Basic Information
Name | Outer spore wall assembly protein SHE10 (Sensitivity to high expression protein 10) |
Uniprot ID | P53075 |
Systematic gene name | YGL228W |
Standard gene name | SHE10 |
Gene names | SHE10 YGL228W |
Description from SGD | YGL228W SHE10 SGDID:S000003197, Chr VII from 67598-69331, Genome Release 64-3-1, Verified ORF, "Protein involved in outer spore wall assembly; likely involved directly in dityrosine layer assembly; putative GPI-anchored protein; overexpression causes growth arrest;; SWAT-GFP, seamless-GFP and mCherry fusion proteins localize to the endoplasmic reticulum; SHE10 has a paralog, OSW7/YFR039C, that arose from the whole genome duplication; paralogs are redundant for spore wall dityrosine assembly" |
Protein length | 577 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MGKLIKLITT LTVLVSLLQY CCEFNSGSIS CERTQTLCHY TNPRVWNTYF
SRNCELYKNK VSPGFDIVAR KYDTAVKPVI DDATVKVNKV AIQPAFKVIH
SQCKKWNCGK YYQLVRSPMV KTRRFFFAKY NAFVKPNLDK FFTAEFRSHL
KERILKYKNI GHYYFTITSR CIKSKYDFIV GNTEEKLMGK FKNKDTHGIH
GSVTREPSSE DMVLTVSTME SDEEELTTTS TQTVVETITL DQEEASAVAN
HAHDDEASTD VEGSTDVNVN EQALLQEDFD MWSETILQKT QDVIQLFEKD
VSKYINGKLV EEANHFKAKF QSLDDKSKKF FSKISLAIND IECVEGIDSE
TGKKIFFDKS GSTEISQYIT RELVREYFNE TRSTLDELTN AMEKDLSEIT
DEIEKKVNAI REENVEVFEE WGDIIVNEWS KRMAYVDVIN AHMGADDDTT
LDEEKAKSSV NWKKFLKGKK QIIESRDKLA HHSADLSRVN AFRQKVQKKI
LSFTQESGEF LYILRSKANL QFQERERKER ERKEREKAAA EEFQRQQELL
RQQEEEDEED VSYTSTSTIT TTITMTL
SRNCELYKNK VSPGFDIVAR KYDTAVKPVI DDATVKVNKV AIQPAFKVIH
SQCKKWNCGK YYQLVRSPMV KTRRFFFAKY NAFVKPNLDK FFTAEFRSHL
KERILKYKNI GHYYFTITSR CIKSKYDFIV GNTEEKLMGK FKNKDTHGIH
GSVTREPSSE DMVLTVSTME SDEEELTTTS TQTVVETITL DQEEASAVAN
HAHDDEASTD VEGSTDVNVN EQALLQEDFD MWSETILQKT QDVIQLFEKD
VSKYINGKLV EEANHFKAKF QSLDDKSKKF FSKISLAIND IECVEGIDSE
TGKKIFFDKS GSTEISQYIT RELVREYFNE TRSTLDELTN AMEKDLSEIT
DEIEKKVNAI REENVEVFEE WGDIIVNEWS KRMAYVDVIN AHMGADDDTT
LDEEKAKSSV NWKKFLKGKK QIIESRDKLA HHSADLSRVN AFRQKVQKKI
LSFTQESGEF LYILRSKANL QFQERERKER ERKEREKAAA EEFQRQQELL
RQQEEEDEED VSYTSTSTIT TTITMTL
Legend
- X Phoshorylation
- X Glycosylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[202, 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) |
[204, 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) |
[379, 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) |
[483, 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) |
[483, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |