LDHB_HUMAN
ID LDHB_HUMAN Reviewed; 334 AA.
AC P07195;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=L-lactate dehydrogenase B chain;
DE Short=LDH-B;
DE EC=1.1.1.27 {ECO:0000269|PubMed:11276087, ECO:0000269|PubMed:27618187};
DE AltName: Full=LDH heart subunit;
DE Short=LDH-H {ECO:0000303|PubMed:11276087};
DE AltName: Full=Renal carcinoma antigen NY-REN-46;
GN Name=LDHB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2930497; DOI=10.1042/bj2570921;
RA Takeno T., Li S.S.-L.;
RT "Structure of the human lactate dehydrogenase B gene.";
RL Biochem. J. 257:921-924(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T-cell;
RX PubMed=3435492; DOI=10.1042/bj2480933;
RA Sakai I., Sharief F.S., Pan Y.-C.E., Li S.S.-L.;
RT "The cDNA and protein sequences of human lactate dehydrogenase B.";
RL Biochem. J. 248:933-936(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-23; 44-58; 78-100; 108-113; 120-127; 159-170;
RP 234-244; 271-279 AND 300-329, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 8-23; 44-58; 78-91; 108-113; 120-127; 159-170; 234-244;
RP 280-299 AND 300-318, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND TYR-240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-58; LYS-119 AND LYS-329,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=27618187; DOI=10.1038/nchembio.2172;
RA Chen Y.J., Mahieu N.G., Huang X., Singh M., Crawford P.A., Johnson S.L.,
RA Gross R.W., Schaefer J., Patti G.J.;
RT "Lactate metabolism is associated with mammalian mitochondria.";
RL Nat. Chem. Biol. 12:937-943(2016).
RN [16]
RP INTERACTION WITH MP31, AND MUTAGENESIS OF ASP-53 AND ARG-100.
RX PubMed=33406399; DOI=10.1016/j.cmet.2020.12.008;
RA Huang N., Li F., Zhang M., Zhou H., Chen Z., Ma X., Yang L., Wu X.,
RA Zhong J., Xiao F., Yang X., Zhao K., Li X., Xia X., Liu Z., Gao S.,
RA Zhang N.;
RT "An Upstream Open Reading Frame in Phosphatase and Tensin Homolog Encodes a
RT Circuit Breaker of Lactate Metabolism.";
RL Cell Metab. 33:128-144(2021).
RN [17]
RP ERRATUM OF PUBMED:33406399.
RX PubMed=33535099; DOI=10.1016/j.cmet.2021.01.008;
RA Huang N., Li F., Zhang M., Zhou H., Chen Z., Ma X., Yang L., Wu X.,
RA Zhong J., Xiao F., Yang X., Zhao K., Li X., Xia X., Liu Z., Gao S.,
RA Zhang N.;
RL Cell Metab. 33:454-454(2021).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE
RP ANALOG, HOMOTETRAMERIZATION, CATALYTIC ACTIVITY, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11276087;
RX DOI=10.1002/1097-0134(20010501)43:2<175::aid-prot1029>3.0.co;2-#;
RA Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.;
RT "Structural basis for altered activity of M- and H-isozyme forms of human
RT lactate dehydrogenase.";
RL Proteins 43:175-185(2001).
RN [19]
RP VARIANT LDHBD GLU-7.
RX PubMed=8314553; DOI=10.1007/bf00217765;
RA Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.;
RT "Analysis of a genetic mutation in an electrophoretic variant of the human
RT lactate dehydrogenase-B(H) subunit.";
RL Hum. Genet. 91:423-426(1993).
RN [20]
RP VARIANTS LDHBD GLU-35; VAL-171 AND LEU-175.
RX PubMed=8462975; DOI=10.1007/bf00222718;
RA Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.;
RT "Detection and characterization of new genetic mutations in individuals
RT heterozygous for lactate dehydrogenase-B(H) deficiency using DNA
RT conformation polymorphism analysis and silver staining.";
RL Hum. Genet. 91:163-168(1993).
RN [21]
RP VARIANTS LDHBD ARG-129 AND HIS-172.
RX PubMed=1587525; DOI=10.1007/bf00217116;
RA Sudo K., Maekawa M., Tomonaga A., Tsukada T., Nakayama T., Kitamura M.,
RA Li S.S.-L., Kanno T., Toriumi J.;
RT "Molecular characterization of genetic mutations in human lactate
RT dehydrogenase (LDH) B (H) variant.";
RL Hum. Genet. 89:158-162(1992).
RN [22]
RP VARIANT LDHBD HIS-172.
RX PubMed=2334429; DOI=10.1016/0006-291x(90)92373-8;
RA Sudo K., Maekawa M., Ikawa S., Machida K., Kitamura M., Li S.S.-L.;
RT "A missense mutation found in human lactate dehydrogenase-B (H) variant
RT gene.";
RL Biochem. Biophys. Res. Commun. 168:672-676(1990).
RN [23]
RP VARIANT LDHBD VAL-322.
RA Maekawa M., Sudo K., Fujita K., Yoshioka N., Sakurabayashi I., Li S.S.-L.,
RA Kanno T.;
RT "DNA analysis of slow type of electrophoretic lactate dehydrogenase B(H)
RT variant.";
RL Seibutsu Butsuri Kagaku 38:25-29(1994).
RN [24]
RP VARIANT LDHBD TRP-107.
RX PubMed=8611651; DOI=10.1016/0925-4439(95)00089-5;
RA Shonnard G.C., Hud N.V., Mohrenweiser H.W.;
RT "Arginine to tryptophan substitution in the active site of a human lactate
RT dehydrogenase variant -- LDHB GUA1: postulated effects on subunit structure
RT and catalysis.";
RL Biochim. Biophys. Acta 1315:9-14(1996).
RN [25]
RP VARIANT LDHBD ASN-223 DEL.
RX PubMed=10211631; DOI=10.1016/s0009-9120(98)00097-6;
RA Sudo K., Maekawa M., Houki N., Okuda T., Akizuki S., Magara T., Kawano K.;
RT "A novel in-frame deletion mutation in a case of lactate dehydrogenase (LD)
RT H subunit deficiency showing an atypical LD isoenzyme pattern in serum and
RT erythrocytes.";
RL Clin. Biochem. 32:137-141(1999).
RN [26]
RP VARIANT LDHBD PRO-172.
RX PubMed=9929983; DOI=10.1007/s100380050111;
RA Hidaka K., Ueda N., Hirata I., Watanabe Y., Minatogawa Y., Iuchi I.;
RT "First case of missense mutation (LDH-H:R171P) in exon 4 of the lactate
RT dehydrogenase gene detected in a Japanese patient.";
RL J. Hum. Genet. 44:69-72(1999).
RN [27]
RP VARIANT LDHBD GLU-69.
RX PubMed=11509017; DOI=10.1006/mgme.2001.3203;
RA Takatani T., Takaoka N., Tatsumi M., Kawamoto H., Okuno Y., Morita K.,
RA Masutani T., Murakawa K., Okamoto Y.;
RT "A novel missense mutation in human lactate dehydrogenase b-subunit gene.";
RL Mol. Genet. Metab. 73:344-348(2001).
CC -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate
CC and lactate with concomitant interconversion of NADH and NAD(+).
CC {ECO:0000269|PubMed:27618187}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC Evidence={ECO:0000269|PubMed:11276087, ECO:0000269|PubMed:27618187};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC Evidence={ECO:0000269|PubMed:11276087};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC Evidence={ECO:0000269|PubMed:11276087};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000305|PubMed:27618187}.
CC -!- SUBUNIT: Homotetramer (PubMed:11276087). Interacts with PTEN upstream
CC reading frame protein MP31; the interaction leads to inhibition of
CC mitochondrial lactate dehydrogenase activity, preventing conversion of
CC lactate to pyruvate in mitochondria (PubMed:33406399).
CC {ECO:0000269|PubMed:11276087, ECO:0000269|PubMed:33406399}.
CC -!- INTERACTION:
CC P07195; P42858: HTT; NbExp=9; IntAct=EBI-358748, EBI-466029;
CC P07195; P00338: LDHA; NbExp=3; IntAct=EBI-358748, EBI-372327;
CC P07195; P00338-3: LDHA; NbExp=9; IntAct=EBI-358748, EBI-10195200;
CC P07195; P07195: LDHB; NbExp=6; IntAct=EBI-358748, EBI-358748;
CC P07195; Q5S007: LRRK2; NbExp=2; IntAct=EBI-358748, EBI-5323863;
CC P07195; P50542: PEX5; NbExp=3; IntAct=EBI-358748, EBI-597835;
CC P07195; O00560: SDCBP; NbExp=3; IntAct=EBI-358748, EBI-727004;
CC P07195; P54274: TERF1; NbExp=2; IntAct=EBI-358748, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27618187}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in aerobic tissues such as
CC cardiac muscle. {ECO:0000305|PubMed:11276087}.
CC -!- DISEASE: Lactate dehydrogenase B deficiency (LDHBD) [MIM:614128]: A
CC condition with no deleterious effects on health. LDHBD is of interest
CC to laboratory medicine mainly because it can cause misdiagnosis in
CC those disorders in which elevation of serum LDH is expected.
CC {ECO:0000269|PubMed:10211631, ECO:0000269|PubMed:11509017,
CC ECO:0000269|PubMed:1587525, ECO:0000269|PubMed:2334429,
CC ECO:0000269|PubMed:8314553, ECO:0000269|PubMed:8462975,
CC ECO:0000269|PubMed:8611651, ECO:0000269|PubMed:9929983,
CC ECO:0000269|Ref.23}. Note=The disease is caused by variants affecting
CC the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Lactate dehydrogenase entry;
CC URL="https://en.wikipedia.org/wiki/Lactate_dehydrogenase";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Another dark horse - Issue
CC 109 of September 2009;
CC URL="https://web.expasy.org/spotlight/back_issues/109";
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DR EMBL; X13794; CAA32033.1; -; Genomic_DNA.
DR EMBL; X13795; CAA32033.1; JOINED; Genomic_DNA.
DR EMBL; X13796; CAA32033.1; JOINED; Genomic_DNA.
DR EMBL; X13797; CAA32033.1; JOINED; Genomic_DNA.
DR EMBL; X13798; CAA32033.1; JOINED; Genomic_DNA.
DR EMBL; X13799; CAA32033.1; JOINED; Genomic_DNA.
DR EMBL; X13800; CAA32033.1; JOINED; Genomic_DNA.
DR EMBL; Y00711; CAA68701.1; -; mRNA.
DR EMBL; BC002362; AAH02362.1; -; mRNA.
DR EMBL; BC015122; AAH15122.1; -; mRNA.
DR EMBL; BC071860; AAH71860.1; -; mRNA.
DR CCDS; CCDS8691.1; -.
DR PIR; S02795; DEHULH.
DR RefSeq; NP_001167568.1; NM_001174097.2.
DR RefSeq; NP_001302466.1; NM_001315537.1.
DR RefSeq; NP_002291.1; NM_002300.7.
DR PDB; 1I0Z; X-ray; 2.10 A; A/B=2-334.
DR PDB; 1T2F; X-ray; 3.00 A; A/B/C/D=2-332.
DR PDB; 7DBJ; X-ray; 1.55 A; A/B/C/D=2-334.
DR PDB; 7DBK; X-ray; 1.80 A; A/B/C/D/E/F/G/H=2-334.
DR PDBsum; 1I0Z; -.
DR PDBsum; 1T2F; -.
DR PDBsum; 7DBJ; -.
DR PDBsum; 7DBK; -.
DR AlphaFoldDB; P07195; -.
DR SMR; P07195; -.
DR BioGRID; 110137; 252.
DR ComplexPortal; CPX-6592; L-lactate dehydrogenase complex, A3B1 variant.
DR ComplexPortal; CPX-6594; L-lactate dehydrogenase complex, A2B2 variant.
DR ComplexPortal; CPX-6598; L-lactate dehydrogenase complex, A1B3 variant.
DR ComplexPortal; CPX-6599; L-lactate dehydrogenase B complex.
DR IntAct; P07195; 65.
DR MINT; P07195; -.
DR STRING; 9606.ENSP00000379386; -.
DR BindingDB; P07195; -.
DR ChEMBL; CHEMBL4940; -.
DR DrugBank; DB02401; 4-Hydroxy-1,2,5-oxadiazole-3-carboxylic acid.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB03940; Oxamic Acid.
DR DrugBank; DB09118; Stiripentol.
DR GlyGen; P07195; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07195; -.
DR MetOSite; P07195; -.
DR PhosphoSitePlus; P07195; -.
DR SwissPalm; P07195; -.
DR BioMuta; LDHB; -.
DR DMDM; 126041; -.
DR DOSAC-COBS-2DPAGE; P07195; -.
DR OGP; P07195; -.
DR REPRODUCTION-2DPAGE; IPI00219217; -.
DR SWISS-2DPAGE; P07195; -.
DR UCD-2DPAGE; P07195; -.
DR EPD; P07195; -.
DR jPOST; P07195; -.
DR MassIVE; P07195; -.
DR PaxDb; P07195; -.
DR PeptideAtlas; P07195; -.
DR PRIDE; P07195; -.
DR ProteomicsDB; 51960; -.
DR TopDownProteomics; P07195; -.
DR Antibodypedia; 3304; 447 antibodies from 39 providers.
DR DNASU; 3945; -.
DR Ensembl; ENST00000350669.5; ENSP00000229319.1; ENSG00000111716.14.
DR Ensembl; ENST00000396076.5; ENSP00000379386.1; ENSG00000111716.14.
DR GeneID; 3945; -.
DR KEGG; hsa:3945; -.
DR MANE-Select; ENST00000350669.5; ENSP00000229319.1; NM_002300.8; NP_002291.1.
DR CTD; 3945; -.
DR DisGeNET; 3945; -.
DR GeneCards; LDHB; -.
DR HGNC; HGNC:6541; LDHB.
DR HPA; ENSG00000111716; Tissue enhanced (heart muscle, kidney).
DR MalaCards; LDHB; -.
DR MIM; 150100; gene.
DR MIM; 614128; phenotype.
DR neXtProt; NX_P07195; -.
DR OpenTargets; ENSG00000111716; -.
DR Orphanet; 284435; Glycogen storage disease due to lactate dehydrogenase H-subunit deficiency.
DR PharmGKB; PA30325; -.
DR VEuPathDB; HostDB:ENSG00000111716; -.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000153525; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; P07195; -.
DR OMA; AFTRHCT; -.
DR OrthoDB; 1204514at2759; -.
DR PhylomeDB; P07195; -.
DR TreeFam; TF314963; -.
DR BRENDA; 1.1.1.27; 2681.
DR PathwayCommons; P07195; -.
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR SABIO-RK; P07195; -.
DR SignaLink; P07195; -.
DR SIGNOR; P07195; -.
DR UniPathway; UPA00554; UER00611.
DR BioGRID-ORCS; 3945; 11 hits in 1040 CRISPR screens.
DR ChiTaRS; LDHB; human.
DR EvolutionaryTrace; P07195; -.
DR GenomeRNAi; 3945; -.
DR Pharos; P07195; Tchem.
DR PRO; PR:P07195; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P07195; protein.
DR Bgee; ENSG00000111716; Expressed in renal medulla and 208 other tissues.
DR ExpressionAtlas; P07195; baseline and differential.
DR Genevisible; P07195; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR GO; GO:0006089; P:lactate metabolic process; IDA:ComplexPortal.
DR GO; GO:0019674; P:NAD metabolic process; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:ComplexPortal.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disease variant; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..334
FT /note="L-lactate dehydrogenase B chain"
FT /id="PRO_0000168459"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT BINDING 31..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11276087"
FT BINDING 107
FT /ligand="substrate"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11276087"
FT BINDING 139
FT /ligand="substrate"
FT BINDING 170
FT /ligand="substrate"
FT BINDING 249
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 240
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 7
FT /note="K -> E (in LDHBD; slightly decreased activity;
FT dbSNP:rs118203897)"
FT /evidence="ECO:0000269|PubMed:8314553"
FT /id="VAR_004173"
FT VARIANT 35
FT /note="A -> E (in LDHBD)"
FT /evidence="ECO:0000269|PubMed:8462975"
FT /id="VAR_004174"
FT VARIANT 69
FT /note="G -> E (in LDHBD)"
FT /evidence="ECO:0000269|PubMed:11509017"
FT /id="VAR_011634"
FT VARIANT 107
FT /note="R -> W (in LDHBD; inactive; dbSNP:rs777954556)"
FT /evidence="ECO:0000269|PubMed:8611651"
FT /id="VAR_011635"
FT VARIANT 129
FT /note="S -> R (in LDHBD; dbSNP:rs118203896)"
FT /evidence="ECO:0000269|PubMed:1587525"
FT /id="VAR_004175"
FT VARIANT 171
FT /note="F -> V (in LDHBD)"
FT /evidence="ECO:0000269|PubMed:8462975"
FT /id="VAR_004176"
FT VARIANT 172
FT /note="R -> H (in LDHBD; dbSNP:rs118203895)"
FT /evidence="ECO:0000269|PubMed:1587525,
FT ECO:0000269|PubMed:2334429"
FT /id="VAR_004177"
FT VARIANT 172
FT /note="R -> P (in LDHBD)"
FT /evidence="ECO:0000269|PubMed:9929983"
FT /id="VAR_011636"
FT VARIANT 175
FT /note="M -> L (in LDHBD)"
FT /evidence="ECO:0000269|PubMed:8462975"
FT /id="VAR_004178"
FT VARIANT 175
FT /note="M -> V (in dbSNP:rs7966339)"
FT /id="VAR_049758"
FT VARIANT 223
FT /note="Missing (in LDHBD)"
FT /evidence="ECO:0000269|PubMed:10211631"
FT /id="VAR_011637"
FT VARIANT 322
FT /note="D -> V (in LDHBD)"
FT /evidence="ECO:0000269|Ref.23"
FT /id="VAR_004179"
FT VARIANT 325
FT /note="W -> R (in LDHBD; dbSNP:rs267607212)"
FT /id="VAR_011638"
FT MUTAGEN 53
FT /note="D->A: Abolishes interaction with MP31."
FT /evidence="ECO:0000269|PubMed:33406399"
FT MUTAGEN 100
FT /note="R->A: Abolishes interaction with MP31."
FT /evidence="ECO:0000269|PubMed:33406399"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:7DBJ"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1T2F"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:7DBJ"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:1T2F"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:7DBJ"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:7DBJ"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:7DBJ"
SQ SEQUENCE 334 AA; 36638 MW; 3AD605DEED0D54A2 CRC64;
MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF
IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG
IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL
