UniProt ID | MRL1_YEAST | |
---|---|---|
UniProt AC | Q06815 | |
Protein Name | Mannose 6-phosphate receptor-like protein 1 | |
Gene Name | MRL1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 381 | |
Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Single-pass type I membrane protein. Endosome membrane Single-pass type I membrane protein. |
|
Protein Description | Sorting receptor involved in the transport of vacuolar enzymes from the Golgi complex to the vacuole. Involved in the delivery and maturation of PEP4 (vacuolar proteinase A) and PRB1 (vacuolar proteinase B).. | |
Protein Sequence | MLKRSSLIYLSCVLIITIPILLHVYNGPGLSHEANEHRASHKQKRTLANPDKPKSENDEDLFCAVTNPVTGSYIDLSQLSSTPNKLREGQKQISGNNKHESSKTKWSVRGWGYDTNFTLGICSSPVGEAESQQLSNLTGAFYVDQLNENNLVSIGDFSTRPALVGGSTAKKLTLKYENGSMCPNGKDKKATLLNFVCDKEIQSKAQISYIGNLHNCSYFFEVRSIHACPTSNKKNEVNVLGIFIGIFAIFFLVEFAGRRWIYAKLNRHLKNDDELHDISPSLNEQPHWDLIEDGSRWSKFFNGIIKTTRRFTKSLMRSLVRGRNSRQGGIRLRSSPSASSSSLANREFFRDMEAQNEIIDSLDINSHTTESDHPTLADNSV | |
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 |
---|---|---|---|---|---|
77 | Phosphorylation | TGSYIDLSQLSSTPN CCCEECHHHCCCCCC | 25.90 | 28889911 | |
116 | N-linked_Glycosylation | RGWGYDTNFTLGICS EECCCCCCEEEEEEC | 25.63 | - | |
136 | N-linked_Glycosylation | AESQQLSNLTGAFYV HHHHHHHHCCCCEEE | 50.65 | - | |
178 | N-linked_Glycosylation | KLTLKYENGSMCPNG CEEEEEECCCCCCCC | 44.76 | - | |
215 | N-linked_Glycosylation | SYIGNLHNCSYFFEV EECCCCCCCEEEEEE | 21.42 | - | |
279 | Phosphorylation | DDELHDISPSLNEQP CHHHHCCCCCCCCCC | 17.94 | 22369663 | |
281 | Phosphorylation | ELHDISPSLNEQPHW HHHCCCCCCCCCCCC | 36.72 | 22369663 | |
299 | Acetylation | EDGSRWSKFFNGIIK CCCCHHHHHHHHHHH | 47.19 | 24489116 | |
306 | Acetylation | KFFNGIIKTTRRFTK HHHHHHHHHHHHHHH | 41.76 | 24489116 | |
314 | Phosphorylation | TTRRFTKSLMRSLVR HHHHHHHHHHHHHHC | 25.08 | 26447709 | |
318 | Phosphorylation | FTKSLMRSLVRGRNS HHHHHHHHHHCCCCC | 19.76 | 27017623 | |
325 | Phosphorylation | SLVRGRNSRQGGIRL HHHCCCCCCCCCEEE | 25.31 | 30377154 | |
334 | Phosphorylation | QGGIRLRSSPSASSS CCCEEEECCCCCCCC | 51.71 | 22369663 | |
335 | Phosphorylation | GGIRLRSSPSASSSS CCEEEECCCCCCCCH | 19.21 | 22369663 | |
337 | Phosphorylation | IRLRSSPSASSSSLA EEEECCCCCCCCHHH | 42.61 | 22369663 | |
339 | Phosphorylation | LRSSPSASSSSLANR EECCCCCCCCHHHCH | 34.78 | 22369663 | |
340 | Phosphorylation | RSSPSASSSSLANRE ECCCCCCCCHHHCHH | 24.54 | 22369663 | |
341 | Phosphorylation | SSPSASSSSLANREF CCCCCCCCHHHCHHH | 27.20 | 22369663 | |
342 | Phosphorylation | SPSASSSSLANREFF CCCCCCCHHHCHHHH | 33.19 | 22369663 | |
361 | Phosphorylation | AQNEIIDSLDINSHT HHHHHHHHCCCCCCC | 19.96 | 19779198 | |
366 | Phosphorylation | IDSLDINSHTTESDH HHHCCCCCCCCCCCC | 23.65 | 19779198 | |
368 | Phosphorylation | SLDINSHTTESDHPT HCCCCCCCCCCCCCC | 31.89 | 19779198 | |
371 | Phosphorylation | INSHTTESDHPTLAD CCCCCCCCCCCCCCC | 38.84 | 28889911 | |
375 | Phosphorylation | TTESDHPTLADNSV- CCCCCCCCCCCCCC- | 31.03 | 19779198 | |
380 | Phosphorylation | HPTLADNSV------ CCCCCCCCC------ | 29.74 | 28889911 |
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 MRL1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MRL1_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 MRL1_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-334; SER-335; SER-337;SER-339; SER-340; SER-371 AND SER-380, AND MASS 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-335 AND SER-337, ANDMASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-339 ANDSER-342, AND MASS 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-335 AND SER-339, ANDMASS SPECTROMETRY. |