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P00338 (LDHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 176. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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):
Cell proliferation-inducing gene 19 protein
LDH muscle subunit
Short name=LDH-M
Renal carcinoma antigen NY-REN-59
Gene names
Name:LDHA
ORF Names:PIG19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.22

Subcellular location

Cytoplasm HAMAP-Rule MF_00488.

Post-translational modification

ISGylated. Ref.15

Involvement in disease

Glycogen storage disease 11 (GSD11) [MIM:612933]: A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPA8P111424EBI-372327,EBI-351896

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00338-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P00338-2)

The sequence of this isoform differs from the canonical sequence as follows:
     230-274: VHKQVVESAY...KNLRRVHPVS → CRYTLGDPKG...ACCPFYLICD
     275-332: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P00338-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGEPSGGYTYTQTSIFLFHAKIPFGSKSNM
Isoform 4 (identifier: P00338-4)

The sequence of this isoform differs from the canonical sequence as follows:
     82-139: Missing.
Isoform 5 (identifier: P00338-5)

The sequence of this isoform differs from the canonical sequence as follows:
     237-241: SAYEV → RVFTE
     242-332: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 332331L-lactate dehydrogenase A chain HAMAP-Rule MF_00488
PRO_0000168411

Regions

Nucleotide binding29 – 5729NAD HAMAP-Rule MF_00488

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.17 Ref.19 Ref.21
Modified residue51N6-acetyllysine; alternate Ref.19
Modified residue51N6-succinyllysine; alternate By similarity
Modified residue101Phosphotyrosine Ref.18
Modified residue141N6-acetyllysine Ref.19
Modified residue571N6-acetyllysine Ref.19
Modified residue811N6-acetyllysine Ref.19
Modified residue1181N6-acetyllysine; alternate Ref.19
Modified residue1181N6-succinyllysine; alternate By similarity
Modified residue1261N6-acetyllysine Ref.19
Modified residue2241N6-acetyllysine By similarity
Modified residue2321N6-acetyllysine By similarity
Modified residue2391Phosphotyrosine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine; alternate Ref.19
Modified residue3181N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence11M → MGEPSGGYTYTQTSIFLFHA KIPFGSKSNM in isoform 3.
VSP_042206
Alternative sequence82 – 13958Missing in isoform 4.
VSP_042786
Alternative sequence230 – 27445VHKQV…VHPVS → CRYTLGDPKGAAILKSSDVI SFHCLGYNRILGGGCACCPF YLICD in isoform 2.
VSP_014261
Alternative sequence237 – 2415SAYEV → RVFTE in isoform 5.
VSP_042788
Alternative sequence242 – 33291Missing in isoform 5.
VSP_042789
Alternative sequence275 – 33258Missing in isoform 2.
VSP_042787
Natural variant1611S → R.
Corresponds to variant rs5030621 [ dbSNP | Ensembl ].
VAR_059374
Natural variant2221K → E. Ref.6 Ref.24
VAR_004180
Natural variant3151R → C. Ref.23
VAR_004181

Secondary structure

....................................................... 332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 401E8604CEB7F908

FASTA33236,689
        10         20         30         40         50         60 
MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI 

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

       190        200        210        220        230        240 
HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI 

       310        320        330 
SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF 

« Hide

Isoform 2 [UniParc].

Checksum: D43CB4ACB426D6F0
Show »

FASTA27430,057
Isoform 3 [UniParc].

Checksum: D47D88F7C90BF11D
Show »

FASTA36139,837
Isoform 4 [UniParc].

Checksum: 1EB83D11978134AD
Show »

FASTA27430,205
Isoform 5 [UniParc].

Checksum: 20B4A3E33A1ED002
Show »

FASTA24126,712

References

« Hide 'large scale' references
[1]"Nucleotide sequences of the cDNA and an intronless pseudogene for human lactate dehydrogenase-A isozyme."
Tsujibo H., Tiano H.F., Li S.S.-L.
Eur. J. Biochem. 147:9-15(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Genomic organization of human lactate dehydrogenase-A gene."
Chung F.Z., Tsujibo H., Bhattacharyya U., Sharief F.S., Li S.S.-L.
Biochem. J. 231:537-541(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]"Identification of a human proliferation-inducing gene."
Kim J.W.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
Tissue: Umbilical cord.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-222.
Tissue: Gastric carcinoma.
[7]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM 1).
Tissue: Bone marrow.
[10]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14; 43-57; 60-73; 77-112; 133-149; 158-169; 233-243; 306-315 AND 319-328, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[11]"Analysis of genetic mutations in human lactate dehydrogenase-A(M) deficiency using DNA conformation polymorphism in combination with polyacrylamide gradient gel and silver staining."
Maekawa M., Sudo K., Li S.S., Kanno T.
Biochem. Biophys. Res. Commun. 180:1083-1090(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-121 AND 160-175.
[12]"Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification."
Maekawa M., Sudo K., Li S.S., Kanno T.
Hum. Genet. 88:34-38(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-254.
[13]"Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency."
Maekawa M., Sudo K., Kanno T., Li S.S.
Biochem. Biophys. Res. Commun. 168:677-682(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GSD11.
[14]"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.
[15]"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.
[16]"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].
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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 TYR-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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 ALA-2; LYS-5; LYS-14; LYS-57; LYS-81; LYS-118; LYS-126 AND LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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 (2.3 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE ANALOG, HOMOTETRAMERIZATION.
[23]"Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit."
Sudo K., Maekawa M., Shioya M., Ikeda K., Takahashi N., Isogai Y., Li S.S.-L., Kanno T., Machida K., Toriumi J.
Biochem. Int. 27:1051-1057(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-315.
[24]"Fast-type electrophoretic variant of lactate dehydrogenase M(A) and comparison with other missense mutations in lactate dehydrogenase M(A) and H(B) genes."
Maekawa M., Sudo K., Kobayashi A., Sugiyama E., Li S.S.-L., Kanno T.
Clin. Chem. 40:665-668(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-222.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Lactate dehydrogenase entry

Protein Spotlight

Another dark horse - Issue 109 of September 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02152 mRNA. Translation: CAA26088.1.
X03077 expand/collapse EMBL AC list , X03078, X03079, X03080, X03081, X03082, X03083 Genomic DNA. Translation: CAA26879.1.
AY423727 mRNA. Translation: AAS00490.1.
AK130587 mRNA. Translation: BAC85389.1.
AK296667 mRNA. Translation: BAG59264.1.
AK298834 mRNA. Translation: BAH12879.1.
CR456775 mRNA. Translation: CAG33056.1.
CR541714 mRNA. Translation: CAG46515.1.
AK223078 mRNA. Translation: BAD96798.1.
AC084117 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68395.1.
CH471064 Genomic DNA. Translation: EAW68396.1.
BC067223 mRNA. Translation: AAH67223.1.
S66853 Genomic DNA. Translation: AAB20418.1.
PIRDEHULM. A00347.
RefSeqNP_001128711.1. NM_001135239.1.
NP_001158886.1. NM_001165414.1.
NP_001158887.1. NM_001165415.1.
NP_001158888.1. NM_001165416.1.
NP_005557.1. NM_005566.3.
UniGeneHs.2795.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I10X-ray2.30A/B/C/D/E/F/G/H2-332[»]
4AJPX-ray2.38A/B/C/D2-332[»]
4JNKX-ray1.90A/B/C/D2-332[»]
4M49X-ray2.05A/B/C/D2-332[»]
ProteinModelPortalP00338.
SMRP00338. Positions 2-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110131. 60 interactions.
IntActP00338. 16 interactions.
MINTMINT-4998672.
STRING9606.ENSP00000395337.

Chemistry

BindingDBP00338.
ChEMBLCHEMBL4835.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP00338.

Polymorphism databases

DMDM126047.

2D gel databases

DOSAC-COBS-2DPAGEP00338.
OGPP00338.
REPRODUCTION-2DPAGEIPI00217966.

Proteomic databases

PaxDbP00338.
PeptideAtlasP00338.
PRIDEP00338.

Protocols and materials databases

DNASU3939.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227157; ENSP00000227157; ENSG00000134333. [P00338-5]
ENST00000379412; ENSP00000368722; ENSG00000134333. [P00338-1]
ENST00000396222; ENSP00000379524; ENSG00000134333. [P00338-2]
ENST00000422447; ENSP00000395337; ENSG00000134333. [P00338-1]
ENST00000430553; ENSP00000406172; ENSG00000134333. [P00338-4]
ENST00000540430; ENSP00000445175; ENSG00000134333. [P00338-3]
ENST00000542179; ENSP00000445331; ENSG00000134333. [P00338-1]
GeneID3939.
KEGGhsa:3939.
UCSCuc001mok.3. human. [P00338-1]
uc001mol.3. human. [P00338-5]
uc009yho.2. human. [P00338-4]
uc010rdd.2. human. [P00338-3]
uc021qep.1. human. [P00338-2]

Organism-specific databases

CTD3939.
GeneCardsGC11P018415.
HGNCHGNC:6535. LDHA.
HPACAB015336.
MIM150000. gene.
612933. phenotype.
neXtProtNX_P00338.
Orphanet284426. Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency.
PharmGKBPA30319.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213793.
HOVERGENHBG000462.
InParanoidP00338.
KOK00016.
OMAGANSYEA.
OrthoDBEOG7X0VH3.
PhylomeDBP00338.
TreeFamTF314963.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP00338.
UniPathwayUPA00554; UER00611.

Gene expression databases

ArrayExpressP00338.
BgeeP00338.
CleanExHS_LDHA.
GenevestigatorP00338.

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. human.
EvolutionaryTraceP00338.
GeneWikiLDHA.
GenomeRNAi3939.
NextBio15469.
PROP00338.
SOURCESearch...

Entry information

Entry nameLDHA_HUMAN
AccessionPrimary (citable) accession number: P00338
Secondary accession number(s): B4DKQ2 expand/collapse secondary AC list , B7Z5E3, D3DQY3, F8W819, Q53G53, Q6IBM7, Q6ZNV1, Q9UDE8, Q9UDE9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 176 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 11

Human chromosome 11: entries, gene names and cross-references to MIM