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UniProtKB/Swiss-Prot entry P07195


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LDHB_HUMAN
Primary accession number P07195
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 109)
Name and origin of the protein
Protein name L-lactate dehydrogenase B chain
Synonyms LDH-B
EC 1.1.1.27
LDH heart subunit
LDH-H
Renal carcinoma antigen NY-REN-46
Gene name
Name: LDHB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2930497 [NCBI, ExPASy, EBI, Israel, Japan]
Takeno T., Li S.S.-L.;
"Structure of the human lactate dehydrogenase B gene.";
Biochem. J. 257:921-924(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=3435492 [NCBI, ExPASy, EBI, Israel, Japan]
Sakai I., Sharief F.S., Pan Y.-C.E., Li S.S.-L.;
"The cDNA and protein sequences of human lactate dehydrogenase B.";
Biochem. J. 248:933-936(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-23; 44-58; 78-100; 108-113; 120-127; 159-170; 234-244; 271-279 AND 300-329, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAY-2005) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 44-58; 120-127 AND 280-299, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[6]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE ANALOG, AND HOMOTETRAMERIZATION.
DOI=10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#; PubMed=11276087 [NCBI, ExPASy, EBI, Israel, Japan]
Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.;
"Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.";
Proteins 43:175-185(2001).
[10]
VARIANT GLU-7.
DOI=10.1007/BF00217765; PubMed=8314553 [NCBI, ExPASy, EBI, Israel, Japan]
Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.;
"Analysis of a genetic mutation in an electrophoretic variant of the human lactate dehydrogenase-B(H) subunit.";
Hum. Genet. 91:423-426(1993).
[11]
VARIANTS GLU-35; VAL-171 AND LEU-175.
DOI=10.1007/BF00222718; PubMed=8462975 [NCBI, ExPASy, EBI, Israel, Japan]
Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.;
"Detection and characterization of new genetic mutations in individuals heterozygous for lactate dehydrogenase-B(H) deficiency using DNA conformation polymorphism analysis and silver staining.";
Hum. Genet. 91:163-168(1993).
[12]
VARIANTS ARG-129 AND HIS-172.
DOI=10.1007/BF00217116; PubMed=1587525 [NCBI, ExPASy, EBI, Israel, Japan]
Sudo K., Maekawa M., Tomonaga A., Tsukada T., Nakayama T., Kitamura M., Li S.S.-L., Kanno T., Toriumi J.;
"Molecular characterization of genetic mutations in human lactate dehydrogenase (LDH) B (H) variant.";
Hum. Genet. 89:158-162(1992).
[13]
VARIANT HIS-172.
DOI=10.1016/0006-291X(90)92373-8; PubMed=2334429 [NCBI, ExPASy, EBI, Israel, Japan]
Sudo K., Maekawa M., Ikawa S., Machida K., Kitamura M., Li S.S.-L.;
"A missense mutation found in human lactate dehydrogenase-B (H) variant gene.";
Biochem. Biophys. Res. Commun. 168:672-676(1990).
[14]
VARIANT VAL-322.
Maekawa M., Sudo K., Fujita K., Yoshioka N., Sakurabayashi I., Li S.S.-L., Kanno T.;
"DNA analysis of slow type of electrophoretic lactate dehydrogenase B(H) variant.";
Seibutsu Butsuri Kagaku 38:25-29(1994).
[15]
VARIANT GUA1 TRP-107.
DOI=10.1016/0925-4439(95)00089-5; PubMed=8611651 [NCBI, ExPASy, EBI, Israel, Japan]
Shonnard G.C., Hud N.V., Mohrenweiser H.W.;
"Arginine to tryptophan substitution in the active site of a human lactate dehydrogenase variant -- LDHB GUA1: postulated effects on subunit structure and catalysis.";
Biochim. Biophys. Acta 1315:9-14(1996).
[16]
VARIANT ASN-223 DEL.
DOI=10.1016/S0009-9120(98)00097-6; PubMed=10211631 [NCBI, ExPASy, EBI, Israel, Japan]
Sudo K., Maekawa M., Houki N., Okuda T., Akizuki S., Magara T., Kawano K.;
"A novel in-frame deletion mutation in a case of lactate dehydrogenase (LD) H subunit deficiency showing an atypical LD isoenzyme pattern in serum and erythrocytes.";
Clin. Biochem. 32:137-141(1999).
[17]
VARIANT PRO-172.
DOI=10.1007/s100380050111; PubMed=9929983 [NCBI, ExPASy, EBI, Israel, Japan]
Hidaka K., Ueda N., Hirata I., Watanabe Y., Minatogawa Y., Iuchi I.;
"First case of missense mutation (LDH-H:R171P) in exon 4 of the lactate dehydrogenase gene detected in a Japanese patient.";
J. Hum. Genet. 44:69-72(1999).
[18]
VARIANT GLU-69.
DOI=10.1006/mgme.2001.3203; PubMed=11509017 [NCBI, ExPASy, EBI, Israel, Japan]
Takatani T., Takaoka N., Tatsumi M., Kawamoto H., Okuno Y., Morita K., Masutani T., Murakawa K., Okamoto Y.;
"A novel missense mutation in human lactate dehydrogenase b-subunit gene.";
Mol. Genet. Metab. 73:344-348(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13794; CAA32033.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13795; CAA32033.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13796; CAA32033.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13797; CAA32033.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13798; CAA32033.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13799; CAA32033.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13800; CAA32033.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00711; CAA68701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002362; AAH02362.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015122; AAH15122.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071860; AAH71860.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02795; DEHULH.
