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P60174

- TPIS_HUMAN

UniProt

P60174 - TPIS_HUMAN

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Protein

Triosephosphate isomerase

Gene
TPI1, TPI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.UniRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. triose-phosphate isomerase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. embryo development Source: Ensembl
  3. gluconeogenesis Source: Reactome
  4. glucose metabolic process Source: Reactome
  5. glyceraldehyde-3-phosphate metabolic process Source: Ensembl
  6. glycolytic process Source: Reactome
  7. pentose-phosphate shunt Source: UniProtKB-KW
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

BioCyciMetaCyc:HS03441-MONOMER.
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: Chromosome 12

Organism-specific databases

HGNCiHGNC:12009. TPI1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Triosephosphate isomerase deficiency (TPID) [MIM:615512]: An autosomal recessive multisystem disorder characterized by congenital hemolytic anemia, progressive neuromuscular dysfunction, susceptibility to bacterial infection, and cardiomyopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Triosephosphate isomeraseUniRule annotationPRO_0000090113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine1 Publication
Modified residuei58 – 581Phosphoserine9 Publications
Modified residuei105 – 1051Nitrated tyrosine By similarity
Modified residuei117 – 1171Phosphoserine1 Publication
Modified residuei186 – 1861N6-succinyllysine By similarity
Modified residuei193 – 1931N6-acetyllysine; alternate By similarity
Modified residuei193 – 1931N6-succinyllysine; alternate By similarity
Modified residuei231 – 2311N6-acetyllysine; alternate1 Publication
Modified residuei231 – 2311N6-succinyllysine; alternate By similarity
Modified residuei246 – 2461Nitrated tyrosine By similarity
Modified residuei249 – 2491Phosphoserine By similarity
Modified residuei275 – 2751N6-acetyllysine1 Publication

Post-translational modificationi

The initiator methionine for isoform 2 is removed.UniRule annotation

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.
GenevestigatoriP60174.

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. 40 interactions.
IntActiP60174. 14 interactions.
MINTiMINT-1384176.
STRINGi9606.ENSP00000379933.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 496
Helixi56 – 6813
Beta strandi75 – 806
Helixi83 – 853
Helixi86 – 927
Beta strandi97 – 1026
Beta strandi106 – 1116
Helixi118 – 1236
Beta strandi128 – 1325
Helixi134 – 1385
Helixi144 – 15613
Beta strandi160 – 1656
Helixi169 – 1735
Helixi177 – 19014
Helixi195 – 1973
Beta strandi198 – 2025
Helixi205 – 2073
Beta strandi208 – 2114
Helixi216 – 23116
Helixi236 – 2416
Beta strandi244 – 2463
Turni252 – 2543
Helixi255 – 2595
Beta strandi266 – 2705
Helixi271 – 2744
Helixi277 – 2826
Turni283 – 2853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP60174.
SMRiP60174. Positions 41-286.

Miscellaneous databases

EvolutionaryTraceiP60174.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0149.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP60174.
KOiK01803.
OMAiPAIYLDQ.
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. Align

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

MAEDGEEAEF HFAALYISGQ WPRLRADTDL QRLGSSAMAP SRKFFVGGNW    50
KMNGRKQSLG ELIGTLNAAK VPADTEVVCA PPTAYIDFAR QKLDPKIAVA 100
AQNCYKVTNG AFTGEISPGM IKDCGATWVV LGHSERRHVF GESDELIGQK 150
VAHALAEGLG VIACIGEKLD EREAGITEKV VFEQTKVIAD NVKDWSKVVL 200
AYEPVWAIGT GKTATPQQAQ EVHEKLRGWL KSNVSDAVAQ STRIIYGGSV 250
TGATCKELAS QPDVDGFLVG GASLKPEFVD IINAKQ 286
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 AAH70129.1 differs from that shown. Reason: Sequence differs at the C-terminus.
The sequence AAN86636.1 differs from that shown. Reason: Frameshift at position 23.
The sequence AAB51316.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAB59511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH07086.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH07812.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH09329.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH11611.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH15100.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH17917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH70129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAG36090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA49379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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. VSP_045310Add
BLAST
Alternative sequencei1 – 3737Missing in isoform 2. VSP_041895Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 264RLRA → TAR in AAB59511. 1 Publication
Sequence conflicti36 – 361Missing in AAB59511. 1 Publication
Sequence conflicti36 – 361Missing in AAN86636. 1 Publication
Sequence conflicti57 – 582QS → KN AA sequence 1 Publication
Sequence conflicti64 – 641G → S AA sequence 1 Publication
Sequence conflicti67 – 682NA → QG AA sequence 1 Publication
Sequence conflicti80 – 812AP → IG AA sequence 1 Publication
Sequence conflicti95 – 951P → Q AA sequence 1 Publication
Sequence conflicti192 – 1921V → A in AAH17917. 1 Publication
Sequence conflicti204 – 2041P → N AA sequence 1 Publication
Sequence conflicti281 – 2811I → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000595390; ENSP00000469350; ENSG00000268548. [P60174-1]
ENST00000598287; ENSP00000469966; ENSG00000268548. [P60174-4]
ENST00000599583; ENSP00000476032; ENSG00000268548. [P60174-4]
ENST00000601074; ENSP00000469782; ENSG00000268548. [P60174-3]
GeneIDi7167.
KEGGihsa:7167.
UCSCiuc001qrk.4. human. [P60174-3]

Polymorphism databases

DMDMi353526311.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Triosephosphate isomerase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53740.1. [P60174-3 ]
CCDS58206.1. [P60174-4 ]
CCDS8566.1. [P60174-1 ]
PIRi S29743. ISHUT.
RefSeqi NP_000356.1. NM_000365.5. [P60174-1 ]
NP_001152759.1. NM_001159287.1. [P60174-3 ]
NP_001244955.1. NM_001258026.1. [P60174-4 ]
UniGenei Hs.524219.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HTI X-ray 2.80 A/B 39-286 [» ]
1KLG X-ray 2.40 C 60-74 [» ]
1KLU X-ray 1.93 C 60-74 [» ]
1WYI X-ray 2.20 A/B 39-286 [» ]
2IAM X-ray 2.80 P 60-74 [» ]
2IAN X-ray 2.80 C/H/M/R 60-74 [» ]
2JK2 X-ray 1.70 A/B 39-286 [» ]
2VOM X-ray 1.85 A/B/C/D 39-286 [» ]
4BR1 X-ray 1.90 A/B 41-286 [» ]
4E41 X-ray 2.60 C/H 60-74 [» ]
ProteinModelPortali P60174.
SMRi P60174. Positions 41-286.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113020. 40 interactions.
IntActi P60174. 14 interactions.
MINTi MINT-1384176.
STRINGi 9606.ENSP00000379933.

Chemistry

BindingDBi P60174.
ChEMBLi CHEMBL4880.

PTM databases

PhosphoSitei P60174.

Polymorphism databases

DMDMi 353526311.

2D gel databases

DOSAC-COBS-2DPAGE P60174.
REPRODUCTION-2DPAGE IPI00797687.
P60174.
SWISS-2DPAGE P60174.
UCD-2DPAGE P00938.
P60174.

Proteomic databases

MaxQBi P60174.
PaxDbi P60174.
PRIDEi P60174.

Protocols and materials databases

DNASUi 7167.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229270 ; ENSP00000229270 ; ENSG00000111669 . [P60174-3 ]
ENST00000396705 ; ENSP00000379933 ; ENSG00000111669 . [P60174-1 ]
ENST00000488464 ; ENSP00000475620 ; ENSG00000111669 . [P60174-4 ]
ENST00000535434 ; ENSP00000443599 ; ENSG00000111669 . [P60174-4 ]
ENST00000595390 ; ENSP00000469350 ; ENSG00000268548 . [P60174-1 ]
ENST00000598287 ; ENSP00000469966 ; ENSG00000268548 . [P60174-4 ]
ENST00000599583 ; ENSP00000476032 ; ENSG00000268548 . [P60174-4 ]
ENST00000601074 ; ENSP00000469782 ; ENSG00000268548 . [P60174-3 ]
GeneIDi 7167.
KEGGi hsa:7167.
UCSCi uc001qrk.4. human. [P60174-3 ]

Organism-specific databases

CTDi 7167.
GeneCardsi GC12P007112.
HGNCi HGNC:12009. TPI1.
HPAi CAB004675.
HPA050924.
HPA053568.
MIMi 190450. gene.
615512. phenotype.
neXtProti NX_P60174.
Orphaneti 868. Triose phosphate-isomerase deficiency.
PharmGKBi PA36689.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0149.
HOGENOMi HOG000226413.
HOVERGENi HBG002599.
InParanoidi P60174.
KOi K01803.
OMAi PAIYLDQ.
OrthoDBi EOG76DTT8.
PhylomeDBi P60174.
TreeFami TF300829.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00189 .
UPA00138 .
BioCyci MetaCyc:HS03441-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P60174.

Miscellaneous databases

ChiTaRSi TPI1. human.
EvolutionaryTracei P60174.
GeneWikii TPI1.
GenomeRNAii 7167.
NextBioi 28066.
PROi P60174.
SOURCEi Search...

Gene expression databases

Bgeei P60174.
CleanExi HS_TPI1.
Genevestigatori P60174.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00147_B. TIM_B.
InterProi IPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view ]
PANTHERi PTHR21139. PTHR21139. 1 hit.
Pfami PF00121. TIM. 1 hit.
[Graphical view ]
SUPFAMi SSF51351. SSF51351. 1 hit.
TIGRFAMsi TIGR00419. tim. 1 hit.
PROSITEi PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. "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: September 3, 2014
This is version 128 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

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