| UniProt ID | NRP1_YEAST | |
|---|---|---|
| UniProt AC | P32770 | |
| Protein Name | Asparagine-rich protein | |
| Gene Name | NRP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 719 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MHYVVLELQVAHLPDTPKDQCRIANIAFQIVNAETLVCHYGTNSLPSIEVNGTTKSLESAMVQLDKDIHDVIGNDDFVLVSLYSTWHIRVTLPRQARDDGFILTSYLQHPKVFDLWKEFDRWCVNHPEILGQKKAISNNNCNTKSISINAAKNTKDLDEIVRILEVSIPTEEAGSVPEIYSLLKRTTDILIQLHKKCTSPEDMESVLTKPYDSHTDIRAFLQEKSKILYMNNLPPDTTQSELESWFTQYGVRPVGFWTVKNIVEDTSNVNNNWSLNNSPYVEDQDSISGFVVFQTHEEATEVLALNGRSILSNLANTKQPRVVEHVLELQPSSTGVLDKAQEILSPFPQSKNKPRPGDWNCPSCGFSNFQRRTACFRCSFPAPSNSQIHTANSNNNVNSSRNNLNNRVNSGSSSNISNTAANHPYGAPEFNMIANNTPAALTYNRAHFPAITPLSRQNSLNMAPSNSGSPIIIADHFSGNNNIAPNYRYNNNINNNNNNINNMTNNRYNINNNINGNGNGNGNNSNNNNNHNNNHNNNHHNGSINSNSNTNNNNNNNNGNNSNNCNSNIGMGGCGSNMPFRAGDWKCSTCTYHNFAKNVVCLRCGGPKSISGDASETNHYIDSSTFGPASRTPSNNNISVNTNGGSNAGRTDGNDNKGRDISLMEFMSPPLSMATKSMKEGDGNGSSFNEFKSDKANVNFSNVGDNSAFGNGFNSSIRW | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 339 | Ubiquitination | SSTGVLDKAQEILSP CCCCHHHHHHHHHCC | 48.05 | 15699485 | |
| 345 | Phosphorylation | DKAQEILSPFPQSKN HHHHHHHCCCCCCCC | 30.10 | 21551504 | |
| 351 | Ubiquitination | LSPFPQSKNKPRPGD HCCCCCCCCCCCCCC | 64.84 | 15699485 | |
| 384 | Phosphorylation | RCSFPAPSNSQIHTA EECCCCCCCCCCCCC | 51.74 | 19779198 | |
| 393 | Phosphorylation | SQIHTANSNNNVNSS CCCCCCCCCCCCCCC | 38.17 | 19779198 | |
| 410 | Phosphorylation | NLNNRVNSGSSSNIS CCCCCCCCCCCCCCC | 36.88 | 21440633 | |
| 412 | Phosphorylation | NNRVNSGSSSNISNT CCCCCCCCCCCCCCC | 30.34 | 28889911 | |
| 414 | Phosphorylation | RVNSGSSSNISNTAA CCCCCCCCCCCCCCC | 39.62 | 25752575 | |
| 417 | Phosphorylation | SGSSSNISNTAANHP CCCCCCCCCCCCCCC | 32.17 | 23749301 | |
| 419 | Phosphorylation | SSSNISNTAANHPYG CCCCCCCCCCCCCCC | 21.98 | 30377154 | |
| 425 | Phosphorylation | NTAANHPYGAPEFNM CCCCCCCCCCCCHHC | 20.54 | 28889911 | |
| 437 | Phosphorylation | FNMIANNTPAALTYN HHCCCCCCCCHHEEC | 17.70 | 30377154 | |
| 452 | Phosphorylation | RAHFPAITPLSRQNS HHHCCCCCCCCCCCC | 21.93 | 22369663 | |
| 455 | Phosphorylation | FPAITPLSRQNSLNM CCCCCCCCCCCCCCC | 32.78 | 22369663 | |
| 459 | Phosphorylation | TPLSRQNSLNMAPSN CCCCCCCCCCCCCCC | 16.87 | 25752575 | |
| 465 | Phosphorylation | NSLNMAPSNSGSPII CCCCCCCCCCCCCEE | 33.80 | 19779198 | |
| 467 | Phosphorylation | LNMAPSNSGSPIIIA CCCCCCCCCCCEEEE | 45.01 | 23749301 | |
| 469 | Phosphorylation | MAPSNSGSPIIIADH CCCCCCCCCEEEEEC | 16.85 | 23749301 | |
| 478 | Phosphorylation | IIIADHFSGNNNIAP EEEEECCCCCCCCCC | 36.87 | 30377154 | |
| 630 | Phosphorylation | SSTFGPASRTPSNNN CCCCCCCCCCCCCCC | 39.56 | 25704821 | |
| 632 | Phosphorylation | TFGPASRTPSNNNIS CCCCCCCCCCCCCEE | 28.68 | 22369663 | |
| 634 | Phosphorylation | GPASRTPSNNNISVN CCCCCCCCCCCEEEE | 52.13 | 22369663 | |
| 639 | Phosphorylation | TPSNNNISVNTNGGS CCCCCCEEEECCCCC | 16.07 | 19779198 | |
| 651 | Phosphorylation | GGSNAGRTDGNDNKG CCCCCCCCCCCCCCC | 47.55 | 27017623 | |
| 668 | Phosphorylation | ISLMEFMSPPLSMAT CCHHHHCCCCHHHHC | 28.78 | 28889911 | |
| 686 | Phosphorylation | KEGDGNGSSFNEFKS CCCCCCCCCHHHHHC | 35.44 | 30377154 | |
| 687 | Phosphorylation | EGDGNGSSFNEFKSD CCCCCCCCHHHHHCC | 33.23 | 30377154 |
| 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 NRP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NRP1_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 NRP1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-345; SER-455 ANDSER-634, 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-455, 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-455, AND MASSSPECTROMETRY. | |
| "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-345, AND MASSSPECTROMETRY. | |