LOCUS       NP_033414                623 aa            linear   ROD 28-APR-2025
DEFINITION  transketolase [Mus musculus].
ACCESSION   NP_033414
VERSION     NP_033414.1
DBSOURCE    REFSEQ: accession NM_009388.6
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Liu,M.J., Zhao,Y., Li,Q.T., Lei,X.Y., He,K.Y., Guo,J.R., Yang,J.Y.,
            Yan,Z.H., Wu,D.H., Zhang,L., Jian,Y.P. and Xu,Z.X.
  TITLE     HMGA1 promotes the progression of esophageal squamous cell
            carcinoma by elevating TKT-mediated upregulation of pentose
            phosphate pathway
  JOURNAL   Cell Death Dis 15 (7), 541 (2024)
   PUBMED   39080260
  REMARK    GeneRIF: HMGA1 promotes the progression of esophageal squamous cell
            carcinoma by elevating TKT-mediated upregulation of pentose
            phosphate pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Liu,Q., Zhu,F., Liu,X., Lu,Y., Yao,K., Tian,N., Tong,L.,
            Figge,D.A., Wang,X., Han,Y., Li,Y., Zhu,Y., Hu,L., Ji,Y., Xu,N.,
            Li,D., Gu,X., Liang,R., Gan,G., Wu,L., Zhang,P., Xu,T., Hu,H.,
            Hu,Z., Xu,H., Ye,D., Yang,H., Li,B. and Tong,X.
  TITLE     Non-oxidative pentose phosphate pathway controls regulatory T cell
            function by integrating metabolism and epigenetics
  JOURNAL   Nat Metab 4 (5), 559-574 (2022)
   PUBMED   35606596
  REMARK    GeneRIF: Non-oxidative pentose phosphate pathway controls
            regulatory T cell function by integrating metabolism and
            epigenetics.
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Wang,Z., Qiu,Z., Hua,S., Yang,W., Chen,Y., Huang,F., Fan,Y.,
            Tong,L., Xu,T., Tong,X., Yang,K. and Jin,W.
  TITLE     Nuclear Tkt promotes ischemic heart failure via the cleaved
            Parp1/Aif axis
  JOURNAL   Basic Res Cardiol 117 (1), 18 (2022)
   PUBMED   35380314
  REMARK    GeneRIF: Nuclear Tkt promotes ischemic heart failure via the
            cleaved Parp1/Aif axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Tian,N., Hu,L., Lu,Y., Tong,L., Feng,M., Liu,Q., Li,Y., Zhu,Y.,
            Wu,L., Ji,Y., Zhang,P., Xu,T. and Tong,X.
  TITLE     TKT maintains intestinal ATP production and inhibits
            apoptosis-induced colitis
  JOURNAL   Cell Death Dis 12 (10), 853 (2021)
   PUBMED   34535624
  REMARK    GeneRIF: TKT maintains intestinal ATP production and inhibits
            apoptosis-induced colitis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Salamon,C., Chervenak,M., Piatigorsky,J. and Sax,C.M.
  TITLE     The mouse transketolase (TKT) gene: cloning, characterization, and
            functional promoter analysis
  JOURNAL   Genomics 48 (2), 209-220 (1998)
   PUBMED   9521875
REFERENCE   7  (residues 1 to 623)
  AUTHORS   James,H.M., Williams,S.G., Bais,R., Rofe,A.M., Edwards,J.B. and
            Conyers,R.A.
  TITLE     The metabolic production of oxalate from xylitol: activities of
            transketolase, transaldolase, fructokinase and aldolase in liver,
            kidney, brain, heart and muscle in the rat, mouse, guinea pig,
            rabbit and human
  JOURNAL   Int J Vitam Nutr Res Suppl 28, 29-46 (1985)
   PUBMED   3009653
REFERENCE   8  (residues 1 to 623)
  AUTHORS   Trebukhina,R.V., Ostrovsky,Y.M., Mikhaltsevich,G.N., Velichko,M.G.
            and Tumanov,V.N.
  TITLE     Transketolase, pyruvate and oxoglutarate dehydrogenase activities
            and [14C]thiamin turnover in tissues of mice fed thiamin-deficient
            diet
  JOURNAL   J Nutr 113 (7), 1285-1291 (1983)
   PUBMED   6864328
REFERENCE   9  (residues 1 to 623)
  AUTHORS   Blass,J.P., Piacentini,S., Boldizsar,E. and Baker,A.
  TITLE     Kinetic studies of mouse brain transketolase
  JOURNAL   J Neurochem 39 (3), 729-733 (1982)
   PUBMED   7097279
REFERENCE   10 (residues 1 to 623)
  AUTHORS   Gumaa,K.A. and McLean,P.
  TITLE     The pentose phosphate pathway of glucose metabolism. Enzyme
            profiles and transient and steady-state content of intermediates of
            alternative pathways of glucose metabolism in Krebs ascites cells
  JOURNAL   Biochem J 115 (5), 1009-1029 (1969)
   PUBMED   5360673
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BY276711.1, AK166763.1,
            AK030446.1, AC154646.2 and AI837706.1.
            
            Summary: This gene encodes an enzyme that binds magnesium and
            thiamine pyrophosphate and catalyzes the transfer of sugar
            phosphates to an aldose acceptor. This enzyme is a key component of
            the pentose phosphate pathway during glycolysis. It is
            significantly expressed in the cornea and may be involved in the
            cellular response against oxidative stress. Haploinsufficiency of
            this gene leads to decreased growth and reduction of adipose
            tissue. [provided by RefSeq, Dec 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK030446.1, AK167084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 18.79 cM"
     Protein         1..623
                     /product="transketolase"
                     /EC_number="2.2.1.1"
                     /note="TK"
                     /calculated_mol_wt=67500
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Region          8..620
                     /region_name="PRK05899"
                     /note="transketolase; Reviewed"
                     /db_xref="CDD:235639"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            37
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            258
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50137; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            538
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     Site            603
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P40142.1)"
     CDS             1..623
                     /gene="Tkt"
                     /gene_synonym="p68"
                     /coded_by="NM_009388.6:144..2015"
                     /db_xref="CCDS:CCDS26894.1"
                     /db_xref="GeneID:21881"
                     /db_xref="MGI:MGI:105992"
ORIGIN      
        1 megyhkpdqq klqalkdtan rlrissiqat taagsghpts ccsaaeimav lffhtmryka
       61 ldprnphndr fvlskghaap ilyavwaeag flpeaellnl rkissdldgh pvpkqaftdv
      121 atgslgqglg aacgmaytgk yfdkasyrvy cmlgdgevse gsvweamafa giykldnlva
      181 ifdinrlgqs dpaplqhqvd iyqkrceafg whtiivdghs veelckafgq akhqptaiia
      241 ktfkgrgitg iedkeawhgk plpknmaeqi iqeiysqvqs kkkilatppq edapsvdian
      301 irmptppsyk vgdkiatrka yglalaklgh asdriialdg dtknstfsel fkkehpdrfi
      361 ecyiaeqnmv siavgcatrd rtvpfcstfa afftrafdqi rmaaisesni nlcgshcgvs
      421 igedgpsqma ledlamfrsv pmstvfypsd gvatekavel aantkgicfi rtsrpenaii
      481 ysnnedfqvg qakvvlkskd dqvtvigagv tlhealaaae slkkdkisir vldpftikpl
      541 drklildsar atkgriltve dhyyeggige avsaavvgep gvtvtrlavs qvprsgkpae
      601 llkmfgidkd aivqavkglv tkg
//
