Basic Information
Name | Cell wall protein YJL171C |
Uniprot ID | P46992 |
Systematic gene name | YJL171C |
Standard gene name | YJR1 |
Gene names | YJR1 YJL171C J0512 |
Description from SGD | YJL171C TOH1 SGDID:S000003707, Chr X from 100894-99704, Genome Release 64-3-1, reverse complement, Verified ORF, "GPI-anchored cell wall protein of unknown function; induced in response to cell wall damaging agents and by mutations in genes involved in cell wall biogenesis; sequence similarity to YBR162C/TOS1, a covalently bound cell wall protein; protein abundance increases in response to DNA replication stress" |
Protein length | 396 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLQSIVLSVC MFMLHTVAAS GPQSYQKLDF TNVGFTGSYV DVNKFKDITN
NESCTCEVGD RVWFSGKNAP LADYLSVHFR GPLKLKQFAF YTSPGFTVNN
SRSSSDWNRL AYYESSSKTA DNVTFLNHGG EASPCLGNAL SYASSNGTGS
ASEATVLADG TLISSDQEYI IYSNVSCPKS GYDKGCGVYR SGIPAYYGYG
GTTKMFLFEF EMPTETEKNS SSIGYYDLPA IWLLNDHIAR TSQYPTNANC
SCWASGCGEY DIFEAMNGTE KNHLYSTFHT FQGIEDLGTG IQSYGYITRN
TTGTMKGGVV FDSSGNVVSF ISDATPFNGT VSADTVNDLL AAIPENETYS
SQLMSISATA PSTTSKSNGV ALTKMQNGVW YYILAIFTAF TQVVLI
NESCTCEVGD RVWFSGKNAP LADYLSVHFR GPLKLKQFAF YTSPGFTVNN
SRSSSDWNRL AYYESSSKTA DNVTFLNHGG EASPCLGNAL SYASSNGTGS
ASEATVLADG TLISSDQEYI IYSNVSCPKS GYDKGCGVYR SGIPAYYGYG
GTTKMFLFEF EMPTETEKNS SSIGYYDLPA IWLLNDHIAR TSQYPTNANC
SCWASGCGEY DIFEAMNGTE KNHLYSTFHT FQGIEDLGTG IQSYGYITRN
TTGTMKGGVV FDSSGNVVSF ISDATPFNGT VSADTVNDLL AAIPENETYS
SQLMSISATA PSTTSKSNGV ALTKMQNGVW YYILAIFTAF TQVVLI
Legend
- X Glycosylation
- X Ubiquitination
- 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
[51, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[122, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[146, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[184, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[191, 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) |
[219, Glyc] | Poljak, K., Selevsek, N., Ngwa, E., Grossmann, J., Losfeld, M.E., Aebi, M. (2018). Quantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae. Mol Cell Proteomics 17: 18-30. (Publication) (All modifications) |
[219, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[249, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[300, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[328, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[346, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |