| UniProt ID | NAP1_YEAST | |
|---|---|---|
| UniProt AC | P25293 | |
| Protein Name | Nucleosome assembly protein | |
| Gene Name | NAP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 417 | |
| Subcellular Localization | Cytoplasm. Nucleus. Bud neck. Phosphorylation by CK2 promotes the import into the nucleus. | |
| Protein Description | Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.. | |
| Protein Sequence | MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSDPIRTKP ------CCCCCCCCC | 52.69 | 27717283 | |
| 11 | Phosphorylation | PIRTKPKSSMQIDNA CCCCCCCCCCCCCCC | 39.30 | 22890988 | |
| 12 | Phosphorylation | IRTKPKSSMQIDNAP CCCCCCCCCCCCCCC | 22.34 | 22890988 | |
| 13 | Oxidation | RTKPKSSMQIDNAPT CCCCCCCCCCCCCCC | 5.37 | 15665377 | |
| 20 | Phosphorylation | MQIDNAPTPHNTPAS CCCCCCCCCCCCCHH | 34.47 | 22369663 | |
| 24 | Phosphorylation | NAPTPHNTPASVLNP CCCCCCCCCHHHCCH | 19.73 | 22369663 | |
| 27 | Phosphorylation | TPHNTPASVLNPSYL CCCCCCHHHCCHHHH | 28.48 | 22369663 | |
| 32 | Phosphorylation | PASVLNPSYLKNGNP CHHHCCHHHHHCCCC | 41.86 | 22890988 | |
| 33 | Phosphorylation | ASVLNPSYLKNGNPV HHHCCHHHHHCCCCC | 23.97 | 22890988 | |
| 35 | Acetylation | VLNPSYLKNGNPVRA HCCHHHHHCCCCCCH | 55.35 | 24489116 | |
| 50 | Acetylation | QAQEQDDKIGTINEE HHHHCCCCCCCCCHH | 51.85 | 24489116 | |
| 50 | Ubiquitination | QAQEQDDKIGTINEE HHHHCCCCCCCCCHH | 51.85 | 23749301 | |
| 53 | Phosphorylation | EQDDKIGTINEEDIL HCCCCCCCCCHHHHH | 24.89 | 28889911 | |
| 69 | Phosphorylation | NQPLLLQSIQDRLGS CCCHHHHHHHHHHHH | 23.37 | 23749301 | |
| 76 | Phosphorylation | SIQDRLGSLVGQDSG HHHHHHHHHHCCCCC | 25.19 | 22369663 | |
| 82 | Phosphorylation | GSLVGQDSGYVGGLP HHHHCCCCCCCCCCC | 24.92 | 19823750 | |
| 84 | Phosphorylation | LVGQDSGYVGGLPKN HHCCCCCCCCCCCCC | 10.40 | 22890988 | |
| 98 | Phosphorylation | NVKEKLLSLKTLQSE CHHHHHHCCHHHHHH | 37.95 | 28889911 | |
| 104 | Phosphorylation | LSLKTLQSELFEVEK HCCHHHHHHHHHHHH | 39.10 | 21440633 | |
| 127 | Acetylation | LENKFLQKYKPIWEQ HHHHHHHHHHCHHHH | 58.34 | 24489116 | |
| 136 | Phosphorylation | KPIWEQRSRIISGQE HCHHHHHHHHHCCCC | 27.76 | 24961812 | |
| 140 | Phosphorylation | EQRSRIISGQEQPKP HHHHHHHCCCCCCCH | 31.86 | 22369663 | |
| 159 | Phosphorylation | KGQEIVESLNETELL HHHHHHHHHCCCCEE | 26.12 | 29136822 | |
| 177 | Phosphorylation | EEKAQNDSEEEQVKG HHHHCCCCHHHHHCC | 55.23 | 22369663 | |
| 237 | Phosphorylation | KLLFRFDSSANPFFT EEEEEECCCCCCCCC | 28.74 | 30377154 | |
| 238 | Phosphorylation | LLFRFDSSANPFFTN EEEEECCCCCCCCCC | 33.63 | 30377154 | |
| 250 | Ubiquitination | FTNDILCKTYFYQKE CCCCEEEEHHHHCCC | 42.70 | 24961812 | |
| 397 | Phosphorylation | LEDDDGESAEEQDDF CCCCCCCCHHHHCCC | 46.65 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 159 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 159 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 177 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 177 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 397 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 397 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NAP1_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 NAP1_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 THR-20; THR-24; SER-27;SER-76; SER-82; SER-140 AND SER-177, AND MASS SPECTROMETRY. | |
| "Phosphorylation by casein kinase 2 regulates Nap1 localization andfunction."; Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,Pemberton L.F.; Mol. Cell. Biol. 28:1313-1325(2008). Cited for: FUNCTION, INTERACTION WITH RPL18A OR RPL18B; CKA2; CKI1; TEF1 OR TEF2;FOL1; HSC82; HTA2; HTB2; HTZ1; KAP114; KCC4; NIS1; SSA1; SSA2; SSB1;SSC1; SHM1; SIP5; TCO89 AND NBA1, SUBCELLULAR LOCATION, DISRUPTIONPHENOTYPE, PHOSPHORYLATION AT SER-82; SER-98; SER-104 AND SER-140,PHOSPHORYLATION AT SER-159; SER-177 AND SER-397 BY CK2, MUTAGENESIS OFLEU-99; SER-159; SER-177 AND SER-397, 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 THR-20; SER-140 AND SER-177,AND MASS 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 THR-20; THR-24; SER-27;SER-76 AND SER-177, 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 THR-20; THR-24 AND SER-76,AND MASS SPECTROMETRY. | |
