YME1/YPR024W Protein Information Help

Standard Name Yme1p
Systematic Name Ypr024wp
Alias Osd1p , Yta11p 1
ORF Classification Verified
Description Catalytic subunit of the mitochondrial inner membrane i-AAA protease complex, which is responsible for degradation of unfolded or misfolded mitochondrial gene products; also has a role in intermembrane space protein folding; mutation causes an elevated rate of mitochondrial turnover (2, 3, 4, 5, 6)
Name Description Yeast Mitochondrial Escape 2
Experimental Data
Molecules/cell 20100 7
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 747
Molecular Weight (Da) 81,771
Isoelectric Point (pI) 7.06

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Yme1p (InterPro)
Physical Interactions There are 16 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000013B999 | P32795
MIPS: YPR024W
NCBI: 1314098 | 295582 | 418575 | 531752 | 6325281 | 684978 | 809589 | NP_015349.1
GenBank/EMBL/DDBJ: DAA11450.1 | D16332 | L14616 | X81067 | Z49274 | Z71255
External Classifications EC: 3.4.24.- [Metalloendopeptidases]
Amino Acid Sequence (or in FASTA format)
 
       1  MNVSKILVSP TVTTNVLRIF APRLPQIGAS LLVQKKWALR SKKFYRFYSE
      51  KNSGEMPPKK EADSSGKASN KSTISSIDNS QPPPPSNTND KTKQANVAVS
     101  HAMLATREQE ANKDLTSPDA QAAFYKLLLQ SNYPQYVVSR FETPGIASSP
     151  ECMELYMEAL QRIGRHSEAD AVRQNLLTAS SAGAVNPSLA SSSSNQSGYH
     201  GNFPSMYSPL YGSRKEPLHV VVSESTFTVV SRWVKWLLVF GILTYSFSEG
     251  FKYITENTTL LKSSEVADKS VDVAKTNVKF DDVCGCDEAR AELEEIVDFL
     301  KDPTKYESLG GKLPKGVLLT GPPGTGKTLL ARATAGEAGV DFFFMSGSEF
     351  DEVYVGVGAK RIRDLFAQAR SRAPAIIFID ELDAIGGKRN PKDQAYAKQT
     401  LNQLLVELDG FSQTSGIIII GATNFPEALD KALTRPGRFD KVVNVDLPDV
     451  RGRADILKHH MKKITLADNV DPTIIARGTP GLSGAELANL VNQAAVYACQ
     501  KNAVSVDMSH FEWAKDKILM GAERKTMVLT DAARKATAFH EAGHAIMAKY
     551  TNGATPLYKA TILPRGRALG ITFQLPEMDK VDITKRECQA RLDVCMGGKI
     601  AEELIYGKDN TTSGCGSDLQ SATGTARAMV TQYGMSDDVG PVNLSENWES
     651  WSNKIRDIAD NEVIELLKDS EERARRLLTK KNVELHRLAQ GLIEYETLDA
     701  HEIEQVCKGE KLDKLKTSTN TVVEGPDSDE RKDIGDDKPK IPTMLNA*

external links for Yme1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB GeneMANIA

YOGY


References cited on this page View Complete Literature Guide for Yme1p
1) Schnall R, et al.  (1994) Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10(9):1141-55
2) Thorsness PE and Fox TD  (1993) Nuclear mutations in Saccharomyces cerevisiae that affect the escape of DNA from mitochondria to the nucleus. Genetics 134(1):21-8
3) Campbell CL and Thorsness PE  (1998) Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments. J Cell Sci 111 ( Pt 16)():2455-64
4) Leonhard K, et al.  (1999) Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature 398(6725):348-51
5) Dunn CD, et al.  (2006) A genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex. Mol Biol Cell 17(1):213-26
6) Schreiner B, et al.  (2012) Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria. Mol Biol Cell 23(22):4335-46
7) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41