ACHA_MOUSE - dbPTM
ACHA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACHA_MOUSE
UniProt AC P04756
Protein Name Acetylcholine receptor subunit alpha
Gene Name Chrna1
Organism Mus musculus (Mouse).
Sequence Length 457
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein.
Protein Description After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane..
Protein Sequence MELSTVLLLLGLCSAGLVLGSEHETRLVAKLFEDYSSVVRPVEDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKEARGWKHWVFYSCCPTTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTSLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHIMPEWVRKVFIDTIPNIMFFSTMKRPSRDKQEKRIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGVKYIAETMKSDQESNNAAEEWKYVAMVMDHILLGVFMLVCLIGTLAVFAGRLIELHQQG
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
124UbiquitinationDGDFAIVKFTKVLLD
CCCEEEEEEEEEHHH
41.00-
161N-linked_GlycosylationHFPFDEQNCSMKLGT
ECCCCCCCCEEEEEE
20.1317643119
369PhosphorylationFTEDIDISDISGKPG
EECCCCHHHCCCCCC
25.7422817900
372PhosphorylationDIDISDISGKPGPPP
CCCHHHCCCCCCCCC
45.8420415495

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 ACHA_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACHA_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 ACHA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACHA_MOUSEChrna1physical
22956146
ACTN1_MOUSEActn1physical
22956146

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of the extracellular domain of nAChR alpha1 boundto alpha-bungarotoxin at 1.94 A resolution.";
Dellisanti C.D., Yao Y., Stroud J.C., Wang Z.Z., Chen L.;
Nat. Neurosci. 10:953-962(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 21-231 IN COMPLEX WITHALPHA-BUNGAROTOXIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-161.

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