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P00338

- LDHA_HUMAN

UniProt

P00338 - LDHA_HUMAN

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Protein

L-lactate dehydrogenase A chain

Gene

LDHA

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 sitei99 – 991NAD1 Publication
Binding sitei106 – 1061Substrate
Binding sitei138 – 1381NAD or substrate1 Publication
Binding sitei169 – 1691Substrate
Active sitei193 – 1931Proton acceptor
Binding sitei248 – 2481Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5729NAD1 PublicationAdd
BLAST

GO - Molecular functioni

  1. L-lactate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. cellular metabolic process Source: Reactome
  3. cellular response to extracellular stimulus Source: Ensembl
  4. glycolytic process Source: UniProtKB
  5. pyruvate metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. substantia nigra development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_2071. Pyruvate metabolism.
SABIO-RKP00338.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase A chain (EC:1.1.1.27)
Short name:
LDH-A
Alternative name(s):
Cell proliferation-inducing gene 19 protein
LDH muscle subunit
Short name:
LDH-M
Renal carcinoma antigen NY-REN-59
Gene namesi
Name:LDHA
ORF Names:PIG19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:6535. LDHA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. nucleus Source: UniProt
  6. sperm fibrous sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 11 (GSD11) [MIM:612933]: A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi612933. phenotype.
Orphaneti284426. Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency.
PharmGKBiPA30319.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 332331L-lactate dehydrogenase A chainPRO_0000168411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
Modified residuei5 – 51N6-succinyllysine; alternateBy similarity
Modified residuei10 – 101Phosphotyrosine1 Publication
Modified residuei14 – 141N6-acetyllysine1 Publication
Modified residuei57 – 571N6-acetyllysine1 Publication
Modified residuei81 – 811N6-acetyllysine1 Publication
Modified residuei118 – 1181N6-acetyllysine; alternate1 Publication
Modified residuei118 – 1181N6-succinyllysine; alternateBy similarity
Modified residuei126 – 1261N6-acetyllysine1 Publication
Modified residuei224 – 2241N6-acetyllysineBy similarity
Modified residuei232 – 2321N6-acetyllysineBy similarity
Modified residuei239 – 2391PhosphotyrosineBy similarity
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei318 – 3181N6-acetyllysine; alternate1 Publication
Modified residuei318 – 3181N6-succinyllysine; alternateBy similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00338.
PaxDbiP00338.
PeptideAtlasiP00338.
PRIDEiP00338.

2D gel databases

DOSAC-COBS-2DPAGEP00338.
OGPiP00338.
REPRODUCTION-2DPAGEIPI00217966.

PTM databases

PhosphoSiteiP00338.

Expressioni

Gene expression databases

BgeeiP00338.
CleanExiHS_LDHA.
ExpressionAtlasiP00338. baseline and differential.
GenevestigatoriP00338.

Organism-specific databases

HPAiCAB015336.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPA8P111424EBI-372327,EBI-351896

Protein-protein interaction databases

BioGridi110131. 67 interactions.
IntActiP00338. 18 interactions.
MINTiMINT-4998672.
STRINGi9606.ENSP00000395337.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85
Beta strandi9 – 124
Beta strandi20 – 267
Helixi30 – 4112
Beta strandi46 – 516
Helixi55 – 6713
Helixi68 – 714
Beta strandi77 – 793
Helixi83 – 864
Beta strandi90 – 945
Helixi107 – 12721
Beta strandi132 – 1354
Beta strandi137 – 1393
Helixi140 – 15112
Helixi155 – 1573
Beta strandi158 – 1603
Helixi164 – 17815
Helixi182 – 1843
Beta strandi189 – 1935
Helixi194 – 1963
Helixi201 – 2033
Helixi211 – 2144
Turni216 – 2194
Beta strandi220 – 2223
Helixi228 – 24518
Helixi250 – 26415
Beta strandi269 – 2768
Beta strandi288 – 2969
Beta strandi299 – 3046
Helixi310 – 32718

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4L4RX-ray2.10A/H2-332[»]
4L4SX-ray2.90A/H2-332[»]
4M49X-ray2.05A/B/C/D2-332[»]
4QO7X-ray2.14A/B/C/D2-332[»]
4QO8X-ray2.00A/B/C/D2-332[»]
ProteinModelPortaliP00338.
SMRiP00338. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00338.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00550000074541.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP00338.
KOiK00016.
OMAiYAPSAFV.
OrthoDBiEOG7X0VH3.
PhylomeDBiP00338.
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]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P00338-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL
60 70 80 90 100
VDVIEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ
110 120 130 140 150
QEGESRLNLV QRNVNIFKFI IPNVVKYSPN CKLLIVSNPV DILTYVAWKI
160 170 180 190 200
SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV
210 220 230 240 250
WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE VIKLKGYTSW
260 270 280 290 300
AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI
310 320 330
SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF
Length:332
Mass (Da):36,689
Last modified:January 23, 2007 - v2
Checksum:i401E8604CEB7F908
GO
Isoform 2 (identifier: P00338-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:274
Mass (Da):30,057
Checksum:iD43CB4ACB426D6F0
GO
Isoform 3 (identifier: P00338-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGEPSGGYTYTQTSIFLFHAKIPFGSKSNM

Show »
Length:361
Mass (Da):39,837
Checksum:iD47D88F7C90BF11D
GO
Isoform 4 (identifier: P00338-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-139: Missing.

Show »
Length:274
Mass (Da):30,205
Checksum:i1EB83D11978134AD
GO
Isoform 5 (identifier: P00338-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:241
Mass (Da):26,712
Checksum:i20B4A3E33A1ED002
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti161 – 1611S → R.
Corresponds to variant rs5030621 [ dbSNP | Ensembl ].
VAR_059374
Natural varianti222 – 2221K → E.2 Publications
VAR_004180
Natural varianti315 – 3151R → C.1 Publication
VAR_004181

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGEPSGGYTYTQTSIFLFHA KIPFGSKSNM in isoform 3. 1 PublicationVSP_042206
Alternative sequencei82 – 13958Missing in isoform 4. 1 PublicationVSP_042786Add
BLAST
Alternative sequencei230 – 27445VHKQV…VHPVS → CRYTLGDPKGAAILKSSDVI SFHCLGYNRILGGGCACCPF YLICD in isoform 2. 1 PublicationVSP_014261Add
BLAST
Alternative sequencei237 – 2415SAYEV → RVFTE in isoform 5. CuratedVSP_042788
Alternative sequencei242 – 33291Missing in isoform 5. CuratedVSP_042789Add
BLAST
Alternative sequencei275 – 33258Missing in isoform 2. 1 PublicationVSP_042787Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS44549.1. [P00338-4]
CCDS53609.1. [P00338-3]
CCDS53610.1. [P00338-2]
CCDS53611.1. [P00338-5]
CCDS7839.1. [P00338-1]
PIRiA00347. DEHULM.
RefSeqiNP_001128711.1. NM_001135239.1. [P00338-4]
NP_001158886.1. NM_001165414.1. [P00338-3]
NP_001158887.1. NM_001165415.1. [P00338-2]
NP_001158888.1. NM_001165416.1. [P00338-5]
NP_005557.1. NM_005566.3. [P00338-1]
UniGeneiHs.2795.

Genome annotation databases

EnsembliENST00000227157; 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]
GeneIDi3939.
KEGGihsa:3939.
UCSCiuc001mok.3. human. [P00338-1]
uc001mol.3. human. [P00338-5]
uc009yho.2. human. [P00338-4]
uc010rdd.2. human. [P00338-3]
uc021qep.1. human. [P00338-2]

Polymorphism databases

DMDMi126047.

Keywords - Coding sequence diversityi

Alternative splicing, 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
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 .
CCDSi CCDS44549.1. [P00338-4 ]
CCDS53609.1. [P00338-3 ]
CCDS53610.1. [P00338-2 ]
CCDS53611.1. [P00338-5 ]
CCDS7839.1. [P00338-1 ]
PIRi A00347. DEHULM.
RefSeqi NP_001128711.1. NM_001135239.1. [P00338-4 ]
NP_001158886.1. NM_001165414.1. [P00338-3 ]
NP_001158887.1. NM_001165415.1. [P00338-2 ]
NP_001158888.1. NM_001165416.1. [P00338-5 ]
NP_005557.1. NM_005566.3. [P00338-1 ]
UniGenei Hs.2795.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4JNK X-ray 1.90 A/B/C/D 2-332 [» ]
4L4R X-ray 2.10 A/H 2-332 [» ]
4L4S X-ray 2.90 A/H 2-332 [» ]
4M49 X-ray 2.05 A/B/C/D 2-332 [» ]
4QO7 X-ray 2.14 A/B/C/D 2-332 [» ]
4QO8 X-ray 2.00 A/B/C/D 2-332 [» ]
ProteinModelPortali P00338.
SMRi P00338. Positions 2-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110131. 67 interactions.
IntActi P00338. 18 interactions.
MINTi MINT-4998672.
STRINGi 9606.ENSP00000395337.

Chemistry

BindingDBi P00338.
ChEMBLi CHEMBL4835.

PTM databases

PhosphoSitei P00338.

Polymorphism databases

DMDMi 126047.

2D gel databases

DOSAC-COBS-2DPAGE P00338.
OGPi P00338.
REPRODUCTION-2DPAGE IPI00217966.

Proteomic databases

MaxQBi P00338.
PaxDbi P00338.
PeptideAtlasi P00338.
PRIDEi P00338.

Protocols and materials databases

DNASUi 3939.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227157 ; 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 ]
GeneIDi 3939.
KEGGi hsa:3939.
UCSCi uc001mok.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

CTDi 3939.
GeneCardsi GC11P018415.
HGNCi HGNC:6535. LDHA.
HPAi CAB015336.
MIMi 150000. gene.
612933. phenotype.
neXtProti NX_P00338.
Orphaneti 284426. Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency.
PharmGKBi PA30319.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0039.
GeneTreei ENSGT00550000074541.
HOGENOMi HOG000213793.
HOVERGENi HBG000462.
InParanoidi P00338.
KOi K00016.
OMAi YAPSAFV.
OrthoDBi EOG7X0VH3.
PhylomeDBi P00338.
TreeFami TF314963.

Enzyme and pathway databases

UniPathwayi UPA00554 ; UER00611 .
Reactomei REACT_2071. Pyruvate metabolism.
SABIO-RK P00338.

Miscellaneous databases

ChiTaRSi LDHA. human.
EvolutionaryTracei P00338.
GeneWikii LDHA.
GenomeRNAii 3939.
NextBioi 15469.
PROi P00338.
SOURCEi Search...

Gene expression databases

Bgeei P00338.
CleanExi HS_LDHA.
ExpressionAtlasi P00338. baseline and differential.
Genevestigatori P00338.

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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  15. 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. 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.

Entry informationi

Entry nameiLDHA_HUMAN
AccessioniPrimary (citable) accession number: P00338
Secondary accession number(s): B4DKQ2
, B7Z5E3, D3DQY3, F8W819, Q53G53, Q6IBM7, Q6ZNV1, Q9UDE8, Q9UDE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 182 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 11
    Human chromosome 11: 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