PIM1/YBL022C Protein Information Help

Standard Name Pim1p 1
Systematic Name Ybl022cp
ORF Classification Verified
Description ATP-dependent Lon protease, involved in degradation of misfolded proteins in mitochondria; required for biogenesis and maintenance of mitochondria (1, 2, 3)
Name Description Proteolysis In Mitochondria 4
Experimental Data
Molecules/cell 14500 5
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,133
Molecular Weight (Da) 127,111
Isoelectric Point (pI) 5.36

Click on image for expanded interactive view
pbrowse

Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Pim1p (InterPro)
Physical Interactions There are 22 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000053295 | P36775
MIPS: YBL022C
NCBI: 171644 | 453236 | 454438 | 536019 | 585414 | 6319449 | NP_009531.1
GenBank/EMBL/DDBJ: DAA07098.1 | L28110 | M20318 | X74544 | Z35783
External Classifications EC: 3.4.21.- [Serine endopeptidases]
Amino Acid Sequence (or in FASTA format)
 
       1  MLRTRTTKTL STVARTTRAI QYYRSIAKTA AVSQRRFAST LTVRDVENIK
      51  PSHIIKSPTW QEFQHQLKDP RYMEHFAQLD AQFARHFMAT NSGKSILAKD
     101  DSTSQKKDED VKIVPDEKDT DNDVEPTRDD EIVNKDQEGE ASKNSRSSAS
     151  GGGQSSSSRS DSGDGSSKQK PPKDVPEVYP QMLALPIARR PLFPGFYKAV
     201  VISDERVMKA IKEMLDRQQP YIGAFMLKNS EEDTDVITDK NDVYDVGVLA
     251  QITSAFPSKD EKTGTETMTA LLYPHRRIKI DELFPPNEEK EKSKEQAKDT
     301  DTETTVVEDA NNPEDQESTS PATPKLEDIV VERIPDSELQ HHKRVEATEE
     351  ESEELDDIQE GEDINPTEFL KNYNVSLVNV LNLEDEPFDR KSPVINALTS
     401  EILKVFKEIS QLNTMFREQI ATFSASIQSA TTNIFEEPAR LADFAAAVSA
     451  GEEDELQDIL SSLNIEHRLE KSLLVLKKEL MNAELQNKIS KDVETKIQKR
     501  QREYYLMEQL KGIKRELGID DGRDKLIDTY KERIKSLKLP DSVQKIFDDE
     551  ITKLSTLETS MSEFGVIRNY LDWLTSIPWG KHSKEQYSIP RAKKILDEDH
     601  YGMVDVKDRI LEFIAVGKLL GKVDGKIICF VGPPGVGKTS IGKSIARALN
     651  RKFFRFSVGG MTDVAEIKGH RRTYIGALPG RVVQALKKCQ TQNPLILIDE
     701  IDKIGHGGIH GDPSAALLEV LDPEQNNSFL DNYLDIPIDL SKVLFVCTAN
     751  SLETIPRPLL DRMEVIELTG YVAEDKVKIA EQYLVPSAKK SAGLENSHVD
     801  MTEDAITALM KYYCRESGVR NLKKHIEKIY RKAALQVVKK LSIEDSPTSS
     851  ADSKPKESVS SEEKAENNAK SSSEKTKDNN SEKTSDDIEA LKTSEKINVS
     901  ISQKNLKDYV GPPVYTTDRL YETTPPGVVM GLAWTNMGGC SLYVESVLEQ
     951  PLHNCKHPTF ERTGQLGDVM KESSRLAYSF AKMYLAQKFP ENRFFEKASI
    1001  HLHCPEGATP KDGPSAGVTM ATSFLSLALN KSIDPTVAMT GELTLTGKVL
    1051  RIGGLREKAV AAKRSGAKTI IFPKDNLNDW EELPDNVKEG LEPLAADWYN
    1101  DIFQKLFKDV NTKEGNSVWK AEFEILDAKK EKD*

external links for Pim1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
YGOB CYC2008 (complexes) Pfam domains
YOGY Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Pim1p
1) Van Dyck L, et al.  (1994) PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. J Biol Chem 269(1):238-42
2) Wagner I, et al.  (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45
3) Suzuki CK, et al.  (1994) Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 264(5156):273-6
4) Major T, et al.  (2006) Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1. Mol Cell Biol 26(3):762-76
5) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41