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P60174 (TPIS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Triosephosphate isomerase

Short name=TIM
EC=5.3.1.1
Alternative name(s):
Triose-phosphate isomerase
Gene names
Name:TPI1
Synonyms:TPI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP-Rule MF_00147_B

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00147_B

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP-Rule MF_00147_B

Subunit structure

Homodimer. Ref.27 Ref.29

Post-translational modification

The initiator methionine for isoform 2 is removed. HAMAP-Rule MF_00147_B

Involvement in disease

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. Ref.30 Ref.31 Ref.33 Ref.34 Ref.35

Sequence similarities

Belongs to the triosephosphate isomerase family.

Sequence caution

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 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 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PCNAP120042EBI-717475,EBI-358311

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: P60174-3)

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.
Isoform 2 (identifier: P60174-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.
Isoform 4 (identifier: P60174-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Triosephosphate isomerase HAMAP-Rule MF_00147_B
PRO_0000090113

Sites

Active site1331Electrophile
Active site2031Proton acceptor
Binding site491Substrate
Binding site511Substrate

Amino acid modifications

Modified residue511N6-acetyllysine Ref.23
Modified residue581Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.26
Modified residue1051Nitrated tyrosine By similarity
Modified residue1171Phosphoserine Ref.22
Modified residue1861N6-succinyllysine By similarity
Modified residue1931N6-acetyllysine; alternate By similarity
Modified residue1931N6-succinyllysine; alternate By similarity
Modified residue2311N6-acetyllysine; alternate Ref.23
Modified residue2311N6-succinyllysine; alternate By similarity
Modified residue2461Nitrated tyrosine By similarity
Modified residue2491Phosphoserine By similarity
Modified residue2751N6-acetyllysine Ref.23

Natural variations

Alternative sequence1 – 119119Missing in isoform 4.
VSP_045310
Alternative sequence1 – 3737Missing in isoform 2.
VSP_041895
Natural variant791C → Y in TPID. Ref.35
VAR_007534
Natural variant1101G → A in TPID. Ref.34
VAR_007535
Natural variant1421E → D in TPID; the enzyme becomes thermolabile. Ref.29 Ref.30 Ref.31 Ref.34 Ref.35
VAR_007536
Natural variant1601G → R in Manchester; thermolabile. Ref.32
VAR_007537
Natural variant1921V → M in TPID. Ref.34
Corresponds to variant rs188138723 [ dbSNP | Ensembl ].
VAR_007538
Natural variant2081I → V in TPID. Ref.35
VAR_007539
Natural variant2691V → M in TPID. Ref.31
VAR_007540
Natural variant2781F → L in TPID; Hungary; thermolabile. Ref.33
VAR_007541

Experimental info

Sequence conflict23 – 264RLRA → TAR in AAB59511. Ref.1
Sequence conflict361Missing in AAB59511. Ref.1
Sequence conflict361Missing in AAN86636. Ref.6
Sequence conflict57 – 582QS → KN AA sequence Ref.11
Sequence conflict641G → S AA sequence Ref.11
Sequence conflict67 – 682NA → QG AA sequence Ref.11
Sequence conflict80 – 812AP → IG AA sequence Ref.11
Sequence conflict951P → Q AA sequence Ref.11
Sequence conflict1921V → A in AAH17917. Ref.9
Sequence conflict2041P → N AA sequence Ref.11
Sequence conflict2811I → L AA sequence Ref.11

Secondary structure

................................................. 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 19, 2011. Version 3.
Checksum: E6C2157706AE97F8

FASTA28630,791
        10         20         30         40         50         60 
MAEDGEEAEF HFAALYISGQ WPRLRADTDL QRLGSSAMAP SRKFFVGGNW KMNGRKQSLG 

        70         80         90        100        110        120 
ELIGTLNAAK VPADTEVVCA PPTAYIDFAR QKLDPKIAVA AQNCYKVTNG AFTGEISPGM 

       130        140        150        160        170        180 
IKDCGATWVV LGHSERRHVF GESDELIGQK VAHALAEGLG VIACIGEKLD EREAGITEKV 

       190        200        210        220        230        240 
VFEQTKVIAD NVKDWSKVVL AYEPVWAIGT GKTATPQQAQ EVHEKLRGWL KSNVSDAVAQ 

       250        260        270        280 
STRIIYGGSV TGATCKELAS QPDVDGFLVG GASLKPEFVD IINAKQ 

« Hide

Isoform 2 [UniParc].

Checksum: 73844175635F858E
Show »

FASTA24926,669
Isoform 4 [UniParc].

Checksum: 1E9ADB034A513E18
Show »

FASTA16717,958

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Triosephosphate isomerase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRISHUT. S29743.
RefSeqNP_000356.1. NM_000365.5.
NP_001152759.1. NM_001159287.1.
NP_001244955.1. NM_001258026.1.
UniGeneHs.524219.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HTIX-ray2.80A/B39-286[»]
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[»]
ProteinModelPortalP60174.
SMRP60174. Positions 41-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113020. 36 interactions.
IntActP60174. 14 interactions.
MINTMINT-1384176.
STRING9606.ENSP00000379933.

Chemistry

BindingDBP60174.
ChEMBLCHEMBL4880.

PTM databases

PhosphoSiteP60174.

Polymorphism databases

DMDM353526311.

2D gel databases

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

Proteomic databases

PaxDbP60174.
PRIDEP60174.

Protocols and materials databases

DNASU7167.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229270; 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]
GeneID7167.
KEGGhsa:7167.
UCSCuc001qrk.4. human. [P60174-3]

Organism-specific databases

CTD7167.
GeneCardsGC12P007112.
HGNCHGNC:12009. TPI1.
HPACAB004675.
HPA050924.
HPA053568.
MIM190450. gene.
615512. phenotype.
neXtProtNX_P60174.
Orphanet868. Triose phosphate-isomerase deficiency.
PharmGKBPA36689.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0149.
HOGENOMHOG000226413.
HOVERGENHBG002599.
InParanoidP60174.
KOK01803.
OMALYISGQW.
OrthoDBEOG76DTT8.
TreeFamTF300829.

Enzyme and pathway databases

BioCycMetaCyc:HS03441-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP60174.
UniPathwayUPA00109; UER00189.
UPA00138.

Gene expression databases

BgeeP60174.
CleanExHS_TPI1.
GenevestigatorP60174.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00147_B. TIM_B.
InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERPTHR21139. PTHR21139. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMSSF51351. SSF51351. 1 hit.
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTPI1. human.
EvolutionaryTraceP60174.
GeneWikiTPI1.
GenomeRNAi7167.
NextBio28066.
PROP60174.
SOURCESearch...

Entry information

Entry nameTPIS_HUMAN
AccessionPrimary (citable) accession number: P60174
Secondary accession number(s): B7Z5D8 expand/collapse secondary AC list , D3DUS9, P00938, Q6FHP9, Q6IS07, Q8WWD0, Q96AG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 19, 2011
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM