ZMIZ2_HUMAN - dbPTM
ZMIZ2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZMIZ2_HUMAN
UniProt AC Q8NF64
Protein Name Zinc finger MIZ domain-containing protein 2
Gene Name ZMIZ2
Organism Homo sapiens (Human).
Sequence Length 920
Subcellular Localization Nucleus . Detected at replication foci throughout S phase.
Protein Description Increases ligand-dependent transcriptional activity of AR and other nuclear hormone receptors..
Protein Sequence MNSMNPMKPALPPAPHGDGSFAYESVPWQQSATQPAGSLSVVTTVWGVGNATQSQVLGNPMGPAGSPSGSSMMPGVAGGSSALTSPQCLGQQAFAEGGANKGYVQQGVYSRGGYPGAPGFTTGYAGGPGGLGLPSHAARPSTDFTQAAAAAAVAAAAATATATATATVAALQEKQSQELSQYGAMGAGQSFNSQFLQHGGPRGPSVPAGMNPTGIGGVMGPSGLSPLAMNPTRAAGMTPLYAGQRLPQHGYPGPPQAQPLPRQGVKRTYSEVYPGQQYLQGGQYAPSTAQFAPSPGQPPAPSPSYPGHRLPLQQGMTQSLSVPGPTGLHYKPTEQFNGQGASFNGGSVSYSQPGLSGPTRSIPGYPSSPLPGNPTPPMTPSSSVPYMSPNQEVKSPFLPDLKPNLNSLHSSPSGSGPCDELRLTFPVRDGVVLEPFRLQHNLAVSNHVFQLRDSVYKTLIMRPDLELQFKCYHHEDRQMNTNWPASVQVSVNATPLTIERGDNKTSHKPLYLKHVCQPGRNTIQITVTACCCSHLFVLQLVHRPSVRSVLQGLLKKRLLPAEHCITKIKRNFSSGTIPGTPGPNGEDGVEQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMLGILIYIQNSDYEEITIDPTCSWKPVPVKPDMHIKEEPDGPALKRCRTVSPAHVLMPSVMEMIAALGPGAAPFAPLQPPSVPAPSDYPGQGSSFLGPGTFPESFPPTTPSTPTLAEFTPGPPPISYQSDIPSSLLTSEKSTACLPSQMAPAGHLDPTHNPGTPGLHTSNLGAPPGPQLHHSNPPPASRQSLGQASLGPTGELAFSPATGVMGPPSMSGAGEAPEPALDLLPELTNPDELLSYLGPPDLPTNNNDDLLSLFENN
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
101SumoylationFAEGGANKGYVQQGV
HHCCCCCCCCCEECC		51.60-
103PhosphorylationEGGANKGYVQQGVYS
CCCCCCCCCEECCCC		9.1927642862
109PhosphorylationGYVQQGVYSRGGYPG
CCCEECCCCCCCCCC		10.2421447384
111MethylationVQQGVYSRGGYPGAP
CEECCCCCCCCCCCC		25.5258860389
190PhosphorylationGAMGAGQSFNSQFLQ
CCCCCCHHHHHHHHH		26.02-
193PhosphorylationGAGQSFNSQFLQHGG
CCCHHHHHHHHHCCC		21.94-
225PhosphorylationVMGPSGLSPLAMNPT
CCCCCCCCCCCCCCC		22.7624275569
232PhosphorylationSPLAMNPTRAAGMTP
CCCCCCCCCCCCCCC		28.1224275569
238PhosphorylationPTRAAGMTPLYAGQR
CCCCCCCCCCCCCCC		14.8224275569
245MethylationTPLYAGQRLPQHGYP
CCCCCCCCCCCCCCC		47.6324129315
245Asymmetric dimethylarginineTPLYAGQRLPQHGYP
CCCCCCCCCCCCCCC		47.63-
262Asymmetric dimethylargininePQAQPLPRQGVKRTY
CCCCCCCCCCCCCCE		54.27-
262MethylationPQAQPLPRQGVKRTY
CCCCCCCCCCCCCCE		54.2724129315
266MethylationPLPRQGVKRTYSEVY
CCCCCCCCCCEEEEC		45.94115920381
317PhosphorylationLPLQQGMTQSLSVPG
CCCCCCCCCCCCCCC		23.1022210691
319PhosphorylationLQQGMTQSLSVPGPT
CCCCCCCCCCCCCCC		17.2822210691
359PhosphorylationQPGLSGPTRSIPGYP
CCCCCCCCCCCCCCC		40.3422210691
365PhosphorylationPTRSIPGYPSSPLPG
CCCCCCCCCCCCCCC		8.45-
367PhosphorylationRSIPGYPSSPLPGNP
CCCCCCCCCCCCCCC		35.7826074081
368PhosphorylationSIPGYPSSPLPGNPT
CCCCCCCCCCCCCCC		26.4226074081
375PhosphorylationSPLPGNPTPPMTPSS
CCCCCCCCCCCCCCC		43.9826074081
379PhosphorylationGNPTPPMTPSSSVPY
CCCCCCCCCCCCCCC		26.2826074081
381PhosphorylationPTPPMTPSSSVPYMS
CCCCCCCCCCCCCCC		26.5326074081
382PhosphorylationTPPMTPSSSVPYMSP
CCCCCCCCCCCCCCC		36.2426074081
383PhosphorylationPPMTPSSSVPYMSPN
CCCCCCCCCCCCCCC		31.3026074081
386PhosphorylationTPSSSVPYMSPNQEV
CCCCCCCCCCCCCCC		14.2026074081
388PhosphorylationSSSVPYMSPNQEVKS
CCCCCCCCCCCCCCC		18.1726074081
395PhosphorylationSPNQEVKSPFLPDLK
CCCCCCCCCCCCCCC		26.5125159151
402SumoylationSPFLPDLKPNLNSLH
CCCCCCCCCCHHHCC		38.96-
402SumoylationSPFLPDLKPNLNSLH
CCCCCCCCCCHHHCC		38.9628112733
407PhosphorylationDLKPNLNSLHSSPSG
CCCCCHHHCCCCCCC		30.5327080861
410PhosphorylationPNLNSLHSSPSGSGP
CCHHHCCCCCCCCCC		49.6025159151
411PhosphorylationNLNSLHSSPSGSGPC
CHHHCCCCCCCCCCC		16.6125159151
413PhosphorylationNSLHSSPSGSGPCDE
HHCCCCCCCCCCCCE		47.7627080861
415PhosphorylationLHSSPSGSGPCDELR
CCCCCCCCCCCCEEE		43.8527080861
457SumoylationQLRDSVYKTLIMRPD
ECCHHHHHHHCCCCC		34.4028112733
504UbiquitinationTIERGDNKTSHKPLY
EEECCCCCCCCCCEE		57.03-
505PhosphorylationIERGDNKTSHKPLYL
EECCCCCCCCCCEEE		42.17-
506PhosphorylationERGDNKTSHKPLYLK
ECCCCCCCCCCEEEE		30.99-
555SumoylationSVLQGLLKKRLLPAE
HHHHHHHHHCCCCHH		40.67-
555SumoylationSVLQGLLKKRLLPAE
HHHHHHHHHCCCCHH		40.67-
555AcetylationSVLQGLLKKRLLPAE
HHHHHHHHHCCCCHH		40.6725953088
573PhosphorylationTKIKRNFSSGTIPGT
HHHHHHCCCCCCCCC		31.2630624053
574PhosphorylationKIKRNFSSGTIPGTP
HHHHHCCCCCCCCCC		35.5030624053
576PhosphorylationKRNFSSGTIPGTPGP
HHHCCCCCCCCCCCC		26.4129978859
580PhosphorylationSSGTIPGTPGPNGED
CCCCCCCCCCCCCCC		21.5125159151
592PhosphorylationGEDGVEQTAIKVSLK
CCCCCEEEEEEEEEE		19.4922210691
692SumoylationVKPDMHIKEEPDGPA
CCCCCCCCCCCCCHH		41.1528112733
701AcetylationEPDGPALKRCRTVSP
CCCCHHHHCCCCCCH		52.117710447
705PhosphorylationPALKRCRTVSPAHVL
HHHHCCCCCCHHHHH		29.0324275569
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 ZMIZ2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZMIZ2_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 ZMIZ2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
17584785
PIAS3_HUMANPIAS3physical
20159969
ANDR_HUMANARphysical
16051670
SMCA4_HUMANSMARCA4physical
16051670
SMCE1_HUMANSMARCE1physical
16051670
SMAKA_HUMANC2orf88physical
25416956
INT4_HUMANINTS4physical
25416956
SELV_HUMANSELVphysical
25416956
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 ZMIZ2_HUMAN

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Related Literatures of Post-Translational Modification

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