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Protein

L-lactate dehydrogenase B chain

Gene

Ldhb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase B chain (Ldhb), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldhal6b), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase A chain (Ldha), L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase C chain (Ldhc), L-lactate dehydrogenase (Ldhc)
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001NADBy similarity
Binding sitei107 – 1071SubstrateBy similarity
Binding sitei139 – 1391NAD or substrateBy similarity
Binding sitei170 – 1701SubstrateBy similarity
Active sitei194 – 1941Proton acceptorBy similarity
Binding sitei249 – 2491SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 5829NADBy similarityAdd
BLAST

GO - Molecular functioni

  • L-lactate dehydrogenase activity Source: MGI
  • NAD binding Source: Ensembl

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • lactate biosynthetic process from pyruvate Source: MGI
  • NAD metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-MMU-70268. Pyruvate metabolism.
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
Gene namesi
Name:Ldhb
Synonyms:Ldh-2, Ldh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:96763. Ldhb.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • membrane raft Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 334333L-lactate dehydrogenase B chainPRO_0000168461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysineBy similarity
Modified residuei119 – 1191N6-acetyllysineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei240 – 2401PhosphotyrosineCombined sources
Modified residuei319 – 3191N6-acetyllysineBy similarity
Modified residuei329 – 3291N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP16125.
MaxQBiP16125.
PaxDbiP16125.
PRIDEiP16125.
TopDownProteomicsiP16125.

2D gel databases

REPRODUCTION-2DPAGEP16125.
Q545Y4.
UCD-2DPAGEP16125.

PTM databases

iPTMnetiP16125.
PhosphoSiteiP16125.
SwissPalmiP16125.

Expressioni

Gene expression databases

BgeeiP16125.
CleanExiMM_LDHB.
ExpressionAtlasiP16125. baseline and differential.
GenevisibleiP16125. MM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi201130. 3 interactions.
IntActiP16125. 7 interactions.
MINTiMINT-4100306.
STRINGi10090.ENSMUSP00000032373.

Structurei

3D structure databases

ProteinModelPortaliP16125.
SMRiP16125. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
GeneTreeiENSGT00550000074541.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP16125.
KOiK00016.
OMAiDSDSENW.
OrthoDBiEOG7X0VH3.
PhylomeDBiP16125.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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.

P16125-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLKEKLIA SVADDEAAVP NNKITVVGVG QVGMACAISI LGKSLADELA
60 70 80 90 100
LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR
110 120 130 140 150
QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCTIIVVSNP VDILTYVTWK
160 170 180 190 200
LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA
210 220 230 240 250
VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVDSAY EVIKLKGYTN
260 270 280 290 300
WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
310 320 330
LTSVINQKLK DDEVAQLRKS ADTLWDIQKD LKDL
Length:334
Mass (Da):36,572
Last modified:January 23, 2007 - v2
Checksum:i86E6CDCDD251285D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51905 mRNA. Translation: CAA36185.1.
AK002257 mRNA. Translation: BAB21970.1.
AK019391 mRNA. Translation: BAB31697.1.
AK131637 mRNA. Translation: BAE20732.1.
BC046755 mRNA. Translation: AAH46755.1.
CCDSiCCDS20684.1.
PIRiS09954.
RefSeqiNP_001289694.1. NM_001302765.1.
NP_001303251.1. NM_001316322.1.
NP_032518.1. NM_008492.3.
UniGeneiMm.9745.

Genome annotation databases

EnsembliENSMUST00000032373; ENSMUSP00000032373; ENSMUSG00000030246.
GeneIDi16832.
KEGGimmu:16832.
UCSCiuc009epj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51905 mRNA. Translation: CAA36185.1.
AK002257 mRNA. Translation: BAB21970.1.
AK019391 mRNA. Translation: BAB31697.1.
AK131637 mRNA. Translation: BAE20732.1.
BC046755 mRNA. Translation: AAH46755.1.
CCDSiCCDS20684.1.
PIRiS09954.
RefSeqiNP_001289694.1. NM_001302765.1.
NP_001303251.1. NM_001316322.1.
NP_032518.1. NM_008492.3.
UniGeneiMm.9745.

3D structure databases

ProteinModelPortaliP16125.
SMRiP16125. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201130. 3 interactions.
IntActiP16125. 7 interactions.
MINTiMINT-4100306.
STRINGi10090.ENSMUSP00000032373.

PTM databases

iPTMnetiP16125.
PhosphoSiteiP16125.
SwissPalmiP16125.

2D gel databases

REPRODUCTION-2DPAGEP16125.
Q545Y4.
UCD-2DPAGEP16125.

Proteomic databases

EPDiP16125.
MaxQBiP16125.
PaxDbiP16125.
PRIDEiP16125.
TopDownProteomicsiP16125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032373; ENSMUSP00000032373; ENSMUSG00000030246.
GeneIDi16832.
KEGGimmu:16832.
UCSCiuc009epj.2. mouse.

Organism-specific databases

CTDi3945.
MGIiMGI:96763. Ldhb.

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
GeneTreeiENSGT00550000074541.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP16125.
KOiK00016.
OMAiDSDSENW.
OrthoDBiEOG7X0VH3.
PhylomeDBiP16125.
TreeFamiTF314963.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
ReactomeiR-MMU-70268. Pyruvate metabolism.

Miscellaneous databases

NextBioi290742.
PROiP16125.
SOURCEiSearch...

Gene expression databases

BgeeiP16125.
CleanExiMM_LDHB.
ExpressionAtlasiP16125. baseline and differential.
GenevisibleiP16125. MM.

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cDNA and protein sequences of mouse lactate dehydrogenase B. Molecular evolution of vertebrate lactate dehydrogenase genes A (muscle), B (heart) and C (testis)."
    Hiraoka B.Y., Sharief F.S., Yang Y.W., Li W.H., Li S.S.-L.
    Eur. J. Biochem. 189:215-220(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Head and Kidney.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 24-77; 120-127; 159-170 AND 271-299, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  5. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiLDHB_MOUSE
AccessioniPrimary (citable) accession number: P16125
Secondary accession number(s): Q545Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.