Basic Information

NameRibonuclease P protein component, mitochondrial (RNase P) (EC 3.1.26.5)
Uniprot IDQ02773
Systematic gene nameYML091C
Standard gene nameRPM2
Gene namesRPM2 YML091C
Description from SGDYML091C RPM2 SGDID:S000004556, Chr XIII from 90731-87123, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein subunit of mitochondrial RNase P; has roles in nuclear transcription, cytoplasmic and mitochondrial RNA processing, and mitochondrial translation; distributed to mitochondria, cytoplasmic processing bodies, and the nucleus"
Protein length1202
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MAFKSFIYSK GYHRSAAQKK TATSFFDSSY QYLRQNQGLV NSDPVLHASH
LHPHPVVVAN VNYNNVDDIL HPHDLDSSIN NTNNPLTHEE LLYNQNVSLR
SLKQQQSTNY VNNNNNNQHR YYSTGPTLPT NQYDPLNFSN RNFQDLSLKT
SQPSVQQPQN EYSLLKDENA PVWKEDTEPC LNKSTYLQTH IDEINRCYEQ
KNYNKINSLY QSLKRNDIVP PLEIFTKVLD SLCKRPLDNN DLDNKMYELL
TCYQDMINNR LKPPDEIYNI VLLSLFKGSI LAYQFENPNG SDFYKIAIEL
FNTTTNDPKQ KSVVKFRNFS KDVLDYNLLA MNIYPGHITL SKAQQVIKSS
PAFIKDSFYF IACFSYAKLT NDKFAIKELY EDFRLSLSSG SPDQGLFDDQ
FEIYSVILSS FIETGEVELA TNLLDDLVSK IQSSNGLASN ISLLLSSFLI
SMSKVDPSKA YEIWFKFHNL NWIPEFSYEF YLVFMANSFQ DWNLTKKIYD
YIFPMERNLS PLKKQKLSDY LLHPIGVDSI TTSLLDYSLQ LKDNEVIMKI
LEESIVKNFS FDIGIYPFVF NYLREIQCGE DYLMRFIESH AEFIKKSNSI
NKFQFLNMIV DNFQSQSLLN KISHAKFFKN FVEDFNLENC ELVSYNGLIS
CINNFIKIPK TIKDFPYILE IHAILVTKLF DFDTYPILQN GNNEVLLKFR
DQIEHQFKML AQNFCRLNLD PNLLAGVVSQ AMKMVNLDDT ANGQDLLNFF
NHPGDWDKSY PLSLGSFIRN SPRGGIREFT KLSKEGYCFD YDTYKELIIK
RAINKQIIDK CLEVCPDSIE LKNIVNLMIS KIPGRNLTQL IINNPKFSKV
FVPNLRNDSM LKLIENCESL SNFIRICDFP EKFKSIAIQA ENKNAIELIY
ERLFDGGKYA DILRYNNIVP VLNLELLLKS CIRSGEFKKY ESLSKKFNDK
ISESSKIDIQ LEYLINKNDL KGAFTLFEKT PRELRTPHKT MDLYTFALFL
DSFNRNITYY ESPENTLQFA NILSSQTSFI NLLSTYNLIA HSDHLMNFNV
GGMAAKVKKE ILNQMLNNLY DSIRLLSPSI ENDKSMKEKL REKVKNYCRF
KAYLKSPELD MDELKTLVSV ESFLNPFTPS MLFNNLIETI YINEHASSLV
LQNGLIYSLQ QKGLNKILSY LEESFITSGN DANIEKVREF RSLLRKSKPL
QA

Legend

  • X Phoshorylation
  • X K-Succinylation
  • 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

[110, 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)
[110, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[513, K-succ]Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications)
[518, 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)
[518, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[818, 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)
[952, 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)
[952, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[954, 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)
[954, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[955, 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)
[955, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[963, 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)
[963, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1077, 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)
[1084, 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)