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Protein

Malate dehydrogenase, cytoplasmic

Gene

MDH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.1 Publication
3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH.1 Publication

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 – 1621Substrate
Active sitei187 – 1871Proton acceptorBy similarity

Regions

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

GO - Molecular functioni

  1. diiodophenylpyruvate reductase activity Source: UniProtKB-EC
  2. L-malate dehydrogenase activity Source: Reactome
  3. malic enzyme activity Source: ProtInc
  4. NAD binding Source: Ensembl

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular carbohydrate metabolic process Source: InterPro
  3. gluconeogenesis Source: Reactome
  4. glucose metabolic process Source: Reactome
  5. malate metabolic process Source: InterPro
  6. NADH metabolic process Source: Ensembl
  7. oxaloacetate metabolic process Source: Ensembl
  8. pathogenesis Source: Reactome
  9. small molecule metabolic process Source: Reactome
  10. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS00361-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
SABIO-RKP40925.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
Alternative name(s):
Cytosolic malate dehydrogenase
Diiodophenylpyruvate reductase (EC:1.1.1.96)
Gene namesi
Name:MDH1
Synonyms:MDHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6970. MDH1.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30714.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000113409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei110 – 1101N6-succinyllysineBy similarity
Modified residuei118 – 1181N6-acetyllysine2 Publications
Modified residuei121 – 1211N6-acetyllysine1 Publication
Modified residuei214 – 2141N6-succinyllysineBy similarity
Modified residuei241 – 2411Phosphoserine1 Publication
Modified residuei298 – 2981N6-acetyllysine; alternate2 Publications
Modified residuei298 – 2981N6-succinyllysine; alternateBy similarity
Modified residuei318 – 3181N6-succinyllysineBy similarity
Modified residuei333 – 3331Phosphoserine1 Publication

Post-translational modificationi

ISGylated.1 Publication
Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP40925.
PaxDbiP40925.
PeptideAtlasiP40925.
PRIDEiP40925.

2D gel databases

REPRODUCTION-2DPAGEIPI00291005.
UCD-2DPAGEP40925.

PTM databases

PhosphoSiteiP40925.

Expressioni

Gene expression databases

BgeeiP40925.
CleanExiHS_MDH1.
ExpressionAtlasiP40925. baseline and differential.
GenevestigatoriP40925.

Organism-specific databases

HPAiCAB047333.
HPA027296.
HPA054276.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi110355. 22 interactions.
IntActiP40925. 5 interactions.
MINTiMINT-4999585.
STRINGi9606.ENSP00000233114.

Structurei

3D structure databases

ProteinModelPortaliP40925.
SMRiP40925. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00530000063410.
HOVERGENiHBG006340.
InParanoidiP40925.
KOiK00025.
OMAiFVTTVQQ.
OrthoDBiEOG78H3TM.
PhylomeDBiP40925.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40925-1) [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
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL
60 70 80 90 100
DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD
110 120 130 140 150
LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE
160 170 180 190 200
NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV
210 220 230 240 250
KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI
260 270 280 290 300
CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV
310 320 330
EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSA
Length:334
Mass (Da):36,426
Last modified:January 23, 2007 - v4
Checksum:i5F7ED9789CA1DB55
GO
Isoform 2 (identifier: P40925-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Show »
Length:245
Mass (Da):27,025
Checksum:iDEBC412374575BD9
GO
Isoform 3 (identifier: P40925-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.

Show »
Length:352
Mass (Da):38,628
Checksum:i058B25735B30BBC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Q → R in BAH12223 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 2. 1 PublicationVSP_042661Add
BLAST
Alternative sequencei1 – 11M → MRRCSYFPKDVTVFDKDDK in isoform 3. 1 PublicationVSP_045847

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55654 mRNA. Translation: BAA09513.1.
U20352 mRNA. Translation: AAC16436.1.
CR457405 mRNA. Translation: CAG33686.1.
AK295931 mRNA. Translation: BAH12223.1.
AK300719 mRNA. Translation: BAG62394.1.
AK312331 mRNA. Translation: BAG35252.1.
AC016734 Genomic DNA. Translation: AAY14893.1.
CH471053 Genomic DNA. Translation: EAW99959.1.
BC001484 mRNA. Translation: AAH01484.1.
CCDSiCCDS1874.1. [P40925-1]
CCDS56121.1. [P40925-3]
CCDS56122.1. [P40925-2]
PIRiG01650.
RefSeqiNP_001186040.1. NM_001199111.1. [P40925-3]
NP_001186041.1. NM_001199112.1. [P40925-2]
NP_005908.1. NM_005917.3. [P40925-1]
XP_005264377.1. XM_005264320.1. [P40925-2]
UniGeneiHs.526521.

Genome annotation databases

EnsembliENST00000233114; ENSP00000233114; ENSG00000014641. [P40925-1]
ENST00000539945; ENSP00000438144; ENSG00000014641. [P40925-3]
ENST00000544381; ENSP00000446395; ENSG00000014641. [P40925-2]
GeneIDi4190.
KEGGihsa:4190.
UCSCiuc002scj.2. human. [P40925-1]

Polymorphism databases

DMDMi1708967.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Malate dehydrogenase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55654 mRNA. Translation: BAA09513.1.
U20352 mRNA. Translation: AAC16436.1.
CR457405 mRNA. Translation: CAG33686.1.
AK295931 mRNA. Translation: BAH12223.1.
AK300719 mRNA. Translation: BAG62394.1.
AK312331 mRNA. Translation: BAG35252.1.
AC016734 Genomic DNA. Translation: AAY14893.1.
CH471053 Genomic DNA. Translation: EAW99959.1.
BC001484 mRNA. Translation: AAH01484.1.
CCDSiCCDS1874.1. [P40925-1]
CCDS56121.1. [P40925-3]
CCDS56122.1. [P40925-2]
PIRiG01650.
RefSeqiNP_001186040.1. NM_001199111.1. [P40925-3]
NP_001186041.1. NM_001199112.1. [P40925-2]
NP_005908.1. NM_005917.3. [P40925-1]
XP_005264377.1. XM_005264320.1. [P40925-2]
UniGeneiHs.526521.

3D structure databases

ProteinModelPortaliP40925.
SMRiP40925. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110355. 22 interactions.
IntActiP40925. 5 interactions.
MINTiMINT-4999585.
STRINGi9606.ENSP00000233114.

Chemistry

BindingDBiP40925.
ChEMBLiCHEMBL3560.

PTM databases

PhosphoSiteiP40925.

Polymorphism databases

DMDMi1708967.

2D gel databases

REPRODUCTION-2DPAGEIPI00291005.
UCD-2DPAGEP40925.

Proteomic databases

MaxQBiP40925.
PaxDbiP40925.
PeptideAtlasiP40925.
PRIDEiP40925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233114; ENSP00000233114; ENSG00000014641. [P40925-1]
ENST00000539945; ENSP00000438144; ENSG00000014641. [P40925-3]
ENST00000544381; ENSP00000446395; ENSG00000014641. [P40925-2]
GeneIDi4190.
KEGGihsa:4190.
UCSCiuc002scj.2. human. [P40925-1]

Organism-specific databases

CTDi4190.
GeneCardsiGC02P063727.
HGNCiHGNC:6970. MDH1.
HPAiCAB047333.
HPA027296.
HPA054276.
MIMi154200. gene.
neXtProtiNX_P40925.
PharmGKBiPA30714.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0039.
GeneTreeiENSGT00530000063410.
HOVERGENiHBG006340.
InParanoidiP40925.
KOiK00025.
OMAiFVTTVQQ.
OrthoDBiEOG78H3TM.
PhylomeDBiP40925.
TreeFamiTF105826.

Enzyme and pathway databases

BioCyciMetaCyc:HS00361-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
SABIO-RKP40925.

Miscellaneous databases

ChiTaRSiMDH1. human.
GenomeRNAii4190.
NextBioi16510.
PROiP40925.
SOURCEiSearch...

Gene expression databases

BgeeiP40925.
CleanExiHS_MDH1.
ExpressionAtlasiP40925. baseline and differential.
GenevestigatoriP40925.

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. "Molecular cloning and mapping of a human cDNA for cytosolic malate dehydrogenase (MDH1)."
    Tanaka T., Inazawa J., Nakamura Y.
    Genomics 32:128-130(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  2. Lo A.S.Y., Waye M.M.Y.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) 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 1; 2 AND 3).
    Tissue: Cerebellum and Substantia nigra.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Placenta.
  8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18; 205-213 AND 324-334, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  9. "The human myocardial two-dimensional gel protein database: update 1994."
    Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
    Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 168-181.
    Tissue: Heart.
  10. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 180-201 AND 299-310, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  11. "Biochemical and genetic identity of alpha-keto acid reductase and cytoplasmic malate dehydrogenase from human erythrocytes."
    Friedrich C.A., Ferrell R.E., Siciliano M.J., Kitto G.B.
    Ann. Hum. Genet. 52:25-37(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  12. Cited for: ISGYLATION.
  13. "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 LYS-118 AND LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity."
    Kim E.Y., Kim W.K., Kang H.J., Kim J.H., Chung S.J., Seo Y.S., Park S.G., Lee S.C., Bae K.H.
    J. Lipid Res. 53:1864-1876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-118; LYS-121 AND LYS-298.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMDHC_HUMAN
AccessioniPrimary (citable) accession number: P40925
Secondary accession number(s): B2R5V5
, B4DUN2, B7Z3I7, F5H098, Q6I9V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 158 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.