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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)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.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791C → Y in TPID. 1 Publication
Corresponds to variant rs121964848 [ dbSNP | Ensembl ].
VAR_007534
Natural varianti110 – 1101G → A in TPID. 1 Publication
VAR_007535
Natural varianti142 – 1421E → D in TPID; the enzyme becomes thermolabile. 5 Publications
Corresponds to variant rs121964845 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121964849 [ dbSNP | Ensembl ].
VAR_007539
Natural varianti269 – 2691V → M in TPID. 1 Publication
VAR_007540
Natural varianti278 – 2781F → L in TPID; Hungary; thermolabile. 1 Publication
Corresponds to variant rs121964847 [ dbSNP | Ensembl ].
VAR_007541

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL4880.

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-acetyllysineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei105 – 1051Nitrated tyrosineBy similarity
Modified residuei117 – 1171PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineBy similarity
Cross-linki179 – 179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei186 – 1861N6-succinyllysineBy similarity
Modified residuei193 – 1931N6-acetyllysine; alternateBy similarity
Modified residuei193 – 1931N6-succinyllysine; alternateBy similarity
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei210 – 2101PhosphothreonineBy similarity
Modified residuei231 – 2311N6-acetyllysine; alternateCombined sources
Modified residuei231 – 2311N6-succinyllysine; alternateBy similarity
Modified residuei235 – 2351PhosphoserineBy similarity
Modified residuei246 – 2461Nitrated tyrosineBy similarity
Modified residuei249 – 2491PhosphoserineCombined sources
Modified residuei251 – 2511PhosphothreonineCombined sources
Modified residuei260 – 2601PhosphoserineCombined sources
Modified residuei275 – 2751N6-acetyllysineCombined sources

Post-translational modificationi

The initiator methionine for isoform 2 is removed.

Keywords - PTMi

Acetylation, Isopeptide bond, 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.
PhosphoSiteiP60174.
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. 85 interactions.
IntActiP60174. 17 interactions.
MINTiMINT-1384176.
STRINGi9606.ENSP00000229270.

Chemistry

BindingDBiP60174.

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[»]
4ZVJX-ray1.70A/B38-286[»]
ProteinModelPortaliP60174.
SMRiP60174. Positions 41-286.
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)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
Corresponds to variant rs121964848 [ dbSNP | Ensembl ].
VAR_007534
Natural varianti110 – 1101G → A in TPID. 1 Publication
VAR_007535
Natural varianti142 – 1421E → D in TPID; the enzyme becomes thermolabile. 5 Publications
Corresponds to variant rs121964845 [ dbSNP | Ensembl ].
VAR_007536
Natural varianti160 – 1601G → R in Manchester; thermolabile. 1 Publication
Corresponds to variant rs121964846 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121964849 [ dbSNP | Ensembl ].
VAR_007539
Natural varianti269 – 2691V → M in TPID. 1 Publication
VAR_007540
Natural varianti278 – 2781F → L in TPID; Hungary; thermolabile. 1 Publication
Corresponds to variant rs121964847 [ dbSNP | Ensembl ].
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. [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
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. Positions 41-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113020. 85 interactions.
IntActiP60174. 17 interactions.
MINTiMINT-1384176.
STRINGi9606.ENSP00000229270.

Chemistry

BindingDBiP60174.
ChEMBLiCHEMBL4880.

PTM databases

iPTMnetiP60174.
PhosphoSiteiP60174.
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.
GeneCardsiTPI1.
HGNCiHGNC:12009. TPI1.
HPAiCAB004675.
HPA050924.
HPA053568.
MalaCardsiTPI1.
MIMi190450. gene.
615512. phenotype.
neXtProtiNX_P60174.
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.
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: September 7, 2016
This is version 150 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.