ACHA9_HUMAN - dbPTM
ACHA9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACHA9_HUMAN
UniProt AC Q9UGM1
Protein Name Neuronal acetylcholine receptor subunit alpha-9
Gene Name CHRNA9
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein .
Protein Description Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane. [PubMed: 11752216]
Protein Sequence MNWSHSCISFCWIYFAASRLRAAETADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWARVVILKYMSRVLFVYDVGESCLSPHHSRERDHLTKVYSKLPESNLKAARNKDLSRKKDMNKRLKNDLGCQGKNPQEAESYCAQYKVLTRNIEYIAKCLKDHKATNSKGSEWKKVAKVIDRFFMWIFFIMVFVMTILIIARAD
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
57N-linked_GlycosylationEDTDKVLNVTLQITL
CCCHHHHEEEEEEEH
27.93UniProtKB CARBOHYD
65PhosphorylationVTLQITLSQIKDMDE
EEEEEEHHHCCCHHH
22.6224719451
122UbiquitinationPDIVLYNKADDESSE
CCEEEEECCCCCCCC
39.3721963094
170N-linked_GlycosylationPFDNQQCNLTFGSWT
CCCCCEEEEEEEEEE
37.47UniProtKB CARBOHYD
357PhosphorylationFVYDVGESCLSPHHS
EEEECCHHHCCCCHH
17.9028348404
360PhosphorylationDVGESCLSPHHSRER
ECCHHHCCCCHHHCH
26.8928348404
374PhosphorylationRDHLTKVYSKLPESN
HHHHHHHHHHCCHHH
11.1421712546
375PhosphorylationDHLTKVYSKLPESNL
HHHHHHHHHCCHHHH
30.6121712546
376UbiquitinationHLTKVYSKLPESNLK
HHHHHHHHCCHHHHH
50.83-
380PhosphorylationVYSKLPESNLKAARN
HHHHCCHHHHHHHHC
45.5921712546
383UbiquitinationKLPESNLKAARNKDL
HCCHHHHHHHHCCCH
44.2229967540
409UbiquitinationNDLGCQGKNPQEAES
HHCCCCCCCHHHHHH
39.3121963094
422UbiquitinationESYCAQYKVLTRNIE
HHHHHHHHHHHHCHH
20.77-
430PhosphorylationVLTRNIEYIAKCLKD
HHHHCHHHHHHHHHH
11.4629083192

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 ACHA9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACHA9_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 ACHA9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P121A_HUMANPOM121physical
26186194
T131L_HUMANKIAA0922physical
26186194
FA76B_HUMANFAM76Bphysical
26186194
NUFP2_HUMANNUFIP2physical
26186194
ZNT1_HUMANSLC30A1physical
26186194
CYTSA_HUMANSPECC1Lphysical
26186194
S12A9_HUMANSLC12A9physical
26186194
TMX2_HUMANTMX2physical
26186194
METL9_HUMANMETTL9physical
26186194
NETO2_HUMANNETO2physical
26186194
KINH_HUMANKIF5Bphysical
26186194
KIF5A_HUMANKIF5Aphysical
26186194
CA043_HUMANC1orf43physical
26186194
CCPG1_HUMANCCPG1physical
26186194
PMGT2_HUMANPOMGNT2physical
26186194
CKAP4_HUMANCKAP4physical
26186194
TM39B_HUMANTMEM39Bphysical
26186194
KLC2_HUMANKLC2physical
26186194
KLC4_HUMANKLC4physical
26186194
DHRS7_HUMANDHRS7physical
26186194
ZNT5_HUMANSLC30A5physical
26186194
LRC59_HUMANLRRC59physical
26186194
DIA1_HUMANC3orf58physical
26186194
PBIP1_HUMANPBXIP1physical
26186194
CISD2_HUMANCISD2physical
26186194
CELR1_HUMANCELSR1physical
26186194
LEMD2_HUMANLEMD2physical
26186194
LNP_HUMANKIAA1715physical
26186194
GOLM1_HUMANGOLM1physical
26186194
RNC_HUMANDROSHAphysical
26186194
GHDC_HUMANGHDCphysical
26186194
BT2A2_HUMANBTN2A2physical
26186194
HS2ST_HUMANHS2ST1physical
26186194
HYEP_HUMANEPHX1physical
26186194
HMOX1_HUMANHMOX1physical
26186194
GRM1A_HUMANGRAMD1Aphysical
26186194
ATF6B_HUMANATF6Bphysical
26186194
HMDH_HUMANHMGCRphysical
26186194
TMUB1_HUMANTMUB1physical
26186194
MACOI_HUMANTMEM57physical
26186194
CHK1_HUMANCHEK1physical
26186194
ZNT6_HUMANSLC30A6physical
26186194
AT11C_HUMANATP11Cphysical
26186194
H6ST1_HUMANHS6ST1physical
26186194
FUT8_HUMANFUT8physical
26186194
ZDHC9_HUMANZDHHC9physical
26186194
PDE3B_HUMANPDE3Bphysical
26186194
TM39A_HUMANTMEM39Aphysical
26186194
SNX14_HUMANSNX14physical
26186194
ZNT7_HUMANSLC30A7physical
26186194
PDZD8_HUMANPDZD8physical
26186194
DJC18_HUMANDNAJC18physical
26186194
ERGI2_HUMANERGIC2physical
26186194
RER1_HUMANRER1physical
26186194
YKT6_HUMANYKT6physical
26186194
MAVS_HUMANMAVSphysical
26186194
F189B_HUMANFAM189Bphysical
26186194
TIM29_HUMANC19orf52physical
26186194
DDRGK_HUMANDDRGK1physical
26186194
E2AK3_HUMANEIF2AK3physical
26186194
ST7_HUMANST7physical
26186194
T120B_HUMANTMEM120Bphysical
26186194
MAP7_HUMANMAP7physical
26186194
DJC30_HUMANDNAJC30physical
26186194
LCLT1_HUMANLCLAT1physical
26186194
CHK1_HUMANCHEK1physical
28514442
KLC4_HUMANKLC4physical
28514442
ZNT1_HUMANSLC30A1physical
28514442
KLC2_HUMANKLC2physical
28514442
TIM29_HUMANC19orf52physical
28514442
DJC18_HUMANDNAJC18physical
28514442
ZNT5_HUMANSLC30A5physical
28514442
GOLM1_HUMANGOLM1physical
28514442
DJC30_HUMANDNAJC30physical
28514442
ZNT6_HUMANSLC30A6physical
28514442
LNP_HUMANKIAA1715physical
28514442
PBIP1_HUMANPBXIP1physical
28514442
CISD2_HUMANCISD2physical
28514442
LEMD2_HUMANLEMD2physical
28514442
SNX14_HUMANSNX14physical
28514442
CA043_HUMANC1orf43physical
28514442
ZDHC9_HUMANZDHHC9physical
28514442
YKT6_HUMANYKT6physical
28514442
GHDC_HUMANGHDCphysical
28514442
MAP7_HUMANMAP7physical
28514442
RNC_HUMANDROSHAphysical
28514442
E2AK3_HUMANEIF2AK3physical
28514442
H6ST1_HUMANHS6ST1physical
28514442
CCPG1_HUMANCCPG1physical
28514442
DHRS7_HUMANDHRS7physical
28514442
T120B_HUMANTMEM120Bphysical
28514442
TM268_HUMANC9orf91physical
28514442
CKAP4_HUMANCKAP4physical
28514442
TM39B_HUMANTMEM39Bphysical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
ST7_HUMANST7physical
28514442
P121A_HUMANPOM121physical
28514442
BT2A2_HUMANBTN2A2physical
28514442
KIF5A_HUMANKIF5Aphysical
28514442
METL9_HUMANMETTL9physical
28514442
ZNT7_HUMANSLC30A7physical
28514442
TM39A_HUMANTMEM39Aphysical
28514442
NGBR_HUMANNUS1physical
28514442
TMUB1_HUMANTMUB1physical
28514442
PDE3B_HUMANPDE3Bphysical
28514442
DDRGK_HUMANDDRGK1physical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACHA9_HUMAN

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Related Literatures of Post-Translational Modification

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