ZHX3_HUMAN - dbPTM
ZHX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZHX3_HUMAN
UniProt AC Q9H4I2
Protein Name Zinc fingers and homeoboxes protein 3
Gene Name ZHX3
Organism Homo sapiens (Human).
Sequence Length 956
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA..
Protein Sequence MASKRKSTTPCMIPVKTVVLQDASMEAQPAETLPEGPQQDLPPEASAASSEAAQNPSSTDGSTLANGHRSTLDGYLYSCKYCDFRSHDMTQFVGHMNSEHTDFNKDPTFVCSGCSFLAKTPEGLSLHNATCHSGEASFVWNVAKPDNHVVVEQSIPESTSTPDLAGEPSAEGADGQAEIIITKTPIMKIMKGKAEAKKIHTLKENVPSQPVGEALPKLSTGEMEVREGDHSFINGAVPVSQASASSAKNPHAANGPLIGTVPVLPAGIAQFLSLQQQPPVHAQHHVHQPLPTAKALPKVMIPLSSIPTYNAAMDSNSFLKNSFHKFPYPTKAELCYLTVVTKYPEEQLKIWFTAQRLKQGISWSPEEIEDARKKMFNTVIQSVPQPTITVLNTPLVASAGNVQHLIQAALPGHVVGQPEGTGGGLLVTQPLMANGLQATSSPLPLTVTSVPKQPGVAPINTVCSNTTSAVKVVNAAQSLLTACPSITSQAFLDASIYKNKKSHEQLSALKGSFCRNQFPGQSEVEHLTKVTGLSTREVRKWFSDRRYHCRNLKGSRAMIPGDHSSIIIDSVPEVSFSPSSKVPEVTCIPTTATLATHPSAKRQSWHQTPDFTPTKYKERAPEQLRALESSFAQNPLPLDEELDRLRSETKMTRREIDSWFSERRKKVNAEETKKAEENASQEEEEAAEDEGGEEDLASELRVSGENGSLEMPSSHILAERKVSPIKINLKNLRVTEANGRNEIPGLGACDPEDDESNKLAEQLPGKVSCKKTAQQRHLLRQLFVQTQWPSNQDYDSIMAQTGLPRPEVVRWFGDSRYALKNGQLKWYEDYKRGNFPPGLLVIAPGNRELLQDYYMTHKMLYEEDLQNLCDKTQMSSQQVKQWFAEKMGEETRAVADTGSEDQGPGTGELTAVHKGMGDTYSEVSENSESWEPRVPEASSEPFDTSSPQAGRQLETD
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
7Phosphorylation-MASKRKSTTPCMIP
-CCCCCCCCCCCCCE		41.3625159151
8PhosphorylationMASKRKSTTPCMIPV
CCCCCCCCCCCCCEE		37.4825159151
9PhosphorylationASKRKSTTPCMIPVK
CCCCCCCCCCCCEEE		22.9128555341
75PhosphorylationHRSTLDGYLYSCKYC
CCCCCCCCEEECCCC		11.35-
98PhosphorylationQFVGHMNSEHTDFNK
HHHCCCCCCCCCCCC		24.1524719451
101PhosphorylationGHMNSEHTDFNKDPT
CCCCCCCCCCCCCCC		37.9324719451
115PhosphorylationTFVCSGCSFLAKTPE
CEEECCCHHEECCCC		27.1624719451
193AcetylationIMKIMKGKAEAKKIH
HHHHHCCCHHHHHHH		37.2269535
219O-linked_GlycosylationGEALPKLSTGEMEVR
HHCCCCCCCCCEEEE		40.2630059200
231O-linked_GlycosylationEVREGDHSFINGAVP
EEEECCCCEECCEEE		32.3430059200
240O-linked_GlycosylationINGAVPVSQASASSA
ECCEEEHHHHCHHHC		17.6030059200
292PhosphorylationHVHQPLPTAKALPKV
CCCCCCCCCCCCCCE		48.7724719451
309PhosphorylationPLSSIPTYNAAMDSN
EHHHCCCCCCCCCCC		9.4630576142
315PhosphorylationTYNAAMDSNSFLKNS
CCCCCCCCCCHHHHC		22.6830576142
317PhosphorylationNAAMDSNSFLKNSFH
CCCCCCCCHHHHCCC		35.5924719451
501UbiquitinationASIYKNKKSHEQLSA
HHHHCCCCCHHHHHH		67.4529967540
507PhosphorylationKKSHEQLSALKGSFC
CCCHHHHHHHCCCHH		31.1126074081
510MethylationHEQLSALKGSFCRNQ
HHHHHHHCCCHHCCC		52.83115978309
510UbiquitinationHEQLSALKGSFCRNQ
HHHHHHHCCCHHCCC		52.8329967540
512PhosphorylationQLSALKGSFCRNQFP
HHHHHCCCHHCCCCC		21.4226074081
555PhosphorylationHCRNLKGSRAMIPGD
EECCCCCCCCCCCCC		18.4520068231
564PhosphorylationAMIPGDHSSIIIDSV
CCCCCCCCCEEEECC		28.1524719451
565PhosphorylationMIPGDHSSIIIDSVP
CCCCCCCCEEEECCC		17.8724719451
570PhosphorylationHSSIIIDSVPEVSFS
CCCEEEECCCEEEEC		29.2120068231
575PhosphorylationIDSVPEVSFSPSSKV
EECCCEEEECCCCCC		20.5329255136
577PhosphorylationSVPEVSFSPSSKVPE
CCCEEEECCCCCCCC		19.1629255136
579PhosphorylationPEVSFSPSSKVPEVT
CEEEECCCCCCCCEE		41.4126074081
580PhosphorylationEVSFSPSSKVPEVTC
EEEECCCCCCCCEEE		40.8529255136
586PhosphorylationSSKVPEVTCIPTTAT
CCCCCCEEECCCCCH		11.7626074081
590O-linked_GlycosylationPEVTCIPTTATLATH
CCEEECCCCCHHCCC		14.7830059200
590PhosphorylationPEVTCIPTTATLATH
CCEEECCCCCHHCCC		14.7820068231
591PhosphorylationEVTCIPTTATLATHP
CEEECCCCCHHCCCC		16.5820068231
591O-linked_GlycosylationEVTCIPTTATLATHP
CEEECCCCCHHCCCC		16.5830059200
593PhosphorylationTCIPTTATLATHPSA
EECCCCCHHCCCCCH		18.1626074081
596PhosphorylationPTTATLATHPSAKRQ
CCCCHHCCCCCHHCC		37.1220068231
599PhosphorylationATLATHPSAKRQSWH
CHHCCCCCHHCCCCC		38.5325159151
601AcetylationLATHPSAKRQSWHQT
HCCCCCHHCCCCCCC		56.1425953088
604PhosphorylationHPSAKRQSWHQTPDF
CCCHHCCCCCCCCCC		30.4725159151
608PhosphorylationKRQSWHQTPDFTPTK
HCCCCCCCCCCCCCH		16.3720068231
612PhosphorylationWHQTPDFTPTKYKER
CCCCCCCCCCHHHHH		37.1125159151
614PhosphorylationQTPDFTPTKYKERAP
CCCCCCCCHHHHHCH		43.9021712546
647PhosphorylationEELDRLRSETKMTRR
HHHHHHHHHHHHHHH		54.9628555341
649PhosphorylationLDRLRSETKMTRREI
HHHHHHHHHHHHHHH		27.6225627689
658PhosphorylationMTRREIDSWFSERRK
HHHHHHHHHHHHHHH		35.3628509920
661PhosphorylationREIDSWFSERRKKVN
HHHHHHHHHHHHHCC		24.7621815630
680PhosphorylationKKAEENASQEEEEAA
HHHHHHHHHHHHHHH		50.1029255136
703PhosphorylationLASELRVSGENGSLE
HHHCEEECCCCCCEE		33.6826503514
708PhosphorylationRVSGENGSLEMPSSH
EECCCCCCEECCCHH		32.5125850435
713PhosphorylationNGSLEMPSSHILAER
CCCEECCCHHHHEEC		32.9825850435
714PhosphorylationGSLEMPSSHILAERK
CCEECCCHHHHEECC		14.5326503514
723PhosphorylationILAERKVSPIKINLK
HHEECCCCCCEEEEE		24.7623927012
730UbiquitinationSPIKINLKNLRVTEA
CCCEEEEECCEEEEC		49.8229967540
735O-linked_GlycosylationNLKNLRVTEANGRNE
EEECCEEEECCCCCC		23.9730059200
768PhosphorylationEQLPGKVSCKKTAQQ
HHCCCCCCCHHHHHH		24.5725159151
790PhosphorylationFVQTQWPSNQDYDSI
HHHCCCCCCCCHHHH		44.1322210691
794PhosphorylationQWPSNQDYDSIMAQT
CCCCCCCHHHHHHHH		11.2222210691
796PhosphorylationPSNQDYDSIMAQTGL
CCCCCHHHHHHHHCC		14.1822210691
817PhosphorylationRWFGDSRYALKNGQL
HEECCCCHHHHCCCC		21.90-
872 (in isoform 2)Phosphorylation-19.0927174698
875 (in isoform 2)Phosphorylation-18.3827174698
876 (in isoform 2)Phosphorylation-21.2027174698
881 (in isoform 2)Phosphorylation-41.4827174698
897PhosphorylationETRAVADTGSEDQGP
HHEEEECCCCCCCCC		32.6326699800
899PhosphorylationRAVADTGSEDQGPGT
EEEECCCCCCCCCCC		39.8430266825
919PhosphorylationVHKGMGDTYSEVSEN
EECCCCCCHHHHCCC		24.1829978859
920PhosphorylationHKGMGDTYSEVSENS
ECCCCCCHHHHCCCC		13.9429978859
921PhosphorylationKGMGDTYSEVSENSE
CCCCCCHHHHCCCCC		33.3527732954
924PhosphorylationGDTYSEVSENSESWE
CCCHHHHCCCCCCCC		27.3230108239
927PhosphorylationYSEVSENSESWEPRV
HHHHCCCCCCCCCCC		29.0230108239
929PhosphorylationEVSENSESWEPRVPE
HHCCCCCCCCCCCCC		36.2427732954
938PhosphorylationEPRVPEASSEPFDTS
CCCCCCCCCCCCCCC		33.3123403867
939PhosphorylationPRVPEASSEPFDTSS
CCCCCCCCCCCCCCC		57.2323927012
944PhosphorylationASSEPFDTSSPQAGR
CCCCCCCCCCCCCCC		31.3323401153
945PhosphorylationSSEPFDTSSPQAGRQ
CCCCCCCCCCCCCCC		41.6925159151
946PhosphorylationSEPFDTSSPQAGRQL
CCCCCCCCCCCCCCC		24.1125159151
955PhosphorylationQAGRQLETD------
CCCCCCCCC------		56.4528102081
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 ZHX3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZHX3_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 ZHX3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZHX2_HUMANZHX2physical
14659886
ZHX1_HUMANZHX1physical
12659632
ZHX3_HUMANZHX3physical
12659632
NLK_HUMANNLKphysical
25416956
NLK_HUMANNLKphysical
21516116
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 ZHX3_HUMAN

loading...

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-946, 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-946, 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-680 AND SER-723, 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-946, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory