Basic Information

NamePeptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (Cyclophilin D) (Rotamase D)
Uniprot IDP35176
Systematic gene nameYDR304C
Standard gene nameCPR5
Gene namesCPR5 CYP5 CYPD YDR304C D9740.14
Description from SGDYDR304C CPR5 SGDID:S000002712, Chr IV from 1072557-1071880, Genome Release 64-3-1, reverse complement, Verified ORF, "Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication"
Protein length225
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MKLQFFSFIT LFACLFTTAI FAKEDTAEDP EITHKVYFDI NHGDKQIGRI
VMGLYGLTTP QTVENFYQLT ISRDPKMGYL NSIFHRVIPN FMIQGGDFTH
RSGIGGKSIF GNTFKDENFD VKHDKPGRLS MANRGKNTNG SQFFITTVPC
PWLDGKHVVF GEVLDGMDVV HYIENVKTDS RNMPVKEVII VESGELETVP
LDNKDAAKLQ EEIKAEASEA AHDEL

Legend

  • X Phoshorylation
  • X SUMOylation
  • X Glycosylation

Structure

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


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References

[33, 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)
[82, 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)
[108, 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)
[115, 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)
[139, Glyc]Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[204, 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)
[214, 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)
[218, 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)
[218, 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)
[218, Phos]Smolka, M.B., Albuquerque, C.P., Chen, S.H., Zhou, H. (2007). Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc Natl Acad Sci U S A 104: 10364-10369. (Publication) (All modifications)
[218, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)