ACHA7_HUMAN - dbPTM
ACHA7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACHA7_HUMAN
UniProt AC P36544
Protein Name Neuronal acetylcholine receptor subunit alpha-7
Gene Name CHRNA7
Organism Homo sapiens (Human).
Sequence Length 502
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. The channel is blocked by alpha-bungarotoxin..
Protein Sequence MRCSPGGVWLALAASLLHVSLQGEFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA
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
30PhosphorylationGEFQRKLYKELVKNY
HHHHHHHHHHHHHHC
12.8822964224
46N-linked_GlycosylationPLERPVANDSQPLTV
CCCCCCCCCCCCCEE
50.10UniProtKB CARBOHYD
83PhosphorylationIWLQMSWTDHYLQWN
EEEEEECCHHHHCCC
12.94-
86PhosphorylationQMSWTDHYLQWNVSE
EEECCHHHHCCCHHH
11.91-
90N-linked_GlycosylationTDHYLQWNVSEYPGV
CHHHHCCCHHHCCCC
17.93UniProtKB CARBOHYD
133N-linked_GlycosylationFHTNVLVNSSGHCQY
EECCEEECCCCCCCC
26.71UniProtKB CARBOHYD
217PhosphorylationYECCKEPYPDVTFTV
HHHHCCCCCCCEEEE
17.10-
221PhosphorylationKEPYPDVTFTVTMRR
CCCCCCCEEEEEECC
22.44-
225PhosphorylationPDVTFTVTMRRRTLY
CCCEEEEEECCCHHH
11.25-
386PhosphorylationASNGNLLYIGFRGLD
CCCCCEEEEEECCCC
11.3616251431
442PhosphorylationKILEEVRYIANRFRC
HHHHHHHHHHHHHCC
15.0116251431

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
386YPhosphorylationKinaseSRCP12931
PSP
386YPhosphorylationKinaseSRC64-PhosphoELM
442YPhosphorylationKinaseSRCP12931
PSP
442YPhosphorylationKinaseSRC64-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACHA7_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 ACHA7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FYN_HUMANFYNphysical
11278378

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
D00611 Mecamylamine hydrochloride (USP); Inversine (TN)
D00999 Acetylcholine chloride (JP16/USP/INN); Miochol (TN)
D02202 Lobeline hydrochloride (JAN)
D02204 Hexamethonium bromide (JAN/INN); Hexamethonium bromide (TN)
D02364 Lobeline (INN)
D02839 Altinicline maleate (USAN)
D08138 Lobeline sulfate; Smokeless (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACHA7_HUMAN

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Related Literatures of Post-Translational Modification

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