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P07195 (LDHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
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. HAMAP-Rule MF_00488

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP-Rule MF_00488

Subunit structure

Homotetramer. Ref.12

Subcellular location

Cytoplasm HAMAP-Rule MF_00488.

Polymorphism

Rare LDHB variants result in deficiency of lactate dehydrogenase, a condition with no deleterious effects on health. LDHB deficiency is of interest to laboratory medicine mainly because it can cause misdiagnosis in those disorders in which elevation of serum LDH is expected. Lactate dehydrogenase deficiency can probably be considered a non-disease [MIM:614128]. HAMAP-Rule MF_00488

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 334333L-lactate dehydrogenase B chain HAMAP-Rule MF_00488
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 residue71N6-acetyllysine Ref.9
Modified residue441Phosphoserine Ref.8
Modified residue581N6-acetyllysine Ref.9
Modified residue1191N6-acetyllysine Ref.9
Modified residue2401Phosphotyrosine Ref.8 Ref.10
Modified residue3291N6-acetyllysine Ref.9

Natural variations

Natural variant71K → E in LDHB deficiency; slightly decreased activity. Ref.13
VAR_004173
Natural variant351A → E in LDHB deficiency. Ref.14
VAR_004174
Natural variant691G → E in LDHB deficiency. Ref.21
VAR_011634
Natural variant1071R → W in LDHB deficiency; inactive. Ref.18
VAR_011635
Natural variant1291S → R in LDHB deficiency. Ref.15
VAR_004175
Natural variant1711F → V in LDHB deficiency. Ref.14
VAR_004176
Natural variant1721R → H in LDHB deficiency; unstable. Ref.15 Ref.16
VAR_004177
Natural variant1721R → P in LDHB deficiency. Ref.20
VAR_011636
Natural variant1751M → L in LDHB deficiency. Ref.14
VAR_004178
Natural variant1751M → V.
Corresponds to variant rs7966339 [ dbSNP | Ensembl ].
VAR_049758
Natural variant2231Missing in LDHB deficiency. Ref.19
VAR_011637
Natural variant3221D → V in LDHB deficiency. Ref.17
VAR_004179
Natural variant3251W → R in LDHB deficiency.
VAR_011638

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P07195 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND TYR-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-58; LYS-119 AND LYS-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE ANALOG, HOMOTETRAMERIZATION.
[13]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LDHB DEFICIENCY GLU-7.
[14]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS LDHB DEFICIENCY GLU-35; VAL-171 AND LEU-175.
[15]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS LDHB DEFICIENCY ARG-129 AND HIS-172.
[16]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LDHB DEFICIENCY HIS-172.
[17]"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 LDHB DEFICIENCY VAL-322.
[18]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LDHB DEFICIENCY TRP-107.
[19]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LDHB DEFICIENCY ASN-223 DEL.
[20]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LDHB DEFICIENCY PRO-172.
[21]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LDHB DEFICIENCY GLU-69.
+Additional computationally mapped references.

Web resources

Wikipedia

Lactate dehydrogenase entry

Protein Spotlight

Another dark horse - Issue 109 of September 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8691.1.
PIRDEHULH. S02795.
RefSeqNP_001167568.1. NM_001174097.1.
NP_002291.1. NM_002300.6.
UniGeneHs.446149.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I0ZX-ray2.10A/B2-334[»]
1T2FX-ray3.00A/B/C/D2-332[»]
ProteinModelPortalP07195.
SMRP07195. Positions 2-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110137. 58 interactions.
IntActP07195. 15 interactions.
MINTMINT-1144561.
STRING9606.ENSP00000229319.

Chemistry

BindingDBP07195.
ChEMBLCHEMBL4940.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP07195.

Polymorphism databases

DMDM126041.

2D gel databases

DOSAC-COBS-2DPAGEP07195.
OGPP07195.
REPRODUCTION-2DPAGEIPI00219217.
SWISS-2DPAGEP07195.
UCD-2DPAGEP07195.

Proteomic databases

MaxQBP07195.
PaxDbP07195.
PRIDEP07195.

Protocols and materials databases

DNASU3945.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000350669; ENSP00000229319; ENSG00000111716.
ENST00000396076; ENSP00000379386; ENSG00000111716.
GeneID3945.
KEGGhsa:3945.
UCSCuc001rfd.3. human.

Organism-specific databases

CTD3945.
GeneCardsGC12M021788.
HGNCHGNC:6541. LDHB.
HPACAB004641.
HPA019007.
MIM150100. gene.
614128. phenotype.
neXtProtNX_P07195.
Orphanet284435. Glycogen storage disease due to lactate dehydrogenase H-subunit deficiency.
PharmGKBPA30325.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
HOVERGENHBG000462.
InParanoidP07195.
KOK00016.
OMAANIMAEV.
OrthoDBEOG7X0VH3.
PhylomeDBP07195.
TreeFamTF314963.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP07195.
UniPathwayUPA00554; UER00611.

Gene expression databases

ArrayExpressP07195.
BgeeP07195.
CleanExHS_LDHB.
GenevestigatorP07195.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00488. Lactate_dehydrog.
InterProIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLDHB. human.
EvolutionaryTraceP07195.
GenomeRNAi3945.
NextBio15479.
PROP07195.
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: July 9, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

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