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P06151 (LDHA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase A chain

Short name=LDH-A
EC=1.1.1.27
Alternative name(s):
LDH muscle subunit
Short name=LDH-M
Gene names
Name:Ldha
Synonyms:Ldh-1, Ldh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length332 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.

Subcellular location

Cytoplasm HAMAP-Rule MF_00488.

Post-translational modification

ISGylated. Ref.7

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HnrnpdQ606682EBI-444940,EBI-299932

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 332331L-lactate dehydrogenase A chain HAMAP-Rule MF_00488
PRO_0000168414

Regions

Nucleotide binding29 – 5729NAD By similarity

Sites

Active site1931Proton acceptor By similarity
Binding site991NAD By similarity
Binding site1061Substrate By similarity
Binding site1381NAD or substrate By similarity
Binding site1691Substrate By similarity
Binding site2481Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue51N6-acetyllysine; alternate Ref.9
Modified residue51N6-succinyllysine; alternate Ref.9
Modified residue141N6-acetyllysine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue811N6-acetyllysine Ref.9
Modified residue1181N6-acetyllysine; alternate Ref.9
Modified residue1181N6-succinyllysine; alternate Ref.9
Modified residue1261N6-acetyllysine Ref.9
Modified residue2241N6-acetyllysine Ref.9
Modified residue2321N6-acetyllysine Ref.9
Modified residue2391Phosphotyrosine Ref.8
Modified residue2431N6-acetyllysine Ref.9
Modified residue3181N6-acetyllysine; alternate Ref.9
Modified residue3181N6-succinyllysine; alternate Ref.9

Experimental info

Sequence conflict111N → I Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06151 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5AEB41E1E0B95100

FASTA33236,499
        10         20         30         40         50         60 
MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNIVKYSPH CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 

       190        200        210        220        230        240 
HALSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI 

       310        320        330 
SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QF 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the mouse lactate dehydrogenase-A functional gene: comparison of the exon-intron organization of dehydrogenase genes."
Fukasawa K.M., Li S.S.-L.
Genetics 116:99-105(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/10.
Tissue: Liver.
[2]"Protein structure and gene organization of mouse lactate dehydrogenase-A isozyme."
Li S.S.-L., Tiano H.F., Fukasawa K.M., Yagi K., Shimizu M., Sharief F.S., Nakashima Y., Pan Y.E.
Eur. J. Biochem. 149:215-225(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Lactate dehydrogenase-A mRNAs in mouse testis and somatic tissues containing different 5' noncoding sequences."
Hiraoka Y., Li S.S.-L.
J. Genet. Mol. Biol. 1:1-6(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: DBA/2J.
[4]"Nucleotide sequence of the putative regulatory region of mouse lactate dehydrogenase-A gene."
Fukasawa K.M., Li S.S.-L.
Biochem. J. 235:435-439(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
[5]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-14; 23-73; 82-99; 107-126; 133-149; 158-169; 172-177; 213-228; 233-243; 246-265; 269-315 AND 319-328, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[6]"Isolation and characterization of a cDNA and a pseudogene for mouse lactate dehydrogenase-A isozyme."
Akai K., Yagi K., Tiano H.F., Pan Y.-C.E., Shimizu M., Fong K., Jungmann R.A., Li S.S.-L.
Int. J. Biochem. 17:645-648(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-332.
[7]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[8]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5; LYS-81; LYS-118; LYS-126; LYS-224; LYS-232; LYS-243 AND LYS-318, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-118 AND LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00309 Genomic DNA. Translation: CAA68410.1.
X02520 expand/collapse EMBL AC list , X02521, X02522, X02523, X02524, X02525, X02526 Genomic DNA. Translation: CAA26360.1.
U13687 mRNA. Translation: AAA21466.1.
X03753 Genomic DNA. Translation: CAA27387.1.
M17516 mRNA. Translation: AAA39424.1.
CCDSCCDS21289.1.
PIRDEMSLM. A25205.
I48240.
RefSeqNP_034829.1. NM_010699.2.
UniGeneMm.29324.

3D structure databases

ProteinModelPortalP06151.
SMRP06151. Positions 4-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201127. 5 interactions.
IntActP06151. 14 interactions.
MINTMINT-1612559.

PTM databases

PhosphoSiteP06151.

2D gel databases

REPRODUCTION-2DPAGEP06151.
SWISS-2DPAGEP06151.
UCD-2DPAGEP06151.

Proteomic databases

MaxQBP06151.
PaxDbP06151.
PRIDEP06151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229.
GeneID16828.
KEGGmmu:16828.
UCSCuc009gzm.2. mouse.

Organism-specific databases

CTD3939.
MGIMGI:96759. Ldha.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
HOVERGENHBG000462.
InParanoidP06151.
KOK00016.
PhylomeDBP06151.

Enzyme and pathway databases

UniPathwayUPA00554; UER00611.

Gene expression databases

ArrayExpressP06151.
BgeeP06151.
CleanExMM_LDHA.
GenevestigatorP06151.

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

ChiTaRSLDHA. mouse.
NextBio290734.
PROP06151.
SOURCESearch...

Entry information

Entry nameLDHA_MOUSE
AccessionPrimary (citable) accession number: P06151
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot