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P07195

- LDHB_HUMAN

UniProt

P07195 - LDHB_HUMAN

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Protein

L-lactate dehydrogenase B chain

Gene

LDHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001NAD1 Publication
Binding sitei107 – 1071Substrate
Binding sitei139 – 1391NAD or substrate1 Publication
Binding sitei170 – 1701Substrate
Active sitei194 – 1941Proton acceptor
Binding sitei249 – 2491Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 5323NADBy similarityAdd
BLAST

GO - Molecular functioni

  1. L-lactate dehydrogenase activity Source: ProtInc
  2. NAD binding Source: Ensembl

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. cellular metabolic process Source: Reactome
  3. lactate metabolic process Source: Ensembl
  4. NAD metabolic process Source: Ensembl
  5. pyruvate metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_121117. Abnormal metabolism in phenylketonuria.
REACT_2071. Pyruvate metabolism.
SABIO-RKP07195.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase B chain (EC:1.1.1.27)
Short name:
LDH-B
Alternative name(s):
LDH heart subunit
Short name:
LDH-H
Renal carcinoma antigen NY-REN-46
Gene namesi
Name:LDHB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6541. LDHB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614128. phenotype.
Orphaneti284435. Glycogen storage disease due to lactate dehydrogenase H-subunit deficiency.
PharmGKBiPA30325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 334333L-lactate dehydrogenase B chainPRO_0000168459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei7 – 71N6-acetyllysine1 Publication
Modified residuei44 – 441Phosphoserine1 Publication
Modified residuei58 – 581N6-acetyllysine1 Publication
Modified residuei119 – 1191N6-acetyllysine1 Publication
Modified residuei240 – 2401Phosphotyrosine2 Publications
Modified residuei329 – 3291N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP07195.
PaxDbiP07195.
PRIDEiP07195.

2D gel databases

DOSAC-COBS-2DPAGEP07195.
OGPiP07195.
REPRODUCTION-2DPAGEIPI00219217.
SWISS-2DPAGEP07195.
UCD-2DPAGEP07195.

PTM databases

PhosphoSiteiP07195.

Expressioni

Gene expression databases

BgeeiP07195.
CleanExiHS_LDHB.
ExpressionAtlasiP07195. baseline and differential.
GenevestigatoriP07195.

Organism-specific databases

HPAiCAB004641.
HPA019007.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-358748,EBI-5323863

Protein-protein interaction databases

BioGridi110137. 60 interactions.
IntActiP07195. 16 interactions.
MINTiMINT-1144561.
STRINGi9606.ENSP00000229319.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85
Beta strandi9 – 135
Beta strandi21 – 277
Helixi31 – 4212
Beta strandi47 – 526
Helixi56 – 6813
Helixi69 – 724
Beta strandi76 – 805
Helixi84 – 874
Beta strandi91 – 955
Helixi107 – 1104
Helixi111 – 12818
Beta strandi133 – 1364
Beta strandi138 – 1403
Helixi141 – 15212
Helixi156 – 1583
Beta strandi159 – 1613
Helixi165 – 17915
Helixi183 – 1853
Beta strandi190 – 1923
Helixi202 – 2043
Helixi212 – 2154
Turni217 – 2204
Beta strandi221 – 2233
Beta strandi225 – 2273
Helixi229 – 24618
Helixi251 – 26515
Beta strandi270 – 2778
Turni279 – 2824
Beta strandi289 – 2979
Beta strandi300 – 3045
Helixi311 – 32818

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I0ZX-ray2.10A/B2-334[»]
1T2FX-ray3.00A/B/C/D2-332[»]
ProteinModelPortaliP07195.
SMRiP07195. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07195.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP07195.
KOiK00016.
OMAiANIMAEV.
OrthoDBiEOG7X0VH3.
PhylomeDBiP07195.
TreeFamiTF314963.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07195-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA
60 70 80 90 100
LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR
110 120 130 140 150
QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK
160 170 180 190 200
LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA
210 220 230 240 250
VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN
260 270 280 290 300
WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
310 320 330
LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL
Length:334
Mass (Da):36,638
Last modified:January 23, 2007 - v2
Checksum:i3AD605DEED0D54A2
GO

Polymorphismi

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 [MIMi:614128].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71K → E in LDHB deficiency; slightly decreased activity. 1 Publication
VAR_004173
Natural varianti35 – 351A → E in LDHB deficiency. 1 Publication
VAR_004174
Natural varianti69 – 691G → E in LDHB deficiency. 1 Publication
VAR_011634
Natural varianti107 – 1071R → W in LDHB deficiency; inactive. 1 Publication
VAR_011635
Natural varianti129 – 1291S → R in LDHB deficiency. 1 Publication
VAR_004175
Natural varianti171 – 1711F → V in LDHB deficiency. 1 Publication
VAR_004176
Natural varianti172 – 1721R → H in LDHB deficiency; unstable. 2 Publications
VAR_004177
Natural varianti172 – 1721R → P in LDHB deficiency. 1 Publication
VAR_011636
Natural varianti175 – 1751M → L in LDHB deficiency. 1 Publication
VAR_004178
Natural varianti175 – 1751M → V.
Corresponds to variant rs7966339 [ dbSNP | Ensembl ].
VAR_049758
Natural varianti223 – 2231Missing in LDHB deficiency. 1 Publication
VAR_011637
Natural varianti322 – 3221D → V in LDHB deficiency. 1 Publication
VAR_004179
Natural varianti325 – 3251W → R in LDHB deficiency.
VAR_011638

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13794
, 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.
CCDSiCCDS8691.1.
PIRiS02795. DEHULH.
RefSeqiNP_001167568.1. NM_001174097.1.
NP_002291.1. NM_002300.6.
UniGeneiHs.446149.

Genome annotation databases

EnsembliENST00000350669; ENSP00000229319; ENSG00000111716.
ENST00000396076; ENSP00000379386; ENSG00000111716.
GeneIDi3945.
KEGGihsa:3945.
UCSCiuc001rfd.3. human.

Polymorphism databases

DMDMi126041.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Lactate dehydrogenase entry

Protein Spotlight

Another dark horse - Issue 109 of September 2009

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13794
, 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 .
CCDSi CCDS8691.1.
PIRi S02795. DEHULH.
RefSeqi NP_001167568.1. NM_001174097.1.
NP_002291.1. NM_002300.6.
UniGenei Hs.446149.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I0Z X-ray 2.10 A/B 2-334 [» ]
1T2F X-ray 3.00 A/B/C/D 2-332 [» ]
ProteinModelPortali P07195.
SMRi P07195. Positions 2-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110137. 60 interactions.
IntActi P07195. 16 interactions.
MINTi MINT-1144561.
STRINGi 9606.ENSP00000229319.

Chemistry

BindingDBi P07195.
ChEMBLi CHEMBL4940.

PTM databases

PhosphoSitei P07195.

Polymorphism databases

DMDMi 126041.

2D gel databases

DOSAC-COBS-2DPAGE P07195.
OGPi P07195.
REPRODUCTION-2DPAGE IPI00219217.
SWISS-2DPAGE P07195.
UCD-2DPAGE P07195.

Proteomic databases

MaxQBi P07195.
PaxDbi P07195.
PRIDEi P07195.

Protocols and materials databases

DNASUi 3945.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000350669 ; ENSP00000229319 ; ENSG00000111716 .
ENST00000396076 ; ENSP00000379386 ; ENSG00000111716 .
GeneIDi 3945.
KEGGi hsa:3945.
UCSCi uc001rfd.3. human.

Organism-specific databases

CTDi 3945.
GeneCardsi GC12M021788.
HGNCi HGNC:6541. LDHB.
HPAi CAB004641.
HPA019007.
MIMi 150100. gene.
614128. phenotype.
neXtProti NX_P07195.
Orphaneti 284435. Glycogen storage disease due to lactate dehydrogenase H-subunit deficiency.
PharmGKBi PA30325.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000213793.
HOVERGENi HBG000462.
InParanoidi P07195.
KOi K00016.
OMAi ANIMAEV.
OrthoDBi EOG7X0VH3.
PhylomeDBi P07195.
TreeFami TF314963.

Enzyme and pathway databases

UniPathwayi UPA00554 ; UER00611 .
Reactomei REACT_121117. Abnormal metabolism in phenylketonuria.
REACT_2071. Pyruvate metabolism.
SABIO-RK P07195.

Miscellaneous databases

ChiTaRSi LDHB. human.
EvolutionaryTracei P07195.
GenomeRNAii 3945.
NextBioi 15479.
PROi P07195.
SOURCEi Search...

Gene expression databases

Bgeei P07195.
CleanExi HS_LDHB.
ExpressionAtlasi P07195. baseline and differential.
Genevestigatori P07195.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_00488. Lactate_dehydrog.
InterProi IPR001557. 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 ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
PRINTSi PR00086. LLDHDRGNASE.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01771. L-LDH-NAD. 1 hit.
PROSITEi PS00064. L_LDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: VARIANT LDHB DEFICIENCY GLU-69.

Entry informationi

Entry nameiLDHB_HUMAN
AccessioniPrimary (citable) accession number: P07195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3