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P60174

- TPIS_HUMAN

UniProt

P60174 - TPIS_HUMAN

Protein

Triosephosphate isomerase

Gene

TPI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (19 Oct 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-glyceraldehyde 3-phosphate = glycerone phosphate.

    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

    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

    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 4 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 isomerasePRO_0000090113Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    The initiator methionine for isoform 2 is removed.

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP60174.
    PaxDbiP60174.
    PRIDEiP60174.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP60174.

    Expressioni

    Gene expression databases

    BgeeiP60174.
    CleanExiHS_TPI1.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60174.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the triosephosphate isomerase family.Curated

    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.

    Experimental Info

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791C → Y in TPID. 1 Publication
    VAR_007534
    Natural varianti110 – 1101G → A in TPID. 1 Publication
    VAR_007535
    Natural varianti142 – 1421E → D in TPID; the enzyme becomes thermolabile. 4 Publications
    VAR_007536
    Natural varianti160 – 1601G → R in Manchester; thermolabile. 1 Publication
    VAR_007537
    Natural varianti192 – 1921V → M in TPID. 1 Publication
    Corresponds to variant rs188138723 [ dbSNP | Ensembl ].
    VAR_007538
    Natural varianti208 – 2081I → V in TPID. 1 Publication
    VAR_007539
    Natural varianti269 – 2691V → M in TPID. 1 Publication
    VAR_007540
    Natural varianti278 – 2781F → L in TPID; Hungary; thermolabile. 1 Publication
    VAR_007541

    Alternative sequence

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

    Sequence databases

    Select the link destinations:
    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]
    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 ]
    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

    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: October 1, 2014
    This is version 129 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