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[General] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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General information about the entry
Entry name TPIS_HUMAN
Primary accession number P00938
Secondary accession numbers None
Entered in Swiss-Prot in Release 01, July 1986
Sequence was last modified in Release 01, July 1986
Annotations were last modified in    Release 41, February 2003
Name and origin of the protein
Protein name Triosephosphate isomerase
Synonyms EC 5.3.1.1
TIM
Gene name
TPI1 or TPI
From
Homo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
References
[1]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=85131186; PubMed=2579079; [NCBI, ExPASy, EBI, Israel, Japan]
Maquat L.E., Chilcote R., Ryan P.M.;
"Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man.";
J. Biol. Chem. 260:3748-3753(1985).
[2]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=85267686; PubMed=4022011; [NCBI, ExPASy, EBI, Israel, Japan]
Brown J.R., Daar I.O., Krug J.R., Maquat L.E.;
"Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family.";
Mol. Cell. Biol. 5:1694-1706(1985).
[3]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
TISSUE=Liver;
Belgrader P., Boyer T., Daar I., Cheng J., Nesic D., Maquat L.E.;
Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
[4]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=96303695; PubMed=8723724; [NCBI, ExPASy, EBI, Israel, Japan]
Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.;
"A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13.";
Genome Res. 6:314-326(1996).
[5]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
TISSUE=Brain, Kidney, Skeletal muscle, and Skin;
Strausberg R.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[6]
SEQUENCE OF 1-4 FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=89174806; PubMed=2925688; [NCBI, ExPASy, EBI, Israel, Japan]
Boyer T.G., Krug J.R., Maquat L.E.;
"Transcriptional regulatory sequences of the housekeeping gene for human triosephosphate isomerase.";
J. Biol. Chem. 264:5177-5187(1989).
[7]
SEQUENCE.
SPECIES=Human;
MEDLINE=85006925; PubMed=6434534; [NCBI, ExPASy, EBI, Israel, Japan]
Lu H.S., Yuan P.M., Gracy R.W.;
"Primary structure of human triosephosphate isomerase.";
J. Biol. Chem. 259:11958-11968(1984).
[8]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=P.troglodytes;
MEDLINE=91216462; PubMed=2022334; [NCBI, ExPASy, EBI, Israel, Japan]
Craig L.C., Pirtle I.L., Gracy R.W., Pirtle R.M.;
"Characterization of the transcription unit and two processed pseudogenes of chimpanzee triosephosphate isomerase (TPI).";
Gene 99:217-227(1991).
[9]
SEQUENCE OF 1-19.
SPECIES=Human;
TISSUE=Breast carcinoma;
MEDLINE=97295304; PubMed=9150946; [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.;
"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2.";
Electrophoresis 18:588-598(1997).
[10]
SEQUENCE OF 1-19.
SPECIES=Human;
TISSUE=Colon carcinoma;
MEDLINE=97295306; PubMed=9150948; [NCBI, ExPASy, EBI, Israel, Japan]
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
MEDLINE=94339841; PubMed=8061610; [NCBI, ExPASy, EBI, Israel, Japan]
Mande S.C., Mainfroid V., Kalk K.H., Goraj K., Martial J.A., Hol W.G.J.;
"Crystal structure of recombinant human triosephosphate isomerase at 2.8-A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.";
Protein Sci. 3:810-821(1994).
[12]
VARIANT ASP-104.
SPECIES=Human;
MEDLINE=87017054; PubMed=2876430; [NCBI, ExPASy, EBI, Israel, Japan]
Daar I.O., Artymiuk P.J., Phillips D.C., Maquat L.E.;
"Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 83:7903-7907(1986).
[13]
VARIANTS ASP-104 AND MET-231.
Neubauer B.A., Pekrun A., Eber S.W., Lakomek M., Schroeter W.;
"Relation between genetic defect, altered protein structure, and enzyme function in triose-phosphate isomerase (TPI) deficiency.";
Eur. J. Pediatr. Suppl. 151:232-232(1992).
[14]
VARIANT MANCHESTER ARG-122.
SPECIES=Human;
MEDLINE=92201826; PubMed=1339398; [NCBI, ExPASy, EBI, Israel, Japan]
Perry B.A., Mohrenweiser H.W.;
"Human triosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electromorph variant, TPI-Manchester.";
Hum. Genet. 88:634-638(1992).
[15]
VARIANT HUNGARY LEU-240.
SPECIES=Human;
MEDLINE=93276899; PubMed=8503454; [NCBI, ExPASy, EBI, Israel, Japan]
Chang M.-L., Artymiuk P.J., Wu X., Hollan S., Lammi A., Maquat L.E.;
"Human triosephosphate isomerase deficiency resulting from mutation of Phe-240.";
Am. J. Hum. Genet. 52:1260-1269(1993).
[16]
VARIANTS ALA-72; ASP-104 AND MET-154.
MEDLINE=96152127; PubMed=8571957; [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe M., Zingg B.C., Mohrenweiser H.W.;
"Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus.";
Am. J. Hum. Genet. 58:308-316(1996).
[17]
VARIANTS TYR-41; ASP-104 AND VAL-170.
MEDLINE=97478287; PubMed=9338582; [NCBI, ExPASy, EBI, Israel, Japan]
Arya R., Lalloz M.R.A., Bellingham A.J., Layton D.M.;
"Evidence for founder effect of the Glu104Asp substitution and identification of new mutations in triosephosphate isomerase deficiency.";
Hum. Mutat. 10:290-294(1997).
Comments
  • CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone phosphate.
  • PATHWAY: Plays an important role in several metabolic pathways.
  • SUBUNIT: Homodimer.
  • DISEASE: TPI DEFICIENCY IS THE MOST SEVERE CLINICAL DISORDER OF GLYCOLYSIS. IT IS ASSOCIATED WITH NEONATAL JAUNDICE, CHRONIC HEMOLYTIC ANEMIA, PROGRESSIVE NEUROMUSCULAR DYSFUNCTION, CARDIOMYOPATHY, AND INCREASED SUSCEPTIBILITY TO INFECTION. TPI DEFICIENCY IS AN AUTOSOMAL RECESSIVE DISORDER.
  • SIMILARITY: BELONGS TO THE TRIOSEPHOSPHATE ISOMERASE FAMILY.
Copyright
This SWISS-PROT entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://www.isb-sib.ch/announce/ or send an email to license@isb-sib.ch).
Cross-references
EMBL
M10036; AAB59511.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04603; -; NOT_ANNOTATED_CDS.[EMBL / GenBank / DDBJ]
X69723; CAA49379.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004230; AAH04230.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007086; AAH07086.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007812; AAH07812.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009329; AAH09329.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011611; AAH11611.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015100; AAH15100.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47924; AAB51316.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
M57946; AAA35438.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01164; ISHUT.
JH0375; ISCZT1.
A05104; A05104.
S29743; S29743.
PDB
1HTI; 26-JAN-95.[ExPASy / RCSB]
SWISS-2DPAGE P00938; HUMAN.
Aarhus/Ghent-2DPAGE 1111; IEF.
2112; IEF.
HSC-2DPAGE P00938; HUMAN.
PMMA-2DPAGE P00938; -.
Siena-2DPAGE P00938; -.
Genew HGNC:12009; TPI1.
CleanEx HGNC:12009; TPI1.
MIM 190450 [NCBI / EBI].
GeneCards TPI1.
GeneLynx TPI1; Homo sapiens.
SOURCE TPI1; Homo sapiens.
Ensembl P00938; Homo sapiens. [Entry / Contig view]
InterPro IPR000652; Triophos_ismrse.
Graphical view of domain structure.
Pfam PF00121; TIM; 1.
ProDom PD001005; Triophos_ismrse; 1.
[Domain structure / List of seq. sharing at least 1 domain].
TIGRFAMs TIGR00419; tim; 1.
PROSITE PS00171; TIM; 1.
BLOCKS P00938.
ProtoNet P00938.
ProtoMap P00938.
PRESAGE P00938.
DIP P00938.
ModBase P00938.
Keywords
Isomerase; Glycolysis; Gluconeogenesis; Fatty acid biosynthesis; Pentose shunt; Disease mutation; Polymorphism; 3D-structure.
Features
KeyFrom   To Length Description
INIT_MET   0     0        
ACT_SITE   95    95        BY SIMILARITY.
ACT_SITE   165   165        BY SIMILARITY.
VARIANT   41    41        C -> Y (IN TPI DEFICIENCY).
/FTId=VAR_007534.
VARIANT   72    72        G -> A (IN TPI DEFICIENCY).
/FTId=VAR_007535.
VARIANT   104   104        E -> D (IN TPI DEFICIENCY; THE ENZYME BECOMES THERMOLABILE).
/FTId=VAR_007536.
VARIANT   122   122        G -> R (IN MANCHESTER; THERMOLABILE).
/FTId=VAR_007537.
VARIANT   154   154        V -> M (IN TPI DEFICIENCY).
/FTId=VAR_007538.
VARIANT   170   170        I -> V (IN TPI DEFICIENCY).
/FTId=VAR_007539.
VARIANT   231   231        V -> M (IN TPI DEFICIENCY).
/FTId=VAR_007540.
VARIANT   240   240        F -> L (IN TPI DEFICIENCY; HUNGARY; THERMOLABILE).
/FTId=VAR_007541.
CONFLICT   19    20        QS -> KN (IN REF. 7).
CONFLICT   26    26        G -> S (IN REF. 7).
CONFLICT   29    30        NA -> QG (IN REF. 7).
CONFLICT   42    43        AP -> IG (IN REF. 7).
CONFLICT   57    57        P -> Q (IN REF. 7).
CONFLICT   166   166        P -> N (IN REF. 7).
CONFLICT   243   243        I -> L (IN REF. 7).
STRAND   6    11  6     
STRAND   14    14  1     
HELIX   18    30  13     
STRAND   37    42  6     
HELIX   45    47  3     
HELIX   48    54  7     
TURN   57    58  2     
STRAND   60    63  4     
STRAND   72    72  1     
TURN   75    76  2     
HELIX   80    85  6     
TURN   86    87  2     
STRAND   90    93  4     
HELIX   96   100  5     
TURN   101   101  1     
HELIX   106   118  13     
TURN   119   120  2     
STRAND   122   127  6     
HELIX   131   135  5     
TURN   136   136  1     
TURN   138   138  1     
HELIX   139   151  13     
TURN   152   153  2     
TURN   157   158  2     
STRAND   160   164  5     
TURN   167   172  6     
HELIX   178   195  18     
TURN   196   196  1     
HELIX   198   201  4     
TURN   202   203  2     
STRAND   206   208  3     
TURN   214   216  3     
HELIX   217   221  5     
TURN   222   222  1     
TURN   224   225  2     
STRAND   228   231  4     
HELIX   234   236  3     
TURN   238   238  1     
HELIX   239   244  6     
HELIX   245   248  4     
SEVIEWER logo Feature table viewer
Sequence information
Length: 248 AA Molecular weight: 26538 Da CRC64: 61BD417548AF858E [This is a checksum on the sequence]
        10         20         30         40         50         60 
         |          |          |          |          |          | 
APSRKFFVGG NWKMNGRKQS LGELIGTLNA AKVPADTEVV CAPPTAYIDF ARQKLDPKIA 

        70         80         90        100        110        120 
         |          |          |          |          |          | 
VAAQNCYKVT NGAFTGEISP GMIKDCGATW VVLGHSERRH VFGESDELIG QKVAHALAEG 

       130        140        150        160        170        180 
         |          |          |          |          |          | 
LGVIACIGEK LDEREAGITE KVVFEQTKVI ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ 

       190        200        210        220        230        240 
         |          |          |          |          |          | 
AQEVHEKLRG WLKSNVSDAV AQSTRIIYGG SVTGATCKEL ASQPDVDGFL VGGASLKPEF 



VDIINAKQ 

P00938 in FASTA format

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