P00338 (LDHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20
Subcellular location	Cytoplasm.
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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Glycogen storage disease
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cellular response to extracellular stimulus Inferred from electronic annotation. Source: Compara glycolysis Non-traceable author statement Ref.11. Source: UniProtKB pyruvate metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	L-lactate dehydrogenase activity Non-traceable author statement Ref.11. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 332

331

L-lactate dehydrogenase A chain

PRO_0000168411

Regions

Nucleotide binding

29 – 57

29

NAD

Sites

Active site

193

1

Proton acceptor

Binding site

99

1

NAD

Binding site

106

1

Substrate

Binding site

138

1

NAD or substrate

Binding site

169

1

Substrate

Binding site

248

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10 Ref.18

Modified residue

5

1

N6-acetyllysine Ref.18

Modified residue

10

1

Phosphotyrosine Ref.17

Modified residue

14

1

N6-acetyllysine Ref.18

Modified residue

57

1

N6-acetyllysine Ref.18

Modified residue

81

1

N6-acetyllysine Ref.18

Modified residue

118

1

N6-acetyllysine Ref.18

Modified residue

126

1

N6-acetyllysine Ref.18

Modified residue

239

1

Phosphotyrosine By similarity

Modified residue

318

1

N6-acetyllysine Ref.18

Natural variations

Alternative sequence

1

1

M → MGEPSGGYTYTQTSIFLFHA KIPFGSKSNM in isoform 3.

VSP_042206

Alternative sequence

82 – 139

58

Missing in isoform 4.

VSP_042786

Alternative sequence

230 – 274

45

VHKQV…VHPVS → CRYTLGDPKGAAILKSSDVI SFHCLGYNRILGGGCACCPF YLICD in isoform 2.

VSP_014261

Alternative sequence

237 – 241

5

SAYEV → RVFTE in isoform 5.

VSP_042788

Alternative sequence

242 – 332

91

Missing in isoform 5.

VSP_042789

Alternative sequence

275 – 332

58

Missing in isoform 2.

VSP_042787

Natural variant

161

1

S → R.
Corresponds to variant rs5030621 [ dbSNP | Ensembl ].

VAR_059374

Natural variant

222

1

K → E. Ref.6 Ref.22

VAR_004180

Natural variant

315

1

R → C. Ref.21

VAR_004181

Secondary structure

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332

Helix Strand Turn

Details...

Helix

4 – 8

5

Beta strand

9 – 13

5

Beta strand

20 – 26

7

Helix

30 – 41

12

Beta strand

46 – 51

6

Helix

55 – 66

12

Helix

67 – 71

5

Beta strand

76 – 79

4

Helix

83 – 86

4

Beta strand

90 – 94

5

Helix

106 – 109

4

Helix

110 – 127

18

Beta strand

132 – 135

4

Beta strand

137 – 139

3

Helix

140 – 151

12

Helix

155 – 157

3

Beta strand

158 – 160

3

Helix

164 – 178

15

Helix

182 – 184

3

Beta strand

189 – 191

3

Helix

201 – 203

3

Helix

211 – 214

4

Turn

216 – 219

4

Beta strand

220 – 222

3

Helix

228 – 245

18

Helix

250 – 264

15

Beta strand

269 – 276

8

Beta strand

288 – 296

9

Beta strand

299 – 304

6

Helix

310 – 327

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 401E8604CEB7F908	FASTA	332	36,689
	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
	Isoform 2 [UniParc]. Checksum: D43CB4ACB426D6F0	FASTA	274	30,057
	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 DKDKEQWKEC RYTLGDPKGA 250 260 270 AILKSSDVIS FHCLGYNRIL GGGCACCPFY LICD
	Isoform 3 [UniParc]. Checksum: D47D88F7C90BF11D	FASTA	361	39,837
	10 20 30 40 50 60 MGEPSGGYTY TQTSIFLFHA KIPFGSKSNM ATLKDQLIYN LLKEEQTPQN KITVVGVGAV 70 80 90 100 110 120 GMACAISILM KDLADELALV DVIEDKLKGE MMDLQHGSLF LRTPKIVSGK DYNVTANSKL 130 140 150 160 170 180 VIITAGARQQ EGESRLNLVQ RNVNIFKFII PNVVKYSPNC KLLIVSNPVD ILTYVAWKIS 190 200 210 220 230 240 GFPKNRVIGS GCNLDSARFR YLMGERLGVH PLSCHGWVLG EHGDSSVPVW SGMNVAGVSL 250 260 270 280 290 300 KTLHPDLGTD KDKEQWKEVH KQVVESAYEV IKLKGYTSWA IGLSVADLAE SIMKNLRRVH 310 320 330 340 350 360 PVSTMIKGLY GIKDDVFLSV PCILGQNGIS DLVKVTLTSE EEARLKKSAD TLWGIQKELQ F
	Isoform 4 [UniParc]. Checksum: 1EB83D11978134AD	FASTA	274	30,205
	10 20 30 40 50 60 MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG 70 80 90 100 110 120 EMMDLQHGSL FLRTPKIVSG KVDILTYVAW KISGFPKNRV IGSGCNLDSA RFRYLMGERL 130 140 150 160 170 180 GVHPLSCHGW VLGEHGDSSV PVWSGMNVAG VSLKTLHPDL GTDKDKEQWK EVHKQVVESA 190 200 210 220 230 240 YEVIKLKGYT SWAIGLSVAD LAESIMKNLR RVHPVSTMIK GLYGIKDDVF LSVPCILGQN 250 260 270 GISDLVKVTL TSEEEARLKK SADTLWGIQK ELQF
	Isoform 5 [UniParc]. Checksum: 20B4A3E33A1ED002	FASTA	241	26,712
	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 HKQVVERVFT E

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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, MASS SPECTROMETRY.
[19]	"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].
[20]	"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.
[21]	"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.
[22]	"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 , 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.

IPI

IPI00217966.
IPI00607708.
IPI00947127.

PIR

DEHULM. A00347.

RefSeq

NP_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.

UniGene

Hs.2795.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I10	X-ray	2.30	A/B/C/D/E/F/G/H	2-332	[»]
4AJP	X-ray	2.38	A/B/C/D	2-332	[»]

ProteinModelPortal

P00338.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00338. 15 interactions.

MINT

MINT-4998672.

STRING

9606.ENSP00000395337.

PTM databases

PhosphoSite

P00338.

Polymorphism databases

DMDM

126047.

2D gel databases

DOSAC-COBS-2DPAGE

P00338.

OGP

P00338.

REPRODUCTION-2DPAGE

IPI00217966.

Proteomic databases

PaxDb

P00338.

PeptideAtlas

P00338.

PRIDE

P00338.

Protocols and materials databases

DNASU

3939.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000227157; ENSP00000227157; ENSG00000134333.
ENST00000379412; ENSP00000368722; ENSG00000134333.
ENST00000396222; ENSP00000379524; ENSG00000134333.
ENST00000422447; ENSP00000395337; ENSG00000134333.
ENST00000430553; ENSP00000406172; ENSG00000134333.
ENST00000540430; ENSP00000445175; ENSG00000134333.
ENST00000542179; ENSP00000445331; ENSG00000134333.

GeneID

3939.

KEGG

hsa:3939.

UCSC

uc001mok.3. human.

Organism-specific databases

CTD

3939.

GeneCards

GC11P018415.

HGNC

HGNC:6535. LDHA.

HPA

CAB015336.

MIM

150000. gene.
612933. phenotype.

neXtProt

NX_P00338.

Orphanet

284426. Lactate dehydrogenase M-subunit deficiency.

PharmGKB

PA30319.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0039.

HOGENOM

HOG000213793.

HOVERGEN

HBG000462.

InParanoid

P00338.

KO

K00016.

OMA

DAMTYVM.

OrthoDB

EOG4RR6HR.

PhylomeDB

P00338.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P00338.

UniPathway

UPA00554; UER00611.

Gene expression databases

ArrayExpress

P00338.

Bgee

P00338.

CleanEx

HS_LDHA.

Genevestigator

P00338.

GermOnline

ENSG00000134333. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.
3.90.110.10. 1 hit.

InterPro

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]

PANTHER

PTHR11540. PTHR11540. 1 hit.

Pfam

PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000102. Lac_mal_DH. 1 hit.

PRINTS

PR00086. LLDHDRGNASE.

SUPFAM

SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.

TIGRFAMs

TIGR01771. L-LDH-NAD. 1 hit.

PROSITE

PS00064. L_LDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00338.

ChEMBL

CHEMBL4835.

ChiTaRS

LDHA. human.

DrugBank

DB00157. NADH.

EvolutionaryTrace

P00338.

GenomeRNAi

3939.

NextBio

15469.

SOURCE

Search...

Entry information

Entry name

LDHA_HUMAN

Accession

Primary (citable) accession number: P00338
Secondary accession number(s): B4DKQ2 , 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:	May 1, 2013
This is version 166 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.