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Protein

Malate dehydrogenase, cytoplasmic

Gene

Mdh1

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

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921SubstrateBy similarity
Binding sitei98 – 981SubstrateBy similarity
Binding sitei105 – 1051NADBy similarity
Binding sitei112 – 1121NADBy similarity
Binding sitei131 – 1311SubstrateBy similarity
Binding sitei162 – 1621SubstrateBy similarity
Active sitei187 – 1871Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 177NADBy similarity
Nucleotide bindingi129 – 1313NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
Alternative name(s):
Cytosolic malate dehydrogenase
Gene namesi
Name:Mdh1
Synonyms:Mor2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:97051. Mdh1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space 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 methioninei1 – 11RemovedBy similarity
Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000113410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei110 – 1101N6-succinyllysine1 Publication
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei121 – 1211N6-acetyllysineBy similarity
Modified residuei214 – 2141N6-succinyllysine1 Publication
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei298 – 2981N6-acetyllysine; alternateBy similarity
Modified residuei298 – 2981N6-succinyllysine; alternate1 Publication
Modified residuei318 – 3181N6-succinyllysine1 Publication
Modified residuei333 – 3331PhosphoserineBy similarity

Post-translational modificationi

ISGylated.1 Publication
Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14152.
PaxDbiP14152.
PRIDEiP14152.

2D gel databases

COMPLUYEAST-2DPAGEP14152.
REPRODUCTION-2DPAGEP14152.
SWISS-2DPAGEP14152.
UCD-2DPAGEP14152.

PTM databases

PhosphoSiteiP14152.

Expressioni

Gene expression databases

BgeeiP14152.
CleanExiMM_MDH1.
ExpressionAtlasiP14152. baseline and differential.
GenevisibleiP14152. MM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP14152. 8 interactions.
MINTiMINT-1869753.
STRINGi10090.ENSMUSP00000099938.

Structurei

3D structure databases

ProteinModelPortaliP14152.
SMRiP14152. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 2 family.Curated

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00530000063410.
HOGENOMiHOG000220953.
HOVERGENiHBG006340.
InParanoidiP14152.
KOiK00025.
OMAiFVTTVQQ.
OrthoDBiEOG78H3TM.
PhylomeDBiP14152.
TreeFamiTF105826.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL
60 70 80 90 100
DGVLMELQDC ALPLLQDVIA TDKEEIAFKD LDVAVLVGSM PRREGMERKD
110 120 130 140 150
LLKANVKIFK SQGTALEKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE
160 170 180 190 200
NFSCLTRLDH NRAKSQIALK LGVTADDVKN VIIWGNHSST QYPDVNHAKV
210 220 230 240 250
KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL SSAMSAAKAI
260 270 280 290 300
ADHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV
310 320 330
EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA
Length:334
Mass (Da):36,511
Last modified:January 23, 2007 - v3
Checksum:i3B9F00372AA939DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921R → I in BAB23897 (PubMed:16141072).Curated
Sequence conflicti177 – 1771D → N in BAE37915 (PubMed:16141072).Curated
Sequence conflicti288 – 2881F → L (PubMed:3312200).Curated
Sequence conflicti288 – 2881F → L (PubMed:3172222).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29462 mRNA. Translation: AAA39510.1.
M36084 Genomic DNA. Translation: AAA37423.1.
AK005237 mRNA. Translation: BAB23897.1.
AK164785 mRNA. Translation: BAE37915.1.
AK168545 mRNA. Translation: BAE40421.1.
AL663049 Genomic DNA. Translation: CAI24411.1.
BC050940 mRNA. Translation: AAH50940.2.
CCDSiCCDS24466.1.
PIRiS02654. DEMSMC.
RefSeqiNP_032644.3. NM_008618.3.
UniGeneiMm.212703.

Genome annotation databases

EnsembliENSMUST00000102874; ENSMUSP00000099938; ENSMUSG00000020321.
GeneIDi17449.
KEGGimmu:17449.
UCSCiuc007idv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29462 mRNA. Translation: AAA39510.1.
M36084 Genomic DNA. Translation: AAA37423.1.
AK005237 mRNA. Translation: BAB23897.1.
AK164785 mRNA. Translation: BAE37915.1.
AK168545 mRNA. Translation: BAE40421.1.
AL663049 Genomic DNA. Translation: CAI24411.1.
BC050940 mRNA. Translation: AAH50940.2.
CCDSiCCDS24466.1.
PIRiS02654. DEMSMC.
RefSeqiNP_032644.3. NM_008618.3.
UniGeneiMm.212703.

3D structure databases

ProteinModelPortaliP14152.
SMRiP14152. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14152. 8 interactions.
MINTiMINT-1869753.
STRINGi10090.ENSMUSP00000099938.

Chemistry

ChEMBLiCHEMBL2176827.

PTM databases

PhosphoSiteiP14152.

2D gel databases

COMPLUYEAST-2DPAGEP14152.
REPRODUCTION-2DPAGEP14152.
SWISS-2DPAGEP14152.
UCD-2DPAGEP14152.

Proteomic databases

MaxQBiP14152.
PaxDbiP14152.
PRIDEiP14152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102874; ENSMUSP00000099938; ENSMUSG00000020321.
GeneIDi17449.
KEGGimmu:17449.
UCSCiuc007idv.2. mouse.

Organism-specific databases

CTDi4190.
MGIiMGI:97051. Mdh1.

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00530000063410.
HOGENOMiHOG000220953.
HOVERGENiHBG006340.
InParanoidiP14152.
KOiK00025.
OMAiFVTTVQQ.
OrthoDBiEOG78H3TM.
PhylomeDBiP14152.
TreeFamiTF105826.

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.

Miscellaneous databases

NextBioi292088.
PROiP14152.
SOURCEiSearch...

Gene expression databases

BgeeiP14152.
CleanExiMM_MDH1.
ExpressionAtlasiP14152. baseline and differential.
GenevisibleiP14152. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase."
    Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y.
    J. Biol. Chem. 262:15127-15131(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structural organization of the mouse cytosolic malate dehydrogenase gene: comparison with that of the mouse mitochondrial malate dehydrogenase gene."
    Setoyama C., Joh T., Tsuzuki T., Shimada K.
    J. Mol. Biol. 202:355-364(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C3H/He.
    Tissue: Liver.
  3. "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, Mammary gland and Stomach.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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/6.
    Tissue: Brain.
  6. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 80-92; 126-142; 171-199; 206-230; 299-310 AND 325-334, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  7. Cited for: ISGYLATION.
  8. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-110; LYS-214; LYS-298 AND LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMDHC_MOUSE
AccessioniPrimary (citable) accession number: P14152
Secondary accession number(s): Q3TP22, Q80Y13, Q9DB45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 149 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.