TAZ1/YPR140W Summary Help

Standard Name TAZ1 1
Systematic Name YPR140W
Feature Type ORF, Verified
Description Lyso-phosphatidylcholine acyltransferase; required for normal phospholipid content of mitochondrial membranes; major determinant of the final acyl chain composition of the mitochondrial-specific phospholipid cardiolipin; mutations in human ortholog tafazzin cause Barth syndrome, a rare X-linked disease characterized by skeletal and cardiomyopathy and bouts of cyclic neutropenia (1, 2, 3, 4 and see Summary Paragraph)
Name Description TAfaZzin 1
Chromosomal Location
ChrXVI:814391 to 815536 | ORF Map | GBrowse
Gene Ontology Annotations All TAZ1 GO evidence and references
  View Computational GO annotations for TAZ1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Classical genetics
Large-scale survey
69 total interaction(s) for 54 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 1
  • Co-purification: 1

Genetic Interactions
  • Negative Genetic: 30
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 1
  • Positive Genetic: 10
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 381
Molecular Weight (Da) 44,187
Isoelectric Point (pI) 9.38
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:814391 to 815536 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1146 814391..815536 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006344

TAZ1 encodes a mitochondrial lyso-phosphatidylcholine acyltransferase (3) involved in the remodeling of cardiolipin, a mitochondrial inner and outer membrane phospholipid required for normal respiratory function. Cardiolipin, synthesized by the cardiolipin biosynthesis pathway, has an unique structure with two phosphatidyl moieties linked by a glycerol bridge, giving the molecule four fatty acyl chains and two phosphate groups (1).

The taz1 null mutant accumulates monolyso-cardiolipin, an intermediate in the cardiolipin biosynthesis pathway and also exhibits other phospholipid defects such as increased phosphatidylethanolamine and phosphatidylserine levels and decreased levels of phosphatidic acid. These phopholipid defects are similar to those observed in Barth syndrome, a disease associated with the human homolog of Taz1p, Tafazzin (1, 5). Barth Syndrome is an inherited X-linked recessive disease that is often fatal in childhood and is characterized by skeletal myopathy, neutropenia and abnormal mitochondria.

The taz1 null mutations also affect the stable formation of supercomplexes between Complex III and Complex IV of the respiratory chain, resulting in respiratory defects at elevated or decreased temperatures (6).

Last updated: 2006-11-20 Contact SGD

References cited on this page View Complete Literature Guide for TAZ1
1) Gu Z, et al.  (2004) Aberrant cardiolipin metabolism in the yeast taz1 mutant: a model for Barth syndrome. Mol Microbiol 51(1):149-58
2) Neuwald AF  (1997) Barth syndrome may be due to an acyltransferase deficiency. Curr Biol 7(8):R465-6
3) Testet E, et al.  (2005) Ypr140wp, 'the yeast tafazzin', displays a mitochondrial lysophosphatidylcholine (lyso-PC) acyltransferase activity related to triacylglycerol and mitochondrial lipid synthesis. Biochem J 387(Pt 3):617-26
4) Whited K, et al.  (2013) Seven functional classes of Barth syndrome mutation. Hum Mol Genet 22(3):483-92
5) Vaz FM, et al.  (2003) Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism. J Biol Chem 278(44):43089-94
6) Brandner K, et al.  (2005) Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome. Mol Biol Cell 16(11):5202-14