UniProt ID | TAPT1_YEAST | |
---|---|---|
UniProt AC | P40085 | |
Protein Name | Endoplasmic reticulum membrane protein 65 {ECO:0000305|PubMed:23275891} | |
Gene Name | EMP65 {ECO:0000303|PubMed:23275891} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 556 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Mitochondrion . |
|
Protein Description | May be involved in membrane protein folding.. | |
Protein Sequence | MQHKDTAVAKDTAKKRLLRRNSAPSAIHIISRLDKKWSFLWNTIDRHNIVEEQDESSAAKSEEEHEDDYELEQLLNMIRIPMFLEKFMLFALLTSLDCFLYYFTVLPIRLIKGYVKQFKSYRQHYRLQQRSGHKNKIPFRYRITSREYKERCMIFIIVISSILLSKLDTSKLYHRIKRQSTMKLYMLFSVLEMADKMLASLGQSLLTVMLSRKNSERILLHKCLLVSMSLTYVTIHGYVLVYQAISLNIAVNSYSNALLTLLLSMQFAEIKSSVLKKFDKEGFFQITIADVVERFKLTLLLSITGLRNLQSWSSSLSNTSINFWSPRSTLSIVINILCGPMVSVVGSEVLVDWAKHAYITKFNRIRPQIYDKFYYIIYKDYSTRTHKLEDRLGLPLPAFVVLFIVMVRPTLFKSSEPSYLPSLFRILFMGASVFLLALLAKFTLDLILIKWSKRIEQRFRDQAFNTVVTEEEYVPGLLSGGMGKVDVSTRIALHSDYNKENRIETESVSPMRKRKTTLTAECTPPSLNDIRRQKDSKNPRSLENVARYKMVSKRIW | |
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 |
---|---|---|---|---|---|
22 | Phosphorylation | KRLLRRNSAPSAIHI HHHHHHCCCCCHHHH | 39.48 | 17330950 | |
180 | Phosphorylation | YHRIKRQSTMKLYML HHHHHHHHHHHHHHH | 34.21 | 28889911 | |
181 | Phosphorylation | HRIKRQSTMKLYMLF HHHHHHHHHHHHHHH | 15.24 | 28889911 | |
185 | Phosphorylation | RQSTMKLYMLFSVLE HHHHHHHHHHHHHHH | 6.05 | 27017623 | |
189 | Phosphorylation | MKLYMLFSVLEMADK HHHHHHHHHHHHHHH | 23.10 | 28889911 | |
200 | Phosphorylation | MADKMLASLGQSLLT HHHHHHHHHHHHHHH | 29.13 | 19779198 | |
211 | Phosphorylation | SLLTVMLSRKNSERI HHHHHHHHCCCCHHH | 24.10 | 27017623 | |
314 | Phosphorylation | RNLQSWSSSLSNTSI CCHHHHHHHCCCCEE | 29.10 | 24930733 | |
317 | Phosphorylation | QSWSSSLSNTSINFW HHHHHHCCCCEECCC | 39.75 | 24930733 | |
318 | N-linked_Glycosylation | SWSSSLSNTSINFWS HHHHHCCCCEECCCC | 43.04 | - | |
325 | Phosphorylation | NTSINFWSPRSTLSI CCEECCCCCCHHHHH | 13.29 | 24930733 | |
432 | Phosphorylation | RILFMGASVFLLALL HHHHHHHHHHHHHHH | 13.99 | 27017623 | |
509 | Phosphorylation | RIETESVSPMRKRKT CCCCCCCCCCCCCCC | 23.43 | 21440633 |
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 TAPT1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TAPT1_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 TAPT1_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-22, AND MASSSPECTROMETRY. | |
"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-22, AND MASSSPECTROMETRY. |