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Protein

Triosephosphate isomerase

Gene

Tpi1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateBy similarity
Binding sitei64 – 641SubstrateBy similarity
Active sitei146 – 1461ElectrophileBy similarity
Active sitei216 – 2161Proton acceptorBy similarity

GO - Molecular functioni

  1. isomerase activity Source: MGI
  2. triose-phosphate isomerase activity Source: MGI

GO - Biological processi

  1. gluconeogenesis Source: UniProtKB-UniPathway
  2. glucose metabolic process Source: MGI
  3. glyceraldehyde-3-phosphate metabolic process Source: UniProtKB
  4. glycolytic process Source: MGI
  5. multicellular organismal development Source: MGI
  6. pentose-phosphate shunt Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP17751.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:98797. Tpi1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi213 – 2131L → Q: 50% reduced activity. 1 Publication
Mutagenesisi243 – 2431L → Q: 50% reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Triosephosphate isomerasePRO_0000090116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641N6-acetyllysineBy similarity
Modified residuei118 – 1181Nitrated tyrosine1 Publication
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei199 – 1991N6-succinyllysine1 Publication
Modified residuei206 – 2061N6-acetyllysine; alternate1 Publication
Modified residuei206 – 2061N6-succinyllysine; alternate1 Publication
Modified residuei244 – 2441N6-acetyllysine; alternate1 Publication
Modified residuei244 – 2441N6-succinyllysine; alternate1 Publication
Modified residuei259 – 2591Nitrated tyrosine1 Publication
Modified residuei262 – 2621Phosphoserine1 Publication
Modified residuei264 – 2641PhosphothreonineBy similarity
Modified residuei273 – 2731PhosphoserineBy similarity
Modified residuei288 – 2881N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP17751.
PaxDbiP17751.
PRIDEiP17751.

2D gel databases

COMPLUYEAST-2DPAGEP17751.
REPRODUCTION-2DPAGEIPI00467833.
P17751.
SWISS-2DPAGEP17751.
UCD-2DPAGEP17751.

PTM databases

PhosphoSiteiP17751.

Expressioni

Gene expression databases

BgeeiP17751.
CleanExiMM_TPI1.
ExpressionAtlasiP17751. baseline and differential.
GenevestigatoriP17751.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi204290. 7 interactions.
IntActiP17751. 11 interactions.
MINTiMINT-1869495.

Structurei

3D structure databases

ProteinModelPortaliP17751.
SMRiP17751. Positions 55-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiCOG0149.
GeneTreeiENSGT00390000013354.
HOVERGENiHBG002599.
InParanoidiP17751.
KOiK01803.
OMAiMCAYAKK.
OrthoDBiEOG76DTT8.
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]

Sequencei

Sequence statusi: Complete.

P17751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGKAEQQGA GLTMAEGGEK EEFCFTAIYI SGQWREPCVC TDLQRLEPGT
60 70 80 90 100
MAPTRKFFVG GNWKMNGRKK CLGELICTLN AANVPAGTEV VCAPPTAYID
110 120 130 140 150
FARQKLDPKI AVAAQNCYKV TNGAFTGEIS PGMIKDLGAT WVVLGHSERR
160 170 180 190 200
HVFGESDELI GQKVSHALAE GLGVIACIGE KLDEREAGIT EKVVFEQTKV
210 220 230 240 250
IADNVKDWSK VVLAYEPVWA IGTGKTATPQ QAQEVHEKLR GWLKSNVNDG
260 270 280 290
VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE FVDIINAKQ
Length:299
Mass (Da):32,192
Last modified:October 19, 2011 - v4
Checksum:iD465FD57108A3BD4
GO

Sequence cautioni

The sequence AAC36016.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH46761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB27194.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE26832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE29073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE29810.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE35334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE39523.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE40350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE40594.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA37420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241A → P in CAA37420 (PubMed:2377473).Curated
Sequence conflicti157 – 1571D → G in BAE39523 (PubMed:16141072).Curated
Sequence conflicti244 – 2441K → R in BAB27194 (PubMed:16141072).Curated
Sequence conflicti245 – 2451S → P in BAE26832 (PubMed:16141072).Curated
Sequence conflicti266 – 2661A → G in BAB27194 (PubMed:16141072).Curated
Sequence conflicti272 – 2721A → Q in BAB27194 (PubMed:16141072).Curated
Sequence conflicti273 – 2753SQP → TPA in CAA37420 (PubMed:2377473).Curated
Sequence conflicti277 – 2771V → M in BAB25634 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002397 Genomic DNA. Translation: AAC36016.1. Different initiation.
AC142254 Genomic DNA. No translation available.
AK008373 mRNA. Translation: BAB25634.1.
AK010808 mRNA. Translation: BAB27194.1. Different initiation.
AK146013 mRNA. Translation: BAE26832.1. Different initiation.
AK149768 mRNA. Translation: BAE29073.1. Different initiation.
AK150735 mRNA. Translation: BAE29810.1. Different initiation.
AK159741 mRNA. Translation: BAE35334.1. Different initiation.
AK167437 mRNA. Translation: BAE39523.1. Different initiation.
AK168446 mRNA. Translation: BAE40350.1. Different initiation.
AK168756 mRNA. Translation: BAE40594.1. Different initiation.
X53333 mRNA. Translation: CAA37420.1. Different initiation.
BC046761 mRNA. Translation: AAH46761.1. Different initiation.
L31777 Genomic DNA. Translation: AAB48543.1.
CCDSiCCDS20530.2.
PIRiS10490. ISMST.
RefSeqiNP_033441.2. NM_009415.2.
UniGeneiMm.4222.
Mm.439915.

Genome annotation databases

EnsembliENSMUST00000172132; ENSMUSP00000130858; ENSMUSG00000023456.
GeneIDi21991.
KEGGimmu:21991.
UCSCiuc012esp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002397 Genomic DNA. Translation: AAC36016.1. Different initiation.
AC142254 Genomic DNA. No translation available.
AK008373 mRNA. Translation: BAB25634.1.
AK010808 mRNA. Translation: BAB27194.1. Different initiation.
AK146013 mRNA. Translation: BAE26832.1. Different initiation.
AK149768 mRNA. Translation: BAE29073.1. Different initiation.
AK150735 mRNA. Translation: BAE29810.1. Different initiation.
AK159741 mRNA. Translation: BAE35334.1. Different initiation.
AK167437 mRNA. Translation: BAE39523.1. Different initiation.
AK168446 mRNA. Translation: BAE40350.1. Different initiation.
AK168756 mRNA. Translation: BAE40594.1. Different initiation.
X53333 mRNA. Translation: CAA37420.1. Different initiation.
BC046761 mRNA. Translation: AAH46761.1. Different initiation.
L31777 Genomic DNA. Translation: AAB48543.1.
CCDSiCCDS20530.2.
PIRiS10490. ISMST.
RefSeqiNP_033441.2. NM_009415.2.
UniGeneiMm.4222.
Mm.439915.

3D structure databases

ProteinModelPortaliP17751.
SMRiP17751. Positions 55-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204290. 7 interactions.
IntActiP17751. 11 interactions.
MINTiMINT-1869495.

PTM databases

PhosphoSiteiP17751.

2D gel databases

COMPLUYEAST-2DPAGEP17751.
REPRODUCTION-2DPAGEIPI00467833.
P17751.
SWISS-2DPAGEP17751.
UCD-2DPAGEP17751.

Proteomic databases

MaxQBiP17751.
PaxDbiP17751.
PRIDEiP17751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000172132; ENSMUSP00000130858; ENSMUSG00000023456.
GeneIDi21991.
KEGGimmu:21991.
UCSCiuc012esp.1. mouse.

Organism-specific databases

CTDi7167.
MGIiMGI:98797. Tpi1.

Phylogenomic databases

eggNOGiCOG0149.
GeneTreeiENSGT00390000013354.
HOVERGENiHBG002599.
InParanoidiP17751.
KOiK01803.
OMAiMCAYAKK.
OrthoDBiEOG76DTT8.
TreeFamiTF300829.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP17751.

Miscellaneous databases

ChiTaRSiTpi1. mouse.
NextBioi301728.
PROiP17751.
SOURCEiSearch...

Gene expression databases

BgeeiP17751.
CleanExiMM_TPI1.
ExpressionAtlasiP17751. baseline and differential.
GenevestigatoriP17751.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
    Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.
    Genome Res. 8:29-40(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-299.
    Strain: C57BL/6J.
    Tissue: Bone marrow, Placenta and Stomach.
  4. "Nucleotide sequence of murine triosephosphate isomerase cDNA."
    Cheng J., Mielnicki L.M., Pruitt S.C., Maquat L.E.
    Nucleic Acids Res. 18:4261-4261(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-299.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-299.
    Strain: C57BL/6.
    Tissue: Brain.
  6. Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 56-64; 71-103; 110-181; 193-206; 211-238; 245-256 AND 270-298, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  7. "Molecular analysis of four ENU induced triosephosphate isomerase null mutants in Mus musculus."
    Zingg B.C., Pretsch W., Mohrenweiser H.W.
    Mutat. Res. 328:163-173(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-299, MUTAGENESIS OF LEU-213 AND LEU-243.
  8. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-118 AND TYR-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-244, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-199; LYS-206 AND LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiTPIS_MOUSE
AccessioniPrimary (citable) accession number: P17751
Secondary accession number(s): Q3TJH2
, Q3UC04, Q3UKG9, Q64513, Q9CVF9, Q9CWE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 19, 2011
Last modified: April 1, 2015
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain if Met-1 or Met-14 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.