Basic Information
Name | A-factor-processing enzyme (EC 3.4.24.-) (Insulin-degrading enzyme homolog) |
Uniprot ID | Q06010 |
Systematic gene name | YLR389C |
Standard gene name | STE23 |
Gene names | STE23 YLR389C L8084.12 |
Description from SGD | YLR389C STE23 SGDID:S000004381, Chr XII from 902660-899577, Genome Release 64-3-1, reverse complement, Verified ORF, "Metalloprotease; involved in N-terminal processing of pro-a-factor to mature form; expressed in both haploids and diploids; one of two yeast homologs of human insulin-degrading enzyme (hIDE); homolog Axl1p is also involved in processing of pro-a-factor" |
Protein length | 1027 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MGVSLLASSS AFVTKPLLTQ LVHLSPISLN FTVRRFKPFT CLSRYYTTNP
YNMTSNFKTF NLDFLKPDLD ERSYRFIELP NKLKALLIQD PKADKAAASL
DVNIGAFEDP KNLPGLAHFC EHLLFMGSEK FPDENEYSSY LSKHGGSSNA
YTASQNTNYF FEVNHQHLFG ALDRFSGFFS CPLFNKDSTD KEINAVNSEN
KKNLQNDIWR IYQLDKSLTN TKHPYHKFST GNIETLGTLP KENGLNVRDE
LLKFHKNFYS ANLMKLCILG REDLDTLSDW TYDLFKDVAN NGREVPLYAE
PIMQPEHLQK IIQVRPVKDL KKLEISFTVP DMEEHWESKP PRILSHLIGH
EGSGSLLAHL KKLGWANELS AGGHTVSKGN AFFAVDIDLT DNGLTHYRDV
IVLIFQYIEM LKNSLPQKWI FNELQDISNA TFKFKQAGSP SSTVSSLAKC
LEKDYIPVSR ILAMGLLTKY EPDLLTQYTD ALVPENSRVT LISRSLETDS
AEKWYGTAYK VVDYPADLIK NMKSPGLNPA LTLPRPNEFV STNFKVDKID
GIKPLDEPVL LLSDDVSKLW YKKDDRFWQP RGYIYLSFKL PHTHASIINS
MLSTLYTQLA NDALKDVQYD AACADLRISF NKTNQGLAIT ASGFNEKLII
LLTRFLQGVN SFEPKKDRFE ILKDKTIRHL KNLLYEVPYS QMSNYYNAII
NERSWSTAEK LQVFEKLTFE QLINFIPTIY EGVYFETLIH GNIKHEEALE
VDSLIKSLIP NNIHNLQVSN NRLRSYLLPK GKTFRYETAL KDSQNVNSCI
QHVTQLDVYS EDLSALSGLF AQLIHEPCFD TLRTKEQLGY VVFSSSLNNH
GTANIRILIQ SEHTTPYLEW RINNFYETFG QVLRDMPEED FEKHKEALCN
SLLQKFKNMA EESARYTAAI YLGDYNFTHR QKKAKLVANI TKQQMIDFYE
NYIMSENASK LILHLKSQVE NKELNENELD TAKYPTGQLI EDVGAFKSTL
FVAPVRQPMK DFEISAPPKL NNSSESE
YNMTSNFKTF NLDFLKPDLD ERSYRFIELP NKLKALLIQD PKADKAAASL
DVNIGAFEDP KNLPGLAHFC EHLLFMGSEK FPDENEYSSY LSKHGGSSNA
YTASQNTNYF FEVNHQHLFG ALDRFSGFFS CPLFNKDSTD KEINAVNSEN
KKNLQNDIWR IYQLDKSLTN TKHPYHKFST GNIETLGTLP KENGLNVRDE
LLKFHKNFYS ANLMKLCILG REDLDTLSDW TYDLFKDVAN NGREVPLYAE
PIMQPEHLQK IIQVRPVKDL KKLEISFTVP DMEEHWESKP PRILSHLIGH
EGSGSLLAHL KKLGWANELS AGGHTVSKGN AFFAVDIDLT DNGLTHYRDV
IVLIFQYIEM LKNSLPQKWI FNELQDISNA TFKFKQAGSP SSTVSSLAKC
LEKDYIPVSR ILAMGLLTKY EPDLLTQYTD ALVPENSRVT LISRSLETDS
AEKWYGTAYK VVDYPADLIK NMKSPGLNPA LTLPRPNEFV STNFKVDKID
GIKPLDEPVL LLSDDVSKLW YKKDDRFWQP RGYIYLSFKL PHTHASIINS
MLSTLYTQLA NDALKDVQYD AACADLRISF NKTNQGLAIT ASGFNEKLII
LLTRFLQGVN SFEPKKDRFE ILKDKTIRHL KNLLYEVPYS QMSNYYNAII
NERSWSTAEK LQVFEKLTFE QLINFIPTIY EGVYFETLIH GNIKHEEALE
VDSLIKSLIP NNIHNLQVSN NRLRSYLLPK GKTFRYETAL KDSQNVNSCI
QHVTQLDVYS EDLSALSGLF AQLIHEPCFD TLRTKEQLGY VVFSSSLNNH
GTANIRILIQ SEHTTPYLEW RINNFYETFG QVLRDMPEED FEKHKEALCN
SLLQKFKNMA EESARYTAAI YLGDYNFTHR QKKAKLVANI TKQQMIDFYE
NYIMSENASK LILHLKSQVE NKELNENELD TAKYPTGQLI EDVGAFKSTL
FVAPVRQPMK DFEISAPPKL NNSSESE
Legend
- X K-Succinylation
- X Phoshorylation
- X Ubiquitination
- X Multiple modifications
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[92, K-succ] | Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications) |
[92, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[229, 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) |
[229, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (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] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[439, 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) |
[439, 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) |
[439, 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) |
[439, 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) |
[439, 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) |
[439, 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) |
[439, Phos] | 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) |
[439, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[449, 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) |
[490, 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) |
[495, 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) |
[524, 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) |
[524, 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) |
[972, 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) |
[983, 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) |
[983, SUMO] | Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications) |
[1024, 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) |
[1026, 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) |
[1026, 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) |
[1026, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |