PARG_HUMAN - dbPTM
PARG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARG_HUMAN
UniProt AC Q86W56
Protein Name Poly(ADP-ribose) glycohydrolase
Gene Name PARG
Organism Homo sapiens (Human).
Sequence Length 976
Subcellular Localization Isoform 1: Nucleus . Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage.
Isoform 2: Cytoplasm . Translocates to the nucleus in response to DNA damage.
Isoform 3: Cytoplasm.
Isoform 4: Cytoplasm.
Protein Description Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. [PubMed: 23102699 PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers]
Protein Sequence MNAGPGCEPCTKRPRWGAATTSPAASDARSFPSRQRRVLDPKDAHVQFRVPPSSPACVPGRAGQHRGSATSLVFKQKTITSWMDTKGIKTAESESLDSKENNNTRIESMMSSVQKDNFYQHNVEKLENVSQLSLDKSPTEKSTQYLNQHQTAAMCKWQNEGKHTEQLLESEPQTVTLVPEQFSNANIDRSPQNDDHSDTDSEENRDNQQFLTTVKLANAKQTTEDEQAREAKSHQKCSKSCDPGEDCASCQQDEIDVVPESPLSDVGSEDVGTGPKNDNKLTRQESCLGNSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPGFDEQEDGSSSQTANKPSRFQARDADIEFRKRYSTKGGEVRLHFQFEGGESRTGMNDLNAKLPGNISSLNVECRNSKQHGKKDSKITDHFMRLPKAEDRRKEQWETKHQRTERKIPKYVPPHLSPDKKWLGTPIEEMRRMPRCGIRLPLLRPSANHTVTIRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEENGQGMLQVDFANRFVGGGVTSAGLVQEEIRFLINPELIISRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWSRSHEDGSERDDWQRRCTEIVAIDALHFRRYLDQFVPEKMRRELNKAYCGFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHIFLTERKLTVGDVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESCAETADHSGQRTGT
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
1 (in isoform 2)Acetylation-7.5722814378
12AcetylationPGCEPCTKRPRWGAA
CCCCCCCCCCCCCCC
68.1025953088
20PhosphorylationRPRWGAATTSPAASD
CCCCCCCCCCCCHHH
27.5427732954
21PhosphorylationPRWGAATTSPAASDA
CCCCCCCCCCCHHHH
28.1721815630
22PhosphorylationRWGAATTSPAASDAR
CCCCCCCCCCHHHHH
14.2616964243
26PhosphorylationATTSPAASDARSFPS
CCCCCCHHHHHCCCC
33.6327732954
29PhosphorylationSPAASDARSFPSRQR
CCCHHHHHCCCCHHC
43.7732142685
33UbiquitinationSDARSFPSRQRRVLD
HHHHCCCCHHCCCCC
38.7529967540
53PhosphorylationVQFRVPPSSPACVPG
EEEECCCCCCCCCCC
42.7726552605
54PhosphorylationQFRVPPSSPACVPGR
EEECCCCCCCCCCCC
23.4525159151
55PhosphorylationFRVPPSSPACVPGRA
EECCCCCCCCCCCCC
33.7332142685
65UbiquitinationVPGRAGQHRGSATSL
CCCCCCCCCCCCEEE
34.8422817900
66MethylationPGRAGQHRGSATSLV
CCCCCCCCCCCEEEE
32.64115486421
68PhosphorylationRAGQHRGSATSLVFK
CCCCCCCCCEEEEEE
28.4723917254
69UbiquitinationAGQHRGSATSLVFKQ
CCCCCCCCEEEEEEC
12.2022817900
70UbiquitinationGQHRGSATSLVFKQK
CCCCCCCEEEEEECC
25.0421890473
71PhosphorylationQHRGSATSLVFKQKT
CCCCCCEEEEEECCC
23.4228555341
75MethylationSATSLVFKQKTITSW
CCEEEEEECCCCCCH
43.32115974639
77MethylationTSLVFKQKTITSWMD
EEEEEECCCCCCHHH
42.35115974647
82UbiquitinationKQKTITSWMDTKGIK
ECCCCCCHHHCCCCC
4.6822817900
86UbiquitinationITSWMDTKGIKTAES
CCCHHHCCCCCCHHH
55.1422817900
87UbiquitinationTSWMDTKGIKTAESE
CCHHHCCCCCCHHHH
28.8121890473
91PhosphorylationDTKGIKTAESESLDS
HCCCCCCHHHHCCCC
17.2033259812
95UbiquitinationIKTAESESLDSKENN
CCCHHHHCCCCCCCC
46.9129967540
104PhosphorylationDSKENNNTRIESMMS
CCCCCCCHHHHHHHH
34.8428555341
108PhosphorylationNNNTRIESMMSSVQK
CCCHHHHHHHHHHHH
19.8823532336
111PhosphorylationTRIESMMSSVQKDNF
HHHHHHHHHHHHCCC
20.7924144214
112PhosphorylationRIESMMSSVQKDNFY
HHHHHHHHHHHCCCH
15.6330576142
115UbiquitinationSMMSSVQKDNFYQHN
HHHHHHHHCCCHHHC
53.1129967540
117PhosphorylationMSSVQKDNFYQHNVE
HHHHHHCCCHHHCHH
44.5633259812
119PhosphorylationSVQKDNFYQHNVEKL
HHHHCCCHHHCHHHH
18.3428796482
130PhosphorylationVEKLENVSQLSLDKS
HHHHHCHHHHCCCCC
36.6623927012
132UbiquitinationKLENVSQLSLDKSPT
HHHCHHHHCCCCCCC
4.2321890473
133PhosphorylationLENVSQLSLDKSPTE
HHCHHHHCCCCCCCH
27.2123927012
137PhosphorylationSQLSLDKSPTEKSTQ
HHHCCCCCCCHHHHH
36.4029255136
139PhosphorylationLSLDKSPTEKSTQYL
HCCCCCCCHHHHHHH
64.2429255136
140UbiquitinationSLDKSPTEKSTQYLN
CCCCCCCHHHHHHHH
48.6829967540
142PhosphorylationDKSPTEKSTQYLNQH
CCCCCHHHHHHHHHH
17.9526074081
143PhosphorylationKSPTEKSTQYLNQHQ
CCCCHHHHHHHHHHH
32.0926074081
145PhosphorylationPTEKSTQYLNQHQTA
CCHHHHHHHHHHHHH
14.0126074081
151PhosphorylationQYLNQHQTAAMCKWQ
HHHHHHHHHHHHHHH
17.7926074081
164PhosphorylationWQNEGKHTEQLLESE
HHCCCCCHHHHHHCC
28.9820363803
170PhosphorylationHTEQLLESEPQTVTL
CHHHHHHCCCCEEEE
55.3221406692
174PhosphorylationLLESEPQTVTLVPEQ
HHHCCCCEEEECCHH
26.6121406692
174UbiquitinationLLESEPQTVTLVPEQ
HHHCCCCEEEECCHH
26.6121890473
176PhosphorylationESEPQTVTLVPEQFS
HCCCCEEEECCHHHC
25.9821406692
183PhosphorylationTLVPEQFSNANIDRS
EECCHHHCCCCCCCC
34.4321406692
190PhosphorylationSNANIDRSPQNDDHS
CCCCCCCCCCCCCCC
27.3930278072
191UbiquitinationNANIDRSPQNDDHSD
CCCCCCCCCCCCCCC
37.5821890473
197PhosphorylationSPQNDDHSDTDSEEN
CCCCCCCCCCCCCCC
49.5623401153
199PhosphorylationQNDDHSDTDSEENRD
CCCCCCCCCCCCCCC
44.4330278072
201PhosphorylationDDHSDTDSEENRDNQ
CCCCCCCCCCCCCHH
49.2330278072
212PhosphorylationRDNQQFLTTVKLANA
CCHHHHHHHHHHHCC
30.7220363803
213PhosphorylationDNQQFLTTVKLANAK
CHHHHHHHHHHHCCC
20.1430576142
223PhosphorylationLANAKQTTEDEQARE
HHCCCCCCHHHHHHH
38.6630624053
226UbiquitinationAKQTTEDEQAREAKS
CCCCCHHHHHHHHHH
39.6524816145
240PhosphorylationSHQKCSKSCDPGEDC
HHHHHHHCCCCCCCH
13.8828634120
240UbiquitinationSHQKCSKSCDPGEDC
HHHHHHHCCCCCCCH
13.8829967540
243UbiquitinationKCSKSCDPGEDCASC
HHHHCCCCCCCHHHC
53.0224816145
249PhosphorylationDPGEDCASCQQDEID
CCCCCHHHCCCCCCC
20.8428634120
257UbiquitinationCQQDEIDVVPESPLS
CCCCCCCCCCCCCCH
10.7229967540
261PhosphorylationEIDVVPESPLSDVGS
CCCCCCCCCCHHCCC
25.6828348404
264PhosphorylationVVPESPLSDVGSEDV
CCCCCCCHHCCCCCC
33.3728348404
268PhosphorylationSPLSDVGSEDVGTGP
CCCHHCCCCCCCCCC
30.3926074081
273PhosphorylationVGSEDVGTGPKNDNK
CCCCCCCCCCCCCCC
50.5926074081
276UbiquitinationEDVGTGPKNDNKLTR
CCCCCCCCCCCCCCC
77.5824816145
282PhosphorylationPKNDNKLTRQESCLG
CCCCCCCCCCHHHCC
31.7322199227
286PhosphorylationNKLTRQESCLGNSPP
CCCCCCHHHCCCCCC
13.3019664994
291PhosphorylationQESCLGNSPPFEKES
CHHHCCCCCCCCCCC
31.9530266825
298PhosphorylationSPPFEKESEPESPMD
CCCCCCCCCCCCCCC
70.3125159151
302PhosphorylationEKESEPESPMDVDNS
CCCCCCCCCCCCCCC
35.9225159151
309PhosphorylationSPMDVDNSKNSCQDS
CCCCCCCCCCCCCCC
28.8423927012
312PhosphorylationDVDNSKNSCQDSEAD
CCCCCCCCCCCCCCC
19.5230278072
316PhosphorylationSKNSCQDSEADEETS
CCCCCCCCCCCCCCC
14.6030278072
322PhosphorylationDSEADEETSPGFDEQ
CCCCCCCCCCCCCCC
37.8723927012
323PhosphorylationSEADEETSPGFDEQE
CCCCCCCCCCCCCCC
26.7230278072
323UbiquitinationSEADEETSPGFDEQE
CCCCCCCCCCCCCCC
26.7229967540
333PhosphorylationFDEQEDGSSSQTANK
CCCCCCCCCCCCCCC
38.8523927012
334PhosphorylationDEQEDGSSSQTANKP
CCCCCCCCCCCCCCC
31.8130576142
335PhosphorylationEQEDGSSSQTANKPS
CCCCCCCCCCCCCCC
32.9923927012
337PhosphorylationEDGSSSQTANKPSRF
CCCCCCCCCCCCCHH
33.8630576142
340AcetylationSSSQTANKPSRFQAR
CCCCCCCCCCHHCCC
41.74-
340PhosphorylationSSSQTANKPSRFQAR
CCCCCCCCCCHHCCC
41.7432645325
342PhosphorylationSQTANKPSRFQARDA
CCCCCCCCHHCCCCC
47.5423927012
349UbiquitinationSRFQARDADIEFRKR
CHHCCCCCCCHHHHH
17.7129967540
366PhosphorylationTKGGEVRLHFQFEGG
CCCCEEEEEEEEECC
5.9932645325
375PhosphorylationFQFEGGESRTGMNDL
EEEECCCCCCCCCHH
38.1225159151
385UbiquitinationGMNDLNAKLPGNISS
CCCHHCCCCCCCHHH
54.89-
391PhosphorylationAKLPGNISSLNVECR
CCCCCCHHHCEEEEC
32.5428555341
395AcetylationGNISSLNVECRNSKQ
CCHHHCEEEECCCCC
9.9719608861
401UbiquitinationNVECRNSKQHGKKDS
EEEECCCCCCCCCCC
50.2729967540
421AcetylationFMRLPKAEDRRKEQW
HHHCCCHHHHHHHHH
59.1719608861
427UbiquitinationAEDRRKEQWETKHQR
HHHHHHHHHHHHHHH
46.4729967540
430PhosphorylationRRKEQWETKHQRTER
HHHHHHHHHHHHHHC
30.7628258704
431UbiquitinationRKEQWETKHQRTERK
HHHHHHHHHHHHHCC
26.6529967540
438UbiquitinationKHQRTERKIPKYVPP
HHHHHHCCCCCCCCC
58.0721890473
438 (in isoform 3)Ubiquitination-58.0721890473
442PhosphorylationTERKIPKYVPPHLSP
HHCCCCCCCCCCCCC
16.9123403867
446UbiquitinationIPKYVPPHLSPDKKW
CCCCCCCCCCCCCCC
32.6329967540
448PhosphorylationKYVPPHLSPDKKWLG
CCCCCCCCCCCCCCC
28.1925159151
464UbiquitinationPIEEMRRMPRCGIRL
CHHHHHCCCCCCCCC
1.4121890473
464 (in isoform 2)Ubiquitination-1.4121890473
472UbiquitinationPRCGIRLPLLRPSAN
CCCCCCCCEECCCCC
21.3529967540
483PhosphorylationPSANHTVTIRVDLLR
CCCCCEEEEEEEEHH
12.2924719451
503AcetylationKPFPTHYKDLWDNKH
CCCCCCHHHCCCCCC
38.4523749302
505UbiquitinationFPTHYKDLWDNKHVK
CCCCHHHCCCCCCCC
5.6021890473
509AcetylationYKDLWDNKHVKMPCS
HHHCCCCCCCCCCCC
47.5025953088
509UbiquitinationYKDLWDNKHVKMPCS
HHHCCCCCCCCCCCC
47.5029967540
510AcetylationKDLWDNKHVKMPCSE
HHCCCCCCCCCCCCC
30.5919413330
512AcetylationLWDNKHVKMPCSEQN
CCCCCCCCCCCCCCC
36.5225953088
536AcetylationERTAGSRWELIQTAL
CCCCCHHHHHHHHHH
13.3719413330
541PhosphorylationSRWELIQTALLNKFT
HHHHHHHHHHHHCCC
16.57-
546UbiquitinationIQTALLNKFTRPQNL
HHHHHHHCCCCCCCH
48.3521890473
546UbiquitinationIQTALLNKFTRPQNL
HHHHHHHCCCCCCCH
48.3521890473
546 (in isoform 1)Ubiquitination-48.3521890473
548PhosphorylationTALLNKFTRPQNLKD
HHHHHCCCCCCCHHH
42.95-
554UbiquitinationFTRPQNLKDAILKYN
CCCCCCHHHHHHHCH
53.3029967540
582UbiquitinationDFWDKVLEEAEAQHL
HHHHHHHHHHHHHHH
59.1424816145
608UbiquitinationALCLPNICTQPIPLL
HHHCCCCCCCCHHHH
3.5324816145
616MethylationTQPIPLLKQKMNHSI
CCCHHHHHHHHCCCC
56.40115974631
616UbiquitinationTQPIPLLKQKMNHSI
CCCHHHHHHHHCCCC
56.40-
618AcetylationPIPLLKQKMNHSITM
CHHHHHHHHCCCCCC
39.8319413330
618UbiquitinationPIPLLKQKMNHSITM
CHHHHHHHHCCCCCC
39.83-
622PhosphorylationLKQKMNHSITMSQEQ
HHHHHCCCCCCCHHH
18.1026074081
624PhosphorylationQKMNHSITMSQEQIA
HHHCCCCCCCHHHHH
17.4926074081
626PhosphorylationMNHSITMSQEQIASL
HCCCCCCCHHHHHHH
23.1626074081
632PhosphorylationMSQEQIASLLANAFF
CCHHHHHHHHHHHHH
26.0819413330
649UbiquitinationFPRRNAKMKSEYSSY
CCCCCCCCCHHHCCC
5.5424816145
650UbiquitinationPRRNAKMKSEYSSYP
CCCCCCCCHHHCCCC
39.15-
651PhosphorylationRRNAKMKSEYSSYPD
CCCCCCCHHHCCCCC
37.9625072903
653PhosphorylationNAKMKSEYSSYPDIN
CCCCCHHHCCCCCCC
15.2625072903
654PhosphorylationAKMKSEYSSYPDINF
CCCCHHHCCCCCCCH
21.2425072903
656PhosphorylationMKSEYSSYPDINFNR
CCHHHCCCCCCCHHH
10.05-
690UbiquitinationFRRVTEKKPTGLVTF
HHHCCCCCCCCEEEE
41.3924816145
912PhosphorylationSELMRDIYSMHIFLT
HHHHHHHHHEEEEEE
12.2921406692
913PhosphorylationELMRDIYSMHIFLTE
HHHHHHHHEEEEEEC
12.2921406692
919PhosphorylationYSMHIFLTERKLTVG
HHEEEEEECCCCCHH
24.0121406692
945PhosphorylationEECRNCSTPGPDIKL
HHHHCCCCCCCCCCH
34.1721712546

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 PARG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARG_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 PARG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
25252691
BARD1_HUMANBARD1physical
25252691

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PARG_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-503, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197AND THR-199, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND THR-139, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASSSPECTROMETRY.

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