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UniProtKB/Swiss-Prot entry P40925


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MDHC_HUMAN
Primary accession number P40925
Secondary accession number Q6I9V0
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 89)
Name and origin of the protein
Protein name Malate dehydrogenase, cytoplasmic
Synonyms EC 1.1.1.37
Cytosolic malate dehydrogenase
Gene name
Name: MDH1
Synonyms: MDHA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
DOI=10.1006/geno.1996.0087; PubMed=8786100 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T., Inazawa J., Nakamura Y.;
"Molecular cloning and mapping of a human cDNA for cytosolic malate dehydrogenase (MDH1).";
Genomics 32:128-130(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
Lo A.S.Y., Waye M.M.Y.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-18; 205-213 AND 324-334, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 168-181.
TISSUE=Heart;
PubMed=7895732 [NCBI, ExPASy, EBI, Israel, Japan]
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
"The human myocardial two-dimensional gel protein database: update 1994.";
Electrophoresis 15:1459-1465(1994).
[8]
PROTEIN SEQUENCE OF 180-201 AND 299-310, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D55654; BAA09513.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U20352; AAC16436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457405; CAG33686.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC016734; AAY14893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001484; AAH01484.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G01650; G01650.
RefSeq NP_005908.1; -.
UniGene Hs.526521
3D structure databases
HSSP P11708; 4MDH. [HSSP ENTRY / PDB]
SMR P40925; 2-334.
ModBase P40925.
Protein-protein interaction databases
IntAct P40925; -.
PTM databases
PhosphoSite P40925; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13034; -.
Reactome REACT_1709; Metabolism of small molecules.
2D gel databases
HSC-2DPAGE P40925; -.
REPRODUCTION-2DPAGE IPI00291005; -.
Organism-specific databases
H-InvDB HIX0002092; -.
HGNC HGNC:6970; MDH1.
GenAtlas MDH1.
MIM 154200; gene. [NCBI / EBI]
PharmGKB PA30714; -.
GeneCards P40925.
Gene expression databases
ArrayExpress P40925; -.
CleanEx HS_MDH1; -.
GermOnline ENSG00000014641; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from ProtInc).
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from experiment from Reactome).
GO:0004470; Molecular function: malic enzyme activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR011274; Malate_DHase_NAD-dep_euk.
IPR010945; Malate_DHase_SF1.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR23382; MDH_SF1; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
ProDom PD003052; Mal_dehydrog; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01759; MalateDH-SF1; 1.
TIGR01758; MDH_euk_cyt; 1.
PROSITE PS00068; MDH; 1.
BLOCKS P40925.
Proteomic databases
PeptideAtlas P40925; -.
Genome annotation databases
Ensembl ENSG00000014641; Homo sapiens. [Contig view]
GeneID 4190; -.
KEGG hsa:4190; -.
Phylogenomic databases
HOGENOM P40925; -.
HOVERGEN P40925; -.
Other
DrugBank DB00157; NADH.
LinkHub P40925; -.
SOURCE MDH1; Homo sapiens.
ProtoNet P40925.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   334  333     Malate dehydrogenase, cytoplasmic. PRO_0000113409
NP_BIND   11    17  7     NAD (By similarity). 
NP_BIND   129   131  3     NAD (By similarity). 
ACT_SITE   187   187        Proton acceptor (By similarity). 
BINDING   92    92        Substrate (By similarity). 
BINDING   98    98        Substrate (By similarity). 
BINDING   105   105        NAD (By similarity). 
BINDING   112   112        NAD (By similarity). 
BINDING   131   131        Substrate (By similarity). 
BINDING   162   162        Substrate. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   210   210        Phosphotyrosine (By similarity). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 36426 Da [This is the MW of the unprocessed precursor] CRC64: 5F7ED9789CA1DB55 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC 

        70         80         90        100        110        120 
ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD LLKANVKIFK SQGAALDKYA 

       130        140        150        160        170        180 
KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTANDVKN 

       190        200        210        220        230        240 
VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL 

       250        260        270        280        290        300 
SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV 

       310        320        330 
EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSA 

P40925 in FASTA format

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