ZN594_HUMAN - dbPTM
ZN594_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN594_HUMAN
UniProt AC Q96JF6
Protein Name Zinc finger protein 594
Gene Name ZNF594
Organism Homo sapiens (Human).
Sequence Length 807
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MKEWKSKMEISEEKKSARAASEKLQRQITQECELVETSNSEDRLLKHWVSPLKDAMRHLPSQESGIREMHIIPQKAIVGEIGHGCNEGEKILSAGESSHRYEVSGQNFKQKSGLTEHQKIHNINKTYECKECEKTFNRSSNLIIHQRIHTGNKPYVCNECGKDSNQSSNLIIHQRIHTGKKPYICHECGKDFNQSSNLVRHKQIHSGGNPYECKECGKAFKGSSNLVLHQRIHSRGKPYLCNKCGKAFSQSTDLIIHHRIHTGEKPYECYDCGQMFSQSSHLVPHQRIHTGEKPLKCNECEKAFRQHSHLTEHQRLHSGEKPYECHRCGKTFSGRTAFLKHQRLHAGEKIEECEKTFSKDEELREEQRIHQEEKAYWCNQCGRNFQGTSDLIRHQVTHTGEKPYECKECGKTFNQSSDLLRHHRIHSGEKPCVCSKCGKSFRGSSDLIRHHRVHTGEKPYECSECGKAFSQRSHLVTHQKIHTGEKPYQCTECGKAFRRRSLLIQHRRIHSGEKPYECKECGKLFIWRTAFLKHQSLHTGEKLECEKTFSQDEELRGEQKIHQEAKAYWCNQCGRAFQGSSDLIRHQVTHTREKPYECKECGKTFNQSSDLLRHHRIHSGEKPYVCNKCGKSFRGSSDLIKHHRIHTGEKPYECSECGKAFSQRSHLATHQKIHTGEKPYQCSECGNAFRRRSLLIQHRRLHSGEKPYECKECGKLFMWHTAFLKHQRLHAGEKLEECEKTFSKDEELRKEQRTHQEKKVYWCNQCSRTFQGSSDLIRHQVTHTREKPYECKECGKTQSELRPSETS
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
23AcetylationSARAASEKLQRQITQ
HHHHHHHHHHHHHHH		47.6425953088
50PhosphorylationRLLKHWVSPLKDAMR
HHHHHHHHHHHHHHH		21.2323312004
112PhosphorylationGQNFKQKSGLTEHQK
CCCHHCCCCCCHHHH		36.22-
139PhosphorylationCEKTFNRSSNLIIHQ
HHHHHCCCCCEEEEE		25.3625332170
140PhosphorylationEKTFNRSSNLIIHQR
HHHHCCCCCEEEEEE		32.2125332170
164PhosphorylationCNECGKDSNQSSNLI
CCCCCCCCCCCCCEE		40.0127732954
167PhosphorylationCGKDSNQSSNLIIHQ
CCCCCCCCCCEEEEE		25.9927732954
168PhosphorylationGKDSNQSSNLIIHQR
CCCCCCCCCEEEEEE		26.3727732954
196PhosphorylationGKDFNQSSNLVRHKQ
CCCCCCCCCCHHHCE		25.1524719451
206PhosphorylationVRHKQIHSGGNPYEC
HHHCEECCCCCCEEC		50.45-
214SumoylationGGNPYECKECGKAFK
CCCCEECCHHHHHCC		44.06-
214SumoylationGGNPYECKECGKAFK
CCCCEECCHHHHHCC		44.06-
221MethylationKECGKAFKGSSNLVL
CHHHHHCCCCCCEEE		63.84115978133
234PhosphorylationVLHQRIHSRGKPYLC
EEEEHHHHCCCCEEC		40.1222210691
237SumoylationQRIHSRGKPYLCNKC
EHHHHCCCCEECCCC		29.40-
237SumoylationQRIHSRGKPYLCNKC
EHHHHCCCCEECCCC		29.40-
262PhosphorylationIIHHRIHTGEKPYEC
EEEEECCCCCCCEEE		44.6728111955
290PhosphorylationVPHQRIHTGEKPLKC
CCCCCCCCCCCCCCC		44.6729396449
397PhosphorylationDLIRHQVTHTGEKPY
HHHHHCCCCCCCCCC		13.7227251275
399PhosphorylationIRHQVTHTGEKPYEC
