Basic Information

NameProtein VMS1 (VCP/CDC48-associated mitochondrial stress-responsive protein 1)
Uniprot IDQ04311
Systematic gene nameYDR049W
Standard gene nameVMS1
Gene namesVMS1 YDR049W
Description from SGDYDR049W VMS1 SGDID:S000002456, Chr IV from 553254-555152, Genome Release 64-3-1, Verified ORF, "Peptidyl-tRNA hydrolase that releases stalled peptides from ribosomes, component of a Cdc48p-complex; involved in protein quality control; exhibits cytosolic and ER-membrane localization; contributes to ER-associated degradation (ERAD) of specific substrates at a step after their ubiquitination; translocates to mitochondria under oxidative stress and forms a complex with Cdc48p and Npl4p that is required for ubiquitin-mediated mitochondria-associated protein degradation (MAD)"
Protein length632
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MNSQKASKMT GSLKKNDLYI FDLSEQLLNS LKLMSFDSTL REVEVEKTSD
NDRNKESGDL QIARKKVTSN VMRCSVCQMS FDSRNEQKAH YQTDYHLMNV
KRNLRGLDIL SVEEFDALIS KEHGIKSEDE NSGGEQTSSD HEESEEASDR
DPDLQTNNYM ETIIENDLQK LGFQKDESDA ISHINTQSPY IYFKSKYLQK
NEVLAIYKSL FNKRSLSNPN EALTFWNSQE NPMAISALFM VGGGHFAGAI
VSHQRLNVKG NAHKKDETLI EQAVNFLEHK TFHRYTTRRK QGGSQSAMDN
AKGKANSAGS ALRRYNESAL KTDIQGVLKD WEPYLSKCDN IFIRARNVSD
KKIFTDNTVL NKGDERIKSF PFTTNRPTVL ELKKAWCELS YLKILPKPEP
LAVKETVQKL EVSNKKDEFK EKQEPLLEEI QTEEIISLLK KGRAPLLISF
LKKNKLDGNF RLKPESKYSL TPTMLHYASQ QGMKQMALIL LSNIKCDPTI
KNRLGRTAWD LNRNDDVRHA FQIARYNLGE SFTNWDETHI GQPLSREQVD
EINEKKKAIE NEKAEKLIKL ELEAAKEKQR FAKDAERGPG KKLTNIPSIQ
QQNLNSLTDE QRRRLMREQR ARAAEERMKK KY

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

[48, 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)
[49, 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)
[57, 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)
[57, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[139, 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)
[139, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[349, 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)
[349, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[355, 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)
[355, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[592, 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)