Basic Information

NameUncharacterized protein YGR266W
Uniprot IDP53326
Systematic gene nameYGR266W
Standard gene nameYGR266W
Gene namesYGR266W
Description from SGDYGR266W YGR266W SGDID:S000003498, Chr VII from 1022656-1024761, Genome Release 64-3-1, Verified ORF, "Protein of unknown function; predicted to contain a single transmembrane domain; mutant has increased aneuploidy tolerance; localized to both the mitochondrial outer membrane and the plasma membrane; protein abundance increases in response to DNA replication stress"
Protein length701
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MHATNWFDDW NPEALYRDDV TGCDDCSETS PIPKSGIICG PILRLINMDF
KEKTYEGSIM VVVRGEENFP KITYQLGPSL PSEDEDIEVN EAFFEGKLFH
KDILKDDNIW FYRYEIKLPM SNYEQMVKYA VDGTMEPHYR FFVPSFTQNS
NVISYSCNGF SLSVDTSKFK GSLWYDVLKK HRYVHYHAIL GGGDQIYSDN
IKLHAPNLKA WLETKDPIKK YNTQTTEETK EQIRQFYLEH YLNWYGYGHW
YGSTPKSKTT QKCFVKSLAC IPAINVWDDH DIIDGYGSYN DSFMKTENFL
TVGRMAYRYY MLFQQHVSAS KQDGDEYAYL KSKQWILGNE KGSSYIGERS
HSIFSWLGPK MAMLGLDCRT ERKLHEIFSE RSYSLIWERV EREIKNLKGG
HLLLMLGIPI AYPRLVWLEW LFTSKLLAPI KYLSKKGIFA SGFVNEFNGD
VELLDDLNDH WCARHHKKER NYLIMKLQDI GAKYGVRITI LSGDVHLASV
GRFRAKIHRH HLIMSEEKEK ENTRIIEEPT KDVRLIFNII ASAIVNTPPP
DAMATLLQKR CRLHHFDLET DEDAVPIFAK EVDGVHKRKE SCFMNKRNWS
DIIPIENLLN NPQLSKELGV KVGDIVIPGI ITEQQKLQKL ENDDQINSYP
VTSGGLFTTI HVERDANQTN SQTVSYCLPI PELTVTCERL SHKGIKHLNI
T

Legend

  • X Phoshorylation
  • X Ubiquitination

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[27, 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)
[27, 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)
[27, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[30, 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)
[30, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[34, 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)
[531, 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)
[591, 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)