UniProt ID | ATC3_YEAST | |
---|---|---|
UniProt AC | P39524 | |
Protein Name | Probable phospholipid-transporting ATPase DRS2 | |
Gene Name | DRS2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1355 | |
Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Multi-pass membrane protein . |
|
Protein Description | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly.. | |
Protein Sequence | MNDDRETPPKRKPGEDDTLFDIDFLDDTTSHSGSRSKVTNSHANANYIPPSHVLPEETIDLDADDDNIENDVHENLFMSNNHDDQTSWNANRFDSDAYQPQSLRAVKPPGLFARFGNGLKNAFTFKRKKGPESFEMNHYNAVTNNELDDNYLDSRNKFNIKILFNRYILRKNVGDAEGNGEPRVIHINDSLANSSFGYSDNHISTTKYNFATFLPKFLFQEFSKYANLFFLCTSAIQQVPHVSPTNRYTTIGTLLVVLIVSAMKECIEDIKRANSDKELNNSTAEIFSEAHDDFVEKRWIDIRVGDIIRVKSEEPIPADTIILSSSEPEGLCYIETANLDGETNLKIKQSRVETAKFIDVKTLKNMNGKVVSEQPNSSLYTYEGTMTLNDRQIPLSPDQMILRGATLRNTAWIFGLVIFTGHETKLLRNATATPIKRTAVEKIINRQIIALFTVLIVLILISSIGNVIMSTADAKHLSYLYLEGTNKAGLFFKDFLTFWILFSNLVPISLFVTVELIKYYQAFMIGSDLDLYYEKTDTPTVVRTSSLVEELGQIEYIFSDKTGTLTRNIMEFKSCSIAGHCYIDKIPEDKTATVEDGIEVGYRKFDDLKKKLNDPSDEDSPIINDFLTLLATCHTVIPEFQSDGSIKYQAASPDEGALVQGGADLGYKFIIRKPNSVTVLLEETGEEKEYQLLNICEFNSTRKRMSAIFRFPDGSIKLFCKGADTVILERLDDEANQYVEATMRHLEDYASEGLRTLCLAMRDISEGEYEEWNSIYNEAATTLDNRAEKLDEAANLIEKNLILIGATAIEDKLQDGVPETIHTLQEAGIKIWVLTGDRQETAINIGMSCRLLSEDMNLLIINEETRDDTERNLLEKINALNEHQLSTHDMNTLALVIDGKSLGFALEPELEDYLLTVAKLCKAVICCRVSPLQKALVVKMVKRKSSSLLLAIGDGANDVSMIQAAHVGVGISGMEGMQAARSADIAVGQFKFLKKLLLVHGSWSYQRISVAILYSFYKNTALYMTQFWYVFANAFSGQSIMESWTMSFYNLFFTVWPPFVIGVFDQFVSSRLLERYPQLYKLGQKGQFFSVYIFWGWIINGFFHSAIVFIGTILIYRYGFALNMHGELADHWSWGVTVYTTSVIIVLGKAALVTNQWTKFTLIAIPGSLLFWLIFFPIYASIFPHANISREYYGVVKHTYGSGVFWLTLIVLPIFALVRDFLWKYYKRMYEPETYHVIQEMQKYNISDSRPHVQQFQNAIRKVRQVQRMKKQRGFAFSQAEEGGQEKIVRMYDTTQKRGKYGELQDASANPFNDNNGLGSNDFESAEPFIENPFADGNQNSNRFSSSRDDISFDI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MNDDRETPPKRKPG -CCCCCCCCCCCCCC | 45.87 | 28889911 | |
18 | Phosphorylation | RKPGEDDTLFDIDFL CCCCCCCCCEEEEEC | 41.46 | 22369663 | |
28 | Phosphorylation | DIDFLDDTTSHSGSR EEEECCCCCCCCCCC | 29.84 | 22369663 | |
29 | Phosphorylation | IDFLDDTTSHSGSRS EEECCCCCCCCCCCC | 31.28 | 22369663 | |
30 | Phosphorylation | DFLDDTTSHSGSRSK EECCCCCCCCCCCCC | 20.11 | 22369663 | |
32 | Phosphorylation | LDDTTSHSGSRSKVT CCCCCCCCCCCCCCC | 37.93 | 22369663 | |
34 | Phosphorylation | DTTSHSGSRSKVTNS CCCCCCCCCCCCCCC | 36.07 | 19779198 | |
36 | Phosphorylation | TSHSGSRSKVTNSHA CCCCCCCCCCCCCCC | 32.92 | 24961812 | |
95 | Phosphorylation | WNANRFDSDAYQPQS CCCCCCCCCCCCCCC | 22.79 | 30377154 | |
102 | Phosphorylation | SDAYQPQSLRAVKPP CCCCCCCCHHCCCCC | 26.89 | 28889911 | |
120 | Acetylation | ARFGNGLKNAFTFKR HCCCCCHHCCCCCCC | 47.86 | 24489116 | |
133 | Phosphorylation | KRKKGPESFEMNHYN CCCCCCCCCCCCCCC | 29.64 | 27017623 | |
139 | Phosphorylation | ESFEMNHYNAVTNNE CCCCCCCCCCCCCCC | 10.38 | 27017623 | |
143 | Phosphorylation | MNHYNAVTNNELDDN CCCCCCCCCCCCCCC | 29.89 | 27017623 | |
535 | Ubiquitination | DLDLYYEKTDTPTVV CCEEEEECCCCCCEE | 35.26 | 17644757 | |
536 | Phosphorylation | LDLYYEKTDTPTVVR CEEEEECCCCCCEEE | 32.92 | 28889911 | |
544 | Phosphorylation | DTPTVVRTSSLVEEL CCCCEEECHHHHHHH | 15.85 | 28889911 | |
556 | Phosphorylation | EELGQIEYIFSDKTG HHHCCCEEEEECCCC | 14.64 | 28889911 | |
559 | Phosphorylation | GQIEYIFSDKTGTLT CCCEEEEECCCCCEE | 28.74 | 28889911 | |
561 | Ubiquitination | IEYIFSDKTGTLTRN CEEEEECCCCCEEEE | 47.89 | 17644757 | |
725 | Phosphorylation | LFCKGADTVILERLD EEECCCCEEEEEECC | 14.65 | 27017623 | |
738 | Phosphorylation | LDDEANQYVEATMRH CCHHHHHHHHHHHHH | 10.48 | 27017623 | |
742 | Phosphorylation | ANQYVEATMRHLEDY HHHHHHHHHHHHHHH | 10.96 | 27017623 | |
900 | Ubiquitination | LALVIDGKSLGFALE EEEEECCEECCCCCC | 38.47 | 17644757 | |
919 | Ubiquitination | DYLLTVAKLCKAVIC HHHHHHHHHHCHHHH | 50.51 | 17644757 | |
1287 | Ubiquitination | AEEGGQEKIVRMYDT HHCCCCEEEEEEEEC | 38.32 | 23749301 | |
1297 | Ubiquitination | RMYDTTQKRGKYGEL EEEECCCCCCCCCCC | 62.11 | 23749301 | |
1345 | Phosphorylation | NQNSNRFSSSRDDIS CCCCCCCCCCCCCCC | 24.94 | 22369663 | |
1346 | Phosphorylation | QNSNRFSSSRDDISF CCCCCCCCCCCCCCC | 27.04 | 22369663 | |
1347 | Phosphorylation | NSNRFSSSRDDISFD CCCCCCCCCCCCCCC | 38.23 | 22369663 | |
1352 | Phosphorylation | SSSRDDISFDI---- CCCCCCCCCCC---- | 24.70 | 22369663 |
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 ATC3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATC3_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 ATC3_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-102 AND SER-1347, ANDMASS SPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352, AND MASSSPECTROMETRY. |