ZNF22_HUMAN - dbPTM
ZNF22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF22_HUMAN
UniProt AC P17026
Protein Name Zinc finger protein 22
Gene Name ZNF22
Organism Homo sapiens (Human).
Sequence Length 224
Subcellular Localization Nucleus.
Protein Description Binds DNA through the consensus sequence 5'-CAATG-3'. May be involved in transcriptional regulation and may play a role in tooth formation (By similarity)..
Protein Sequence MRLAKPKAGISRSSSQGKAYENKRKTGRQRQKWGMTIRFDSSFSRLRRSLDDKPYKCTECEKSFSQSSTLFQHQKIHTGKKSHKCADCGKSFFQSSNLIQHRRIHTGEKPYKCDECGESFKQSSNLIQHQRIHTGEKPYQCDECGRCFSQSSHLIQHQRTHTGEKPYQCSECGKCFSQSSHLRQHMKVHKEEKPRKTRGKNIRVKTHLPSWKAGTGRKSVAGLR
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
13PhosphorylationPKAGISRSSSQGKAY
CCCCCCCCCCCCHHH		27.7926074081
14PhosphorylationKAGISRSSSQGKAYE
CCCCCCCCCCCHHHH		26.1026074081
15PhosphorylationAGISRSSSQGKAYEN
CCCCCCCCCCHHHHC		44.1726074081
18AcetylationSRSSSQGKAYENKRK
CCCCCCCHHHHCCCC		39.9123749302
20PhosphorylationSSSQGKAYENKRKTG
CCCCCHHHHCCCCCC		24.4229449344
23AcetylationQGKAYENKRKTGRQR
CCHHHHCCCCCCCHH		43.25-
32UbiquitinationKTGRQRQKWGMTIRF
CCCCHHHHHCCEEEE		48.15-
41PhosphorylationGMTIRFDSSFSRLRR
CCEEEECCHHHHHHH		30.4830266825
42PhosphorylationMTIRFDSSFSRLRRS
CEEEECCHHHHHHHH		29.1423401153
44PhosphorylationIRFDSSFSRLRRSLD
EEECCHHHHHHHHCC		32.1423090842
49PhosphorylationSFSRLRRSLDDKPYK
HHHHHHHHCCCCCCC		29.7123401153
55PhosphorylationRSLDDKPYKCTECEK
HHCCCCCCCCCHHHH		25.1623403867
62UbiquitinationYKCTECEKSFSQSST
CCCCHHHHHCCCCHH		69.34-
63PhosphorylationKCTECEKSFSQSSTL
CCCHHHHHCCCCHHH		14.0823312004
65PhosphorylationTECEKSFSQSSTLFQ
CHHHHHCCCCHHHHC		35.9223312004
67PhosphorylationCEKSFSQSSTLFQHQ
HHHHCCCCHHHHCCC		24.8823312004
68PhosphorylationEKSFSQSSTLFQHQK
HHHCCCCHHHHCCCC		22.8423312004
106PhosphorylationIQHRRIHTGEKPYKC
HHCCEECCCCCCCCC		44.6729496963
121UbiquitinationDECGESFKQSSNLIQ
CCCCHHHHHHCCHHC		59.56-
134PhosphorylationIQHQRIHTGEKPYQC
HCCCCCCCCCCCCCC		44.6728111955
160PhosphorylationHLIQHQRTHTGEKPY
HHHHCCCCCCCCCCE		19.7428111955
162PhosphorylationIQHQRTHTGEKPYQC
HHCCCCCCCCCCEEC		46.5623898821
165UbiquitinationQRTHTGEKPYQCSEC
CCCCCCCCCEECCCC		50.82-
165SumoylationQRTHTGEKPYQCSEC
CCCCCCCCCEECCCC		50.82-
165SumoylationQRTHTGEKPYQCSEC
CCCCCCCCCEECCCC		50.82-
167PhosphorylationTHTGEKPYQCSECGK
CCCCCCCEECCCCHH		32.9728111955
193AcetylationMKVHKEEKPRKTRGK
HHHCCCCCCCCCCCC		51.7412432385
210PhosphorylationRVKTHLPSWKAGTGR
EEEECCCCCCCCCCC		47.7923401153
212UbiquitinationKTHLPSWKAGTGRKS
EECCCCCCCCCCCCC		41.08-
215PhosphorylationLPSWKAGTGRKSVAG
CCCCCCCCCCCCCCC		38.38-
218AcetylationWKAGTGRKSVAGLR-
CCCCCCCCCCCCCC-		51.1023749302
219PhosphorylationKAGTGRKSVAGLR--
CCCCCCCCCCCCC--		18.8124719451
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 ZNF22_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF22_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 ZNF22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RL26L_HUMANRPL26L1physical
26186194
SRRM1_HUMANSRRM1physical
26186194
ZN808_HUMANZNF808physical
26186194
ZN624_HUMANZNF624physical
26186194
DDX52_HUMANDDX52physical
26186194
H12_HUMANHIST1H1Cphysical
26186194
RS3A_HUMANRPS3Aphysical
26186194
NPM_HUMANNPM1physical
26186194
RL36L_HUMANRPL36ALphysical
26186194
RM27_HUMANMRPL27physical
26186194
RM09_HUMANMRPL9physical
26186194
RM30_HUMANMRPL30physical
26186194
RM20_HUMANMRPL20physical
26186194
RT18A_HUMANMRPS18Aphysical
26186194
TRA2A_HUMANTRA2Aphysical
26186194
ZN808_HUMANZNF808physical
28514442
H12_HUMANHIST1H1Cphysical
28514442
RL36L_HUMANRPL36ALphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
TPM2_HUMANTPM2physical
28514442
DDX52_HUMANDDX52physical
28514442
RL7_HUMANRPL7physical
28514442
NPM_HUMANNPM1physical
28514442
ZN624_HUMANZNF624physical
28514442
RL30_HUMANRPL30physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
SRRM1_HUMANSRRM1physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZNF22_HUMAN

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Related Literatures of Post-Translational Modification

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