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Q16635 (TAZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tafazzin
Alternative name(s):
Protein G4.5
Gene names
Name:TAZ
Synonyms:EFE2, G4.5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Some isoforms may be involved in cardiolipin (CL) metabolism. Ref.6 Ref.7

Subcellular location

Isoform 1: Membrane; Single-pass membrane protein.

Isoform 2: Cytoplasm Probable.

Isoform 3: Membrane; Single-pass membrane protein.

Isoform 4: Membrane; Single-pass membrane protein.

Isoform 5: Membrane; Single-pass membrane protein.

Isoform 6: Cytoplasm Probable.

Isoform 7: Membrane; Single-pass membrane protein.

Isoform 8: Cytoplasm Probable.

Isoform 9: Cytoplasm Probable.

Tissue specificity

High levels in cardiac and skeletal muscle. Up to 10 isoforms can be present in different amounts in different tissues. Most isoforms are ubiquitous. Isoforms that lack the N-terminus are found in leukocytes and fibroblasts, but not in heart and skeletal muscle. Some forms appear restricted to cardiac and skeletal muscle or to leukocytes.

Domain

The hydrophilic domain may serve as an exposed loop interacting with other proteins.

Involvement in disease

Barth syndrome (BTHS) [MIM:302060]: An X-linked disease characterized by dilated cardiomyopathy with endocardial fibroelastosis, a predominantly proximal skeletal myopathy, growth retardation, neutropenia, and organic aciduria, particularly excess of 3-methylglutaconic acid. Additional features include hypertrophic cardiomyopathy, isolated left ventricular non-compaction, ventricular arrhythmia, motor delay, poor appetite, fatigue and exercise intolerance, hypoglycemia, lactic acidosis, hyperammonemia, and dramatic late catch-up growth after growth delay throughout childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the taffazin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseCardiomyopathy
Disease mutation
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle contraction

Inferred from mutant phenotype PubMed 17043667. Source: BHF-UCL

cardiac muscle tissue development

Inferred from mutant phenotype PubMed 17043667. Source: HGNC

cardiolipin acyl-chain remodeling

Traceable author statement. Source: Reactome

cardiolipin biosynthetic process

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cristae formation

Inferred from mutant phenotype PubMed 17043667. Source: HGNC

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

heart development

Inferred from mutant phenotype PubMed 17043667. Source: HGNC

hemopoiesis

Inferred from mutant phenotype PubMed 17043667. Source: HGNC

mitochondrial ATP synthesis coupled electron transport

Inferred from direct assay PubMed 15304507. Source: BHF-UCL

mitochondrial respiratory chain complex I assembly

Inferred from mutant phenotype PubMed 16857210. Source: HGNC

muscle contraction

Inferred from mutant phenotype PubMed 17043667. Source: HGNC

phospholipid metabolic process

Traceable author statement. Source: Reactome

skeletal muscle tissue development

Inferred from mutant phenotype PubMed 17043667. Source: HGNC

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 15304507. Source: BHF-UCL

   Molecular_function1-acylglycerophosphocholine O-acyltransferase activity

Inferred from direct assay Ref.6. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LATS1O958354EBI-723166,EBI-444209

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16635-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16635-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
Isoform 3 (identifier: Q16635-3)

Also known as: Del_exon_5;

The sequence of this isoform differs from the canonical sequence as follows:
     124-153: Missing.
Isoform 4 (identifier: Q16635-4)

Also known as: Del_exon_6;

The sequence of this isoform differs from the canonical sequence as follows:
     154-180: Missing.
Isoform 5 (identifier: Q16635-5)

Also known as: Del_exon_7;

The sequence of this isoform differs from the canonical sequence as follows:
     181-194: Missing.
Isoform 6 (identifier: Q16635-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     181-194: Missing.
Isoform 7 (identifier: Q16635-7)

The sequence of this isoform differs from the canonical sequence as follows:
     124-153: Missing.
     181-194: Missing.
Isoform 8 (identifier: Q16635-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     124-153: Missing.
Isoform 9 (identifier: Q16635-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     124-153: Missing.
     181-194: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Tafazzin
PRO_0000220928

Regions

Transmembrane1 – 3030Helical; Signal-anchor; Potential
Region124 – 19471Hydrophilic

Natural variations

Alternative sequence1 – 2424Missing in isoform 2, isoform 6, isoform 8 and isoform 9.
VSP_011609
Alternative sequence124 – 15330Missing in isoform 3, isoform 7, isoform 8 and isoform 9.
VSP_004451
Alternative sequence154 – 18027Missing in isoform 4.
VSP_004452
Alternative sequence181 – 19414Missing in isoform 5, isoform 6, isoform 7 and isoform 9.
VSP_004453
Natural variant941R → S in BTHS. Ref.11
VAR_014110
Natural variant1181C → R in BTHS. Ref.10
VAR_014111
Natural variant1971G → R in BTHS. Ref.9
VAR_014112
Natural variant2401G → R in BTHS. Ref.8
VAR_068434

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2805E0962DC4FE52

FASTA29233,459
        10         20         30         40         50         60 
MPLHVKWPFP AVPPLTWTLA SSVVMGLVGT YSCFWTKYMN HLTVHNREVL YELIEKRGPA 

        70         80         90        100        110        120 
TPLITVSNHQ SCMDDPHLWG ILKLRHIWNL KLMRWTPAAA DICFTKELHS HFFSLGKCVP 

       130        140        150        160        170        180 
VCRGAEFFQA ENEGKGVLDT GRHMPGAGKR REKGDGVYQK GMDFILEKLN HGDWVHIFPE 

       190        200        210        220        230        240 
GKVNMSSEFL RFKWGIGRLI AECHLNPIIL PLWHVGMNDV LPNSPPYFPR FGQKITVLIG 

       250        260        270        280        290 
KPFSALPVLE RLRAENKSAV EMRKALTDFI QEEFQHLKTQ AEQLHNHLQP GR 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 857BFA0FC9DFB6EA
Show »

FASTA26830,803
Isoform 3 (Del_exon_5) [UniParc].

Checksum: AE7F4EBF505C7F63
Show »

FASTA26230,203
Isoform 4 (Del_exon_6) [UniParc].

Checksum: E2FFF553E9576B5A
Show »

FASTA26530,331
Isoform 5 (Del_exon_7) [UniParc].

Checksum: 350624E72B677BE8
Show »

FASTA27831,748
Isoform 6 [UniParc].

Checksum: CA3073742FC132D0
Show »

FASTA25429,092
Isoform 7 [UniParc].

Checksum: E23FAFFC359721CA
Show »

FASTA24828,492
Isoform 8 [UniParc].

Checksum: 53323D6698054515
Show »

FASTA23827,547
Isoform 9 [UniParc].

Checksum: 94B5C890BB4DEAAC
Show »

FASTA22425,836

References

« Hide 'large scale' references
[1]"A novel X-linked gene, G4.5. is responsible for Barth syndrome."
Bione S., D'Adamo P., Maestrini E., Gedeon A.K., Bolhuis P.A., Toniolo D.
Nat. Genet. 12:385-389(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Heart and Skeletal muscle.
[2]"Identification and characterization of human tafazzins."
Lu B., Gong Y., Hatch G.M., Choy P.C.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3; 5; 6; 7; 8 AND 9).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism."
Vaz F.M., Houtkooper R.H., Valianpour F., Barth P.G., Wanders R.J.
J. Biol. Chem. 278:43089-43094(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CARDIOLIPIN METABOLISM.
[7]"Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome."
Malhotra A., Edelman-Novemsky I., Xu Y., Plesken H., Ma J., Schlame M., Ren M.
Proc. Natl. Acad. Sci. U.S.A. 106:2337-2341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The X-linked gene G4.5 is responsible for different infantile dilated cardiomyopathies."
D'Adamo P., Fassone L., Gedeon A., Janssen E.A., Bione S., Bolhuis P.A., Barth P.G., Wilson M., Haan E., Orstavik K.H., Patton M.A., Green A.J., Zammarchi E., Donati M.A., Toniolo D.
Am. J. Hum. Genet. 61:862-867(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BTHS ARG-240.
[9]"Neonatal, lethal noncompaction of the left ventricular myocardium is allelic with Barth syndrome."
Bleyl S.B., Mumford B.R., Thompson V., Carey J.C., Pysher T.J., Chin T.K., Ward K.
Am. J. Hum. Genet. 61:868-872(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BTHS ARG-197.
[10]"Novel gene mutations in patients with left ventricular noncompaction or Barth syndrome."
Ichida F., Tsubata S., Bowles K.R., Haneda N., Uese K., Miyawaki T., Dreyer W.J., Messina J., Li H., Bowles N.E., Towbin J.A.
Circulation 103:1256-1263(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BTHS ARG-118.
[11]"Novel missense mutation (R94S) in the TAZ (G4.5) gene in a Japanese patient with Barth syndrome."
Sakamoto O., Kitoh T., Ohura T., Ohya N., Iinuma K.
J. Hum. Genet. 47:229-231(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BTHS SER-94.

