ZCCHV_HUMAN - dbPTM
ZCCHV_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZCCHV_HUMAN
UniProt AC Q7Z2W4
Protein Name Zinc finger CCCH-type antiviral protein 1
Gene Name ZC3HAV1
Organism Homo sapiens (Human).
Sequence Length 902
Subcellular Localization Isoform 1: Cytoplasm. Nucleus. Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner..
Isoform 2: Cytoplasm.
Protein Description Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs)..
Protein Sequence MADPEVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVATTRARVCRRKYCQRPCDNLHLCKLNLLGRCNYSQSERNLCKYSHEVLSEENFKVLKNHELSGLNKEELAVLLLQSDPFFMPEICKSYKGEGRQQICNQQPPCSRLHICDHFTRGNCRFPNCLRSHNLMDRKVLAIMREHGLNPDVVQNIQDICNSKHMQKNPPGPRAPSSHRRNMAYRARSKSRDRFFQGSQEFLASASASAERSCTPSPDQISHRASLEDAPVDDLTRKFTYLGSQDRARPPSGSSKATDLGGTSQAGTSQRFLENGSQEDLLHGNPGSTYLASNSTSAPNWKSLTSWTNDQGARRKTVFSPTLPAARSSLGSLQTPEAVTTRKGTGLLSSDYRIINGKSGTQDIQPGPLFNNNADGVATDITSTRSLNYKSTSSGHREISSPRIQDAGPASRDVQATGRIADDADPRVALVNDSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVHFHLPYRWQMLIGKTWTDFEHMETIEKGYCNPGIHLCSVGSYTINFRVMSCDSFPIRRLSTPSSVTKPANSVFTTKWIWYWKNESGTWIQYGEEKDKRKNSNVDSSYLESLYQSCPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDVIRRPTFVPQWYVQQMKRGPDHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPEYVRVSEHFKASMKNFKIEKIKKIENSELLDKFTWKKSQMKEEGKLLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPPQFDSCVDTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS
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------MADPEVCCF
------CCCHHHHHH		40.8522223895
12UbiquitinationEVCCFITKILCAHGG
HHHHHHHHHHHHCCH		28.9433845483
12 (in isoform 3)Ubiquitination-28.94-
61PhosphorylationTGGEAGITRSVVATT
CCCCCCCCHHHHHHH		18.9022817900
63PhosphorylationGEAGITRSVVATTRA
CCCCCCHHHHHHHHH		16.5822210691
76UbiquitinationRARVCRRKYCQRPCD
HHHHHCHHHCCCCCC		30.90-
77PhosphorylationARVCRRKYCQRPCDN
HHHHCHHHCCCCCCC		7.6328152594
89UbiquitinationCDNLHLCKLNLLGRC
CCCEEEEHHHCCCCC		46.9329967540
89AcetylationCDNLHLCKLNLLGRC
CCCEEEEHHHCCCCC		46.9326051181
98PhosphorylationNLLGRCNYSQSERNL
HCCCCCCCCHHHHCH		16.2428796482
99PhosphorylationLLGRCNYSQSERNLC
CCCCCCCCHHHHCHH		17.1528796482
101PhosphorylationGRCNYSQSERNLCKY
CCCCCCHHHHCHHHH		32.3628857561
107UbiquitinationQSERNLCKYSHEVLS
HHHHCHHHHHHHHCC		53.6122505724
107 (in isoform 3)Ubiquitination-53.61-
107AcetylationQSERNLCKYSHEVLS
HHHHCHHHHHHHHCC		53.6125953088
108PhosphorylationSERNLCKYSHEVLSE
HHHCHHHHHHHHCCH		17.7922210691
109PhosphorylationERNLCKYSHEVLSEE
HHCHHHHHHHHCCHH		9.9222210691
114PhosphorylationKYSHEVLSEENFKVL
HHHHHHCCHHHHHHH		48.3028450419
119UbiquitinationVLSEENFKVLKNHEL
HCCHHHHHHHHCCCC		59.2332015554
119 (in isoform 3)Ubiquitination-59.23-
119AcetylationVLSEENFKVLKNHEL
HCCHHHHHHHHCCCC		59.2326051181
122UbiquitinationEENFKVLKNHELSGL
HHHHHHHHCCCCCCC		60.2829967540
127PhosphorylationVLKNHELSGLNKEEL
HHHCCCCCCCCHHHH		37.9427251275
131UbiquitinationHELSGLNKEELAVLL
CCCCCCCHHHHHHHH		58.5729967540
151AcetylationFFMPEICKSYKGEGR
CCCHHHHHHCCCCCH		63.5811791509
154AcetylationPEICKSYKGEGRQQI
HHHHHHCCCCCHHHH		58.5411791521
179MethylationHICDHFTRGNCRFPN
ECCCCCCCCCCCCCC		33.1281441475
197UbiquitinationSHNLMDRKVLAIMRE
HCCCCCHHHHHHHHH		37.02-
202SulfoxidationDRKVLAIMREHGLNP
CHHHHHHHHHCCCCH		3.2321406390
221PhosphorylationNIQDICNSKHMQKNP
HHHHHHHCHHHHHCC		21.3720873877
222UbiquitinationIQDICNSKHMQKNPP
HHHHHHCHHHHHCCC		29.1632015554
222AcetylationIQDICNSKHMQKNPP
HHHHHHCHHHHHCCC		29.1626051181
226UbiquitinationCNSKHMQKNPPGPRA
HHCHHHHHCCCCCCC		64.9429967540
235PhosphorylationPPGPRAPSSHRRNMA
CCCCCCCCHHHHHHH		37.4823882029
236PhosphorylationPGPRAPSSHRRNMAY
CCCCCCCHHHHHHHH		21.6923882029
243PhosphorylationSHRRNMAYRARSKSR
HHHHHHHHHHHHHCC		8.27-
244 (in isoform 4)Ubiquitination-17.6221890473
247PhosphorylationNMAYRARSKSRDRFF
HHHHHHHHHCCCHHC		33.7223882029
249PhosphorylationAYRARSKSRDRFFQG
HHHHHHHCCCHHCCC		40.4325159151
257PhosphorylationRDRFFQGSQEFLASA
CCHHCCCCHHHHHHH		18.7629255136
263PhosphorylationGSQEFLASASASAER
CCHHHHHHHCHHHCC		25.5528176443
265PhosphorylationQEFLASASASAERSC
HHHHHHHCHHHCCCC		21.9128176443
267PhosphorylationFLASASASAERSCTP
HHHHHCHHHCCCCCC		28.3225159151
271PhosphorylationASASAERSCTPSPDQ
HCHHHCCCCCCCHHH		17.5329255136
273PhosphorylationASAERSCTPSPDQIS
HHHCCCCCCCHHHCC		28.2219664994
275PhosphorylationAERSCTPSPDQISHR
HCCCCCCCHHHCCCC		23.9719664994
280PhosphorylationTPSPDQISHRASLED
CCCHHHCCCCCCCCC		10.9922167270
284PhosphorylationDQISHRASLEDAPVD
HHCCCCCCCCCCCHH		32.0419664994
294PhosphorylationDAPVDDLTRKFTYLG
CCCHHHHHHHEEECC		38.5223927012
296UbiquitinationPVDDLTRKFTYLGSQ
CHHHHHHHEEECCCC		36.5029901268
296AcetylationPVDDLTRKFTYLGSQ
CHHHHHHHEEECCCC		36.5025953088
298PhosphorylationDDLTRKFTYLGSQDR
HHHHHHEEECCCCCC		22.3723401153
299PhosphorylationDLTRKFTYLGSQDRA
HHHHHEEECCCCCCC		16.5221945579
302PhosphorylationRKFTYLGSQDRARPP
HHEEECCCCCCCCCC		26.7225159151
310PhosphorylationQDRARPPSGSSKATD
CCCCCCCCCCCCCCC		54.7330266825
312PhosphorylationRARPPSGSSKATDLG
CCCCCCCCCCCCCCC		32.7630266825
313PhosphorylationARPPSGSSKATDLGG
CCCCCCCCCCCCCCC		29.8130266825
314UbiquitinationRPPSGSSKATDLGGT
CCCCCCCCCCCCCCC		57.9324816145
316PhosphorylationPSGSSKATDLGGTSQ
CCCCCCCCCCCCCCC		35.1827174698
321PhosphorylationKATDLGGTSQAGTSQ
CCCCCCCCCCCCCCH		18.8329255136
322PhosphorylationATDLGGTSQAGTSQR
CCCCCCCCCCCCCHH		22.7029255136
322O-linked_GlycosylationATDLGGTSQAGTSQR
CCCCCCCCCCCCCHH		22.7023301498
326PhosphorylationGGTSQAGTSQRFLEN
CCCCCCCCCHHHHHC		25.3829255136
327PhosphorylationGTSQAGTSQRFLENG
CCCCCCCCHHHHHCC		20.5929507054
335PhosphorylationQRFLENGSQEDLLHG
HHHHHCCCHHHHCCC		41.8125159151
346PhosphorylationLLHGNPGSTYLASNS
HCCCCCCCCEECCCC		18.3521945579
347PhosphorylationLHGNPGSTYLASNST
CCCCCCCCEECCCCC		28.5921945579
348PhosphorylationHGNPGSTYLASNSTS
CCCCCCCEECCCCCC		11.2821945579
351PhosphorylationPGSTYLASNSTSAPN
CCCCEECCCCCCCCC		28.8121945579
353PhosphorylationSTYLASNSTSAPNWK
CCEECCCCCCCCCCC		22.6523401153
354PhosphorylationTYLASNSTSAPNWKS
CEECCCCCCCCCCCC		32.9121945579
355PhosphorylationYLASNSTSAPNWKSL
EECCCCCCCCCCCCC		41.3621945579
360MethylationSTSAPNWKSLTSWTN
CCCCCCCCCCCCCCC		42.08115978407
360UbiquitinationSTSAPNWKSLTSWTN
CCCCCCCCCCCCCCC		42.0822505724
360 (in isoform 3)Ubiquitination-42.08-
361PhosphorylationTSAPNWKSLTSWTND
CCCCCCCCCCCCCCC		28.6125159151
363PhosphorylationAPNWKSLTSWTNDQG
CCCCCCCCCCCCCCC		29.3423684312
364PhosphorylationPNWKSLTSWTNDQGA
CCCCCCCCCCCCCCC		36.8828857561
366PhosphorylationWKSLTSWTNDQGARR
CCCCCCCCCCCCCCE		28.7826434776
374MethylationNDQGARRKTVFSPTL
CCCCCCEECCCCCCH		43.41115978411
374UbiquitinationNDQGARRKTVFSPTL
CCCCCCEECCCCCCH		43.4129967540
375PhosphorylationDQGARRKTVFSPTLP
CCCCCEECCCCCCHH		25.6030266825
378PhosphorylationARRKTVFSPTLPAAR
CCEECCCCCCHHHHH		16.7919664994
380PhosphorylationRKTVFSPTLPAARSS
EECCCCCCHHHHHHH		44.1430266825
385MethylationSPTLPAARSSLGSLQ
CCCHHHHHHHHCCCC		28.96115387343
386PhosphorylationPTLPAARSSLGSLQT
CCHHHHHHHHCCCCC		25.7822167270
387PhosphorylationTLPAARSSLGSLQTP
CHHHHHHHHCCCCCC		31.0622167270
390PhosphorylationAARSSLGSLQTPEAV
HHHHHHCCCCCCCCC		23.6925159151
393PhosphorylationSSLGSLQTPEAVTTR
HHHCCCCCCCCCCCC		28.5223927012
398PhosphorylationLQTPEAVTTRKGTGL
CCCCCCCCCCCCCCC		28.1223927012
399PhosphorylationQTPEAVTTRKGTGLL
CCCCCCCCCCCCCCC		24.6423927012
401UbiquitinationPEAVTTRKGTGLLSS
CCCCCCCCCCCCCCC		59.7533845483
403PhosphorylationAVTTRKGTGLLSSDY
CCCCCCCCCCCCCCE		27.9120873877
407PhosphorylationRKGTGLLSSDYRIIN
CCCCCCCCCCEEEEC		26.6325159151
408PhosphorylationKGTGLLSSDYRIING
CCCCCCCCCEEEECC		38.3325159151
410PhosphorylationTGLLSSDYRIINGKS
CCCCCCCEEEECCCC		12.9827273156
416UbiquitinationDYRIINGKSGTQDIQ
CEEEECCCCCCCCCC		41.0229967540
417PhosphorylationYRIINGKSGTQDIQP
EEEECCCCCCCCCCC		48.7725627689
419PhosphorylationIINGKSGTQDIQPGP
EECCCCCCCCCCCCC		30.1125627689
437PhosphorylationNNADGVATDITSTRS
CCCCCCEEECCCCCC		26.0620873877
440PhosphorylationDGVATDITSTRSLNY
CCCEEECCCCCCCCE		27.1927251275
441PhosphorylationGVATDITSTRSLNYK
CCEEECCCCCCCCEE		23.3527251275
442PhosphorylationVATDITSTRSLNYKS
CEEECCCCCCCCEEC		18.6727251275
444PhosphorylationTDITSTRSLNYKSTS
EECCCCCCCCEECCC		22.5124719451
447PhosphorylationTSTRSLNYKSTSSGH
CCCCCCCEECCCCCC		16.1729507054
448UbiquitinationSTRSLNYKSTSSGHR
CCCCCCEECCCCCCC		46.3029967540
449PhosphorylationTRSLNYKSTSSGHRE
CCCCCEECCCCCCCE		24.1427174698
450PhosphorylationRSLNYKSTSSGHREI
CCCCEECCCCCCCEE		23.8227174698
451PhosphorylationSLNYKSTSSGHREIS
CCCEECCCCCCCEEC		41.2225159151
452PhosphorylationLNYKSTSSGHREISS
CCEECCCCCCCEECC		38.4127174698
458PhosphorylationSSGHREISSPRIQDA
CCCCCEECCCCCCCC		29.5430576142
459PhosphorylationSGHREISSPRIQDAG
CCCCEECCCCCCCCC		24.6921815630
469PhosphorylationIQDAGPASRDVQATG
CCCCCCCCCCCCCCC		31.9521815630
492PhosphorylationRVALVNDSLSDVTST
CEEEECCCHHHCCCC		25.2729255136
494PhosphorylationALVNDSLSDVTSTTS
EEECCCHHHCCCCCC		33.7129255136
497PhosphorylationNDSLSDVTSTTSSRV
CCCHHHCCCCCCCCC		25.9130108239
498PhosphorylationDSLSDVTSTTSSRVD
CCHHHCCCCCCCCCC		29.5430108239
499PhosphorylationSLSDVTSTTSSRVDD
CHHHCCCCCCCCCCC		22.7230108239
500PhosphorylationLSDVTSTTSSRVDDH
HHHCCCCCCCCCCCC		25.1930108239
501PhosphorylationSDVTSTTSSRVDDHD
HHCCCCCCCCCCCCC		19.0830108239
502PhosphorylationDVTSTTSSRVDDHDS
HCCCCCCCCCCCCCC		33.9430108239
509PhosphorylationSRVDDHDSEEICLDH
CCCCCCCCCCHHHHH		33.4429214152
518 (in isoform 3)Phosphorylation-2.9829083192
519UbiquitinationICLDHLCKGCPLNGS
HHHHHHCCCCCCCCC		70.66-
519 (in isoform 3)Phosphorylation-70.6629083192
547PhosphorylationMLIGKTWTDFEHMET
HHHCCCCCCHHHHHH		35.72-
554PhosphorylationTDFEHMETIEKGYCN
CCHHHHHHHHCCCCC		27.1923186163
555 (in isoform 3)Phosphorylation-3.0829978859
556 (in isoform 3)Phosphorylation-48.0922199227
560 (in isoform 3)Phosphorylation-7.2622199227
561 (in isoform 3)Phosphorylation-29.3722199227
567 (in isoform 3)Phosphorylation-1.5929978859
568 (in isoform 3)Phosphorylation-35.5529978859
572 (in isoform 3)Phosphorylation-13.0025159151
577 (in isoform 3)Phosphorylation-20.8128450419
578 (in isoform 3)Phosphorylation-2.6428450419
579SulfoxidationYTINFRVMSCDSFPI
EEEEEEEEECCCCCE		2.6221406390
579 (in isoform 3)Phosphorylation-2.6228450419
580PhosphorylationTINFRVMSCDSFPIR
EEEEEEEECCCCCEE		16.3528348404
590PhosphorylationSFPIRRLSTPSSVTK
CCCEEECCCCCCCCC		36.1425635049
591PhosphorylationFPIRRLSTPSSVTKP
CCEEECCCCCCCCCC		31.6128857561
593PhosphorylationIRRLSTPSSVTKPAN
EEECCCCCCCCCCCC		37.2123186163
594PhosphorylationRRLSTPSSVTKPANS
EECCCCCCCCCCCCC		34.7023186163
596PhosphorylationLSTPSSVTKPANSVF
CCCCCCCCCCCCCCE		33.0023186163
597UbiquitinationSTPSSVTKPANSVFT
CCCCCCCCCCCCCEE		39.7229967540
597AcetylationSTPSSVTKPANSVFT
CCCCCCCCCCCCCEE		39.7226051181
601PhosphorylationSVTKPANSVFTTKWI
CCCCCCCCCEEEEEE		22.2523186163
604PhosphorylationKPANSVFTTKWIWYW
CCCCCCEEEEEEEEE		25.8823186163
605PhosphorylationPANSVFTTKWIWYWK
CCCCCEEEEEEEEEE		16.9623186163
607 (in isoform 3)Phosphorylation-5.5720860994
608 (in isoform 3)Phosphorylation-1.8420860994
610 (in isoform 3)Phosphorylation-9.4320860994
625UbiquitinationWIQYGEEKDKRKNSN
EEECCCHHCCCCCCC		65.3329967540
629UbiquitinationGEEKDKRKNSNVDSS
CCHHCCCCCCCCCHH		71.16-
629MalonylationGEEKDKRKNSNVDSS
CCHHCCCCCCCCCHH		71.1626320211
631PhosphorylationEKDKRKNSNVDSSYL
HHCCCCCCCCCHHHH		41.0625849741
635PhosphorylationRKNSNVDSSYLESLY
CCCCCCCHHHHHHHH		19.3228450419
636PhosphorylationKNSNVDSSYLESLYQ
CCCCCCHHHHHHHHH		29.3130576142
637PhosphorylationNSNVDSSYLESLYQS
CCCCCHHHHHHHHHH		20.5928450419
640PhosphorylationVDSSYLESLYQSCPR
CCHHHHHHHHHHCCC		29.7627080861
642PhosphorylationSSYLESLYQSCPRGV
HHHHHHHHHHCCCCC		13.9928450419
644PhosphorylationYLESLYQSCPRGVVP
HHHHHHHHCCCCCCC		16.7227732954
659PhosphorylationFQAGSRNYELSFQGM
CCCCCCCEEEEEHHH		19.6922210691
662PhosphorylationGSRNYELSFQGMIQT
CCCCEEEEEHHHHHH		12.0020068231
669O-linked_GlycosylationSFQGMIQTNIASKTQ
EEHHHHHHCCCCCCC		20.0523301498
669PhosphorylationSFQGMIQTNIASKTQ
EEHHHHHHCCCCCCC		20.0528258704
673PhosphorylationMIQTNIASKTQKDVI
HHHHCCCCCCCCHHH		32.2220068231
673O-linked_GlycosylationMIQTNIASKTQKDVI
HHHHCCCCCCCCHHH		32.2223301498
675PhosphorylationQTNIASKTQKDVIRR
HHCCCCCCCCHHHHC		38.0525311616
677UbiquitinationNIASKTQKDVIRRPT
CCCCCCCCHHHHCCC		60.2329967540
684PhosphorylationKDVIRRPTFVPQWYV
CHHHHCCCCCCHHHH		35.1424129246
690PhosphorylationPTFVPQWYVQQMKRG
CCCCCHHHHHHHHCC		5.3221945579
694SulfoxidationPQWYVQQMKRGPDHQ
CHHHHHHHHCCCCCC		1.4628183972
695UbiquitinationQWYVQQMKRGPDHQP
HHHHHHHHCCCCCCC		50.2829967540
695AcetylationQWYVQQMKRGPDHQP
HHHHHHHHCCCCCCC		50.2826051181
705PhosphorylationPDHQPAKTSSVSLTA
CCCCCCCCCEEEEEE		28.4828348404
706PhosphorylationDHQPAKTSSVSLTAT
CCCCCCCCEEEEEEE		28.2128348404
707PhosphorylationHQPAKTSSVSLTATF
CCCCCCCEEEEEEEE		22.4328348404
709PhosphorylationPAKTSSVSLTATFRP
CCCCCEEEEEEEECC		23.1928348404
711PhosphorylationKTSSVSLTATFRPQE
CCCEEEEEEEECCCC		19.0227251275
726UbiquitinationDFCFLSSKKYKLSEI
CEEEEECCCEEHHHH		57.6629967540
7262-HydroxyisobutyrylationDFCFLSSKKYKLSEI
CEEEEECCCEEHHHH		57.66-
729UbiquitinationFLSSKKYKLSEIHHL
EEECCCEEHHHHHHC		55.1829967540
729AcetylationFLSSKKYKLSEIHHL
EEECCCEEHHHHHHC		55.1825953088
740PhosphorylationIHHLHPEYVRVSEHF
HHHCCHHHHHHHHHH		9.67-
748UbiquitinationVRVSEHFKASMKNFK
HHHHHHHHHHHHCCC		41.2729967540
750PhosphorylationVSEHFKASMKNFKIE
HHHHHHHHHHCCCEE		30.7728258704
752UbiquitinationEHFKASMKNFKIEKI
HHHHHHHHCCCEEEE		57.6529967540
761UbiquitinationFKIEKIKKIENSELL
CCEEEEEECCCCHHH		59.7433845483
765PhosphorylationKIKKIENSELLDKFT
EEEECCCCHHHHHHC		19.4821406692
770UbiquitinationENSELLDKFTWKKSQ
CCCHHHHHHCCCHHH		44.6729967540
779UbiquitinationTWKKSQMKEEGKLLF
CCCHHHCCHHCEEEE		45.0023000965
783UbiquitinationSQMKEEGKLLFYATS
HHCCHHCEEEEEECH		45.3423000965
783 (in isoform 1)Ubiquitination-45.3421890473
813AcetylationLHETHENKYGKGIYF
HCHHHCCCCCCCEEE		53.0126051181
816UbiquitinationTHENKYGKGIYFAKD
HHCCCCCCCEEEECH		38.7629967540
822UbiquitinationGKGIYFAKDAIYSHK
CCCEEEECHHHHCCC		37.4829967540
826PhosphorylationYFAKDAIYSHKNCPY
EEECHHHHCCCCCCC		13.3728064214
827PhosphorylationFAKDAIYSHKNCPYD
EECHHHHCCCCCCCC		23.1328102081
829UbiquitinationKDAIYSHKNCPYDAK
CHHHHCCCCCCCCHH		55.0629967540
829AcetylationKDAIYSHKNCPYDAK
CHHHHCCCCCCCCHH		55.0625953088
872PhosphorylationDSCVDTRSNPSVFVI
CCCCCCCCCCCEEEE		56.0021712546
883UbiquitinationVFVIFQKDQVYPQYV
EEEEEECCCEECEEE		32.1833845483
901UbiquitinationTEDKACVIS------
CCCCEEEEC------		3.9923000965
905UbiquitinationACVIS----------
EEEEC----------		21890473
905 (in isoform 3)Ubiquitination-21890473
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
257SPhosphorylationKinaseGSK3-BETAP49841
Uniprot
263SPhosphorylationKinaseGSK3-BETAP49841
Uniprot
267SPhosphorylationKinaseGSK3-BETAP49841
Uniprot
271SPhosphorylationKinaseGSK3-BETAP49841
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
257SPhosphorylation

19690332
263SPhosphorylation

-
267SPhosphorylation

-
271SPhosphorylation

18669648
275SPhosphorylation

18669648
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 ZCCHV_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TRI25_HUMANTRIM25physical
28060952
TRI25_HUMANTRIM25physical
28202764
H13_HUMANHIST1H1Dphysical
28514442
H12_HUMANHIST1H1Cphysical
28514442
ZN777_HUMANZNF777physical
28514442
RRP8_HUMANRRP8physical
28514442
BAZ1B_HUMANBAZ1Bphysical
28514442
KHNYN_HUMANKHNYNphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
Z354A_HUMANZNF354Aphysical
28514442
NOG2_HUMANGNL2physical
28514442
NOP2_HUMANNOP2physical
28514442
DKC1_HUMANDKC1physical
28514442
RBM28_HUMANRBM28physical
28514442
LARP1_HUMANLARP1physical
28514442
RBM19_HUMANRBM19physical
28514442
RT09_HUMANMRPS9physical
28514442
RL17_HUMANRPL17physical
28514442
ZN574_HUMANZNF574physical
28514442
BRX1_HUMANBRIX1physical
28514442
YBOX1_HUMANYBX1physical
28514442
RL36_HUMANRPL36physical
28514442
DHX30_HUMANDHX30physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
RS15_HUMANRPS15physical
28514442
PRD15_HUMANPRDM15physical
28514442
GLYR1_HUMANGLYR1physical
28514442
YBOX3_HUMANYBX3physical
28514442
G45IP_HUMANGADD45GIP1physical
28514442
STAU2_HUMANSTAU2physical
28514442
NOP16_HUMANNOP16physical
28514442
HP1B3_HUMANHP1BP3physical
28514442
EBP2_HUMANEBNA1BP2physical
28514442
NMNA1_HUMANNMNAT1physical
28514442
KRR1_HUMANKRR1physical
28514442
NOG1_HUMANGTPBP4physical
28514442
RL12_HUMANRPL12physical
28514442
NGRN_HUMANNGRNphysical
28514442
DDX24_HUMANDDX24physical
28514442
PAPD5_HUMANPAPD5physical
28514442
RL32_HUMANRPL32physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
RT35_HUMANMRPS35physical
28514442
DDX27_HUMANDDX27physical
28514442
RS13_HUMANRPS13physical
28514442
LN28B_HUMANLIN28Bphysical
28514442
RL26_HUMANRPL26physical
28514442
MOV10_HUMANMOV10physical
28514442
RENT1_HUMANUPF1physical
28514442
DDX10_HUMANDDX10physical
28514442
NIP7_HUMANNIP7physical
28514442
RLA0_HUMANRPLP0physical
28514442
RT31_HUMANMRPS31physical
28514442
LLPH_HUMANLLPHphysical
28514442
MPP10_HUMANMPHOSPH10physical
28514442
NSD2_HUMANWHSC1physical
28514442
RS6_HUMANRPS6physical
28514442
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 ZCCHV_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-257; THR-273; SER-275; SER-378; SER-387;SER-390 AND THR-393, 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-257; SER-284; SER-335;SER-378; SER-387 AND THR-393, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-257; THR-273; SER-275; SER-378; SER-387;SER-390 AND THR-393, AND MASS 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-271; THR-273; SER-275;SER-284; SER-302; SER-378; SER-387 AND THR-393, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-284; SER-378;SER-387 AND THR-393, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-387 ANDTHR-393, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-378 ANDTHR-393, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-273; SER-275AND SER-284, AND MASS 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-378, AND MASSSPECTROMETRY.

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