TPI1/YDR050C Protein Information

Standard Name	Tpi1p
Systematic Name	Ydr050cp
ORF Classification	Verified
Description	Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human TPI causes a rare autosomal disease (1, 2, 3, 4, 5)
Name Description	Triose-Phosphate Isomerase 3

Experimental Data
Molecules/cell	207000 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	248
Molecular Weight (Da)	26,795
Isoelectric Point (pI)	5.86

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 Tpi1p (InterPro)
Physical Interactions	There are 37 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000052EE3 \| P00942 MIPS: YDR050C NCBI: 1197083 \| 136069 \| 14719493 \| 14719494 \| 230405 \| 230406 \| 230791 \| 230792 \| 28374002 \| 28374003 \| 349951 \| 349952 \| 401871562 \| 401871563 \| 433552082 \| 433552083 \| 443550 \| 443551 \| 45269201 \| 6320255 \| 798902 \| NP_010335.1 GenBank/EMBL/DDBJ: DAA11897.1 \| AY557654 \| J01366 \| Z49209
External Classifications	EC: 5.3.1.1 [Triose-phosphate isomerase]

Amino Acid Sequence (or in FASTA format)
1 MARTFFVGGN FKLNGSKQSI KEIVERLNTA SIPENVEVVI CPPATYLDYS 51 VSLVKKPQVT VGAQNAYLKA SGAFTGENSV DQIKDVGAKW VILGHSERRS 101 YFHEDDKFIA DKTKFALGQG VGVILCIGET LEEKKAGKTL DVVERQLNAV 151 LEEVKDWTNV VVAYEPVWAI GTGLAATPED AQDIHASIRK FLASKLGDKA 201 ASELRILYGG SANGSNAVTF KDKADVDGFL VGGASLKPEF VDIINSRN*

Amino Acid Sequence (or in FASTA format)

       1  MARTFFVGGN FKLNGSKQSI KEIVERLNTA SIPENVEVVI CPPATYLDYS
      51  VSLVKKPQVT VGAQNAYLKA SGAFTGENSV DQIKDVGAKW VILGHSERRS
     101  YFHEDDKFIA DKTKFALGQG VGVILCIGET LEEKKAGKTL DVVERQLNAV
     151  LEEVKDWTNV VVAYEPVWAI GTGLAATPED AQDIHASIRK FLASKLGDKA
     201  ASELRILYGG SANGSNAVTF KDKADVDGFL VGGASLKPEF VDIINSRN*

external links for Tpi1p

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	DIP
YOGY	GeneMANIA
	YeastRC Mass Spec (Seattle)

References cited on this page View Complete Literature Guide for Tpi1p

1)	Krieger K and Ernst JF (1994) Iron regulation of triosephosphate isomerase transcript stability in the yeast Saccharomyces cerevisiae. Microbiology 140 ( Pt 5):1079-84
2)	Scott EW and Baker HV (1993) Concerted action of the transcriptional activators REB1, RAP1, and GCR1 in the high-level expression of the glycolytic gene TPI. Mol Cell Biol 13(1):543-50
3)	Alber T and Kawasaki G (1982) Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae. J Mol Appl Genet 1(5):419-34
4)	Gruning NM, et al. (2011) Pyruvate Kinase Triggers a Metabolic Feedback Loop that Controls Redox Metabolism in Respiring Cells. Cell Metab 14(3):415-27
5)	Rodriguez-Almazan C, et al. (2008) Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J Biol Chem 283(34):23254-63
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41