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Reviewed, UniProtKB/Swiss-Prot P07195 (LDHB_HUMAN)

Last modified June 16, 2009. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-lactate dehydrogenase B chain
      Short name=LDH-B
    EC=1.1.1.27
Alternative name(s):
    LDH heart subunit
      Short name=LDH-H
    Renal carcinoma antigen NY-REN-46
Gene names
Name: LDHB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

(S)-lactate + NAD+ = pyruvate + NADH.

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.

Subunit structure

Homotetramer. Ref.10

Subcellular location

Cytoplasm.

Involvement in disease

Defects in LDHB are a cause of hereditary LDHB deficiency [MIM:150100]. LDHB deficiency is usually asymptomatic.

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processanaerobic glycolysis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Traceable author statement. Source: UniProtKB

   Molecular functionL-lactate dehydrogenase activity Ref.11

Traceable author statement. Source: ProtInc

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 334333L-lactate dehydrogenase B chain
PRO_0000168459

Regions

Nucleotide binding31 – 5323NAD By similarity

Sites

Active site1941Proton acceptor
Binding site1001NAD
Binding site1071Substrate
Binding site1391NAD or substrate
Binding site1701Substrate
Binding site2491Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue2401Phosphotyrosine Ref.7 Ref.8

Natural variations

Natural variant71K → E in LDHB deficiency; slightly decreased activity.
VAR_004173
Natural variant351A → E in LDHB deficiency.
VAR_004174
Natural variant691G → E in LDHB deficiency.
VAR_011634
Natural variant1071R → W in GUA1; LDHB deficiency; inactive. Ref.16
VAR_011635
Natural variant1291S → R in LDHB deficiency.
VAR_004175
Natural variant1711F → V in LDHB deficiency.
VAR_004176
Natural variant1721R → H in LDHB deficiency; unstable.
VAR_004177
Natural variant1721R → P in LDHB deficiency.
VAR_011636
Natural variant1751M → L in LDHB deficiency.
VAR_004178
Natural variant1751M → V: dbSNP rs7966339. Ref.12
VAR_049758
Natural variant2231Missing in LDHB deficiency.
VAR_011637
Natural variant3221D → V in LDHB deficiency.
VAR_004179
Natural variant3251W → R in LDHB deficiency.
VAR_011638

Secondary structure

....................................................... 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07195-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3AD605DEED0D54A2

FASTA33436,638
        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 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the human lactate dehydrogenase B gene."
Takeno T., Li S.S.-L.
Biochem. J. 257:921-924(1989) [PubMed: 2930497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The cDNA and protein sequences of human lactate dehydrogenase B."
Sakai I., Sharief F.S., Pan Y.-C.E., Li S.S.-L.
Biochem. J. 248:933-936(1987) [PubMed: 3435492] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: T-cell.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle and Urinary bladder.
[4]Bienvenut W.V.
Submitted (MAY-2005) to UniProtKB
Cited for: 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, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[5]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 8-23; 44-58; 78-91; 108-113; 120-127; 159-170; 234-244; 280-299 AND 300-318, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[6]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
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.
Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, MASS SPECTROMETRY.
[8]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, MASS SPECTROMETRY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]"Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase."
Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.
Proteins 43:175-185(2001) [PubMed: 11276087] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE ANALOG, HOMOTETRAMERIZATION.
[11]"Analysis of a genetic mutation in an electrophoretic variant of the human lactate dehydrogenase-B(H) subunit."
Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.
Hum. Genet. 91:423-426(1993) [PubMed: 8314553] [Abstract]
Cited for: VARIANT GLU-7.
[12]"Detection and characterization of new genetic mutations in individuals heterozygous for lactate dehydrogenase-B(H) deficiency using DNA conformation polymorphism analysis and silver staining."
Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.
Hum. Genet. 91:163-168(1993) [PubMed: 8462975] [Abstract]
Cited for: VARIANTS GLU-35; VAL-171 AND LEU-175.
[13]"Molecular characterization of genetic mutations in human lactate dehydrogenase (LDH) B (H) variant."
Sudo K., Maekawa M., Tomonaga A., Tsukada T., Nakayama T., Kitamura M., Li S.S.-L., Kanno T., Toriumi J.
Hum. Genet. 89:158-162(1992) [PubMed: 1587525] [Abstract]
Cited for: VARIANTS ARG-129 AND HIS-172.
[14]"A missense mutation found in human lactate dehydrogenase-B (H) variant gene."
Sudo K., Maekawa M., Ikawa S., Machida K., Kitamura M., Li S.S.-L.
Biochem. Biophys. Res. Commun. 168:672-676(1990) [PubMed: 2334429] [Abstract]
Cited for: VARIANT HIS-172.
[15]"DNA analysis of slow type of electrophoretic lactate dehydrogenase B(H) variant."
Maekawa M., Sudo K., Fujita K., Yoshioka N., Sakurabayashi I., Li S.S.-L., Kanno T.
Seibutsu Butsuri Kagaku 38:25-29(1994)
Cited for: VARIANT VAL-322.
[16]"Arginine to tryptophan substitution in the active site of a human lactate dehydrogenase variant -- LDHB GUA1: postulated effects on subunit structure and catalysis."
Shonnard G.C., Hud N.V., Mohrenweiser H.W.
Biochim. Biophys. Acta 1315:9-14(1996) [PubMed: 8611651] [Abstract]
Cited for: VARIANT GUA1 TRP-107.
[17]"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."
Sudo K., Maekawa M., Houki N., Okuda T., Akizuki S., Magara T., Kawano K.
Clin. Biochem. 32:137-141(1999) [PubMed: 10211631] [Abstract]
Cited for: VARIANT ASN-223 DEL.
[18]"First case of missense mutation (LDH-H:R171P) in exon 4 of the lactate dehydrogenase gene detected in a Japanese patient."
Hidaka K., Ueda N., Hirata I., Watanabe Y., Minatogawa Y., Iuchi I.
J. Hum. Genet. 44:69-72(1999) [PubMed: 9929983] [Abstract]
Cited for: VARIANT PRO-172.
[19]"A novel missense mutation in human lactate dehydrogenase b-subunit gene."
Takatani T., Takaoka N., Tatsumi M., Kawamoto H., Okuno Y., Morita K., Masutani T., Murakawa K., Okamoto Y.
Mol. Genet. Metab. 73:344-348(2001) [PubMed: 11509017] [Abstract]
Cited for: VARIANT GLU-69.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Lactate dehydrogenase entry

Cross-references

Sequence databases

X13794 expand/collapse EMBL AC list , X13795, X13796, X13797, X13798, X13799, X13800 Genomic DNA. Translation: CAA32033.1.
Y00711 mRNA. Translation: CAA68701.1.
BC002362 mRNA. Translation: AAH02362.1.
BC015122 mRNA. Translation: AAH15122.1.
BC071860 mRNA. Translation: AAH71860.1.
IPIIPI00219217.
PIRDEHULH. S02795.
RefSeqNP_002291.1.
UniGeneHs.446149

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1I0ZX-ray2.10A/B2-334[»]
1T2FX-ray3.00A/B/C/D2-332[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP07195. 2 interactions.

PTM databases

PhosphoSiteP07195.

2-D gel databases

SWISS-2DPAGEP07195.
Cornea-2DPAGEP07195.
DOSAC-COBS-2DPAGEP07195.
HSC-2DPAGEP07195.
OGPP07195.
REPRODUCTION-2DPAGEIPI00219217.

Proteomic databases

PRIDEP07195.

Genome annotation databases

EnsemblENSG00000111716. Homo sapiens. [Contig view]
GeneID3945.
KEGGhsa:3945.

Organism-specific databases

GeneCardsGC12M021679.
H-InvDBHIX0010481.
HGNCHGNC:6541. LDHB.
HPACAB004641.
MIM150100. gene+phenotype.
Orphanet2364. Lactate dehydrogenase deficiency.
79338. Lactate dehydrogenase deficiency type B.
PharmGKBPA30325.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP07195.
HOVERGENP07195.
OMAP07195. YSPDCTI.

Enzyme and pathway databases

BRENDA1.1.1.27. 247.
ReactomeREACT_1046. Pyruvate metabolism and TCA cycle.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpressP07195.
BgeeP07195.
CleanExHS_LDHB.
GermOnlineENSG00000111716. Homo sapiens.

Family and domain databases

InterProIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR001236. Lactate/malate_DH.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
[Graphical view]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP07195.
DrugBankDB00157. NADH.
NextBio15479.
SOURCESearch...

Entry information

Entry nameLDHB_HUMAN
AccessionPrimary (citable) accession number: P07195
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents