ZCHC8_HUMAN - dbPTM
ZCHC8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZCHC8_HUMAN
UniProt AC Q6NZY4
Protein Name Zinc finger CCHC domain-containing protein 8
Gene Name ZCCHC8
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Nucleus, nucleoplasm . Nucleus . Excluded from nucleolus.
Protein Description Scaffolding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that directs a subset of non-coding short-lived RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters. [PubMed: 27871484 May be involved in pre-mRNA splicing (Probable]
Protein Sequence MAAEVYFGDLELFEPFDHPEESIPKPVHTRFKDDDGDEEDENGVGDAELRERLRQCEETIEQLRAENQELKRKLNILTRPSGILVNDTKLDGPILQILFMNNAISKQYHQEIEEFVSNLVKRFEEQQKNDVEKTSFNLLPQPSSIVLEEDHKVEESCAIKNNKEAFSVVGSVLYFTNFCLDKLGQPLLNENPQLSEGWEIPKYHQVFSHIVSLEGQEIQVKAKRPKPHCFNCGSEEHQMKDCPMPRNAARISEKRKEYMDACGEANNQNFQQRYHAEEVEERFGRFKPGVISEELQDALGVTDKSLPPFIYRMRQLGYPPGWLKEAELENSGLALYDGKDGTDGETEVGEIQQNKSVTYDLSKLVNYPGFNISTPRGIPDEWRIFGSIPMQACQQKDVFANYLTSNFQAPGVKSGNKRSSSHSSPGSPKKQKNESNSAGSPADMELDSDMEVPHGSQSSESFQFQPPLPPDTPPLPRGTPPPVFTPPLPKGTPPLTPSDSPQTRTASGAVDEDALTLEELEEQQRRIWAALEQAESVNSDSDVPVDTPLTGNSVASSPCPNELDLPVPEGKTSEKQTLDEPEVPEIFTKKSEAGHASSPDSEVTSLCQKEKAELAPVNTEGALLDNGSVVPNCDISNGGSQKLFPADTSPSTATKIHSPIPDMSKFATGITPFEFENMAESTGMYLRIRSLLKNSPRNQQKNKKASE
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------MAAEVYFGD
------CCCEEEECC		16.6019413330
6Phosphorylation--MAAEVYFGDLELF
--CCCEEEECCCCCC		8.0527642862
32AcetylationKPVHTRFKDDDGDEE
CCCCCCCCCCCCCCC		57.8926051181
32UbiquitinationKPVHTRFKDDDGDEE
CCCCCCCCCCCCCCC		57.8929967540
73UbiquitinationENQELKRKLNILTRP
HHHHHHHHHCHHHCC		44.28-
81PhosphorylationLNILTRPSGILVNDT
HCHHHCCCCEEECCC		34.8620068231
88PhosphorylationSGILVNDTKLDGPIL
CCEEECCCCCCCHHH		28.4420068231
125 (in isoform 2)Ubiquitination-56.4521890473
128UbiquitinationKRFEEQQKNDVEKTS
HHHHHHHCCCCHHCC		55.60-
133UbiquitinationQQKNDVEKTSFNLLP
HHCCCCHHCCCCCCC		49.6829967540
157UbiquitinationDHKVEESCAIKNNKE
CCCCCHHHEECCCHH		5.2624816145
165UbiquitinationAIKNNKEAFSVVGSV
EECCCHHHHHHHHHH		12.0124816145
179UbiquitinationVLYFTNFCLDKLGQP
HHHHHHHHHHHHCCC		5.3624816145
241PhosphorylationSEEHQMKDCPMPRNA
CCCCCCCCCCCCCHH		36.0932142685
247PhosphorylationKDCPMPRNAARISEK
CCCCCCCHHHHHHHH		31.8932142685
252PhosphorylationPRNAARISEKRKEYM
CCHHHHHHHHHHHHH		31.3520068231
256UbiquitinationARISEKRKEYMDACG
HHHHHHHHHHHHHHH		65.3524816145
264UbiquitinationEYMDACGEANNQNFQ
HHHHHHHHHHHHHHH		48.3721890473
272UbiquitinationANNQNFQQRYHAEEV
HHHHHHHHHHCHHHH		43.7021890473
286UbiquitinationVEERFGRFKPGVISE
HHHHHCCCCCCCCCH		13.1721890473
287UbiquitinationEERFGRFKPGVISEE
HHHHCCCCCCCCCHH		39.2329967540
305PhosphorylationALGVTDKSLPPFIYR
HHCCCCCCCCHHHHH		49.2528555341
331PhosphorylationKEAELENSGLALYDG
CHHHHCCCCEEEECC		26.3021815630
336PhosphorylationENSGLALYDGKDGTD
CCCCEEEECCCCCCC		19.6228450419
342PhosphorylationLYDGKDGTDGETEVG
EECCCCCCCCCCCCC		51.4725159151
346PhosphorylationKDGTDGETEVGEIQQ
CCCCCCCCCCCHHCC		41.3128450419
355UbiquitinationVGEIQQNKSVTYDLS
CCHHCCCCEEEEEHH		41.8029967540
356PhosphorylationGEIQQNKSVTYDLSK
CHHCCCCEEEEEHHH		27.5225159151
358PhosphorylationIQQNKSVTYDLSKLV
HCCCCEEEEEHHHHH		20.5729083192
359PhosphorylationQQNKSVTYDLSKLVN
CCCCEEEEEHHHHHC		16.8432142685
360PhosphorylationQNKSVTYDLSKLVNY
CCCEEEEEHHHHHCC		34.7932142685
362PhosphorylationKSVTYDLSKLVNYPG
CEEEEEHHHHHCCCC		22.5029083192
363UbiquitinationSVTYDLSKLVNYPGF
EEEEEHHHHHCCCCC		64.8522817900
363 (in isoform 1)Ubiquitination-64.8521890473
367PhosphorylationDLSKLVNYPGFNIST
EHHHHHCCCCCCCCC		9.3920068231
373PhosphorylationNYPGFNISTPRGIPD
CCCCCCCCCCCCCCC		33.2029978859
374PhosphorylationYPGFNISTPRGIPDE
CCCCCCCCCCCCCCC		17.1329978859
380PhosphorylationSTPRGIPDEWRIFGS
CCCCCCCCCCEEECC		67.1932142685
386PhosphorylationPDEWRIFGSIPMQAC
CCCCEEECCCCCHHH		23.4632142685
402PhosphorylationQKDVFANYLTSNFQA
CHHHHHHHHCCCCCC		14.1332142685
408PhosphorylationNYLTSNFQAPGVKSG
HHHCCCCCCCCCCCC		51.3932142685
411PhosphorylationTSNFQAPGVKSGNKR
CCCCCCCCCCCCCCC		42.3632645325
413SumoylationNFQAPGVKSGNKRSS
CCCCCCCCCCCCCCC		59.5728112733
414PhosphorylationFQAPGVKSGNKRSSS
CCCCCCCCCCCCCCC		45.2321712546
419PhosphorylationVKSGNKRSSSHSSPG
CCCCCCCCCCCCCCC		37.4928176443
419O-linked_GlycosylationVKSGNKRSSSHSSPG
CCCCCCCCCCCCCCC		37.4923301498
420PhosphorylationKSGNKRSSSHSSPGS
CCCCCCCCCCCCCCC		35.7818669648
421PhosphorylationSGNKRSSSHSSPGSP
CCCCCCCCCCCCCCC		28.7428176443
423PhosphorylationNKRSSSHSSPGSPKK
CCCCCCCCCCCCCCC		39.9325849741
424PhosphorylationKRSSSHSSPGSPKKQ
CCCCCCCCCCCCCCC		28.0528176443
427PhosphorylationSSHSSPGSPKKQKNE
CCCCCCCCCCCCCCC		36.6128176443
435PhosphorylationPKKQKNESNSAGSPA
CCCCCCCCCCCCCCC		45.5428348404
437PhosphorylationKQKNESNSAGSPADM
CCCCCCCCCCCCCCC		43.2028348404
440PhosphorylationNESNSAGSPADMELD
CCCCCCCCCCCCCCC		19.3428348404
472PhosphorylationQPPLPPDTPPLPRGT
CCCCCCCCCCCCCCC		32.3626074081
479PhosphorylationTPPLPRGTPPPVFTP
CCCCCCCCCCCCCCC		33.6229255136
485PhosphorylationGTPPPVFTPPLPKGT
CCCCCCCCCCCCCCC		25.0022167270
492PhosphorylationTPPLPKGTPPLTPSD
CCCCCCCCCCCCCCC		28.0523401153
496PhosphorylationPKGTPPLTPSDSPQT
CCCCCCCCCCCCCCC		26.9030266825
498PhosphorylationGTPPLTPSDSPQTRT
CCCCCCCCCCCCCCC		45.5530266825
499PhosphorylationTPPLTPSDSPQTRTA
CCCCCCCCCCCCCCC		66.5932142685
500PhosphorylationPPLTPSDSPQTRTAS
CCCCCCCCCCCCCCC		24.2029255136
503PhosphorylationTPSDSPQTRTASGAV
CCCCCCCCCCCCCCC		33.1130266825
507PhosphorylationSPQTRTASGAVDEDA
CCCCCCCCCCCCCCC		27.0323186163
520PhosphorylationDALTLEELEEQQRRI
CCCCHHHHHHHHHHH		6.8332142685
521PhosphorylationALTLEELEEQQRRIW
CCCHHHHHHHHHHHH		57.9732142685
536PhosphorylationAALEQAESVNSDSDV
HHHHHHHHCCCCCCC		29.6128348404
539PhosphorylationEQAESVNSDSDVPVD
HHHHHCCCCCCCCCC		36.0128348404
541PhosphorylationAESVNSDSDVPVDTP
HHHCCCCCCCCCCCC		40.0928348404
550PhosphorylationVPVDTPLTGNSVASS
CCCCCCCCCCCCCCC		35.2032645325
553PhosphorylationDTPLTGNSVASSPCP
CCCCCCCCCCCCCCC		22.0228348404
556PhosphorylationLTGNSVASSPCPNEL
CCCCCCCCCCCCCCC		32.4326657352
557PhosphorylationTGNSVASSPCPNELD
CCCCCCCCCCCCCCC		22.3026657352
572PhosphorylationLPVPEGKTSEKQTLD
CCCCCCCCCCCCCCC		53.6423186163
573PhosphorylationPVPEGKTSEKQTLDE
CCCCCCCCCCCCCCC		46.4023186163
577PhosphorylationGKTSEKQTLDEPEVP
CCCCCCCCCCCCCCC		47.4422817901
588PhosphorylationPEVPEIFTKKSEAGH
CCCCCHHCCCCCCCC		43.1320068231
589UbiquitinationEVPEIFTKKSEAGHA
CCCCHHCCCCCCCCC		43.4829967540
591PhosphorylationPEIFTKKSEAGHASS
CCHHCCCCCCCCCCC		33.9523401153
597PhosphorylationKSEAGHASSPDSEVT
CCCCCCCCCCCHHHH		36.4122167270
598PhosphorylationSEAGHASSPDSEVTS
CCCCCCCCCCHHHHH		33.2522167270
601PhosphorylationGHASSPDSEVTSLCQ
CCCCCCCHHHHHHHH		37.0330266825
604PhosphorylationSSPDSEVTSLCQKEK
CCCCHHHHHHHHHHC		16.3623927012
605PhosphorylationSPDSEVTSLCQKEKA
CCCHHHHHHHHHHCC		32.1223927012
636PhosphorylationVVPNCDISNGGSQKL
CCCCCCCCCCCCCCC		19.03-
640PhosphorylationCDISNGGSQKLFPAD
CCCCCCCCCCCEECC		26.0717525332
648PhosphorylationQKLFPADTSPSTATK
CCCEECCCCCCCCCC		44.6430266825
649PhosphorylationKLFPADTSPSTATKI
CCEECCCCCCCCCCC		19.8719664994
651PhosphorylationFPADTSPSTATKIHS
EECCCCCCCCCCCCC		30.3730266825
652PhosphorylationPADTSPSTATKIHSP
ECCCCCCCCCCCCCC		41.5523401153
654PhosphorylationDTSPSTATKIHSPIP
CCCCCCCCCCCCCCC		30.5330266825
658PhosphorylationSTATKIHSPIPDMSK
CCCCCCCCCCCCHHH		28.1829255136
664PhosphorylationHSPIPDMSKFATGIT
CCCCCCHHHHCCCCC		31.8123403867
668PhosphorylationPDMSKFATGITPFEF
CCHHHHCCCCCCCCC		32.0527732954
671PhosphorylationSKFATGITPFEFENM
HHHCCCCCCCCCCCH		24.2227732954
681PhosphorylationEFENMAESTGMYLRI
CCCCHHHHHCHHHHH		22.2627732954
682PhosphorylationFENMAESTGMYLRIR
CCCHHHHHCHHHHHH		19.9227732954
685PhosphorylationMAESTGMYLRIRSLL
HHHHHCHHHHHHHHH		8.3227732954
690PhosphorylationGMYLRIRSLLKNSPR
CHHHHHHHHHHCCHH		35.3621712546
695PhosphorylationIRSLLKNSPRNQQKN
HHHHHHCCHHHHHHH		24.5326055452
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
492TPhosphorylationKinaseGSK3-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
492TPhosphorylation

16263084
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 ZCHC8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
17525332
SK2L2_HUMANSKIV2L2physical
16263084
RBM7_HUMANRBM7physical
16263084
A4_HUMANAPPphysical
21832049
SHIP2_HUMANINPPL1physical
26344197
RBM7_HUMANRBM7physical
26344197
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 ZCHC8_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 THR-479; SER-597; SER-598 AND SER-649, AND MASSSPECTROMETRY.
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 THR-479; SER-649 ANDSER-658, 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 THR-479; SER-597; SER-598 AND SER-649, 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 THR-479; THR-485; SER-598AND SER-658, AND MASS SPECTROMETRY.
"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-640, AND MASSSPECTROMETRY.
"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 THR-479; THR-485; THR-492;THR-496 AND SER-500, AND MASS SPECTROMETRY.
"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 THR-485, AND MASSSPECTROMETRY.
"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 THR-479, AND MASSSPECTROMETRY.

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