ZNRF1_HUMAN - dbPTM
ZNRF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNRF1_HUMAN
UniProt AC Q8ND25
Protein Name E3 ubiquitin-protein ligase ZNRF1
Gene Name ZNRF1
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Endosome. Lysosome. Membrane
Peripheral membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Peripheral membrane protein . Associated with synaptic vesicle membranes in neurons.
Protein Description E3 ubiquitin-protein ligase that mediates the ubiquitination of AKT1 and GLUL, thereby playing a role in neuron cells differentiation. Plays a role in the establishment and maintenance of neuronal transmission and plasticity. Regulates Schwann cells differentiation by mediating ubiquitination of GLUL. Promotes neurodegeneration by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of AKT1 in axons: degradation of AKT1 prevents AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and phosphorylation of DPYSL2/CRMP2 followed by destabilization of microtubule assembly in axons (Probable)..
Protein Sequence MGGKQSTAARSRGPFPGVSTDDSAVPPPGGAPHFGHYRTGGGAMGLRSRSVSSVAGMGMDPSTAGGVPFGLYTPASRGTGDSERAPGGGGSASDSTYAHGNGYQETGGGHHRDGMLYLGSRASLADALPLHIAPRWFSSHSGFKCPICSKSVASDEMEMHFIMCLSKPRLSYNDDVLTKDAGECVICLEELLQGDTIARLPCLCIYHKSCIDSWFEVNRSCPEHPAD
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
2Myristoylation------MGGKQSTAA
------CCCCCCCCH		52.5914561866
6Phosphorylation--MGGKQSTAARSRG
--CCCCCCCCHHHCC		24.4130631047
37PhosphorylationGAPHFGHYRTGGGAM
CCCCCCCCCCCCCCC		15.3928796482
48PhosphorylationGGAMGLRSRSVSSVA
CCCCCCCCCCHHHHC		33.6723401153
50PhosphorylationAMGLRSRSVSSVAGM
CCCCCCCCHHHHCCC		27.8322115753
52PhosphorylationGLRSRSVSSVAGMGM
CCCCCCHHHHCCCCC		21.9722617229
53PhosphorylationLRSRSVSSVAGMGMD
CCCCCHHHHCCCCCC		17.5222115753
62PhosphorylationAGMGMDPSTAGGVPF
CCCCCCHHHCCCCCC		26.9928464451
63PhosphorylationGMGMDPSTAGGVPFG
CCCCCHHHCCCCCCE		34.4128464451
72PhosphorylationGGVPFGLYTPASRGT
CCCCCEEECCCCCCC		15.8526074081
73PhosphorylationGVPFGLYTPASRGTG
CCCCEEECCCCCCCC		19.8826074081
76PhosphorylationFGLYTPASRGTGDSE
CEEECCCCCCCCCCC		32.2326074081
79PhosphorylationYTPASRGTGDSERAP
ECCCCCCCCCCCCCC		36.38-
91PhosphorylationRAPGGGGSASDSTYA
CCCCCCCCCCCCCCC		28.0728796482
93PhosphorylationPGGGGSASDSTYAHG
CCCCCCCCCCCCCCC		33.5228796482
95PhosphorylationGGGSASDSTYAHGNG
CCCCCCCCCCCCCCC		22.3325884760
96PhosphorylationGGSASDSTYAHGNGY
CCCCCCCCCCCCCCC		29.7128796482
97PhosphorylationGSASDSTYAHGNGYQ
CCCCCCCCCCCCCCC		10.6828796482
103PhosphorylationTYAHGNGYQETGGGH
CCCCCCCCCCCCCCC		13.7428796482
106PhosphorylationHGNGYQETGGGHHRD
CCCCCCCCCCCCCCC		26.1228796482
117PhosphorylationHHRDGMLYLGSRASL
CCCCCCEEECCCHHH		10.5026552605
120PhosphorylationDGMLYLGSRASLADA
CCCEEECCCHHHHHH		23.2926552605
123PhosphorylationLYLGSRASLADALPL
EEECCCHHHHHHCCC		23.9930266825
138PhosphorylationHIAPRWFSSHSGFKC
CCCCCHHHCCCCCCC		21.8528122231
139PhosphorylationIAPRWFSSHSGFKCP
CCCCHHHCCCCCCCC		16.5228122231
141PhosphorylationPRWFSSHSGFKCPIC
CCHHHCCCCCCCCCC		48.1228290473
144UbiquitinationFSSHSGFKCPICSKS
HHCCCCCCCCCCCCC		42.50-
144 (in isoform 2)Ubiquitination-42.50-
150UbiquitinationFKCPICSKSVASDEM
CCCCCCCCCCCCCCC		44.53-
150 (in isoform 2)Ubiquitination-44.53-
167UbiquitinationHFIMCLSKPRLSYND
HHHHHHCCCCCCCCC		22.62-
167 (in isoform 2)Ubiquitination-22.62-
171PhosphorylationCLSKPRLSYNDDVLT
HHCCCCCCCCCCCCC		24.1427050516
172PhosphorylationLSKPRLSYNDDVLTK
HCCCCCCCCCCCCCC		27.4828634298
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 ZNRF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNRF1_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 ZNRF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433T_HUMANYWHAQphysical
22797923
AT1A2_HUMANATP1A2physical
22797923
UBE2N_HUMANUBE2Nphysical
22797923
ZNRF2_HUMANZNRF2physical
22797923
ZNRF1_HUMANZNRF1physical
19549727
UBE2N_HUMANUBE2Nphysical
19549727
UB2D1_HUMANUBE2D1physical
19549727
UB2D2_HUMANUBE2D2physical
19549727
UB2R1_HUMANCDC34physical
19549727
UB2E1_HUMANUBE2E1physical
19549727
AT1A1_HUMANATP1A1physical
22797923
UBC_HUMANUBCphysical
22797923
UB2D1_HUMANUBE2D1physical
22797923
NMT1_HUMANNMT1physical
26186194
NMT2_HUMANNMT2physical
26186194
SEN2_HUMANTSEN2physical
26186194
BHMT1_HUMANBHMTphysical
26186194
SEN54_HUMANTSEN54physical
26186194
FBXW5_HUMANFBXW5physical
26186194
NCEH1_HUMANNCEH1physical
26186194
SYAM_HUMANAARS2physical
26186194
GLNA_HUMANGLULphysical
20107048
FBXW5_HUMANFBXW5physical
28514442
NMT2_HUMANNMT2physical
28514442
SEN2_HUMANTSEN2physical
28514442
NCEH1_HUMANNCEH1physical
28514442
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 ZNRF1_HUMAN

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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-52 AND SER-53, AND MASSSPECTROMETRY.

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