Z3H7B_HUMAN - dbPTM
Z3H7B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Z3H7B_HUMAN
UniProt AC Q9UGR2
Protein Name Zinc finger CCCH domain-containing protein 7B
Gene Name ZC3H7B
Organism Homo sapiens (Human).
Sequence Length 993
Subcellular Localization Nucleus . Nuclear localization seems to be depleted upon rotavirus A infection.
Protein Description May be a specific regulator of miRNA biogenesis. Binds to microRNAs MIR7-1, MIR16-2 and MIR29A hairpins recognizing the 'ATA(A/T)' motif in the apical loop..
Protein Sequence MERQKRKADIEKGLQFIQSTLPLKQEEYEAFLLKLVQNLFAEGNDLFREKDYKQALVQYMEGLNVADYAASDQVALPRELLCKLHVNRAACYFTMGLYEKALEDSEKALGLDSESIRALFRKARALNELGRHKEAYECSSRCSLALPHDESVTQLGQELAQKLGLRVRKAYKRPQELETFSLLSNGTAAGVADQGTSNGLGSIDDIETGNVPDTREQVEIGAPRDCYVDPRGSPALLPSTPTMPLFPHVLDLLAPLDSSRTLPSTDSLDDFSDGDVFGPELDTLLDSLSLVQGGLSGSGVPSELPQLIPVFPGGTPLLPPVVGGSIPVSSPLPPASFGLVMDPSKKLAASVLDALDPPGPTLDPLDLLPYSETRLDALDSFGSTRGSLDKPDSFMEETNSQDHRPPSGAQKPAPSPEPCMPNTALLIKNPLAATHEFKQACQLCYPKTGPRAGDYTYREGLEHKCKRDILLGRLRSSEDQTWKRIRPRPTKTSFVGSYYLCKDMINKQDCKYGDNCTFAYHQEEIDVWTEERKGTLNRDLLFDPLGGVKRGSLTIAKLLKEHQGIFTFLCEICFDSKPRIISKGTKDSPSVCSNLAAKHSFYNNKCLVHIVRSTSLKYSKIRQFQEHFQFDVCRHEVRYGCLREDSCHFAHSFIELKVWLLQQYSGMTHEDIVQESKKYWQQMEAHAGKASSSMGAPRTHGPSTFDLQMKFVCGQCWRNGQVVEPDKDLKYCSAKARHCWTKERRVLLVMSKAKRKWVSVRPLPSIRNFPQQYDLCIHAQNGRKCQYVGNCSFAHSPEERDMWTFMKENKILDMQQTYDMWLKKHNPGKPGEGTPISSREGEKQIQMPTDYADIMMGYHCWLCGKNSNSKKQWQQHIQSEKHKEKVFTSDSDASGWAFRFPMGEFRLCDRLQKGKACPDGDKCRCAHGQEELNEWLDRREVLKQKLAKARKDMLLCPRDDDFGKYNFLLQEDGDLAGATPEAPAAAATATTGE
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
24UbiquitinationIQSTLPLKQEEYEAF
HHHCCCCCHHHHHHH		54.44-
53UbiquitinationLFREKDYKQALVQYM
HHCHHHHHHHHHHHH		38.95-
83UbiquitinationLPRELLCKLHVNRAA
CCHHHHHHHHHHHHH		41.41-
107UbiquitinationKALEDSEKALGLDSE
HHHHHHHHHHCCCHH		53.52-
133UbiquitinationLNELGRHKEAYECSS
HHHHHCCHHHHHHHC		42.55-
172AcetylationLRVRKAYKRPQELET
HHHHHHHCCHHHHHH		63.5626051181
217PhosphorylationNVPDTREQVEIGAPR
CCCCCHHHCCCCCCC		34.5520068231
217 (in isoform 2)Phosphorylation-34.5525849741
223PhosphorylationEQVEIGAPRDCYVDP
HHCCCCCCCCEEECC		27.6820068231
223 (in isoform 2)Phosphorylation-27.6824719451
224PhosphorylationQVEIGAPRDCYVDPR
HCCCCCCCCEEECCC		46.2020068231
224 (in isoform 2)Phosphorylation-46.2027251275
226PhosphorylationEIGAPRDCYVDPRGS
CCCCCCCEEECCCCC		3.6320068231
226 (in isoform 2)Phosphorylation-3.63-
233PhosphorylationCYVDPRGSPALLPST
EEECCCCCCCCCCCC		14.3122167270
239PhosphorylationGSPALLPSTPTMPLF
CCCCCCCCCCCCCCC		47.1630278072
240PhosphorylationSPALLPSTPTMPLFP
CCCCCCCCCCCCCCH		22.3430278072
242PhosphorylationALLPSTPTMPLFPHV
CCCCCCCCCCCCHHH		31.3530278072
258PhosphorylationDLLAPLDSSRTLPST
HHHHCCCCCCCCCCC		29.4220068231
259PhosphorylationLLAPLDSSRTLPSTD
HHHCCCCCCCCCCCC		29.0220068231
261PhosphorylationAPLDSSRTLPSTDSL
HCCCCCCCCCCCCCC		44.9924275569
330UbiquitinationGGSIPVSSPLPPASF
CCCCCCCCCCCHHHH		30.59-
364PhosphorylationPPGPTLDPLDLLPYS
CCCCCCCHHHCCCCC		30.7723186163
364 (in isoform 2)Phosphorylation-30.7727251275
367PhosphorylationPTLDPLDLLPYSETR
CCCCHHHCCCCCCHH		7.3623186163
367 (in isoform 2)Phosphorylation-7.3627251275
371PhosphorylationPLDLLPYSETRLDAL
HHHCCCCCCHHHHHH		30.47-
380PhosphorylationTRLDALDSFGSTRGS
HHHHHHHHCCCCCCC		32.1521712546
383PhosphorylationDALDSFGSTRGSLDK
HHHHHCCCCCCCCCC		16.9621712546
384PhosphorylationALDSFGSTRGSLDKP
HHHHCCCCCCCCCCC		39.1521815630
387PhosphorylationSFGSTRGSLDKPDSF
HCCCCCCCCCCCCHH		30.0626422651
393PhosphorylationGSLDKPDSFMEETNS
CCCCCCCHHHHHHCC		34.7129449344
398PhosphorylationPDSFMEETNSQDHRP
CCHHHHHHCCCCCCC		27.1923927012
399 (in isoform 2)Phosphorylation-40.7427251275
399PhosphorylationDSFMEETNSQDHRPP
CHHHHHHCCCCCCCC		40.7419413330
400PhosphorylationSFMEETNSQDHRPPS
HHHHHHCCCCCCCCC		44.3923927012
407PhosphorylationSQDHRPPSGAQKPAP
CCCCCCCCCCCCCCC		49.8223927012
415PhosphorylationGAQKPAPSPEPCMPN
CCCCCCCCCCCCCCC		43.9629255136
422UbiquitinationSPEPCMPNTALLIKN
CCCCCCCCCEEEECC		15.88-
423PhosphorylationPEPCMPNTALLIKNP
CCCCCCCCEEEECCC		16.8926074081
431UbiquitinationALLIKNPLAATHEFK
EEEECCCHHHCHHHH		7.67-
438AcetylationLAATHEFKQACQLCY
HHHCHHHHHHHHHHC		33.7226051181
445PhosphorylationKQACQLCYPKTGPRA
HHHHHHHCCCCCCCC		19.16-
448UbiquitinationCQLCYPKTGPRAGDY
HHHHCCCCCCCCCCC		48.16-
455PhosphorylationTGPRAGDYTYREGLE
CCCCCCCCCHHHCCC		12.54-
457PhosphorylationPRAGDYTYREGLEHK
CCCCCCCHHHCCCHH		10.63-
461 (in isoform 2)Phosphorylation-5.5127251275
476PhosphorylationILLGRLRSSEDQTWK
HHHHCCCCCCCCCCH		42.5427251275
477PhosphorylationLLGRLRSSEDQTWKR
HHHCCCCCCCCCCHH		38.4627251275
481PhosphorylationLRSSEDQTWKRIRPR
CCCCCCCCCHHCCCC		45.3224505115
492PhosphorylationIRPRPTKTSFVGSYY
CCCCCCCCCCCCHHH		29.85-
493PhosphorylationRPRPTKTSFVGSYYL
CCCCCCCCCCCHHHC		21.3528555341
533UbiquitinationDVWTEERKGTLNRDL
CCCCHHHCCCCCCHH		60.57-
536PhosphorylationTEERKGTLNRDLLFD
CHHHCCCCCCHHCCC		7.25-
549UbiquitinationFDPLGGVKRGSLTIA
CCCCCCCCCCCCHHH		55.08-
552PhosphorylationLGGVKRGSLTIAKLL
CCCCCCCCCHHHHHH		26.7730266825
554PhosphorylationGVKRGSLTIAKLLKE
CCCCCCCHHHHHHHH		22.1530108239
572PhosphorylationIFTFLCEICFDSKPR
CEEHHHHHHCCCCCC		2.50-
582UbiquitinationDSKPRIISKGTKDSP
CCCCCEEECCCCCCH		23.74-
588PhosphorylationISKGTKDSPSVCSNL
EECCCCCCHHHHHHH		22.1925159151
589UbiquitinationSKGTKDSPSVCSNLA
ECCCCCCHHHHHHHH		40.70-
648PhosphorylationCLREDSCHFAHSFIE
HCCCCCCHHHHHHHH		27.2115592455
648 (in isoform 2)Phosphorylation-27.21-
661UbiquitinationIELKVWLLQQYSGMT
HHHHHHHHHHCCCCC		1.42-
662UbiquitinationELKVWLLQQYSGMTH
HHHHHHHHHCCCCCH		37.69-
664PhosphorylationKVWLLQQYSGMTHED
HHHHHHHCCCCCHHH		8.3328152594
665PhosphorylationVWLLQQYSGMTHEDI
HHHHHHCCCCCHHHH		20.1128442448
668PhosphorylationLQQYSGMTHEDIVQE
HHHCCCCCHHHHHHH		26.1628152594
673UbiquitinationGMTHEDIVQESKKYW
CCCHHHHHHHHHHHH		8.81-
679PhosphorylationIVQESKKYWQQMEAH
HHHHHHHHHHHHHHH		16.5230576142
691PhosphorylationEAHAGKASSSMGAPR
HHHCCCCCCCCCCCC		26.82-
693PhosphorylationHAGKASSSMGAPRTH
HCCCCCCCCCCCCCC		20.8130576142
694UbiquitinationAGKASSSMGAPRTHG
CCCCCCCCCCCCCCC		5.99-
711UbiquitinationTFDLQMKFVCGQCWR
CHHHEEEEECCCCHH		4.63-
714UbiquitinationLQMKFVCGQCWRNGQ
HEEEEECCCCHHCCE		22.00-
719UbiquitinationVCGQCWRNGQVVEPD
ECCCCHHCCEEECCC		22.28-
727AcetylationGQVVEPDKDLKYCSA
CEEECCCCCCCCCCC		75.5625953088
730AcetylationVEPDKDLKYCSAKAR
ECCCCCCCCCCCHHH		55.1126051181
742AcetylationKARHCWTKERRVLLV
HHHHCCCHHHHHEEE		25.4026051181
751PhosphorylationRRVLLVMSKAKRKWV
HHHEEECCCCCCCCE		23.21-
765PhosphorylationVSVRPLPSIRNFPQQ
EECEECCCCCCCCCH		41.6924719451
768UbiquitinationRPLPSIRNFPQQYDL
EECCCCCCCCCHHCE		51.81-
784UbiquitinationIHAQNGRKCQYVGNC
EEECCCCCCEEEECC		27.39-
791UbiquitinationKCQYVGNCSFAHSPE
CCEEEECCCCCCCHH		2.66-
807UbiquitinationRDMWTFMKENKILDM
HCHHHHHHHCCCCCH		54.68-
808UbiquitinationDMWTFMKENKILDMQ
CHHHHHHHCCCCCHH		52.55-
813UbiquitinationMKENKILDMQQTYDM
HHHCCCCCHHHHHHH		36.00-
818PhosphorylationILDMQQTYDMWLKKH
CCCHHHHHHHHHHHH		10.24-
829UbiquitinationLKKHNPGKPGEGTPI
HHHHCCCCCCCCCCC		51.62-
834PhosphorylationPGKPGEGTPISSREG
CCCCCCCCCCCCCCC		17.1025159151
837PhosphorylationPGEGTPISSREGEKQ
CCCCCCCCCCCCCCE		25.2530576142
855UbiquitinationPTDYADIMMGYHCWL
CCCHHHHHHHHEEHH		1.43-
865UbiquitinationYHCWLCGKNSNSKKQ
HEEHHCCCCCCCHHH		57.09-
869UbiquitinationLCGKNSNSKKQWQQH
HCCCCCCCHHHHHHH		40.84-
935UbiquitinationGQEELNEWLDRREVL
CHHHHHHHHHHHHHH		11.50-
948UbiquitinationVLKQKLAKARKDMLL
HHHHHHHHHHHHCEE		60.19-
979PhosphorylationDGDLAGATPEAPAAA
CCCCCCCCCCCCCHH		22.2728348404
988PhosphorylationEAPAAAATATTGE--
CCCCHHCCCCCCC--		21.5828348404
990PhosphorylationPAAAATATTGE----
CCHHCCCCCCC----		30.8628348404
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 Z3H7B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Z3H7B_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 Z3H7B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZYX_HUMANZYXphysical
22939629
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 Z3H7B_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-233, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, 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-664, AND MASSSPECTROMETRY.

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