HHHCCCCCCCCCCCC		37.3629496963
402UbiquitinationQVTHTGEKPYECKEC
CCCCCCCCCCCCCCC		55.00-
407UbiquitinationGEKPYECKECGKTFN
CCCCCCCCCCCCCCC		44.06-
407SumoylationGEKPYECKECGKTFN
CCCCCCCCCCCCCCC		44.06-
407SumoylationGEKPYECKECGKTFN
CCCCCCCCCCCCCCC		44.06-
455PhosphorylationIRHHRVHTGEKPYEC
HHCCCCCCCCCCEEC		44.1528348404
463PhosphorylationGEKPYECSECGKAFS
CCCCEECCHHHHHHH		24.7930631047
483PhosphorylationVTHQKIHTGEKPYQC
EECCCCCCCCCCEEC		50.97-
495UbiquitinationYQCTECGKAFRRRSL
EECCCCHHHHHHHHH		56.88-
501PhosphorylationGKAFRRRSLLIQHRR
HHHHHHHHHHHCCCC		26.2224719451
519SumoylationGEKPYECKECGKLFI
CCCCEECCCCCCEEE		44.06-
519SumoylationGEKPYECKECGKLFI
CCCCEECCCCCCEEE		44.06-
548PhosphorylationEKLECEKTFSQDEEL
CCEEEEEECCCCHHH		13.2623186163
550PhosphorylationLECEKTFSQDEELRG
EEEEEECCCCHHHHC		41.7923186163
566SumoylationQKIHQEAKAYWCNQC
HHHHHHHHHHHHCCC		41.05-
566SumoylationQKIHQEAKAYWCNQC
HHHHHHHHHHHHCCC		41.05-
599SumoylationREKPYECKECGKTFN
CCCCCCCCCCCCCCC		44.06-
599SumoylationREKPYECKECGKTFN
CCCCCCCCCCCCCCC		44.06-
622AcetylationHRIHSGEKPYVCNKC
CCCCCCCCCEEECCC		45.2119812067
636PhosphorylationCGKSFRGSSDLIKHH
CCCCCCCCHHHHHCC		19.2025072903
637PhosphorylationGKSFRGSSDLIKHHR
CCCCCCCHHHHHCCC		38.9825072903
647PhosphorylationIKHHRIHTGEKPYEC
HHCCCCCCCCCCEEC		44.6728258704
652PhosphorylationIHTGEKPYECSECGK
CCCCCCCEECCHHHH		40.41-
655PhosphorylationGEKPYECSECGKAFS
CCCCEECCHHHHHHH		24.7930631047
675PhosphorylationATHQKIHTGEKPYQC
HHCCCCCCCCCCCCC		50.97-
693PhosphorylationGNAFRRRSLLIQHRR
CHHHHHHHHHHHCCC		26.2224719451
703PhosphorylationIQHRRLHSGEKPYEC
HHCCCCCCCCCCCCC		53.9226425664
711SumoylationGEKPYECKECGKLFM
CCCCCCCCHHHCEEE		44.06-
711SumoylationGEKPYECKECGKLFM
CCCCCCCCHHHCEEE		44.06-
761PhosphorylationTHQEKKVYWCNQCSR
HHHCHHEEEECCCCC		17.08-
792SumoylationREKPYECKECGKTQS
CCCCCCCCCCCCCHH		44.06-
792SumoylationREKPYECKECGKTQS
CCCCCCCCCCCCCHH		44.06-
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 ZN594_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN594_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 ZN594_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOGA2_HUMANGOLGA2physical
16169070
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN594_HUMAN

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Related Literatures of Post-Translational Modification

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