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Protein

Triosephosphate isomerase

Gene

TPI1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathway:igluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Pathway:iglycolysis

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Triosephosphate isomerase, Triosephosphate isomerase, Triosephosphate isomerase (TPI1), Triosephosphate isomerase (TPI1), Triosephosphate isomerase (TPI1), Triosephosphate isomerase, Triosephosphate isomerase (HEL-S-49)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491Substrate
Binding sitei51 – 511Substrate
Active sitei133 – 1331Electrophile
Active sitei203 – 2031Proton acceptor

GO - Molecular functioni

  • triose-phosphate isomerase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

BioCyciMetaCyc:HS03441-MONOMER.
BRENDAi5.3.1.1. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP60174.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase (EC:5.3.1.1)
Short name:
TIM
Alternative name(s):
Triose-phosphate isomerase
Gene namesi
Name:TPI1
Synonyms:TPI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12009. TPI1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Triosephosphate isomerase deficiency (TPID)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive multisystem disorder characterized by congenital hemolytic anemia, progressive neuromuscular dysfunction, susceptibility to bacterial infection, and cardiomyopathy.

See also OMIM:615512
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791C → Y in TPID. 1 Publication
VAR_007534
Natural varianti110 – 1101G → A in TPID. 1 Publication
VAR_007535
Natural varianti142 – 1421E → D in TPID; the enzyme becomes thermolabile. 5 Publications
VAR_007536
Natural varianti192 – 1921V → M in TPID. 1 Publication
Corresponds to variant rs188138723 [ dbSNP | Ensembl ].
VAR_007538
Natural varianti208 – 2081I → V in TPID. 1 Publication
VAR_007539
Natural varianti269 – 2691V → M in TPID. 1 Publication
VAR_007540
Natural varianti278 – 2781F → L in TPID; Hungary; thermolabile. 1 Publication
VAR_007541

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi615512. phenotype.
Orphaneti868. Triose phosphate-isomerase deficiency.
PharmGKBiPA36689.

Polymorphism and mutation databases

BioMutaiTPI1.
DMDMi353526311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Triosephosphate isomerasePRO_0000090113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine1 Publication
Modified residuei58 – 581Phosphoserine10 Publications
Modified residuei105 – 1051Nitrated tyrosineBy similarity
Modified residuei117 – 1171Phosphoserine1 Publication
Modified residuei186 – 1861N6-succinyllysineBy similarity
Modified residuei193 – 1931N6-acetyllysine; alternateBy similarity
Modified residuei193 – 1931N6-succinyllysine; alternateBy similarity
Modified residuei231 – 2311N6-acetyllysine; alternate1 Publication
Modified residuei231 – 2311N6-succinyllysine; alternateBy similarity
Modified residuei246 – 2461Nitrated tyrosineBy similarity
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei251 – 2511Phosphothreonine1 Publication
Modified residuei260 – 2601Phosphoserine1 Publication
Modified residuei275 – 2751N6-acetyllysine1 Publication

Post-translational modificationi

The initiator methionine for isoform 2 is removed.

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP60174.
PaxDbiP60174.
PRIDEiP60174.

2D gel databases

DOSAC-COBS-2DPAGEP60174.
REPRODUCTION-2DPAGEIPI00797687.
P60174.
SWISS-2DPAGEP60174.
UCD-2DPAGEP00938.
P60174.

PTM databases

PhosphoSiteiP60174.

Expressioni

Gene expression databases

BgeeiP60174.
CleanExiHS_TPI1.
ExpressionAtlasiP60174. baseline and differential.
GenevisibleiP60174. HS.

Organism-specific databases

HPAiCAB004675.
HPA050924.
HPA053568.

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PCNAP120042EBI-717475,EBI-358311

Protein-protein interaction databases

BioGridi113020. 41 interactions.
IntActiP60174. 14 interactions.
MINTiMINT-1384176.
STRINGi9606.ENSP00000229270.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 496Combined sources
Helixi56 – 6813Combined sources
Beta strandi75 – 806Combined sources
Helixi83 – 853Combined sources
Helixi86 – 927Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi106 – 1116Combined sources
Helixi118 – 1236Combined sources
Beta strandi128 – 1325Combined sources
Helixi134 – 1385Combined sources
Helixi144 – 15613Combined sources
Beta strandi160 – 1656Combined sources
Helixi169 – 1735Combined sources
Helixi177 – 19014Combined sources
Helixi195 – 1973Combined sources
Beta strandi198 – 2025Combined sources
Helixi205 – 2073Combined sources
Turni208 – 2103Combined sources
Helixi216 – 23318Combined sources
Helixi236 – 2416Combined sources
Beta strandi244 – 2463Combined sources
Turni252 – 2543Combined sources
Helixi255 – 2606Combined sources
Beta strandi266 – 2694Combined sources
Helixi271 – 2744Combined sources
Helixi277 – 2826Combined sources
Turni283 – 2853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HTIX-ray2.80A/B39-286[»]
1KLGX-ray2.40C60-74[»]
1KLUX-ray1.93C60-74[»]
1WYIX-ray2.20A/B39-286[»]
2IAMX-ray2.80P60-74[»]
2IANX-ray2.80C/H/M/R60-74[»]
2JK2X-ray1.70A/B39-286[»]
2VOMX-ray1.85A/B/C/D39-286[»]
4BR1X-ray1.90A/B41-286[»]
4E41X-ray2.60C/H60-74[»]
4POCX-ray1.60A/B38-286[»]
4PODX-ray1.99A/B38-286[»]
4UNKX-ray2.00A/B39-286[»]
4UNLX-ray1.50A/B39-286[»]
ProteinModelPortaliP60174.
SMRiP60174. Positions 41-286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60174.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiCOG0149.
GeneTreeiENSGT00390000013354.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP60174.
KOiK01803.
OMAiNALMHRF.
OrthoDBiEOG76DTT8.
PhylomeDBiP60174.
TreeFamiTF300829.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B.
InterProiIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P60174-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAEDGEEAEF HFAALYISGQ WPRLRADTDL QRLGSSAMAP SRKFFVGGNW
60 70 80 90 100
KMNGRKQSLG ELIGTLNAAK VPADTEVVCA PPTAYIDFAR QKLDPKIAVA
110 120 130 140 150
AQNCYKVTNG AFTGEISPGM IKDCGATWVV LGHSERRHVF GESDELIGQK
160 170 180 190 200
VAHALAEGLG VIACIGEKLD EREAGITEKV VFEQTKVIAD NVKDWSKVVL
210 220 230 240 250
AYEPVWAIGT GKTATPQQAQ EVHEKLRGWL KSNVSDAVAQ STRIIYGGSV
260 270 280
TGATCKELAS QPDVDGFLVG GASLKPEFVD IINAKQ
Length:286
Mass (Da):30,791
Last modified:October 19, 2011 - v3
Checksum:iE6C2157706AE97F8
GO
Isoform 2 (identifier: P60174-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.

Show »
Length:249
Mass (Da):26,669
Checksum:i73844175635F858E
GO
Isoform 4 (identifier: P60174-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Note: Produced by alternative splicing.
Show »
Length:167
Mass (Da):17,958
Checksum:i1E9ADB034A513E18
GO

Sequence cautioni

The sequence AAB51316.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAB59511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH07086.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH07812.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH09329.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH11611.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH15100.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH17917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH70129.1 differs from that shown.Sequence differs at the C-terminus.Curated
The sequence AAH70129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAN86636.1 differs from that shown. Reason: Frameshift at position 23. Curated
The sequence BAG36090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA49379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 264RLRA → TAR in AAB59511 (PubMed:2579079).Curated
Sequence conflicti36 – 361Missing in AAB59511 (PubMed:2579079).Curated
Sequence conflicti36 – 361Missing in AAN86636 (PubMed:16541075).Curated
Sequence conflicti57 – 582QS → KN AA sequence (PubMed:6434534).Curated
Sequence conflicti64 – 641G → S AA sequence (PubMed:6434534).Curated
Sequence conflicti67 – 682NA → QG AA sequence (PubMed:6434534).Curated
Sequence conflicti80 – 812AP → IG AA sequence (PubMed:6434534).Curated
Sequence conflicti95 – 951P → Q AA sequence (PubMed:6434534).Curated
Sequence conflicti192 – 1921V → A in AAH17917 (PubMed:15489334).Curated
Sequence conflicti204 – 2041P → N AA sequence (PubMed:6434534).Curated
Sequence conflicti281 – 2811I → L AA sequence (PubMed:6434534).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791C → Y in TPID. 1 Publication
VAR_007534
Natural varianti110 – 1101G → A in TPID. 1 Publication
VAR_007535
Natural varianti142 – 1421E → D in TPID; the enzyme becomes thermolabile. 5 Publications
VAR_007536
Natural varianti160 – 1601G → R in Manchester; thermolabile. 1 Publication
VAR_007537
Natural varianti192 – 1921V → M in TPID. 1 Publication
Corresponds to variant rs188138723 [ dbSNP | Ensembl ].
VAR_007538
Natural varianti208 – 2081I → V in TPID. 1 Publication
VAR_007539
Natural varianti269 – 2691V → M in TPID. 1 Publication
VAR_007540
Natural varianti278 – 2781F → L in TPID; Hungary; thermolabile. 1 Publication
VAR_007541

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 119119Missing in isoform 4. 1 PublicationVSP_045310Add
BLAST
Alternative sequencei1 – 3737Missing in isoform 2. CuratedVSP_041895Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10036 mRNA. Translation: AAB59511.1. Different initiation.
X69723 Genomic DNA. Translation: CAA49379.1. Different initiation.
AK298809 mRNA. Translation: BAH12874.1.
U47924 Genomic DNA. Translation: AAB51316.1. Different initiation.
CH471116 Genomic DNA. Translation: EAW88722.1.
CH471116 Genomic DNA. Translation: EAW88723.1.
J04603 Genomic DNA. Translation: AAN86636.1. Frameshift.
BC007086 mRNA. Translation: AAH07086.1. Different initiation.
BC007812 mRNA. Translation: AAH07812.1. Different initiation.
BC009329 mRNA. Translation: AAH09329.1. Different initiation.
BC011611 mRNA. Translation: AAH11611.1. Different initiation.
BC015100 mRNA. Translation: AAH15100.1. Different initiation.
BC017165 mRNA. Translation: AAH17165.1.
BC017917 mRNA. Translation: AAH17917.1. Different initiation.
BC070129 mRNA. Translation: AAH70129.1. Sequence problems.
AK313282 mRNA. Translation: BAG36090.1. Different initiation.
CR541702 mRNA. Translation: CAG46503.1.
CCDSiCCDS53740.1. [P60174-3]
CCDS58206.1. [P60174-4]
CCDS8566.1. [P60174-1]
PIRiS29743. ISHUT.
RefSeqiNP_000356.1. NM_000365.5. [P60174-1]
NP_001152759.1. NM_001159287.1. [P60174-3]
NP_001244955.1. NM_001258026.1. [P60174-4]
UniGeneiHs.524219.

Genome annotation databases

EnsembliENST00000229270; ENSP00000229270; ENSG00000111669.
ENST00000488464; ENSP00000475620; ENSG00000111669. [P60174-4]
ENST00000535434; ENSP00000443599; ENSG00000111669. [P60174-4]
ENST00000613953; ENSP00000484435; ENSG00000111669.
GeneIDi7167.
KEGGihsa:7167.
UCSCiuc001qrk.4. human. [P60174-3]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Triosephosphate isomerase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10036 mRNA. Translation: AAB59511.1. Different initiation.
X69723 Genomic DNA. Translation: CAA49379.1. Different initiation.
AK298809 mRNA. Translation: BAH12874.1.
U47924 Genomic DNA. Translation: AAB51316.1. Different initiation.
CH471116 Genomic DNA. Translation: EAW88722.1.
CH471116 Genomic DNA. Translation: EAW88723.1.
J04603 Genomic DNA. Translation: AAN86636.1. Frameshift.
BC007086 mRNA. Translation: AAH07086.1. Different initiation.
BC007812 mRNA. Translation: AAH07812.1. Different initiation.
BC009329 mRNA. Translation: AAH09329.1. Different initiation.
BC011611 mRNA. Translation: AAH11611.1. Different initiation.
BC015100 mRNA. Translation: AAH15100.1. Different initiation.
BC017165 mRNA. Translation: AAH17165.1.
BC017917 mRNA. Translation: AAH17917.1. Different initiation.
BC070129 mRNA. Translation: AAH70129.1. Sequence problems.
AK313282 mRNA. Translation: BAG36090.1. Different initiation.
CR541702 mRNA. Translation: CAG46503.1.
CCDSiCCDS53740.1. [P60174-3]
CCDS58206.1. [P60174-4]
CCDS8566.1. [P60174-1]
PIRiS29743. ISHUT.
RefSeqiNP_000356.1. NM_000365.5. [P60174-1]
NP_001152759.1. NM_001159287.1. [P60174-3]
NP_001244955.1. NM_001258026.1. [P60174-4]
UniGeneiHs.524219.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HTIX-ray2.80A/B39-286[»]
1KLGX-ray2.40C60-74[»]
1KLUX-ray1.93C60-74[»]
1WYIX-ray2.20A/B39-286[»]
2IAMX-ray2.80P60-74[»]
2IANX-ray2.80C/H/M/R60-74[»]
2JK2X-ray1.70A/B39-286[»]
2VOMX-ray1.85A/B/C/D39-286[»]
4BR1X-ray1.90A/B41-286[»]
4E41X-ray2.60C/H60-74[»]
4POCX-ray1.60A/B38-286[»]
4PODX-ray1.99A/B38-286[»]
4UNKX-ray2.00A/B39-286[»]
4UNLX-ray1.50A/B39-286[»]
ProteinModelPortaliP60174.
SMRiP60174. Positions 41-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113020. 41 interactions.
IntActiP60174. 14 interactions.
MINTiMINT-1384176.
STRINGi9606.ENSP00000229270.

Chemistry

BindingDBiP60174.
ChEMBLiCHEMBL4880.

PTM databases

PhosphoSiteiP60174.

Polymorphism and mutation databases

BioMutaiTPI1.
DMDMi353526311.

2D gel databases

DOSAC-COBS-2DPAGEP60174.
REPRODUCTION-2DPAGEIPI00797687.
P60174.
SWISS-2DPAGEP60174.
UCD-2DPAGEP00938.
P60174.

Proteomic databases

MaxQBiP60174.
PaxDbiP60174.
PRIDEiP60174.

Protocols and materials databases

DNASUi7167.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229270; ENSP00000229270; ENSG00000111669.
ENST00000488464; ENSP00000475620; ENSG00000111669. [P60174-4]
ENST00000535434; ENSP00000443599; ENSG00000111669. [P60174-4]
ENST00000613953; ENSP00000484435; ENSG00000111669.
GeneIDi7167.
KEGGihsa:7167.
UCSCiuc001qrk.4. human. [P60174-3]

Organism-specific databases

CTDi7167.
GeneCardsiGC12P007138.
HGNCiHGNC:12009. TPI1.
HPAiCAB004675.
HPA050924.
HPA053568.
MIMi190450. gene.
615512. phenotype.
neXtProtiNX_P60174.
Orphaneti868. Triose phosphate-isomerase deficiency.
PharmGKBiPA36689.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0149.
GeneTreeiENSGT00390000013354.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP60174.
KOiK01803.
OMAiNALMHRF.
OrthoDBiEOG76DTT8.
PhylomeDBiP60174.
TreeFamiTF300829.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BioCyciMetaCyc:HS03441-MONOMER.
BRENDAi5.3.1.1. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP60174.

Miscellaneous databases

ChiTaRSiTPI1. human.
EvolutionaryTraceiP60174.
GeneWikiiTPI1.
GenomeRNAii7167.
NextBioi28066.
PROiP60174.
SOURCEiSearch...

Gene expression databases

BgeeiP60174.
CleanExiHS_TPI1.
ExpressionAtlasiP60174. baseline and differential.
GenevisibleiP60174. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B.
InterProiIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man."
    Maquat L.E., Chilcote R., Ryan P.M.
    J. Biol. Chem. 260:3748-3753(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family."
    Brown J.R., Daar I.O., Krug J.R., Maquat L.E.
    Mol. Cell. Biol. 5:1694-1706(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13."
    Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.
    Genome Res. 6:314-326(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
    Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
    Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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.
    , 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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-286 (ISOFORM 1).
    Tissue: Skeletal muscle.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Transcriptional regulatory sequences of the housekeeping gene for human triosephosphate isomerase."
    Boyer T.G., Krug J.R., Maquat L.E.
    J. Biol. Chem. 264:5177-5187(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-286 (ISOFORM 1).
    Tissue: Brain, Kidney, Placenta, Prostate, Skeletal muscle, Skin and Uterus.
  10. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-286 (ISOFORM 1).
  11. "Primary structure of human triosephosphate isomerase."
    Lu H.S., Yuan P.M., Gracy R.W.
    J. Biol. Chem. 259:11958-11968(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-286.
  12. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
    Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
    Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-57.
    Tissue: Mammary carcinoma.
  13. "A two-dimensional gel database of human colon carcinoma proteins."
    Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
    Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-57.
    Tissue: Colon carcinoma.
  14. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 43-51; 56-90; 97-168; 180-193; 198-212 AND 232-256, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  17. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  19. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-231 AND LYS-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-249; THR-251 AND SER-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "Crystal structure of recombinant human triosephosphate isomerase at 2.8-A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme."
    Mande S.C., Mainfroid V., Kalk K.H., Goraj K., Martial J.A., Hol W.G.J.
    Protein Sci. 3:810-821(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 39-286 IN COMPLEX WITH SUBSTRATE ANALOG, HOMODIMERIZATION.
  30. "Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method."
    Kinoshita T., Maruki R., Warizaya M., Nakajima H., Nishimura S.
    Acta Crystallogr. F 61:346-349(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-286.
  31. "Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface."
    Rodriguez-Almazan C., Arreola R., Rodriguez-Larrea D., Aguirre-Lopez B., de Gomez-Puyou M.T., Perez-Montfort R., Costas M., Gomez-Puyou A., Torres-Larios A.
    J. Biol. Chem. 283:23254-23263(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-289 OF MUTANT ASP-142, SUBUNIT, CHARACTERIZATION OF VARIANT ASP-142.
  32. "Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme."
    Daar I.O., Artymiuk P.J., Phillips D.C., Maquat L.E.
    Proc. Natl. Acad. Sci. U.S.A. 83:7903-7907(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TPID ASP-142.
  33. "Relation between genetic defect, altered protein structure, and enzyme function in triose-phosphate isomerase (TPI) deficiency."
    Neubauer B.A., Pekrun A., Eber S.W., Lakomek M., Schroeter W.
    Eur. J. Pediatr. Suppl. 151:232-232(1992)
    Cited for: VARIANTS TPID ASP-142 AND MET-269.
  34. "Human triosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electromorph variant, TPI-Manchester."
    Perry B.A., Mohrenweiser H.W.
    Hum. Genet. 88:634-638(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MANCHESTER ARG-160.
  35. "Human triosephosphate isomerase deficiency resulting from mutation of Phe-240."
    Chang M.-L., Artymiuk P.J., Wu X., Hollan S., Lammi A., Maquat L.E.
    Am. J. Hum. Genet. 52:1260-1269(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TPID HUNGARY LEU-278.
  36. "Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus."
    Watanabe M., Zingg B.C., Mohrenweiser H.W.
    Am. J. Hum. Genet. 58:308-316(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TPID ALA-110; ASP-142 AND MET-192.
  37. "Evidence for founder effect of the Glu104Asp substitution and identification of new mutations in triosephosphate isomerase deficiency."
    Arya R., Lalloz M.R.A., Bellingham A.J., Layton D.M.
    Hum. Mutat. 10:290-294(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TPID TYR-79; ASP-142 AND VAL-208.

Entry informationi

Entry nameiTPIS_HUMAN
AccessioniPrimary (citable) accession number: P60174
Secondary accession number(s): B7Z5D8
, D3DUS9, P00938, Q6FHP9, Q6IS07, Q8WWD0, Q96AG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 19, 2011
Last modified: July 22, 2015
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.