Basic Information
Name | Protein LAS1 |
Uniprot ID | P36146 |
Systematic gene name | YKR063C |
Standard gene name | LAS1 |
Gene names | LAS1 YKR063C |
Description from SGD | YKR063C LAS1 SGDID:S000001771, Chr XI from 562297-560789, Genome Release 64-3-1, reverse complement, Verified ORF, "Endonuclease involved in pre-rRNA processing at both ends of ITS2; functions with Grc3p in a conserved mechanism to cleave pre-rRNA at a specific site during rRNA processing and ribosome biogenesis; may coordinate the action of the Rat1p-Rai1p exoRNAse; required for the G1/S cell cycle transition; human ortholog is Las1L; mutants require the SSD1-v allele for viability" |
Protein length | 502 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MIPPRIVPWR DFAELEELKL WFYPKSKGTI EDKRQRAVQR VQSYRLKGSQ
YLPHVVDSTA QITCAVLLDE KEACLGVHQD SIPIRLSYVM ALIRFVNGLL
DPTQQSQFAI PLHTLAAKIG LPSWFVDLRH WGTHERDLPG LEMLRWAANE
ALSWLYDHYW NDEELEDDRD DDDDDDDTGY GYRRNDKLEK YMESLTKTLD
KWKRLRNEFL EYKWVWENAN DSLITSSNFS GDNLVNYDAE KRKSSHASSS
ETMIRENLRQ WQELWKLSIY HNVVLEKFFN NYDPLLLKVL MLNLNNFDWK
VIEWVARNYR TQQDDSNITT ILKRKFNAWK ELQKRLLDVI INNLNNKNFK
NKWQNWEKLI DENASYLILY FCQSMLAKLE TEKITGNSWR NKKRRKQIDS
TVEIEAKLKE NIDNLSLRFN EGEIKLYDFI PAEKDSVPLK KEVSPALKAD
TNDILGDLAS LKQRMSSFGT VGKKNKQEEN RATPVKNWSR VQNWKPKPFG
VL
YLPHVVDSTA QITCAVLLDE KEACLGVHQD SIPIRLSYVM ALIRFVNGLL
DPTQQSQFAI PLHTLAAKIG LPSWFVDLRH WGTHERDLPG LEMLRWAANE
ALSWLYDHYW NDEELEDDRD DDDDDDDTGY GYRRNDKLEK YMESLTKTLD
KWKRLRNEFL EYKWVWENAN DSLITSSNFS GDNLVNYDAE KRKSSHASSS
ETMIRENLRQ WQELWKLSIY HNVVLEKFFN NYDPLLLKVL MLNLNNFDWK
VIEWVARNYR TQQDDSNITT ILKRKFNAWK ELQKRLLDVI INNLNNKNFK
NKWQNWEKLI DENASYLILY FCQSMLAKLE TEKITGNSWR NKKRRKQIDS
TVEIEAKLKE NIDNLSLRFN EGEIKLYDFI PAEKDSVPLK KEVSPALKAD
TNDILGDLAS LKQRMSSFGT VGKKNKQEEN RATPVKNWSR VQNWKPKPFG
VL
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[230, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[230, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[230, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[230, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[244, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[245, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[444, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[444, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[444, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[444, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[444, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[467, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[467, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[483, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |