| UniProt ID | KRI1_YEAST | |
|---|---|---|
| UniProt AC | P42846 | |
| Protein Name | Protein KRI1 | |
| Gene Name | KRI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 591 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA.. | |
| Protein Sequence | MPRKKSAAKRAREQAKKEAAVPATDTATIKTSETSATTVKPAIEASKSYVPSEDEEEDEEEEEEEDDYGELITDEVENGINQVLDAIKNNKTDKLLDPKVKFFEDPESAAAKLANREGKHKPIYLKDYHRMNILSGDALKEDDEEYEHATVDGKQSFVSQQREEKTQLLNEIKSAFSDEENEESSGDEDDGFLKKKEPSTKKEGKNLPDPTVNEENFLEEFVNQQAWIPKKGDKVISLDLNNNEEDDEEFEDAAEKFENAYNFRYEDPNAAEIISYARSQATLRRSDDSSRRRKREEKRKIKEQIKAEKETALQKKKTKKLNKLTDILEQLTKEYGAEINADMVKKITDTLLKNDFKEEEWDNVVAELFNEEFYQQEGKPTWNEDDEIMGDFYADADGDDQTEEGEVEKEQKEEDEEEGPKRKKSKKEEKLQKKKEKRKVNELVENALEQNKLALIEEVEKEEEERKSRSRTKEEQDLKFRYREVSPESFGLTAREIFAADDTDLNEFIGLKKFAPYRSKELRAKDKRKVMKARRLREWRKKTFKNENGLAPVEAEAGEKDEDTILIPVEKASKSKHKRGHSHKHKGHQKK | |
| 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 |
|---|---|---|---|---|---|
| 26 | Phosphorylation | AAVPATDTATIKTSE HCCCCCCCCEEECCC | 22.73 | 21551504 | |
| 31 | Phosphorylation | TDTATIKTSETSATT CCCCEEECCCCCCCC | 28.13 | 27017623 | |
| 34 | Phosphorylation | ATIKTSETSATTVKP CEEECCCCCCCCCHH | 24.35 | 21440633 | |
| 35 | Phosphorylation | TIKTSETSATTVKPA EEECCCCCCCCCHHH | 21.40 | 23749301 | |
| 94 | Acetylation | IKNNKTDKLLDPKVK HHCCCCCCCCCCCCC | 57.06 | 25381059 | |
| 101 | Acetylation | KLLDPKVKFFEDPES CCCCCCCCCCCCHHH | 50.92 | 24489116 | |
| 112 | Acetylation | DPESAAAKLANREGK CHHHHHHHHHCCCCC | 43.32 | 24489116 | |
| 126 | Acetylation | KHKPIYLKDYHRMNI CCCCCCCCCHHHCCC | 38.99 | 25381059 | |
| 156 | Phosphorylation | ATVDGKQSFVSQQRE CCCCCCHHHHHHHHH | 30.97 | 30377154 | |
| 159 | Phosphorylation | DGKQSFVSQQREEKT CCCHHHHHHHHHHHH | 20.70 | 30377154 | |
| 174 | Phosphorylation | QLLNEIKSAFSDEEN HHHHHHHHHCCCCCC | 39.96 | 22890988 | |
| 177 | Phosphorylation | NEIKSAFSDEENEES HHHHHHCCCCCCCCC | 43.77 | 22369663 | |
| 184 | Phosphorylation | SDEENEESSGDEDDG CCCCCCCCCCCCCCC | 33.18 | 22369663 | |
| 185 | Phosphorylation | DEENEESSGDEDDGF CCCCCCCCCCCCCCC | 54.25 | 22369663 | |
| 323 | Acetylation | KKTKKLNKLTDILEQ HHHHHHHHHHHHHHH | 64.30 | 24489116 | |
| 348 | Phosphorylation | ADMVKKITDTLLKND HHHHHHHHHHHHHCC | 31.63 | 28132839 | |
| 482 | Phosphorylation | EQDLKFRYREVSPES HHHHHHHHHCCCHHH | 17.79 | 17330950 | |
| 486 | Phosphorylation | KFRYREVSPESFGLT HHHHHCCCHHHHCCC | 20.42 | 22369663 | |
| 489 | Phosphorylation | YREVSPESFGLTARE HHCCCHHHHCCCHHH | 28.18 | 22890988 | |
| 493 | Phosphorylation | SPESFGLTAREIFAA CHHHHCCCHHHHHHC | 24.85 | 22890988 | |
| 503 | Phosphorylation | EIFAADDTDLNEFIG HHHHCCCCCHHHHCC | 42.82 | 28152593 | |
| 512 | Acetylation | LNEFIGLKKFAPYRS HHHHCCCHHCCCCCC | 40.40 | 24489116 | |
| 560 | Acetylation | VEAEAGEKDEDTILI CEECCCCCCCCEEEE | 66.55 | 24489116 |
| 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 KRI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KRI1_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 KRI1_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-177; SER-184; TYR-482;SER-486 AND SER-489, 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-486 AND SER-489, 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-177; SER-184; SER-185AND SER-486, 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-486, AND MASSSPECTROMETRY. | |
