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P17751 (TPIS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length299 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.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Caution

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

Sequence caution

The sequence AAC36016.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH46761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB27194.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE26832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE29073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE29810.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE35334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE39523.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE40350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE40594.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA37420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Triosephosphate isomerase HAMAP-Rule MF_00147_B
PRO_0000090116

Sites

Active site1461Electrophile By similarity
Active site2161Proton acceptor By similarity
Binding site621Substrate By similarity
Binding site641Substrate By similarity

Amino acid modifications

Modified residue641N6-acetyllysine By similarity
Modified residue1181Nitrated tyrosine Ref.8
Modified residue1301Phosphoserine By similarity
Modified residue1991N6-succinyllysine Ref.10
Modified residue2061N6-acetyllysine; alternate Ref.10
Modified residue2061N6-succinyllysine; alternate Ref.10
Modified residue2441N6-acetyllysine; alternate Ref.10
Modified residue2441N6-succinyllysine; alternate Ref.10
Modified residue2591Nitrated tyrosine Ref.8
Modified residue2621Phosphoserine Ref.9
Modified residue2881N6-acetyllysine By similarity

Experimental info

Mutagenesis2131L → Q: 50% reduced activity. Ref.7
Mutagenesis2431L → Q: 50% reduced activity. Ref.7
Sequence conflict1241A → P in CAA37420. Ref.4
Sequence conflict1571D → G in BAE39523. Ref.3
Sequence conflict2441K → R in BAB27194. Ref.3
Sequence conflict2451S → P in BAE26832. Ref.3
Sequence conflict2661A → G in BAB27194. Ref.3
Sequence conflict2721A → Q in BAB27194. Ref.3
Sequence conflict273 – 2753SQP → TPA in CAA37420. Ref.4
Sequence conflict2771V → M in BAB25634. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P17751 [UniParc].

Last modified October 19, 2011. Version 4.
Checksum: D465FD57108A3BD4

FASTA29932,192
        10         20         30         40         50         60 
MEGKAEQQGA GLTMAEGGEK EEFCFTAIYI SGQWREPCVC TDLQRLEPGT MAPTRKFFVG 

        70         80         90        100        110        120 
GNWKMNGRKK CLGELICTLN AANVPAGTEV VCAPPTAYID FARQKLDPKI AVAAQNCYKV 

       130        140        150        160        170        180 
TNGAFTGEIS PGMIKDLGAT WVVLGHSERR HVFGESDELI GQKVSHALAE GLGVIACIGE 

       190        200        210        220        230        240 
KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ QAQEVHEKLR 

       250        260        270        280        290 
GWLKSNVNDG VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE FVDIINAKQ 

« Hide

References

« Hide 'large scale' references
[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(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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(2005) [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(1990) [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(2004) [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 (JAN-2009) 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(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-299, MUTAGENESIS OF LEU-213 AND LEU-243.
[8]"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease."
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J.
Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-118 AND TYR-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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(2013) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS20530.2.
PIRISMST. S10490.
RefSeqNP_033441.2. NM_009415.2.
UniGeneMm.4222.
Mm.439915.

3D structure databases

ProteinModelPortalP17751.
SMRP17751. Positions 55-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204290. 5 interactions.
IntActP17751. 11 interactions.
MINTMINT-1869495.

PTM databases

PhosphoSiteP17751.

2D gel databases

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

Proteomic databases

MaxQBP17751.
PaxDbP17751.
PRIDEP17751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000172132; ENSMUSP00000130858; ENSMUSG00000023456.
GeneID21991.
KEGGmmu:21991.
UCSCuc012esp.1. mouse.

Organism-specific databases

CTD7167.
MGIMGI:98797. Tpi1.

Phylogenomic databases

eggNOGCOG0149.
GeneTreeENSGT00390000013354.
HOVERGENHBG002599.
InParanoidP17751.
KOK01803.
OMACVGGNWK.
OrthoDBEOG76DTT8.
TreeFamTF300829.

Enzyme and pathway databases

SABIO-RKP17751.
UniPathwayUPA00109; UER00189.
UPA00138.

Gene expression databases

ArrayExpressP17751.
BgeeP17751.
CleanExMM_TPI1.
GenevestigatorP17751.

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. mouse.
NextBio301728.
PROP17751.
SOURCESearch...

Entry information

Entry nameTPIS_MOUSE
AccessionPrimary (citable) accession number: P17751
Secondary accession number(s): Q3TJH2 expand/collapse secondary AC list , Q3UC04, Q3UKG9, Q64513, Q9CVF9, Q9CWE7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot