UniProt ID | LHP1_YEAST | |
---|---|---|
UniProt AC | P33399 | |
Protein Name | La protein homolog | |
Gene Name | LHP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 275 | |
Subcellular Localization | Nucleus . Imported into nucleus by the nuclear transport factor SXM1. | |
Protein Description | Molecular chaperone that binds nascent RNA polymerase III transcripts, stabilizing these RNAs against exonucleases. Required for the 3' endonucleolytic cleavage that matures tRNA precursors and for efficient folding of certain pre-tRNAs. Cooperaes with GCD14 in the maturation of a subset of RNA polymerase III transcripts. Functions also in the assembly of certain RNA polymerase II-transcribed RNAs into RNPs. Binds and stabilizes newly synthesized U6 snRNA as well as precursors of U3 snRNA from degradation. Facilitates efficient Sm protein binding, thus assisting formation of the U4/U6 snRNP. Required fot Ty3 normal transposition frequency.. | |
Protein Sequence | MSEKPQQEEQEKPQSRRNSFAVIEFTPEVLDRCLKQVEFYFSEFNFPYDRFLRTTAEKNDGWVPISTIATFNRMKKYRPVDKVIEALRSSEILEVSADGENVKRRVPLDLTAARNARIEQNQRTLAVMNFPHEDVEASQIPELQENLEAFFKKLGEINQVRLRRDHRNKKFNGTVLVEFKTIPECEAFLKSYSNDDESNEILSYEGKKLSVLTKKQFDLQREASKSKNFSGRSRSFNGHKKKNLPKFPKNKKKNGKEESKEDSSAIADDDEEHKE | |
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 | ------MSEKPQQEE ------CCCCHHHHH | 55.09 | 22369663 | |
2 | Acetylation | ------MSEKPQQEE ------CCCCHHHHH | 55.09 | 22814378 | |
15 | Phosphorylation | EEQEKPQSRRNSFAV HHHHCCCHHHHCEEE | 41.56 | 22369663 | |
19 | Phosphorylation | KPQSRRNSFAVIEFT CCCHHHHCEEEEEEC | 16.87 | 22369663 | |
26 | Phosphorylation | SFAVIEFTPEVLDRC CEEEEEECHHHHHHH | 13.02 | 20377248 | |
58 | Acetylation | FLRTTAEKNDGWVPI HHHHHCHHCCCEEEH | 58.85 | 24489116 | |
76 | Acetylation | ATFNRMKKYRPVDKV HCHHCCHHCCCHHHH | 36.83 | 25381059 | |
82 | Acetylation | KKYRPVDKVIEALRS HHCCCHHHHHHHHHC | 45.40 | 24489116 | |
103 | Ubiquitination | SADGENVKRRVPLDL CCCCCCCCCCCCCCH | 46.17 | 22817900 | |
104 | Methylation | ADGENVKRRVPLDLT CCCCCCCCCCCCCHH | 40.31 | 23865587 | |
153 | Ubiquitination | NLEAFFKKLGEINQV HHHHHHHHHHHHHHE | 57.47 | 23749301 | |
191 | Phosphorylation | ECEAFLKSYSNDDES HHHHHHHHCCCCCCC | 35.62 | 30377154 | |
193 | Phosphorylation | EAFLKSYSNDDESNE HHHHHHCCCCCCCCC | 40.65 | 30377154 | |
198 | Phosphorylation | SYSNDDESNEILSYE HCCCCCCCCCEEEEC | 46.92 | 27017623 | |
203 | Phosphorylation | DESNEILSYEGKKLS CCCCCEEEECCCEEE | 27.14 | 30377154 | |
207 | Acetylation | EILSYEGKKLSVLTK CEEEECCCEEEEEEH | 38.30 | 24489116 | |
207 | Succinylation | EILSYEGKKLSVLTK CEEEECCCEEEEEEH | 38.30 | 23954790 | |
215 | Acetylation | KLSVLTKKQFDLQRE EEEEEEHHHHHHHHH | 51.46 | 24489116 | |
225 | Acetylation | DLQREASKSKNFSGR HHHHHHHCCCCCCCC | 72.93 | 25381059 | |
227 | Acetylation | QREASKSKNFSGRSR HHHHHCCCCCCCCCC | 66.79 | 25381059 | |
230 | Phosphorylation | ASKSKNFSGRSRSFN HHCCCCCCCCCCCCC | 42.56 | 17287358 | |
233 | Phosphorylation | SKNFSGRSRSFNGHK CCCCCCCCCCCCCCC | 35.48 | 17287358 | |
235 | Phosphorylation | NFSGRSRSFNGHKKK CCCCCCCCCCCCCCC | 25.06 | 19823750 | |
240 | Acetylation | SRSFNGHKKKNLPKF CCCCCCCCCCCCCCC | 67.83 | 25381059 | |
246 | Acetylation | HKKKNLPKFPKNKKK CCCCCCCCCCCCCCC | 76.96 | 24489116 | |
259 | Phosphorylation | KKNGKEESKEDSSAI CCCCCCCCHHHHHCC | 42.30 | 29136822 | |
263 | Phosphorylation | KEESKEDSSAIADDD CCCCHHHHHCCCCCC | 23.82 | 25521595 | |
264 | Phosphorylation | EESKEDSSAIADDDE CCCHHHHHCCCCCCH | 35.70 | 25521595 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of LHP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LHP1_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 LHP1_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-15 AND SER-19, AND MASSSPECTROMETRY. | |
"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-19, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-19; SER-230;SER-233 AND SER-235, 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 SER-19, 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-19, AND MASSSPECTROMETRY. | |
"Phosphorylation of the Saccharomyces cerevisiae La protein does notappear to be required for its functions in tRNA maturation and nascentRNA stabilization."; Long K.S., Cedervall T., Walch-Solimena C., Noe D.A., Huddleston M.J.,Annan R.S., Wolin S.L.; RNA 7:1589-1602(2001). Cited for: PHOSPHORYLATION AT SER-15; SER-19 AND SER-235, MASS SPECTROMETRY,FUNCTION, AND MUTAGENESIS OF SER-15; SER-19 AND SER-235. |