HUMAN:TPIS

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TPI1 (synonyms: TPI)
Protein Name(s)	Triosephosphate isomerase TIM Triose-phosphate isomerase
External Links
UniProt	P60174
EMBL	M10036 X69723 AK298809 U47924 CH471116 CH471116 J04603 BC007086 BC007812 BC009329 BC011611 BC015100 BC017165 BC017917 BC070129 AK313282 CR541702
CCDS	CCDS53740.1 CCDS58206.1 CCDS8566.1
PIR	S29743
RefSeq	NP_000356.1 NP_001152759.1 NP_001244955.1
UniGene	Hs.524219
PDB	1HTI 1KLG 1KLU 1WYI 2IAM 2IAN 2JK2 2VOM 4BR1 4E41
PDBsum	1HTI 1KLG 1KLU 1WYI 2IAM 2IAN 2JK2 2VOM 4BR1 4E41
ProteinModelPortal	P60174
SMR	P60174
BioGrid	113020
IntAct	P60174
MINT	MINT-1384176
STRING	9606.ENSP00000379933
BindingDB	P60174
ChEMBL	CHEMBL4880
PhosphoSite	P60174
DMDM	353526311
DOSAC-COBS-2DPAGE	P60174
REPRODUCTION-2DPAGE	IPI00797687 P60174
SWISS-2DPAGE	P60174
UCD-2DPAGE	P00938 P60174
MaxQB	P60174
PaxDb	P60174
PRIDE	P60174
DNASU	7167
Ensembl	ENST00000229270 ENST00000396705 ENST00000488464 ENST00000535434 ENST00000613953
GeneID	7167
KEGG	hsa:7167
UCSC	uc001qrk.4
CTD	7167
GeneCards	GC12P007138
HGNC	HGNC:12009
HPA	CAB004675 HPA050924 HPA053568
MIM	190450 615512
neXtProt	NX_P60174
Orphanet	868
PharmGKB	PA36689
eggNOG	COG0149
GeneTree	ENSGT00390000013354
HOGENOM	HOG000226413
HOVERGEN	HBG002599
InParanoid	P60174
KO	K01803
OMA	QYHHESS
OrthoDB	EOG76DTT8
PhylomeDB	P60174
TreeFam	TF300829
BioCyc	MetaCyc:HS03441-MONOMER
Reactome	REACT_1383 REACT_1520
SABIO-RK	P60174
UniPathway	UPA00109 UPA00138
ChiTaRS	TPI1
EvolutionaryTrace	P60174
GeneWiki	TPI1
GenomeRNAi	7167
NextBio	28066
PRO	PR:P60174
Proteomes	UP000005640
Bgee	P60174
CleanEx	HS_TPI1
ExpressionAtlas	P60174
Genevestigator	P60174
GO	GO:0005829 GO:0005615 GO:0070062 GO:0005634 GO:0004807 GO:0005975 GO:0006094 GO:0006006 GO:0019682 GO:0006096 GO:0007275 GO:0006098 GO:0044281
Gene3D	3.20.20.70
HAMAP	MF_00147_B
InterPro	IPR013785 IPR022896 IPR000652 IPR020861
PANTHER	PTHR21139
Pfam	PF00121
SUPFAM	SSF51351
TIGRFAMs	TIGR00419
PROSITE	PS00171 PS51440

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0046166	glyceraldehyde-3-phosphate biosynthetic process	PMID:18562316^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008929	methylglyoxal synthase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P00939	F		Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	PMID:18562316^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:18562316^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0019242	methylglyoxal biosynthetic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P00939	P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:19725078^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:23580065^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22664934^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	PMID:2876430^[9]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0046166	glyceraldehyde-3-phosphate biosynthetic process	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000474559 UniProtKB:Q9SKP6	P		Seeded From UniProt	complete
involved_in	GO:0019563	glycerol catabolic process	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000474559 UniProtKB:Q9SKP6	P		Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11015 FB:FBgn0086355 PANTHER:PTN000474559 SGD:S000002457 UniProtKB:P9WG43	P		Seeded From UniProt	complete
involved_in	GO:0006094	gluconeogenesis	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11015 PANTHER:PTN000474559 UniProtKB:P9WG43	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11015 PANTHER:PTN000474559 RGD:3896 UniProtKB:P9WG43 UniProtKB:Q9SKP6	C		Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11015 FB:FBgn0086355 MGI:MGI:98797 PANTHER:PTN000474559 PomBase:SPCC24B10.21 RGD:3896 SGD:S000002457 UniProtKB:P60174 UniProtKB:P9WG43 UniProtKB:Q7KQM0 UniProtKB:Q9SKP6	F		Seeded From UniProt	complete
involved_in	GO:0019682	glyceraldehyde-3-phosphate metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17751 ensembl:ENSMUSP00000130858	P		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17751 ensembl:ENSMUSP00000130858	F		Seeded From UniProt	complete
involved_in	GO:0007275	multicellular organism development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17751 ensembl:ENSMUSP00000130858	P		Seeded From UniProt	complete
involved_in	GO:0006006	glucose metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17751 ensembl:ENSMUSP00000130858	P		Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17751 ensembl:ENSMUSP00000130858	F		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013785	F		Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000652 InterPro:IPR020861 InterPro:IPR022896 InterPro:IPR035990	F		Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR022896	P		Seeded From UniProt	complete
enables	GO:0008929	methylglyoxal synthase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.3.3	F		Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:5.3.1.1	F		Seeded From UniProt	complete
enables	GO:0004807	triose-phosphate isomerase activity	PMID:2579079^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061621	canonical glycolysis	Reactome:R-HSA-70171	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006094	gluconeogenesis	Reactome:R-HSA-70263	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-70481 Reactome:R-HSA-70454	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006096	glycolytic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0324 UniPathway:UPA00109	P		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F		Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F		Seeded From UniProt	complete
involved_in	GO:0006094	gluconeogenesis	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0312 UniPathway:UPA00138	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Rodríguez-Almazán, C et al. (2008) Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J. Biol. Chem. 283 23254-63 PubMed GONUTS page
↑ Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
↑ Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page
↑ Daar, IO et al. (1986) Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme. Proc. Natl. Acad. Sci. U.S.A. 83 7903-7 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Maquat, LE et al. (1985) Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man. J. Biol. Chem. 260 3748-53 PubMed GONUTS page

[PMID:18562316-1] 1.0 ^1.1 ^1.2 Rodríguez-Almazán, C et al. (2008) Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J. Biol. Chem. 283 23254-63 PubMed GONUTS page

[PMID:19725078-2] Davison, EJ et al. (2009) Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9 4284-97 PubMed GONUTS page

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-4] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:21630459-5] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:16502470-6] Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page

[PMID:23580065-7] Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page

[PMID:22664934-8] Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page

[PMID:2876430-9] Daar, IO et al. (1986) Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme. Proc. Natl. Acad. Sci. U.S.A. 83 7903-7 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:2579079-11] Maquat, LE et al. (1985) Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man. J. Biol. Chem. 260 3748-53 PubMed GONUTS page

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HUMAN:TPIS

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Annotations

Notes

References

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