ASIC1_MOUSE - dbPTM
ASIC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASIC1_MOUSE
UniProt AC Q6NXK8
Protein Name Acid-sensing ion channel 1
Gene Name Asic1
Organism Mus musculus (Mouse).
Sequence Length 526
Subcellular Localization Cell membrane
Multi-pass membrane protein. Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4.
Protein Description Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear..
Protein Sequence MELKTEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFCYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEACSAEDFKVVFTRYGKCYTFNSGQDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLIYLPSPWGTCNAVTMDSDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCQKEAKRNSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
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
196UbiquitinationTRYGKCYTFNSGQDG
EECCEEEEECCCCCC
26.3027667366
366N-linked_GlycosylationCVCEMPCNLTRYGKE
EEEECCCCCCCCCCC
38.28-
382AcetylationSMVKIPSKASAKYLA
EEEECCCHHHHHHHH
40.7915616749
386AcetylationIPSKASAKYLAKKFN
CCCHHHHHHHHHHCC
38.0015616761
393N-linked_GlycosylationKYLAKKFNKSEQYIG
HHHHHHCCCCHHHHC
56.68-
454PhosphorylationTVLELFDYAYEVIKH
HHHHHHHHHHHHHHH
12.07-
456PhosphorylationLELFDYAYEVIKHRL
HHHHHHHHHHHHHHH
12.42-
477PhosphorylationQKEAKRNSADKGVAL
HHHHHHCCCCCCCEE
41.7119060867
485PhosphorylationADKGVALSLDDVKRH
CCCCCEECHHHHHHH
21.7322324799
490UbiquitinationALSLDDVKRHNPCES
EECHHHHHHHCCCHH
55.7427667366
491UbiquitinationLSLDDVKRHNPCESL
ECHHHHHHHCCCHHH
34.3627667366
497PhosphorylationKRHNPCESLRGHPAG
HHHCCCHHHCCCCCC
30.0421183079
506PhosphorylationRGHPAGMTYAANILP
CCCCCCCCHHHHCCC
14.75-
507PhosphorylationGHPAGMTYAANILPH
CCCCCCCHHHHCCCC
8.53-
523UbiquitinationPARGTFEDFTC----
CCCCCCCCCCC----
39.7127667366
524UbiquitinationARGTFEDFTC-----
CCCCCCCCCC-----
6.2227667366

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
477SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASIC1_MOUSE !!

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 ASIC1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASIC2_MOUSEAsic2physical
19571134

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASIC1_MOUSE

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Related Literatures of Post-Translational Modification

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