RefSeq NP_002291.1; -.
UniGene Hs.446149
3D structure databases
PDB
1I0Z; X-ray; 2.10 A; A/B=1-334.[ExPASy / RCSB / EBI]
1T2F; X-ray; 3.00 A; A/B/C/D=1-334.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1I0Z; -.
1T2F; -.
ModBase P07195.
Protein-protein interaction databases
IntAct P07195; -.
PTM databases
PhosphoSite P07195; -.
2D gel databases
SWISS-2DPAGE P07195; -.
Cornea-2DPAGE P07195; -.
DOSAC-COBS-2DPAGE P07195; -.
HSC-2DPAGE P07195; -.
OGP P07195; -.
REPRODUCTION-2DPAGE IPI00219217; -.
Organism-specific databases
H-InvDB HIX0010481; -.
HGNC HGNC:6541; LDHB.
GenAtlas LDHB.
HPA CAB004641; -.
MIM 150100; gene+phenotype. [NCBI / EBI]
Orphanet 2364; Lactate dehydrogenase deficiency.
79338; Lactate dehydrogenase deficiency type B.
PharmGKB PA30325; -.
GeneCards P07195.
Gene expression databases
ArrayExpress P07195; -.
CleanEx HS_LDHB; -.
GermOnline ENSG00000111716; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0004459; Molecular function: L-lactate dehydrogenase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR011304; L-lactate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
PRINTS PR00086; LLDHDRGNASE.
TIGRFAMs TIGR01771; L-LDH-NAD; 1.
PROSITE PS00064; L_LDH; 1.
BLOCKS P07195.
ProtoNet P07195.
Genome annotation databases
Ensembl ENSG00000111716; Homo sapiens. [Contig view]
GeneID 3945; -.
KEGG hsa:3945; -.
Phylogenomic databases
HOGENOM P07195; -.
HOVERGEN P07195; -.
Other
DrugBank DB00157; NADH.
LinkHub P07195; -.
NextBio 15479; -.
SOURCE LDHB; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Disease mutation; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   334  333     L-lactate dehydrogenase B chain. PRO_0000168459
NP_BIND   31    53  23     NAD (By similarity). 
ACT_SITE   194   194        Proton acceptor. 
BINDING   100   100        NAD. 
BINDING   107   107        Substrate. 
BINDING   139   139        NAD or substrate. 
BINDING   170   170        Substrate. 
BINDING   249   249        Substrate. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   240   240        Phosphotyrosine. 
VARIANT   7     7  1     K -> E (in LDHB deficiency; slightly decreased activity). VAR_004173 [3D]
VARIANT   35    35  1     A -> E (in LDHB deficiency). VAR_004174 [3D]
VARIANT   69    69  1     G -> E (in LDHB deficiency). VAR_011634 [3D]
VARIANT   107   107  1     R -> W (in GUA1; LDHB deficiency; inactive). VAR_011635 [3D]
VARIANT   129   129  1     S -> R (in LDHB deficiency). VAR_004175 [3D]
VARIANT   171   171  1     F -> V (in LDHB deficiency). VAR_004176 [3D]
VARIANT   172   172  1     R -> H (in LDHB deficiency; unstable). VAR_004177 [3D]
VARIANT   172   172  1     R -> P (in LDHB deficiency). VAR_011636 [3D]
VARIANT   175   175  1     M -> L (in LDHB deficiency). VAR_004178 [3D]
VARIANT   223   223  1     Missing (in LDHB deficiency). VAR_011637
VARIANT   322   322  1     D -> V (in LDHB deficiency). VAR_004179 [3D]
VARIANT   325   325  1     W -> R (in LDHB deficiency). VAR_011638 [3D]
HELIX   4     8  5      
STRAND   9    13  5      
STRAND   21    27  7      
HELIX   31    42  12      
STRAND   47    52  6      
HELIX   56    68  13      
HELIX   69    72  4      
STRAND   76    80  5      
HELIX   84    87  4      
STRAND   91    95  5      
HELIX   107   110  4      
HELIX   111   128  18      
STRAND   133   136  4      
STRAND   138   140  3      
HELIX   141   152  12      
HELIX   156   158  3      
STRAND   159   161  3      
HELIX   165   179  15      
HELIX   183   185  3      
STRAND   190   192  3      
HELIX   202   204  3      
HELIX   212   215  4      
TURN   217   220  4      
STRAND   221   223  3      
HELIX   229   246  18      
HELIX   251   265  15      
STRAND   270   277  8      
STRAND   289   297  9      
STRAND   300   305  6      
HELIX   311   328  18      
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 36638 Da [This is the MW of the unprocessed precursor] CRC64: 3AD605DEED0D54A2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK 

        70         80         90        100        110        120 
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF 

       130        140        150        160        170        180 
IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG 

       190        200        210        220        230        240 
IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY 

       250        260        270        280        290        300 
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG 

       310        320        330 
LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL 

P07195 in FASTA format

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