MDJ1/YFL016C Protein Information

Standard Name	Mdj1p 1
Systematic Name	Yfl016cp
ORF Classification	Verified
Description	Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones (1, 2, 3, 4)
Name Description	Mitochondrial DnaJ 1

Experimental Data
Molecules/cell	7570 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	511
Molecular Weight (Da)	55,561
Isoelectric Point (pI)	9.95

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Mdj1p (InterPro)
Physical Interactions	There are 27 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012EE5F \| P35191 MIPS: YFL016C NCBI: 14318504 \| 431910 \| 462580 \| 559936 \| 836738 \| NP_116638.1 GenBank/EMBL/DDBJ: DAA12424.1 \| D50617 \| Z28336 \| Z46255

Amino Acid Sequence (or in FASTA format)
1 MAFQQGVLSR CSGVFRHHVG HSRHINNILY RHAIAFASIA PRIPKSSFHT 51 SAIRNNEAFK DPYDTLGLKK SATGAEIKKA YYKLAKKYHP DINKEPDAEK 101 KFHDLQNAYE ILSDETKRQQ YDQFGPAAFG GGGAAGGAGG GSGSPFGSQF 151 HDFSGFTSAG GSPFGGINFE DLFGAAFGGG GRGSGGASRS SSMFRQYRGD 201 PIEIVHKVSF KDAVFGSKNV QLRFSALDPC STCSGTGMKP NTHKVSCSTC 251 HGTGTTVHIR GGFQMMSTCP TCNGEGTMKR PQDNCTKCHG EGVQVNRAKT 301 ITVDLPHGLQ DGDVVRIPGQ GSYPDIAVEA DLKDSVKLSR GDILVRIRVD 351 KDPNFSIKNK YDIWYDKEIP ITTAALGGTV TIPTVEGQKI RIKVAPGTQY 401 NQVISIPNMG VPKTSTIRGD MKVQYKIVVK KPQSLAEKCL WEALADVTND 451 DMAKKTMQPG TAAGTAINEE ILKKQKQEEE KHAKKDDDNT LKRLENFITN 501 TFRKIKGDKK N*

Amino Acid Sequence (or in FASTA format)

       1  MAFQQGVLSR CSGVFRHHVG HSRHINNILY RHAIAFASIA PRIPKSSFHT
      51  SAIRNNEAFK DPYDTLGLKK SATGAEIKKA YYKLAKKYHP DINKEPDAEK
     101  KFHDLQNAYE ILSDETKRQQ YDQFGPAAFG GGGAAGGAGG GSGSPFGSQF
     151  HDFSGFTSAG GSPFGGINFE DLFGAAFGGG GRGSGGASRS SSMFRQYRGD
     201  PIEIVHKVSF KDAVFGSKNV QLRFSALDPC STCSGTGMKP NTHKVSCSTC
     251  HGTGTTVHIR GGFQMMSTCP TCNGEGTMKR PQDNCTKCHG EGVQVNRAKT
     301  ITVDLPHGLQ DGDVVRIPGQ GSYPDIAVEA DLKDSVKLSR GDILVRIRVD
     351  KDPNFSIKNK YDIWYDKEIP ITTAALGGTV TIPTVEGQKI RIKVAPGTQY
     401  NQVISIPNMG VPKTSTIRGD MKVQYKIVVK KPQSLAEKCL WEALADVTND
     451  DMAKKTMQPG TAAGTAINEE ILKKQKQEEE KHAKKDDDNT LKRLENFITN
     501  TFRKIKGDKK N*

external links for Mdj1p

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

References cited on this page View Complete Literature Guide for Mdj1p

1)	Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
2)	Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
3)	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
4)	Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41