UniProt ID | ATC6_YEAST | |
---|---|---|
UniProt AC | P39986 | |
Protein Name | Manganese-transporting ATPase 1 | |
Gene Name | SPF1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1215 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis.. | |
Protein Sequence | MTKKSFVSSPIVRDSTLLVPKSLIAKPYVLPFFPLYATFAQLYFQQYDRYIKGPEWTFVYLGTLVSLNILVMLMPAWNVKIKAKFNYSTTKNVNEATHILIYTTPNNGSDGIVEIQRVTEAGSLQTFFQFQKKRFLWHENEQVFSSPKFLVDESPKIGDFQKCKGHSGDLTHLKRLYGENSFDIPIPTFMELFKEHAVAPLFVFQVFCVALWLLDEFWYYSLFNLFMIISMEAAAVFQRLTALKEFRTMGIKPYTINVFRNKKWVALQTNELLPMDLVSITRTAEESAIPCDLILLDGSAIVNEAMLSGESTPLLKESIKLRPSEDNLQLDGVDKIAVLHGGTKALQVTPPEHKSDIPPPPDGGALAIVTKTGFETSQGSLVRVMIYSAERVSVDNKEALMFILFLLIFAVIASWYVWVEGTKMGRIQSKLILDCILIITSVVPPELPMELTMAVNSSLAALAKFYVYCTEPFRIPFAGRIDVCCFDKTGTLTGEDLVFEGLAGISADSENIRHLYSAAEAPESTILVIGAAHALVKLEDGDIVGDPMEKATLKAVGWAVERKNSNYREGTGKLDIIRRFQFSSALKRSASIASHNDALFAAVKGAPETIRERLSDIPKNYDEIYKSFTRSGSRVLALASKSLPKMSQSKIDDLNRDDVESELTFNGFLIFHCPLKDDAIETIKMLNESSHRSIMITGDNPLTAVHVAKEVGIVFGETLILDRAGKSDDNQLLFRDVEETVSIPFDPSKDTFDHSKLFDRYDIAVTGYALNALEGHSQLRDLLRHTWVYARVSPSQKEFLLNTLKDMGYQTLMCGDGTNDVGALKQAHVGIALLNGTEEGLKKLGEQRRLEGMKMMYIKQTEFMARWNQPQPPVPEPIAHLFPPGPKNPHYLKALESKGTVITPEIRKAVEEANSKPVEVIKPNGLSEKKPADLASLLLNSAGDAQGDEAPALKLGDASCAAPFTSKLANVSAVTNIIRQGRCALVNTIQMYKILALNCLISAYSLSIIYMAGVKFGDGQATVSGLLLSVCFLSISRGKPLEKLSKQRPQSGIFNVYIMGSILSQFAVHIATLVYITTEIYKLEPREPQVDLEKEFAPSLLNTGIFIIQLVQQVSTFAVNYQGEPFRENIRSNKGMYYGLLGVTGLALASATEFLPELNEAMKFVPMTDDFKIKLTLTLLLDFFGSWGVEHFFKFFFMDDKPSDISVQQVKIASK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
156 | Acetylation | FLVDESPKIGDFQKC EEECCCCCCCCCHHC | 69.47 | 24489116 | |
244 | Acetylation | FQRLTALKEFRTMGI HHHHHHHHHHHHCCC | 52.95 | 24489116 | |
320 | Acetylation | PLLKESIKLRPSEDN HHHHHHHCCCCCCCC | 47.96 | 24489116 | |
335 | Acetylation | LQLDGVDKIAVLHGG CCCCCCCEEEEEECC | 30.11 | 24489116 | |
354 | Acetylation | QVTPPEHKSDIPPPP EECCCCCCCCCCCCC | 48.43 | 24489116 | |
550 | Acetylation | IVGDPMEKATLKAVG CCCCHHHHHHHHHHH | 40.18 | 24489116 | |
573 | Acetylation | NYREGTGKLDIIRRF CCCCCCCCCHHHHHH | 42.71 | 24489116 | |
587 | Acetylation | FQFSSALKRSASIAS HHHCHHHHHHHHHHC | 43.98 | 24489116 | |
619 | Acetylation | ERLSDIPKNYDEIYK HHHHHCCCCHHHHHH | 69.35 | 24489116 | |
619 | Succinylation | ERLSDIPKNYDEIYK HHHHHCCCCHHHHHH | 69.35 | 23954790 | |
749 | Acetylation | SIPFDPSKDTFDHSK CCCCCCCCCCCCCHH | 67.20 | 24489116 | |
797 | Acetylation | ARVSPSQKEFLLNTL EECCHHHHHHHHHHH | 55.56 | 24489116 | |
842 | Acetylation | NGTEEGLKKLGEQRR CCCHHHHHHHHHHHH | 57.73 | 24489116 | |
887 | Acetylation | HLFPPGPKNPHYLKA HCCCCCCCCHHHHHH | 84.64 | 24489116 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ATC6_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATC6_YEAST !! |
* 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 ATC6_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-936, ANDMASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936, AND MASSSPECTROMETRY. |