Basic Information
Name | tRNA-splicing endonuclease subunit SEN2 (EC 4.6.1.16) (Splicing endonuclease protein 2) (tRNA-intron endonuclease SEN2) |
Uniprot ID | P16658 |
Systematic gene name | YLR105C |
Standard gene name | SEN2 |
Gene names | SEN2 YLR105C L8004.12 |
Description from SGD | YLR105C SEN2 SGDID:S000004095, Chr XII from 348180-347047, Genome Release 64-3-1, reverse complement, Verified ORF, "Subunit of the tRNA splicing endonuclease; tRNA splicing endonuclease (Sen complex) is composed of Sen2p, Sen15p, Sen34p, and Sen54p; Sen complex also cleaves the CBP1 mRNA at the mitochondrial surface; Sen2p contains the active site for tRNA 5' splice site cleavage and has similarity to Sen34p and to Archaeal tRNA splicing endonuclease;" |
Protein length | 377 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSKGRVNQKR YKYPLPIHPV DDLPELILHN PLSWLYWAYR YYKSTNALND
KVHVDFIGDT TLHITVQDDK QMLYLWNNGF FGTGQFSRSE PTWKARTEAR
LGLNDTPLHN RGGTKSNTET EMTLEKVTQQ RRLQRLEFKK ERAKLERELL
ELRKKGGHID EENILLEKQR ESLRKFKLKQ TEDVGIVAQQ QDISESNLRD
EDNNLLDENG DLLPLESLEL MPVEAMFLTF ALPVLDISPA CLAGKLFQFD
AKYKDIHSFV RSYVIYHHYR SHGWCVRSGI KFGCDYLLYK RGPPFQHAEF
CVMGLDHDVS KDYTWYSSIA RVVGGAKKTF VLCYVERLIS EQEAIALWKS
NNFTKLFNSF QVGEVLYKRW VPGRNRD
KVHVDFIGDT TLHITVQDDK QMLYLWNNGF FGTGQFSRSE PTWKARTEAR
LGLNDTPLHN RGGTKSNTET EMTLEKVTQQ RRLQRLEFKK ERAKLERELL
ELRKKGGHID EENILLEKQR ESLRKFKLKQ TEDVGIVAQQ QDISESNLRD
EDNNLLDENG DLLPLESLEL MPVEAMFLTF ALPVLDISPA CLAGKLFQFD
AKYKDIHSFV RSYVIYHHYR SHGWCVRSGI KFGCDYLLYK RGPPFQHAEF
CVMGLDHDVS KDYTWYSSIA RVVGGAKKTF VLCYVERLIS EQEAIALWKS
NNFTKLFNSF QVGEVLYKRW VPGRNRD
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
[106, 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) |
[106, 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) |
[116, Phos] | Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications) |
[116, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[118, 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) |