UniProt ID | SRPR_YEAST | |
---|---|---|
UniProt AC | P32916 | |
Protein Name | Signal recognition particle receptor subunit alpha homolog | |
Gene Name | SRP101 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 621 | |
Subcellular Localization |
Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side . Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain. |
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Protein Description | Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. GTP hydrolysis may enhance the fidelity of and provide unidirectionality to the targeting reaction. It is important but not essential for cell growth. May be directly involved in mitochondrial protein import.. | |
Protein Sequence | MFDQLAVFTPQGQVLYQYNCLGKKFSEIQINSFISQLITSPVTRKESVANANTDGFDFNLLTINSEHKNSPSFNALFYLNKQPELYFVVTFAEQTLELNQETQQTLALVLKLWNSLHLSESILKNRQGQNEKNKHNYVDILQGIEDDLKKFEQYFRIKYEESIKQDHINPDNFTKNGSVPQSHNKNTKKKLRDTKGKKQSTGNVGSGRKWGRDGGMLDEMNHEDAAKLDFSSSNSHNSSQVALDSTINKDSFGDRTEGGDFLIKEIDDLLSSHKDEITSGNEAKNSGYVSTAFGFLQKHVLGNKTINESDLKSVLEKLTQQLITKNVAPEAADYLTQQVSHDLVGSKTANWTSVENTARESLTKALTQILTPGVSVDLLREIQSKRSKKDEEGKCDPYVFSIVGVNGVGKSTNLSKLAFWLLQNNFKVLIVACDTFRSGAVEQLRVHVENLAQLMDDSHVRGSKNKRGKTGNDYVELFEAGYGGSDLVTKIAKQAIKYSRDQNFDIVLMDTAGRRHNDPTLMSPLKSFADQAKPDKIIMVGEALVGTDSVQQAKNFNDAFGKGRNLDFFIISKCDTVGEMLGTMVNMVYATGIPILFVGVGQTYTDLRTLSVKWAVNTLMS | |
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 |
---|---|---|---|---|---|
53 | Phosphorylation | ESVANANTDGFDFNL HHHHCCCCCCCCEEE | 34.78 | 19779198 | |
72 | Phosphorylation | SEHKNSPSFNALFYL CCCCCCCCCEEEEEC | 30.84 | 19779198 | |
78 | Phosphorylation | PSFNALFYLNKQPEL CCCEEEEECCCCCEE | 15.37 | 19779198 | |
158 | Acetylation | FEQYFRIKYEESIKQ HHHHHHHHHHHHHCC | 42.21 | 24489116 | |
164 | Acetylation | IKYEESIKQDHINPD HHHHHHHCCCCCCCC | 59.98 | 24489116 | |
174 | Phosphorylation | HINPDNFTKNGSVPQ CCCCCCCCCCCCCCC | 29.83 | 21551504 | |
178 | Phosphorylation | DNFTKNGSVPQSHNK CCCCCCCCCCCCCCC | 39.76 | 21440633 | |
200 | Phosphorylation | DTKGKKQSTGNVGSG CCCCCCCCCCCCCCC | 47.35 | 28889911 | |
201 | Phosphorylation | TKGKKQSTGNVGSGR CCCCCCCCCCCCCCC | 30.22 | 27017623 | |
206 | Phosphorylation | QSTGNVGSGRKWGRD CCCCCCCCCCCCCCC | 31.01 | 27717283 | |
231 | Phosphorylation | DAAKLDFSSSNSHNS HHHHCCCCCCCCCCC | 32.30 | 22369663 | |
232 | Phosphorylation | AAKLDFSSSNSHNSS HHHCCCCCCCCCCCC | 33.27 | 22369663 | |
233 | Phosphorylation | AKLDFSSSNSHNSSQ HHCCCCCCCCCCCCC | 40.95 | 22369663 | |
235 | Phosphorylation | LDFSSSNSHNSSQVA CCCCCCCCCCCCCEE | 26.45 | 22369663 | |
238 | Phosphorylation | SSSNSHNSSQVALDS CCCCCCCCCCEEEEC | 19.41 | 22369663 | |
239 | Phosphorylation | SSNSHNSSQVALDST CCCCCCCCCEEEECC | 33.71 | 22369663 | |
245 | Phosphorylation | SSQVALDSTINKDSF CCCEEEECCCCCCCC | 31.85 | 22369663 | |
246 | Phosphorylation | SQVALDSTINKDSFG CCEEEECCCCCCCCC | 28.39 | 22369663 | |
251 | Phosphorylation | DSTINKDSFGDRTEG ECCCCCCCCCCCCCC | 32.51 | 19779198 | |
271 | Phosphorylation | KEIDDLLSSHKDEIT HHHHHHHHHCCCCCC | 37.38 | 25521595 | |
272 | Phosphorylation | EIDDLLSSHKDEITS HHHHHHHHCCCCCCC | 34.23 | 27214570 | |
274 | Acetylation | DDLLSSHKDEITSGN HHHHHHCCCCCCCCC | 60.03 | 24489116 | |
278 | Phosphorylation | SSHKDEITSGNEAKN HHCCCCCCCCCCHHH | 28.65 | 19823750 | |
279 | Phosphorylation | SHKDEITSGNEAKNS HCCCCCCCCCCHHHC | 45.33 | 21440633 | |
298 | Acetylation | TAFGFLQKHVLGNKT HHHHHHHHHHHCCCC | 37.52 | 24489116 | |
304 | Acetylation | QKHVLGNKTINESDL HHHHHCCCCCCHHHH | 49.32 | 24489116 | |
312 | Acetylation | TINESDLKSVLEKLT CCCHHHHHHHHHHHH | 43.43 | 24489116 | |
317 | Acetylation | DLKSVLEKLTQQLIT HHHHHHHHHHHHHHH | 53.31 | 24489116 | |
367 | Phosphorylation | ESLTKALTQILTPGV HHHHHHHHHHHCCCC | 20.58 | 27017623 | |
371 | Phosphorylation | KALTQILTPGVSVDL HHHHHHHCCCCCHHH | 21.45 | 27017623 | |
375 | Phosphorylation | QILTPGVSVDLLREI HHHCCCCCHHHHHHH | 18.81 | 27017623 | |
520 | Phosphorylation | GRRHNDPTLMSPLKS CCCCCCCCCCHHHHH | 37.65 | 19779198 | |
523 | Phosphorylation | HNDPTLMSPLKSFAD CCCCCCCHHHHHHHH | 30.14 | 23749301 | |
527 | Phosphorylation | TLMSPLKSFADQAKP CCCHHHHHHHHHCCC | 33.09 | 19779198 |
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 SRPR_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SRPR_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 SRPR_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-231; SER-232; SER-233;SER-235; SER-238; SER-239 AND SER-523, AND MASS SPECTROMETRY. |