ZN598_HUMAN - dbPTM
ZN598_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN598_HUMAN
UniProt AC Q86UK7
Protein Name E3 ubiquitin-protein ligase ZNF598 {ECO:0000305}
Gene Name ZNF598 {ECO:0000312|HGNC:HGNC:28079}
Organism Homo sapiens (Human).
Sequence Length 904
Subcellular Localization
Protein Description E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation. [PubMed: 28065601]
Protein Sequence MAAAGGAEGRRAALEAAAAAAPERGGGSCVLCCGDLEATALGRCDHPVCYRCSTKMRVLCEQRYCAVCREELRQVVFGKKLPAFATIPIHQLQHEKKYDIYFADGKVYALYRQLLQHECPRCPELPPFSLFGDLEQHMRRQHELFCCRLCLQHLQIFTYERKWYSRKDLARHRMQGDPDDTSHRGHPLCKFCDERYLDNDELLKHLRRDHYFCHFCDSDGAQDYYSDYAYLREHFREKHFLCEEGRCSTEQFTHAFRTEIDLKAHRTACHSRSRAEARQNRHIDLQFSYAPRHSRRNEGVVGGEDYEEVDRYSRQGRVARAGTRGAQQSRRGSWRYKREEEDREVAAAVRASVAAQQQEEARRSEDQEEGGRPKKEEAAARGPEDPRGPRRSPRTQGEGPGPKETSTNGPVSQEAFSVTGPAAPGCVGVPGALPPPSPKLKDEDFPSLSASTSSSCSTAATPGPVGLALPYAIPARGRSAFQEEDFPALVSSVPKPGTAPTSLVSAWNSSSSSKKVAQPPLSAQATGSGQPTRKAGKGSRGGRKGGPPFTQEEEEDGGPALQELLSTRPTGSVSSTLGLASIQPSKVGKKKKVGSEKPGTTLPQPPPATCPPGALQAPEAPASRAEGPVAVVVNGHTEGPAPARSAPKEPPGLPRPLGSFPCPTPQEDFPALGGPCPPRMPPPPGFSAVVLLKGTPPPPPPGLVPPISKPPPGFSGLLPSPHPACVPSPATTTTTKAPRLLPAPRAYLVPENFRERNLQLIQSIRDFLQSDEARFSEFKSHSGEFRQGLISAAQYYKSCRDLLGENFQKVFNELLVLLPDTAKQQELLSAHTDFCNREKPLSTKSKKNKKSAWQATTQQAGLDCRVCPTCQQVLAHGDASSHQALHAARDDDFPSLQAIARIIT
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
80UbiquitinationRQVVFGKKLPAFATI
HHHHHCCCCCEEEEE		61.1429967540
80AcetylationRQVVFGKKLPAFATI
HHHHHCCCCCEEEEE		61.1426051181
86PhosphorylationKKLPAFATIPIHQLQ
CCCCEEEEEEHHHCC		22.3420058876
96UbiquitinationIHQLQHEKKYDIYFA
HHHCCCCCCEEEEEC		55.2829967540
97UbiquitinationHQLQHEKKYDIYFAD
HHCCCCCCEEEEECC		45.2129967540
108PhosphorylationYFADGKVYALYRQLL
EECCCHHHHHHHHHH		8.3820393185
111PhosphorylationDGKVYALYRQLLQHE
CCHHHHHHHHHHHCC		6.53-
181PhosphorylationMQGDPDDTSHRGHPL
HCCCCCCCCCCCCCH		33.5421406692
182PhosphorylationQGDPDDTSHRGHPLC
CCCCCCCCCCCCCHH		20.4121406692
190UbiquitinationHRGHPLCKFCDERYL
CCCCCHHHHCCHHHC		57.6229967540
190AcetylationHRGHPLCKFCDERYL
CCCCCHHHHCCHHHC		57.6226051181
204UbiquitinationLDNDELLKHLRRDHY
CCCHHHHHHHHCCCC		53.9023000965
211PhosphorylationKHLRRDHYFCHFCDS
HHHHCCCCEEECCCC		16.52-
224PhosphorylationDSDGAQDYYSDYAYL
CCCCCCCHHHHHHHH		7.87-
230PhosphorylationDYYSDYAYLREHFRE
CHHHHHHHHHHHHHH		10.48-
238UbiquitinationLREHFREKHFLCEEG
HHHHHHHHCCEECCC		35.0923000965
238AcetylationLREHFREKHFLCEEG
HHHHHHHHCCEECCC		35.0926051181
248PhosphorylationLCEEGRCSTEQFTHA
EECCCCCCHHHHHHH		33.3524505115
263MethylationFRTEIDLKAHRTACH
HHHHHHHHHHHHHHH		38.1044510505
263UbiquitinationFRTEIDLKAHRTACH
HHHHHHHHHHHHHHH		38.1033845483
263 (in isoform 1)Ubiquitination-38.1021890473
263 (in isoform 2)Ubiquitination-38.1021890473
263 (in isoform 3)Ubiquitination-38.1021890473
288PhosphorylationRHIDLQFSYAPRHSR
CCCCEEEECCCCCCC		13.8722322096
289PhosphorylationHIDLQFSYAPRHSRR
CCCEEEECCCCCCCC		23.1628796482
292MethylationLQFSYAPRHSRRNEG
EEEECCCCCCCCCCC		32.04115920525
306PhosphorylationGVVGGEDYEEVDRYS
CCCCCCCHHHHHHHH		15.0821945579
312PhosphorylationDYEEVDRYSRQGRVA
CHHHHHHHHHCCCCC		12.0721945579
313PhosphorylationYEEVDRYSRQGRVAR
HHHHHHHHHCCCCCC		21.0121945579
320MethylationSRQGRVARAGTRGAQ
HHCCCCCCCCCCCCH		30.6083445873
324MethylationRVARAGTRGAQQSRR
CCCCCCCCCCHHHCC		37.2254560887
333 (in isoform 2)Phosphorylation-13.4324144214
336PhosphorylationSRRGSWRYKREEEDR
HCCCCCCCCCHHHHH		14.24-
337UbiquitinationRRGSWRYKREEEDRE
CCCCCCCCCHHHHHH		44.7722505724
337AcetylationRRGSWRYKREEEDRE
CCCCCCCCCHHHHHH		44.7726051181
364PhosphorylationQQEEARRSEDQEEGG
HHHHHHHHHHHHCCC		39.7229214152
374UbiquitinationQEEGGRPKKEEAAAR
HHCCCCCHHHHHHHC		72.0324816145
392PhosphorylationDPRGPRRSPRTQGEG
CCCCCCCCCCCCCCC		21.7330576142
395PhosphorylationGPRRSPRTQGEGPGP
CCCCCCCCCCCCCCC		44.2921406692
414 (in isoform 2)Phosphorylation-44.1430266825
416 (in isoform 2)Phosphorylation-6.2522210691
417PhosphorylationPVSQEAFSVTGPAAP
CCCCHHEECCCCCCC		26.3126074081
417 (in isoform 3)Phosphorylation-26.3130266825
419PhosphorylationSQEAFSVTGPAAPGC
CCHHEECCCCCCCCC		35.9329978859
419 (in isoform 3)Phosphorylation-35.9322210691
428 (in isoform 2)Phosphorylation-24.7930266825
431 (in isoform 3)Phosphorylation-37.0230266825
437PhosphorylationPGALPPPSPKLKDED
CCCCCCCCCCCCCCC		40.2025159151
447PhosphorylationLKDEDFPSLSASTSS
CCCCCCCCCCCCCCC		34.6427251275
449PhosphorylationDEDFPSLSASTSSSC
CCCCCCCCCCCCCCC		25.2227251275
451PhosphorylationDFPSLSASTSSSCST
CCCCCCCCCCCCCCC		25.9927251275
452PhosphorylationFPSLSASTSSSCSTA
CCCCCCCCCCCCCCC		32.1427251275
453PhosphorylationPSLSASTSSSCSTAA
CCCCCCCCCCCCCCC		20.1227251275
454PhosphorylationSLSASTSSSCSTAAT
CCCCCCCCCCCCCCC		35.1427251275
455PhosphorylationLSASTSSSCSTAATP
CCCCCCCCCCCCCCC		16.3227251275
457PhosphorylationASTSSSCSTAATPGP
CCCCCCCCCCCCCCC		24.0327251275
458PhosphorylationSTSSSCSTAATPGPV
CCCCCCCCCCCCCCC		25.3327251275
461PhosphorylationSSCSTAATPGPVGLA
CCCCCCCCCCCCCEE		26.7225159151
471PhosphorylationPVGLALPYAIPARGR
CCCEECCCEECCCCC		20.2927642862
479PhosphorylationAIPARGRSAFQEEDF
EECCCCCCCCCCCCC		35.9430576142
498PhosphorylationSSVPKPGTAPTSLVS
HCCCCCCCCCHHHHH		37.6826434776
501PhosphorylationPKPGTAPTSLVSAWN
CCCCCCCHHHHHCCC		32.0326434776
502PhosphorylationKPGTAPTSLVSAWNS
CCCCCCHHHHHCCCC		26.2225159151
505PhosphorylationTAPTSLVSAWNSSSS
CCCHHHHHCCCCCCC		32.6225159151
509PhosphorylationSLVSAWNSSSSSKKV
HHHHCCCCCCCCCCC		22.3925159151
510PhosphorylationLVSAWNSSSSSKKVA
HHHCCCCCCCCCCCC		30.9025159151
511PhosphorylationVSAWNSSSSSKKVAQ
HHCCCCCCCCCCCCC		38.1525159151
512PhosphorylationSAWNSSSSSKKVAQP
HCCCCCCCCCCCCCC		48.3925159151
513PhosphorylationAWNSSSSSKKVAQPP
CCCCCCCCCCCCCCC		38.1425159151
514AcetylationWNSSSSSKKVAQPPL
CCCCCCCCCCCCCCC		53.8926051181
522PhosphorylationKVAQPPLSAQATGSG
CCCCCCCCCCCCCCC		24.9025247763
526PhosphorylationPPLSAQATGSGQPTR
CCCCCCCCCCCCCCC		21.5728555341
528PhosphorylationLSAQATGSGQPTRKA
CCCCCCCCCCCCCCC		29.8725159151
532PhosphorylationATGSGQPTRKAGKGS
CCCCCCCCCCCCCCC		36.5925627689
539PhosphorylationTRKAGKGSRGGRKGG
CCCCCCCCCCCCCCC		31.10-
550PhosphorylationRKGGPPFTQEEEEDG
CCCCCCCCCHHHCCC		40.6226714015
570PhosphorylationELLSTRPTGSVSSTL
HHHHCCCCCCCCCHH		38.5122210691
572PhosphorylationLSTRPTGSVSSTLGL
HHCCCCCCCCCHHCC		22.7022210691
574PhosphorylationTRPTGSVSSTLGLAS
CCCCCCCCCHHCCCC		21.2125627689
575PhosphorylationRPTGSVSSTLGLASI
CCCCCCCCHHCCCCC		26.0425627689
576PhosphorylationPTGSVSSTLGLASIQ
CCCCCCCHHCCCCCC		19.8325627689
655MethylationKEPPGLPRPLGSFPC
CCCCCCCCCCCCCCC		44.08115387425
679MethylationLGGPCPPRMPPPPGF
CCCCCCCCCCCCCCC		35.07115387433
695PhosphorylationAVVLLKGTPPPPPPG
EEEEECCCCCCCCCC		30.9125159151
715PhosphorylationSKPPPGFSGLLPSPH
CCCCCCCCCCCCCCC		34.1523312004
720PhosphorylationGFSGLLPSPHPACVP
CCCCCCCCCCCCCCC		35.4925159151
728PhosphorylationPHPACVPSPATTTTT
CCCCCCCCCCCCCCC		13.5325159151
731PhosphorylationACVPSPATTTTTKAP
CCCCCCCCCCCCCCC		28.2325627689
732PhosphorylationCVPSPATTTTTKAPR
CCCCCCCCCCCCCCC		25.0123312004
733PhosphorylationVPSPATTTTTKAPRL
CCCCCCCCCCCCCCC		28.2823312004
734PhosphorylationPSPATTTTTKAPRLL
CCCCCCCCCCCCCCC		24.9823312004
735PhosphorylationSPATTTTTKAPRLLP
CCCCCCCCCCCCCCC		24.1023312004
763PhosphorylationRNLQLIQSIRDFLQS
HHHHHHHHHHHHHHC		16.7620873877
779MethylationEARFSEFKSHSGEFR
HHHHHHHHHCCHHHH		43.11115978125
780PhosphorylationARFSEFKSHSGEFRQ
HHHHHHHHCCHHHHH		28.3620873877
782PhosphorylationFSEFKSHSGEFRQGL
HHHHHHCCHHHHHHH		47.2920873877
829PhosphorylationAKQQELLSAHTDFCN
HHHHHHHHHCCCCCC		30.5429978859
832PhosphorylationQELLSAHTDFCNREK
HHHHHHCCCCCCCCC		30.4129978859
839AcetylationTDFCNREKPLSTKSK
CCCCCCCCCCCCCCH		48.28165603
844AcetylationREKPLSTKSKKNKKS
CCCCCCCCCHHCHHH		57.83165607
847AcetylationPLSTKSKKNKKSAWQ
CCCCCCHHCHHHHHH		79.62165611
850UbiquitinationTKSKKNKKSAWQATT
CCCHHCHHHHHHHHH		55.5929967540
851PhosphorylationKSKKNKKSAWQATTQ
CCHHCHHHHHHHHHH		36.0328555341
895PhosphorylationARDDDFPSLQAIARI
HHCCCCHHHHHHHHH		32.8620873877
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 ZN598_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN598_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 ZN598_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GGYF2_HUMANGIGYF2physical
22751931
IF4E2_HUMANEIF4E2physical
22751931
UBP2_HUMANUSP2physical
22751931
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 ZN598_HUMAN

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Related Literatures of Post-Translational Modification
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-437, AND MASSSPECTROMETRY.
"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-437, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASSSPECTROMETRY.

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