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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.

Pathwayi: gluconeogenesis

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.

Pathwayi: glycolysis

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 (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)DescriptionActionsGraphical viewLength
Binding sitei49Substrate1
Binding sitei51Substrate1
Active sitei133Electrophile1
Active sitei203Proton acceptor1

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.
ZFISH:HS03441-MONOMER.
BRENDAi5.3.1.1. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12009. TPI1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_00753479C → Y in TPID. 1 PublicationCorresponds to variant rs121964848dbSNPEnsembl.1
Natural variantiVAR_007535110G → A in TPID. 1 Publication1
Natural variantiVAR_007536142E → D in TPID; the enzyme becomes thermolabile. 5 PublicationsCorresponds to variant rs121964845dbSNPEnsembl.1
Natural variantiVAR_007538192V → M in TPID. 1 PublicationCorresponds to variant rs188138723dbSNPEnsembl.1
Natural variantiVAR_007539208I → V in TPID. 1 PublicationCorresponds to variant rs121964849dbSNPEnsembl.1
Natural variantiVAR_007540269V → M in TPID. 1 Publication1
Natural variantiVAR_007541278F → L in TPID; Hungary; thermolabile. 1 PublicationCorresponds to variant rs121964847dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi7167.
MalaCardsiTPI1.
MIMi615512. phenotype.
OpenTargetsiENSG00000111669.
Orphaneti868. Triose phosphate-isomerase deficiency.
PharmGKBiPA36689.

Chemistry databases

ChEMBLiCHEMBL4880.

Polymorphism and mutation databases

BioMutaiTPI1.
DMDMi353526311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000901131 – 286Triosephosphate isomeraseAdd BLAST286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51N6-acetyllysineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei105Nitrated tyrosineBy similarity1
Modified residuei117PhosphoserineCombined sources1
Modified residuei143PhosphoserineBy similarity1
Cross-linki179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei186N6-succinyllysineBy similarity1
Modified residuei193N6-acetyllysine; alternateBy similarity1
Modified residuei193N6-succinyllysine; alternateBy similarity1
Modified residuei196PhosphoserineBy similarity1
Modified residuei210PhosphothreonineBy similarity1
Modified residuei231N6-acetyllysine; alternateCombined sources1
Modified residuei231N6-methyllysine; alternateCombined sources1
Modified residuei231N6-succinyllysine; alternateBy similarity1
Modified residuei235PhosphoserineBy similarity1
Modified residuei246Nitrated tyrosineBy similarity1
Modified residuei249PhosphoserineCombined sources1
Modified residuei251PhosphothreonineCombined sources1
Modified residuei260PhosphoserineCombined sources1
Modified residuei275N6-acetyllysineCombined sources1

Post-translational modificationi

The initiator methionine for isoform 2 is removed.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP60174.
MaxQBiP60174.
PaxDbiP60174.
PeptideAtlasiP60174.
PRIDEiP60174.
TopDownProteomicsiP60174-1. [P60174-1]
P60174-3. [P60174-3]
P60174-4. [P60174-4]

2D gel databases

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

PTM databases

iPTMnetiP60174.
PhosphoSitePlusiP60174.
SwissPalmiP60174.

Expressioni

Gene expression databases

BgeeiENSG00000111669.
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
TERF1P542742EBI-717475,EBI-710997

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi113020. 86 interactors.
IntActiP60174. 17 interactors.
MINTiMINT-1384176.
STRINGi9606.ENSP00000229270.

Chemistry databases

BindingDBiP60174.

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 49Combined sources6
Helixi56 – 68Combined sources13
Beta strandi75 – 80Combined sources6
Helixi83 – 85Combined sources3
Helixi86 – 92Combined sources7
Beta strandi97 – 102Combined sources6
Beta strandi106 – 111Combined sources6
Helixi118 – 123Combined sources6
Beta strandi128 – 132Combined sources5
Helixi134 – 138Combined sources5
Helixi144 – 156Combined sources13
Beta strandi160 – 165Combined sources6
Helixi169 – 173Combined sources5
Helixi177 – 190Combined sources14
Helixi195 – 197Combined sources3
Beta strandi198 – 202Combined sources5
Helixi205 – 207Combined sources3
Turni208 – 210Combined sources3
Helixi216 – 233Combined sources18
Helixi236 – 241Combined sources6
Beta strandi244 – 246Combined sources3
Turni252 – 254Combined sources3
Helixi255 – 260Combined sources6
Beta strandi266 – 269Combined sources4
Helixi271 – 274Combined sources4
Helixi277 – 282Combined sources6
Turni283 – 285Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ZVJX-ray1.70A/B38-286[»]
ProteinModelPortaliP60174.
SMRiP60174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60174.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiKOG1643. Eukaryota.
COG0149. LUCA.
GeneTreeiENSGT00390000013354.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP60174.
KOiK01803.
OMAiFERRKFF.
OrthoDBiEOG091G0LEZ.
PhylomeDBiP60174.
TreeFamiTF300829.

Family and domain databases

CDDicd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B. 1 hit.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAB59511 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH07086 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH07812 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH09329 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH11611 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH15100 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH17917 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH70129 differs from that shown. Sequence differs at the C-terminus.Curated
The sequence AAH70129 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAN86636 differs from that shown. Reason: Frameshift at position 23.Curated
The sequence BAG36090 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA49379 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23 – 26RLRA → TAR in AAB59511 (PubMed:2579079).Curated4
Sequence conflicti36Missing in AAB59511 (PubMed:2579079).Curated1
Sequence conflicti36Missing in AAN86636 (PubMed:16541075).Curated1
Sequence conflicti57 – 58QS → KN AA sequence (PubMed:6434534).Curated2
Sequence conflicti64G → S AA sequence (PubMed:6434534).Curated1
Sequence conflicti67 – 68NA → QG AA sequence (PubMed:6434534).Curated2
Sequence conflicti80 – 81AP → IG AA sequence (PubMed:6434534).Curated2
Sequence conflicti95P → Q AA sequence (PubMed:6434534).Curated1
Sequence conflicti192V → A in AAH17917 (PubMed:15489334).Curated1
Sequence conflicti204P → N AA sequence (PubMed:6434534).Curated1
Sequence conflicti281I → L AA sequence (PubMed:6434534).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00753479C → Y in TPID. 1 PublicationCorresponds to variant rs121964848dbSNPEnsembl.1
Natural variantiVAR_007535110G → A in TPID. 1 Publication1
Natural variantiVAR_007536142E → D in TPID; the enzyme becomes thermolabile. 5 PublicationsCorresponds to variant rs121964845dbSNPEnsembl.1
Natural variantiVAR_007537160G → R in Manchester; thermolabile. 1 PublicationCorresponds to variant rs121964846dbSNPEnsembl.1
Natural variantiVAR_007538192V → M in TPID. 1 PublicationCorresponds to variant rs188138723dbSNPEnsembl.1
Natural variantiVAR_007539208I → V in TPID. 1 PublicationCorresponds to variant rs121964849dbSNPEnsembl.1
Natural variantiVAR_007540269V → M in TPID. 1 Publication1
Natural variantiVAR_007541278F → L in TPID; Hungary; thermolabile. 1 PublicationCorresponds to variant rs121964847dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0453101 – 119Missing in isoform 4. 1 PublicationAdd BLAST119
Alternative sequenceiVSP_0418951 – 37Missing in isoform 2. CuratedAdd BLAST37

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. [P60174-3]
ENST00000396705; ENSP00000379933; ENSG00000111669. [P60174-1]
ENST00000488464; ENSP00000475620; ENSG00000111669. [P60174-4]
ENST00000535434; ENSP00000443599; ENSG00000111669. [P60174-4]
ENST00000613953; ENSP00000484435; ENSG00000111669. [P60174-3]
GeneIDi7167.
KEGGihsa:7167.
UCSCiuc001qrk.5. 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
PDB 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[»]
4ZVJX-ray1.70A/B38-286[»]
ProteinModelPortaliP60174.
SMRiP60174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113020. 86 interactors.
IntActiP60174. 17 interactors.
MINTiMINT-1384176.
STRINGi9606.ENSP00000229270.

Chemistry databases

BindingDBiP60174.
ChEMBLiCHEMBL4880.

PTM databases

iPTMnetiP60174.
PhosphoSitePlusiP60174.
SwissPalmiP60174.

Polymorphism and mutation databases

BioMutaiTPI1.
DMDMi353526311.

2D gel databases

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

Proteomic databases

EPDiP60174.
MaxQBiP60174.
PaxDbiP60174.
PeptideAtlasiP60174.
PRIDEiP60174.
TopDownProteomicsiP60174-1. [P60174-1]
P60174-3. [P60174-3]
P60174-4. [P60174-4]

Protocols and materials databases

DNASUi7167.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229270; ENSP00000229270; ENSG00000111669. [P60174-3]
ENST00000396705; ENSP00000379933; ENSG00000111669. [P60174-1]
ENST00000488464; ENSP00000475620; ENSG00000111669. [P60174-4]
ENST00000535434; ENSP00000443599; ENSG00000111669. [P60174-4]
ENST00000613953; ENSP00000484435; ENSG00000111669. [P60174-3]
GeneIDi7167.
KEGGihsa:7167.
UCSCiuc001qrk.5. human. [P60174-3]

Organism-specific databases

CTDi7167.
DisGeNETi7167.
GeneCardsiTPI1.
HGNCiHGNC:12009. TPI1.
HPAiCAB004675.
HPA050924.
HPA053568.
MalaCardsiTPI1.
MIMi190450. gene.
615512. phenotype.
neXtProtiNX_P60174.
OpenTargetsiENSG00000111669.
Orphaneti868. Triose phosphate-isomerase deficiency.
PharmGKBiPA36689.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1643. Eukaryota.
COG0149. LUCA.
GeneTreeiENSGT00390000013354.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP60174.
KOiK01803.
OMAiFERRKFF.
OrthoDBiEOG091G0LEZ.
PhylomeDBiP60174.
TreeFamiTF300829.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BioCyciMetaCyc:HS03441-MONOMER.
ZFISH:HS03441-MONOMER.
BRENDAi5.3.1.1. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP60174.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000111669.
CleanExiHS_TPI1.
ExpressionAtlasiP60174. baseline and differential.
GenevisibleiP60174. HS.

Family and domain databases

CDDicd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B. 1 hit.
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...

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: November 2, 2016
This is version 152 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

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 one 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.