PMA8_ARATH - dbPTM
PMA8_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMA8_ARATH
UniProt AC Q9M2A0
Protein Name ATPase 8, plasma membrane-type
Gene Name AHA8
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 948
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity)..
Protein Sequence MATEFSWDEIKKENVDLERIPVEEVFEQLKCSKEGLSSDEGAKRLEIFGANKLEEKSENKFLKFLGFMWNPLSWVMESAAIMAIVLANGGGKAPDWQDFIGIMVLLIINSTISFIEENNAGNAAAALMANLAPKTKVLRDGKWGEQEASILVPGDLISIKLGDIVPADARLLEGDPLKIDQSALTGESLPTTKHPGDEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNNVGHFQKVLTSIGNFCICSIGLGMLIEILIMYPIQHRTYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKSLIEVFPKNMDSDSVVLMAARASRIENQDAIDASIVGMLGDPKEARAGITEVHFLPFNPVDKRTAITYIDESGDWHRSSKGAPEQIIELCNLQGETKRKAHEVIDGFAERGLRSLGVAQQTVPEKTKESDGSPWEFVGLLPLFDPPRHDSAETIRRALELGVNVKMITGDQLAIGIETGRRLGMGTNMYPSTSLLGNSKDESLVGIPIDELIEKADGFAGVFPEHKYEIVKKLQERKHICGMTGDGVNDAPALKKADIGIAVADATDAARSASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVLGFMLVALIWRFDFAPFMVLIIAILNDGTIMTISKDRVKPSPVPDSWKLNEIFATGVVLGTYMALTTVLFFWLAHDTDFFSKTFGVRSIQGNEEELMAALYLQVSIISQALIFVTRSRSWSFVERPGFLLLIAFVIAQLVATLIAVYANWGFARIVGCGWGWAGGIWVYSIITYIPLDILKFIIRYALTGKAWDNMINQKTAFTTKKDYGKGEREAQWALAQRTLHGLPPPEAMFNDNKNELSEIAEQAKRRAEVARLRELHTLKGHVESVVKLKGLDIDTIQQHYTV
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
272PhosphorylationMYPIQHRTYRDGIDN
HCCCCCCCCCCCHHH
22.3015308754
294PhosphorylationGIPIAMPTVLSVTMA
CCCCCCHHHHHHHHH
22.4615308754
304PhosphorylationSVTMAIGSHRLSQQG
HHHHHHCCHHHHHCC
10.1829797451
318PhosphorylationGAITKRMTAIEEMAG
CCHHHHHHHHHHHHC
28.6319880383
331PhosphorylationAGMDVLCSDKTGTLT
HCCCEEECCCCCCEE
37.6719880383
343PhosphorylationTLTLNKLSVDKSLIE
CEEECCCCCCHHHHH
29.8519880383
347PhosphorylationNKLSVDKSLIEVFPK
CCCCCCHHHHHHCCC
30.0719880383
514PhosphorylationGVNVKMITGDQLAIG
CCCEEEECCCEEEEE
31.0717317660
524PhosphorylationQLAIGIETGRRLGMG
EEEEECCCCCCCCCC
33.7819880383
884PhosphorylationQWALAQRTLHGLPPP
HHHHHHHHHCCCCCC
15.83-
903PhosphorylationNDNKNELSEIAEQAK
CCCHHHHHHHHHHHH
22.3017317660
930PhosphorylationTLKGHVESVVKLKGL
HHHCHHHEEEEECCC
30.9917483306
947PhosphorylationDTIQQHYTV------
HHHHHHCCC------
20.02-

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 PMA8_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMA8_ARATH !!

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 PMA8_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HHP2_ARATHHHP2physical
24833385
HHP4_ARATHHHP4physical
24833385
UBC34_ARATHUBC34physical
24833385
UBC32_ARATHUBC32physical
24833385
SUB_ARATHSUBphysical
24833385
CNIH1_ARATHAT3G12180physical
24833385
CP21D_ARATHAT3G66654physical
24833385
SPCS1_ARATHAT2G22425physical
24833385
BET12_ARATHATBET12physical
24833385

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMA8_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Mol. Cell. Proteomics 2:1234-1243(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND MASSSPECTROMETRY.

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