECTROMETRY.

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