dbPTM

PMA1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PMA1_SCHPO
UniProt AC	P09627
Protein Name	Plasma membrane ATPase 1
Gene Name	pma1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	919
Subcellular Localization	Cell membrane Multi-pass membrane protein.
Protein Description	The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses..
Protein Sequence	MADNAGEYHDAEKHAPEQQAPPPQQPAHAAAPAQDDEPDDDIDALIEELFSEDVQEEQEDNDDAPAAGEAKAVPEELLQTDMNTGLTMSEVEERRKKYGLNQMKEELENPFLKFIMFFVGPIQFVMEMAAALAAGLRDWVDFGVICALLMLNAVVGFVQEYQAGSIVDELKKSLALKAVVIREGQVHELEANEVVPGDILKLDEGTIICADGRVVTPDVHLQVDQSAITGESLAVDKHYGDPTFASSGVKRGEGLMVVTATGDSTFVGRAASLVNAAAGGTGHFTEVLNGIGTILLVLVLLTLFCIYTAAFYRSVRLARLLEYTLAITIIGVPVGLPAVVTTTMAVGAAYLAEKQAIVQKLSAIESLAGVEVLCSDKTGTLTKNKLSLGEPFTVSGVSGDDLVLTACLAASRKRKGLDAIDKAFLKALKNYPGPRSMLTKYKVIEFQPFDPVSKKVTAYVQAPDGTRITCVKGAPLWVLKTVEEDHPIPEDVLSAYKDKVGDLASRGYRSLGVARKIEGQHWEIMGIMPCSDPPRHDTARTISEAKRLGLRVKMLTGDAVDIAKETARQLGMGTNIYNAERLGLTGGGNMPGSEVYDFVEAADGFGEVFPQHKYAVVDILQQRGYLVAMTGDGVNDAPSLKKADTGIAVEGATDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYSYVVYRIALSLHLEIFLGLWLIIRNQLLNLELVVFIAIFADVATLAIAYDNAPYSMKPVKWNLPRLWGLSTVIGIVLAIGTWITNTTMIAQGQNRGIVQNFGVQDEVLFLEISLTENWLIFVTRCNGPFWSSIPSWQLSGAVLAVDILATMFCIFGWFKGGHQTSIVAVLRIWMYSFGIFCIMAGTYYILSESAGFDRMMNGKPKESRNQRSIEDLVVALQRTSTRHEKGDA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
51	Phosphorylation	ALIEELFSEDVQEEQ HHHHHHHCHHHHHHH	45.57	21712547
87	Phosphorylation	TDMNTGLTMSEVEER CCCCCCCCHHHHHHH	21.72	29996109
89	Phosphorylation	MNTGLTMSEVEERRK CCCCCCHHHHHHHHH	33.00	28889911
494	Phosphorylation	PIPEDVLSAYKDKVG CCCHHHHHHHHHHHH	29.42	28889911
496	Phosphorylation	PEDVLSAYKDKVGDL CHHHHHHHHHHHHHH	19.15	24763107
556	Phosphorylation	GLRVKMLTGDAVDIA CCEEEEHHCCHHHHH	29.53	25720772
593	Phosphorylation	GGGNMPGSEVYDFVE CCCCCCHHHHHHHHH	20.30	29996109
596	Phosphorylation	NMPGSEVYDFVEAAD CCCHHHHHHHHHHCC	10.30	29996109
899	Phosphorylation	KESRNQRSIEDLVVA CCCCCCCCHHHHHHH	22.14	28889911
910	Phosphorylation	LVVALQRTSTRHEKG HHHHHHHHCCCCCCC	22.84	25720772
911	Phosphorylation	VVALQRTSTRHEKGD HHHHHHHCCCCCCCC	26.15	25720772
912	Phosphorylation	VALQRTSTRHEKGDA HHHHHHCCCCCCCCC	35.12	25720772

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 PMA1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PMA1_SCHPO !!

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 PMA1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PMA2_SCHPO	pma2	genetic	1833395

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PMA1_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-494 AND SER-899,AND MASS SPECTROMETRY.	18257517 [Abstract]