Web resources

TAZbase

TAZ mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92763, X92764 Genomic DNA. Translation: CAA63419.1.
X92762 mRNA. Translation: CAA63418.1.
AY231461 mRNA. Translation: AAO84335.1.
AY231462 mRNA. Translation: AAO84336.1.
AY231463 mRNA. Translation: AAO84337.1.
AY231464 mRNA. Translation: AAO84338.1.
AY258036 mRNA. Translation: AAO84339.1.
AY258037 mRNA. Translation: AAO84340.1.
AY258038 mRNA. Translation: AAO84341.1.
AY258039 mRNA. Translation: AAO84342.1.
AK291848 mRNA. Translation: BAF84537.1.
BX936347 Genomic DNA. Translation: CAI43207.1.
BX936347 Genomic DNA. Translation: CAI43208.1.
BX936347 Genomic DNA. Translation: CAI43209.1.
BX936347 Genomic DNA. Translation: CAI43211.1.
BX936347 Genomic DNA. Translation: CAM45851.1.
CH471172 Genomic DNA. Translation: EAW72720.1.
CH471172 Genomic DNA. Translation: EAW72728.1.
RefSeqNP_000107.1. NM_000116.3.
NP_851828.1. NM_181311.2.
NP_851829.1. NM_181312.2.
NP_851830.1. NM_181313.2.
UniGeneHs.409911.

3D structure databases

ProteinModelPortalQ16635.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112764. 7 interactions.
IntActQ16635. 2 interactions.

PTM databases

PhosphoSiteQ16635.

Polymorphism databases

DMDM2498992.

Proteomic databases

PaxDbQ16635.
PRIDEQ16635.

Protocols and materials databases

DNASU6901.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299328; ENSP00000299328; ENSG00000102125. [Q16635-1]
ENST00000350743; ENSP00000338891; ENSG00000102125. [Q16635-3]
ENST00000351413; ENSP00000218246; ENSG00000102125. [Q16635-5]
ENST00000369790; ENSP00000358805; ENSG00000102125. [Q16635-7]
ENST00000475699; ENSP00000419854; ENSG00000102125. [Q16635-4]
GeneID6901.
KEGGhsa:6901.
UCSCuc004fkx.3. human. [Q16635-1]
uc004fky.3. human. [Q16635-5]
uc004fla.3. human. [Q16635-3]
uc004flb.3. human. [Q16635-7]

Organism-specific databases

CTD6901.
GeneCardsGC0XP153639.
HGNCHGNC:11577. TAZ.
HPAHPA039557.
MIM300394. gene.
302060. phenotype.
neXtProtNX_Q16635.
Orphanet111. Barth syndrome.
154. Familial isolated dilated cardiomyopathy.
54260. Left ventricular noncompaction.
PharmGKBPA36341.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313544.
HOVERGENHBG055923.
InParanoidQ16635.
KOK13511.
OMAWPFPQCP.
PhylomeDBQ16635.
TreeFamTF313862.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ16635.
BgeeQ16635.
CleanExHS_TAZ.
GenevestigatorQ16635.

Family and domain databases

InterProIPR002123. Plipid/glycerol_acylTrfase.
IPR000872. Tafazzin.
[Graphical view]
PANTHERPTHR12497. PTHR12497. 1 hit.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PRINTSPR00979. TAFAZZIN.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTAZ. human.
GeneWikiTafazzin.
GenomeRNAi6901.
NextBio26979.
PROQ16635.
SOURCESearch...

Entry information

Entry nameTAZ_HUMAN
AccessionPrimary (citable) accession number: Q16635
Secondary accession number(s): A3KQT2 expand/collapse secondary AC list , D3DWX2, Q5HY43, Q5HY44, Q5HY45, Q5HY48, Q86XQ6, Q86XQ7, Q86XQ8, Q86XQ9, Q86XR0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM