Basic Information

NameMitochondrial distribution and morphology protein 38
Uniprot IDQ08179
Systematic gene nameYOL027C
Standard gene nameMDM38
Gene namesMDM38 YOL027C
Description from SGDYOL027C MDM38 SGDID:S000005387, Chr XV from 273724-272003, Genome Release 64-3-1, reverse complement, Verified ORF, "Membrane-associated mitochondrial ribosome receptor; forms a complex with Mba1p to facilitate recruitment of mRNA-specific translational activators to ribosomes; ribosome-associated protein involved in the insertion of newly synthesized proteins into the mitochondrial inner membrane; role in protein export and K+/H+ exchange; localizes to the inner mitochondrial membrane; human ortholog Letm1 implicated in Wolf-Hirschhorn syndrome"
Protein length573
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLNFASRASC VTRRQASLYF VKNQGPRLIA STIPSCHWPL RAQGVQPNYP
LSLRFYSTDK SKSVTKPVAP TSTDAPAKPK ETLMVKVKHA LKHYANGTKL
LGYEIKVSTK LLIKFAQGYE LSRRERNQLR RTMGDVFRLI PFSAFLIIPF
AELFLPFALK LFPNLLPSTY ESGKDKQAKR NKLIEIRKKT SEFLHETLEE
SNLITYNTIE NAEKKQKFLN FFRKLYSAKE GKIMTFQHDE ISAIAQMFKN
DSVLDNLSRP QLAAMSKFMS LRPFGNDNML RYQIRSKLKD IMNDDKTIDY
EGVESLSQEE LYQACVSRGM KAYGVSKEDL VDNLKVWLEL RLRQKIPSVL
MVLSSTFTFG GLPKENYSKA FSPLAEKKET KSKYDDLLDL YYDGILQVLS
SIPDPVYNVA KLDVSESKSS AAETEAEKQV AEKKIKTEEK PEETAIPKEE
ATAKESVIAT TASAVTPKLV VVNEKAETAK TEEISQEKEN AEPTDSAEAT
EAEEKKTSDD NEFKLNVLKE QEELIKKEEE EAKQRASREH VPDDINLDEE
EEAKSVPPIP ADQAAKTFVI KKD

Legend

  • X Phoshorylation
  • X K-Succinylation
  • X Ubiquitination
  • X Multiple modifications
  • X SUMOylation

Structure

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


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References

[63, 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)
[63, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[66, 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)
[182, 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)
[369, 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)
[418, 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)
[428, 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)
[428, 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)
[436, 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)
[444, 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)
[444, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[461, 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)
[488, 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)