UniProt ID | NPR2_YEAST | |
---|---|---|
UniProt AC | P39923 | |
Protein Name | Nitrogen permease regulator 2 | |
Gene Name | NPR2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 615 | |
Subcellular Localization |
Vacuole membrane Peripheral membrane protein . |
|
Protein Description | Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. Mediates inactivation of the TORC1 complex in response to amino acid starvation. Post-transcriptional regulator of nitrogen permeases. May be involved in putative NPR1-dependent phosphorylation of nitrogen permeases or in the processing and targeting of nitrogen permeases at the level of the endoplasmic reticulum. Involved in cell kill provoked by cisplatin and doxorubicin.. | |
Protein Sequence | MLSYFQGFVPIHTIFYSVFHPTEGSKIKYEFPPNNLKNHGINFNTFKNYIIPKPILCHKLITFKYGTYRIVCYPVTINSPIYARNFFSFNFVFVFPYDCETSPYEPAITRLGKMFKVLEEQNQLLSKSERDPVFFDLKVLENSTTTPSTAGPSSTPNPSSNTTPTHPTSEKDTKDMRSSRYSDLIKDLGLPQSAFSIQDLLMRIFQDLNNYSECLIPIDEGNAVDIKIFPLLRPPTTCVSLEDVPLSSVNLKKIIDVNWDPTMMSIVPYIDGLNSIAKISKLSNSDPGLVIECIRHLIYYKCVTLSDIFQFSNIYAPSSLIRNFLTDPLMASDCQSYVTFPEVSKISNLPLNKSLGSGDQDSPSFSVRRKSKSSSIPSNPDSRTTSFSSTSRVSQNSSLNSSFSSIYKDWRQSQTSCSSSNIHVINNRNRFLPTRSCLFDLYRSLSQGQTLKTWYESKYMILKENNIDIRRFITFGLEKRIIYRCYSFPVMINAGSREPKEMTPIITKDLVNNDKLLEKRNHNHLLSATGSRNTAQSGNLKPERPSKVSFEMQRVSSLATGKSTMPKLSDEEEGILEESIRNAETFDKICVLLSKPKLEVESYLNELGEFKVINS | |
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 |
---|---|---|---|---|---|
143 | Phosphorylation | DLKVLENSTTTPSTA EEEEEECCCCCCCCC | 20.11 | 24961812 | |
144 | Phosphorylation | LKVLENSTTTPSTAG EEEEECCCCCCCCCC | 46.39 | 23749301 | |
145 | Phosphorylation | KVLENSTTTPSTAGP EEEECCCCCCCCCCC | 36.21 | 23749301 | |
146 | Phosphorylation | VLENSTTTPSTAGPS EEECCCCCCCCCCCC | 18.48 | 23749301 | |
148 | Phosphorylation | ENSTTTPSTAGPSST ECCCCCCCCCCCCCC | 28.88 | 23749301 | |
149 | Phosphorylation | NSTTTPSTAGPSSTP CCCCCCCCCCCCCCC | 36.52 | 21440633 | |
153 | Phosphorylation | TPSTAGPSSTPNPSS CCCCCCCCCCCCCCC | 46.02 | 23749301 | |
154 | Phosphorylation | PSTAGPSSTPNPSSN CCCCCCCCCCCCCCC | 51.52 | 23749301 | |
155 | Phosphorylation | STAGPSSTPNPSSNT CCCCCCCCCCCCCCC | 31.27 | 20377248 | |
159 | Phosphorylation | PSSTPNPSSNTTPTH CCCCCCCCCCCCCCC | 42.75 | 20377248 | |
162 | Phosphorylation | TPNPSSNTTPTHPTS CCCCCCCCCCCCCCC | 35.78 | 20377248 | |
163 | Phosphorylation | PNPSSNTTPTHPTSE CCCCCCCCCCCCCCH | 30.36 | 23749301 | |
165 | Phosphorylation | PSSNTTPTHPTSEKD CCCCCCCCCCCCHHH | 38.09 | 23749301 | |
171 | Ubiquitination | PTHPTSEKDTKDMRS CCCCCCHHHCCHHHH | 71.16 | 24961812 | |
178 | Phosphorylation | KDTKDMRSSRYSDLI HHCCHHHHHHHHHHH | 16.72 | 30377154 | |
181 | Phosphorylation | KDMRSSRYSDLIKDL CHHHHHHHHHHHHHC | 14.42 | 23749301 | |
182 | Phosphorylation | DMRSSRYSDLIKDLG HHHHHHHHHHHHHCC | 25.49 | 20377248 | |
347 | Phosphorylation | FPEVSKISNLPLNKS CCCHHHCCCCCCCCC | 35.73 | 28889911 | |
353 | Ubiquitination | ISNLPLNKSLGSGDQ CCCCCCCCCCCCCCC | 55.53 | 24961812 | |
354 | Phosphorylation | SNLPLNKSLGSGDQD CCCCCCCCCCCCCCC | 36.57 | 22369663 | |
357 | Phosphorylation | PLNKSLGSGDQDSPS CCCCCCCCCCCCCCC | 44.48 | 22369663 | |
362 | Phosphorylation | LGSGDQDSPSFSVRR CCCCCCCCCCCEEEE | 19.46 | 22369663 | |
364 | Phosphorylation | SGDQDSPSFSVRRKS CCCCCCCCCEEEECC | 33.82 | 22369663 | |
366 | Phosphorylation | DQDSPSFSVRRKSKS CCCCCCCEEEECCCC | 21.03 | 22369663 | |
371 | Phosphorylation | SFSVRRKSKSSSIPS CCEEEECCCCCCCCC | 35.64 | 19779198 | |
373 | Phosphorylation | SVRRKSKSSSIPSNP EEEECCCCCCCCCCC | 36.09 | 22369663 | |
374 | Phosphorylation | VRRKSKSSSIPSNPD EEECCCCCCCCCCCC | 35.70 | 22369663 | |
375 | Phosphorylation | RRKSKSSSIPSNPDS EECCCCCCCCCCCCC | 45.68 | 22369663 | |
378 | Phosphorylation | SKSSSIPSNPDSRTT CCCCCCCCCCCCCCC | 60.36 | 22369663 | |
382 | Phosphorylation | SIPSNPDSRTTSFSS CCCCCCCCCCCCCCC | 32.55 | 22369663 | |
398 | Phosphorylation | SRVSQNSSLNSSFSS CCCCCCCCCCHHHHH | 38.84 | 27214570 | |
415 | Phosphorylation | KDWRQSQTSCSSSNI HHHHHHHCCCCCCCE | 36.63 | 19779198 | |
416 | Phosphorylation | DWRQSQTSCSSSNIH HHHHHHCCCCCCCEE | 12.36 | 19779198 | |
418 | Phosphorylation | RQSQTSCSSSNIHVI HHHHCCCCCCCEEEE | 36.25 | 23749301 | |
419 | Phosphorylation | QSQTSCSSSNIHVIN HHHCCCCCCCEEEEC | 31.56 | 23749301 | |
420 | Phosphorylation | SQTSCSSSNIHVINN HHCCCCCCCEEEECC | 24.41 | 23749301 | |
503 | Phosphorylation | SREPKEMTPIITKDL CCCCCCCCCCCCHHH | 16.66 | 25752575 | |
507 | Phosphorylation | KEMTPIITKDLVNND CCCCCCCCHHHHCCH | 21.16 | 21551504 | |
549 | Phosphorylation | PERPSKVSFEMQRVS CCCCCCCEEEEEEHH | 21.16 | 21440633 | |
556 | Phosphorylation | SFEMQRVSSLATGKS EEEEEEHHHHHCCCC | 23.09 | 22369663 | |
557 | Phosphorylation | FEMQRVSSLATGKST EEEEEHHHHHCCCCC | 21.11 | 22369663 | |
560 | Phosphorylation | QRVSSLATGKSTMPK EEHHHHHCCCCCCCC | 50.89 | 22369663 | |
563 | Phosphorylation | SSLATGKSTMPKLSD HHHHCCCCCCCCCCH | 31.14 | 22369663 | |
564 | Phosphorylation | SLATGKSTMPKLSDE HHHCCCCCCCCCCHH | 40.76 | 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 NPR2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NPR2_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 NPR2_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-362, AND MASSSPECTROMETRY. |