P60174 (TPIS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Triosephosphate isomerase
Short name=TIM
EC=5.3.1.1

Alternative name(s):
Triose-phosphate isomerase

Gene names

Name:	TPI1
Synonyms:	TPI

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
Subunit structure	Homodimer. Ref.26 Ref.28
Post-translational modification	The initiator methionine for isoform 2 is removed.
Involvement in disease	Triosephosphate isomerase deficiency (TPI deficiency) [MIM:190450]: Autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection. Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis Pentose shunt
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Disease	Disease mutation
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	embryo development Inferred from electronic annotation. Source: Compara gluconeogenesis Traceable author statement. Source: Reactome glyceraldehyde-3-phosphate metabolic process Inferred from electronic annotation. Source: Compara glycolysis Traceable author statement. Source: Reactome pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	triose-phosphate isomerase activity Non-traceable author statement Ref.29. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 286

286

Triosephosphate isomerase

PRO_0000090113

Sites

Active site

133

1

Electrophile

Active site

203

1

Proton acceptor

Binding site

49

1

Substrate

Binding site

51

1

Substrate

Amino acid modifications

Modified residue

51

1

N6-acetyllysine Ref.22

Modified residue

58

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25

Modified residue

117

1

Phosphoserine Ref.21

Modified residue

231

1

N6-acetyllysine Ref.22

Modified residue

275

1

N6-acetyllysine Ref.22

Natural variations

Alternative sequence

1 – 119

119

Missing in isoform 4.

VSP_045310

Alternative sequence

1 – 37

37

Missing in isoform 2.

VSP_041895

Natural variant

79

1

C → Y in TPI deficiency. Ref.34

VAR_007534

Natural variant

110

1

G → A in TPI deficiency. Ref.33

VAR_007535

Natural variant

142

1

E → D in TPI deficiency; the enzyme becomes thermolabile. Ref.28 Ref.29 Ref.30 Ref.33 Ref.34

VAR_007536

Natural variant

160

1

G → R in Manchester; thermolabile. Ref.31

VAR_007537

Natural variant

192

1

V → M in TPI deficiency. Ref.33

VAR_007538

Natural variant

208

1

I → V in TPI deficiency. Ref.34

VAR_007539

Natural variant

269

1

V → M in TPI deficiency. Ref.30

VAR_007540

Natural variant

278

1

F → L in TPI deficiency; Hungary; thermolabile. Ref.32

VAR_007541

Experimental info

Sequence conflict

23 – 26

4

RLRA → TAR in AAB59511. Ref.1

Sequence conflict

36

1

Missing in AAB59511. Ref.1

Sequence conflict

36

1

Missing in AAN86636. Ref.6

Sequence conflict

57 – 58

2

QS → KN AA sequence Ref.11

Sequence conflict

64

1

G → S AA sequence Ref.11

Sequence conflict

67 – 68

2

NA → QG AA sequence Ref.11

Sequence conflict

80 – 81

2

AP → IG AA sequence Ref.11

Sequence conflict

95

1

P → Q AA sequence Ref.11

Sequence conflict

192

1

V → A in AAH17917. Ref.9

Sequence conflict

204

1

P → N AA sequence Ref.11

Sequence conflict

281

1

I → L AA sequence Ref.11

Secondary structure

1

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286

Helix Strand Turn

Details...

Beta strand

44 – 49

6

Helix

56 – 68

13

Beta strand

75 – 80

6

Helix

83 – 85

3

Helix

86 – 92

7

Beta strand

97 – 102

6

Beta strand

106 – 111

6

Helix

118 – 123

6

Beta strand

128 – 132

5

Helix

134 – 138

5

Helix

144 – 156

13

Beta strand

160 – 165

6

Helix

169 – 173

5

Helix

177 – 190

14

Helix

195 – 197

3

Beta strand

198 – 202

5

Helix

205 – 207

3

Beta strand

208 – 211

4

Helix

216 – 231

16

Helix

236 – 241

6

Beta strand

244 – 246

3

Turn

252 – 254

3

Helix

255 – 259

5

Beta strand

266 – 270

5

Helix

271 – 274

4

Helix

277 – 282

6

Turn

283 – 285

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 19, 2011. Version 3. Checksum: E6C2157706AE97F8	FASTA	286	30,791
	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
	Isoform 2 [UniParc]. Checksum: 73844175635F858E	FASTA	249	26,669
	10 20 30 40 50 60 MAPSRKFFVG GNWKMNGRKQ SLGELIGTLN AAKVPADTEV VCAPPTAYID FARQKLDPKI 70 80 90 100 110 120 AVAAQNCYKV TNGAFTGEIS PGMIKDCGAT WVVLGHSERR HVFGESDELI GQKVAHALAE 130 140 150 160 170 180 GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ 190 200 210 220 230 240 QAQEVHEKLR GWLKSNVSDA VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE FVDIINAKQ
	Isoform 4 [UniParc]. Checksum: 1E9ADB034A513E18	FASTA	167	17,958
	10 20 30 40 50 60 MIKDCGATWV VLGHSERRHV FGESDELIGQ KVAHALAEGL GVIACIGEKL DEREAGITEK 70 80 90 100 110 120 VVFEQTKVIA DNVKDWSKVV LAYEPVWAIG TGKTATPQQA QEVHEKLRGW LKSNVSDAVA 130 140 150 160 QSTRIIYGGS VTGATCKELA SQPDVDGFLV GGASLKPEFV DIINAKQ

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"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, MASS SPECTROMETRY.
[23]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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].
[25]	"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, MASS SPECTROMETRY.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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 TPI DEFICIENCY ASP-142.
[30]	"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 TPI DEFICIENCY ASP-142 AND MET-269.
[31]	"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.
[32]	"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 TPI DEFICIENCY HUNGARY LEU-278.
[33]	"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 TPI DEFICIENCY ALA-110; ASP-142 AND MET-192.
[34]	"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 TPI DEFICIENCY 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.

IPI

IPI00451401.
IPI00797270.

PIR

ISHUT. S29743.

RefSeq

NP_000356.1. NM_000365.5.
NP_001152759.1. NM_001159287.1.
NP_001244955.1. NM_001258026.1.

UniGene

Hs.524219.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HTI	X-ray	2.80	A/B	39-286	[»]
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	[»]
4E41	X-ray	2.60	C/H	60-74	[»]

ProteinModelPortal

P60174.

SMR

P60174. Positions 41-286.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60174. 11 interactions.

MINT

MINT-1384176.

STRING

9606.ENSP00000379933.

PTM databases

PhosphoSite

P60174.

Polymorphism databases

DMDM

39932641.

2D gel databases

DOSAC-COBS-2DPAGE

P60174.

REPRODUCTION-2DPAGE

IPI00797687.
P60174.

SWISS-2DPAGE

P60174.

UCD-2DPAGE

P00938.
P60174.

Proteomic databases

PaxDb

P60174.

PRIDE

P60174.

Protocols and materials databases

DNASU

7167.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229270; ENSP00000229270; ENSG00000111669.
ENST00000396705; ENSP00000379933; ENSG00000111669.
ENST00000535434; ENSP00000443599; ENSG00000111669.
ENST00000595390; ENSP00000469350; ENSG00000268548.
ENST00000598287; ENSP00000469966; ENSG00000268548.
ENST00000601074; ENSP00000469782; ENSG00000268548.

GeneID

7167.

KEGG

hsa:7167.

UCSC

uc001qrk.3. human.

Organism-specific databases

CTD

7167.

GeneCards

GC12P007025.

HGNC

HGNC:12009. TPI1.

HPA

CAB004675.

MIM

190450. gene+phenotype.

neXtProt

NX_P60174.

Orphanet

868. Triose phosphate-isomerase deficiency.

PharmGKB

PA36689.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0149.

HOGENOM

HOG000226413.

HOVERGEN

HBG002599.

InParanoid

P60174.

KO

K01803.

OMA

ISGQWPR.

OrthoDB

EOG40S0GF.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03441-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P60174.

UniPathway

UPA00109; UER00189.
UPA00138.

Gene expression databases

ArrayExpress

P60174.

Bgee

P60174.

CleanEx

HS_TPI1.

Genevestigator

P60174.

GermOnline

ENSG00000111669. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]

PANTHER

PTHR21139. PTHR21139. 1 hit.

Pfam

PF00121. TIM. 1 hit.
[Graphical view]

SUPFAM

SSF51351. Triophos_ismrse. 1 hit.

TIGRFAMs

TIGR00419. tim. 1 hit.

PROSITE

PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P60174.

ChEMBL

CHEMBL4880.

ChiTaRS

TPI1. human.

EvolutionaryTrace

P60174.

GenomeRNAi

7167.

NextBio

28066.

SOURCE

Search...

Entry information

Entry name

TPIS_HUMAN

Accession

Primary (citable) accession number: P60174
Secondary accession number(s): B7Z5D8 , D3DUS9, P00938, Q6FHP9, Q6IS07, Q8WWD0, Q96AG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 19, 2011
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.