ZN273_HUMAN - dbPTM
ZN273_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN273_HUMAN
UniProt AC Q14593
Protein Name Zinc finger protein 273
Gene Name ZNF273
Organism Homo sapiens (Human).
Sequence Length 569
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MSSAPRGPPSVAPLPAGIGRSTAKTPGLPGSLEMGPLTFRDVAIEFSLEEWQCLDTSQQNLYRNVMLDNYRNLVFLGIAVSKPDLITCLEQGKEPCNMKRHAMVAKPPVVCSHFAQDLWPKQGLKDSFQKVILRRYGKYGHENLQLRKGCKSADEHKVHKRGYNGLNQCLTTTQSKIFQCDKYVKVLHKFSNSNIHKKRQTGKKPFKCKECGKSCCILSQLTQHKKTATRVNFYKCKTCGKAFNQFSNLTKHKIIHPEVNPYKCEECGKAFNQSLTLTKHKKIHTEEKPYKCEDCGKVFSVFSVLTKHKIIHTGTKPYNCEECGKGFSIFSTLTKHKIIHTGEKPYKCNECGKAFNWSSTLTKHKRIHTGEKPYKCEECGKAFNQSSTLTRHKIVHTGEKPYKCEECGKAFKRSTTLTKHKRIYTKEKPYKCEECGKAFSVFSTLTKHKIIHTGAKPYKCEECGSAFRAFSTLTEHKRVHTGEKPYKCNECGKAFNWSSTLTKHKRIHTGEKPYKCEECGKAFNRSSNLTRHKKIHTGEKPYKPKRCDSAFDNTPNFSRHKRNHMGEKS
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
2Phosphorylation------MSSAPRGPP
------CCCCCCCCC		34.9020363803
3Phosphorylation-----MSSAPRGPPS
-----CCCCCCCCCC		40.7820363803
10PhosphorylationSAPRGPPSVAPLPAG
CCCCCCCCCCCCCCC		33.7620363803
22PhosphorylationPAGIGRSTAKTPGLP
CCCCCCCCCCCCCCC		30.7124719451
38PhosphorylationSLEMGPLTFRDVAIE
CCEECCEEHHHEEEE		21.5422210691
65UbiquitinationQQNLYRNVMLDNYRN
HHHHHHHHHHHHHHC		2.7421890473
98UbiquitinationQGKEPCNMKRHAMVA
CCCCCCCCCCCEECC		5.2721890473
125UbiquitinationLWPKQGLKDSFQKVI
CCCCCCCHHHHHHHH		59.1429967540
130UbiquitinationGLKDSFQKVILRRYG
CCHHHHHHHHHHHHH		29.2721890473
163PhosphorylationHKVHKRGYNGLNQCL
HCCHHCCCCHHHHHC		15.3023403867
172PhosphorylationGLNQCLTTTQSKIFQ
HHHHHCCCCHHHHHC		15.19-
173PhosphorylationLNQCLTTTQSKIFQC
HHHHCCCCHHHHHCC		26.13-
175PhosphorylationQCLTTTQSKIFQCDK
HHCCCCHHHHHCCHH		26.15-
176UbiquitinationCLTTTQSKIFQCDKY
HCCCCHHHHHCCHHH		37.41-
182UbiquitinationSKIFQCDKYVKVLHK
HHHHCCHHHHHHHHH		60.62-
189UbiquitinationKYVKVLHKFSNSNIH
HHHHHHHHHCCCCHH		46.4529967540
227PhosphorylationQLTQHKKTATRVNFY
HHHHCCCCCCCCCEE		37.7629449344
229PhosphorylationTQHKKTATRVNFYKC
HHCCCCCCCCCEEEC		40.1429449344
234PhosphorylationTATRVNFYKCKTCGK
CCCCCCEEECCCCHH		15.4029449344
251SumoylationNQFSNLTKHKIIHPE
HHHHHCCCCCCCCCC		46.17-
251SumoylationNQFSNLTKHKIIHPE
HHHHHCCCCCCCCCC		46.17-
253UbiquitinationFSNLTKHKIIHPEVN
HHHCCCCCCCCCCCC		44.9329967540
263SumoylationHPEVNPYKCEECGKA
CCCCCCCCHHHHHHH		36.11-
263SumoylationHPEVNPYKCEECGKA
CCCCCCCCHHHHHHH		36.11-
263UbiquitinationHPEVNPYKCEECGKA
CCCCCCCCHHHHHHH		36.1129967540
274PhosphorylationCGKAFNQSLTLTKHK
HHHHHHHCCCCCCCC		25.1523403867
276PhosphorylationKAFNQSLTLTKHKKI
HHHHHCCCCCCCCCC		37.3123403867
291SumoylationHTEEKPYKCEDCGKV
CCCCCCEECCCCCCE		39.41-
291SumoylationHTEEKPYKCEDCGKV
CCCCCCEECCCCCCE		39.41-
300PhosphorylationEDCGKVFSVFSVLTK
CCCCCEEEHHHHHHC		25.8227732954
303PhosphorylationGKVFSVFSVLTKHKI
CCEEEHHHHHHCCCE		17.6727732954
335UbiquitinationSIFSTLTKHKIIHTG
CCCCCCCCCCEEECC		46.11-
337UbiquitinationFSTLTKHKIIHTGEK
CCCCCCCCEEECCCC		44.93-
341PhosphorylationTKHKIIHTGEKPYKC
CCCCEEECCCCCEEC		36.3129496963
344UbiquitinationKIIHTGEKPYKCNEC
CEEECCCCCEECCCC		55.80-
346PhosphorylationIHTGEKPYKCNECGK
EECCCCCEECCCCCC		38.9618767875
347SumoylationHTGEKPYKCNECGKA
ECCCCCEECCCCCCC		38.83-
347SumoylationHTGEKPYKCNECGKA
ECCCCCEECCCCCCC		38.83-
363UbiquitinationNWSSTLTKHKRIHTG
CCCCCCCCCCCCCCC		50.68-
369PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCEEH		44.6729496963
372UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.80-
374PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH		39.06-
375SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC		43.63-
375UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC		43.63-
375SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC		43.63-
381UbiquitinationYKCEECGKAFNQSST
EEHHHHHHCCCCCCC		62.5629967540
397PhosphorylationTRHKIVHTGEKPYKC
CCEEEEECCCCCEEH		35.8229496963
400SumoylationKIVHTGEKPYKCEEC
EEEECCCCCEEHHHH		55.80-
400SumoylationKIVHTGEKPYKCEEC
EEEECCCCCEEHHHH		55.80-
400UbiquitinationKIVHTGEKPYKCEEC
EEEECCCCCEEHHHH		55.80-
402PhosphorylationVHTGEKPYKCEECGK
EECCCCCEEHHHHHH		39.06-
403UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
403SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
403SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
431UbiquitinationYTKEKPYKCEECGKA
CCCCCCCCCHHHCCC		43.63-
431SumoylationYTKEKPYKCEECGKA
CCCCCCCCCHHHCCC		43.63-
431SumoylationYTKEKPYKCEECGKA
CCCCCCCCCHHHCCC		43.63-
440PhosphorylationEECGKAFSVFSTLTK
HHHCCCHHHHHHHHC		27.4119413330
447UbiquitinationSVFSTLTKHKIIHTG
HHHHHHHCCCEEECC		46.11-
456UbiquitinationKIIHTGAKPYKCEEC
CEEECCCCCEECHHC		50.6622505724
471PhosphorylationGSAFRAFSTLTEHKR
HHHHHHHHHHHCCCC		22.86-
481PhosphorylationTEHKRVHTGEKPYKC
HCCCCCCCCCCCEEC		44.1529496963
484SumoylationKRVHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
484UbiquitinationKRVHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
484SumoylationKRVHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
487SumoylationHTGEKPYKCNECGKA
CCCCCCEECCCCCCC		38.83-
487SumoylationHTGEKPYKCNECGKA
CCCCCCEECCCCCCC		38.83-
489UbiquitinationGEKPYKCNECGKAFN
CCCCEECCCCCCCCC		43.3622505724
503UbiquitinationNWSSTLTKHKRIHTG
CCCCCCCCCCCCCCC		50.68-
509PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCCCH		44.6729496963
512UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
514PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
515SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
515SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
515UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHC		43.63-
521UbiquitinationYKCEECGKAFNRSSN
CCHHHHHHCCCCCCC		62.5622505724
534UbiquitinationSNLTRHKKIHTGEKP
CCCCCCCCCCCCCCC		33.33-
537PhosphorylationTRHKKIHTGEKPYKP
CCCCCCCCCCCCCCC		50.9729496963
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 ZN273_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN273_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 ZN273_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SP8_HUMANSP8physical
20211142
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 ZN273_HUMAN

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Related Literatures of Post-Translational Modification

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