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UniProtKB/Swiss-Prot entry P48163


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

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Entry information
Entry name MAOX_HUMAN
Primary accession number P48163
Secondary accession numbers Q16797 Q16855 Q53F72 Q5VWA2 Q9BWX8 Q9H1W3 Q9UIY4
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 84)
Name and origin of the protein
Protein name NADP-dependent malic enzyme
Synonyms NADP-ME
EC 1.1.1.40
Malic enzyme 1
Gene name
Name: ME1
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=White adipose tissue;
DOI=10.1016/0014-5793(94)00386-6; PubMed=8187880 [NCBI, ExPASy, EBI, Israel, Japan]
Loeber G., Dworkin M.B., Infante A., Ahorn H.;
"Characterization of cytosolic malic enzyme in human tumor cells.";
FEBS Lett. 344:181-186(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
DOI=10.1016/0378-1119(95)00004-P; PubMed=7622060 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez-Manchon C., Ferrer M., Ayuso M.S., Parrilla R.;
"Cloning, sequencing and functional expression of a cDNA encoding a NADP-dependent malic enzyme from human liver.";
Gene 159:255-260(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-572.
DOI=10.1007/BF01887116; PubMed=8804575 [NCBI, ExPASy, EBI, Israel, Japan]
Chou W.Y., Huang S.M., Chang G.G.;
"Nonidentity of the cDNA sequence of human breast cancer cell malic enzyme to that from the normal human cell.";
J. Protein Chem. 15:273-279(1996).
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
X77244; CAA54460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L34035; AAB01380.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223417; BAD97137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391416; CAH73129.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049699; CAH73129.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136970; CAH73129.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049699; CAI22634.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136970; CAI22634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391416; CAI22634.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136970; CAC19505.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049699; CAC19505.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391416; CAC19505.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025246; AAH25246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43944; AAC50613.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4160; JC4160.
S44415; S44415.
RefSeq NP_002386.1; -.
UniGene Hs.21160
3D structure databases
PDB
2AW5; X-ray; 2.50 A; A/B/C=15-555.[ExPASy / RCSB / EBI]
PDBsum 2AW5; -.
ModBase P48163.
PTM databases
PhosphoSite P48163; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00008215; -.
Organism-specific databases
GeneCards GC06M083977; -.
H-InvDB HIX0019232; -.
HGNC HGNC:6983; ME1.
GenAtlas ME1.
HPA HPA006493; -.
MIM 154250; gene. [NCBI / EBI]
PharmGKB PA134904115; -.
GeneCards P48163.
Gene expression databases
ArrayExpress P48163; -.
CleanEx HS_ME1; -.
GermOnline ENSG00000065833; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0043531; Molecular function: ADP binding (traceable author statement from UniProtKB).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0004473; Molecular function: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity (inferred from direct assay from UniProtKB).
GO:0030145; Molecular function: manganese ion binding (inferred from direct assay from UniProtKB).
GO:0051287; Molecular function: NAD binding (traceable author statement from UniProtKB).
GO:0050661; Molecular function: NADP binding (traceable author statement from UniProtKB).
GO:0005975; Biological process: carbohydrate metabolic process (non-traceable author statement from ProtInc).
GO:0006108; Biological process: malate metabolic process (inferred from direct assay from UniProtKB).
GO:0006741; Biological process: NADP biosynthetic process (traceable author statement from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009743; Biological process: response to carbohydrate stimulus (traceable author statement from UniProtKB).
GO:0009725; Biological process: response to hormone stimulus (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR015884; Malic_enzyme_CS.
IPR012301; Malic_N.
IPR012302; Malic_NAD_bd.
IPR001891; Malic_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00390; malic; 1.
PF03949; Malic_M; 1.
Pfam graphical view of domain structure.
PRINTS PR00072; MALOXRDTASE.
PROSITE PS00331; MALIC_ENZYMES; 1.
Proteomic databases
PeptideAtlas P48163; -.
Proteomics databases
PRIDE P48163; -.
Genome annotation databases
Ensembl ENSG00000065833; Homo sapiens. [Contig view]
GeneID 4199; -.
KEGG hsa:4199; -.
Phylogenomic databases
HOVERGEN P48163; -.
Other
DrugBank DB00157; NADH.
NextBio 16550; -.
SOURCE ME1; Homo sapiens.
ProtoNet P48163.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Metal-binding; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   572  572     NADP-dependent malic enzyme. PRO_0000160192
NP_BIND   301   318  18     NADP (By similarity). 
ACT_SITE   102   102        Proton donor (By similarity). 
ACT_SITE   173   173        Proton acceptor (By similarity). 
METAL   245   245        Divalent metal cation (By similarity). 
METAL   246   246        Divalent metal cation (By similarity). 
METAL   269   269        Divalent metal cation (By similarity). 
BINDING   155   155        NADP (By similarity). 
BINDING   269   269        NADP (By similarity). 
BINDING   408   408        NADP (By similarity). 
SITE   269   269  1     Important for activity (By similarity). 
CONFLICT   266   266        F -> S (in Ref. 3; BAD97137). 
CONFLICT   438   438        P -> S (in Ref. 6; AAC50613). 
CONFLICT   443   448        NGQTLY -> DGRTLF (in Ref. 2; AAB01380). 
CONFLICT   472   477        QITDNI -> HIDDKV (in Ref. 2; AAB01380). 
CONFLICT   486   486        A -> S (in Ref. 2; AAB01380). 
CONFLICT   495   495        E -> Q (in Ref. 2; AAB01380). 
CONFLICT   515   515        E -> V (in Ref. 2; AAB01380). 
CONFLICT   519   519        K -> Q (in Ref. 2; AAB01380). 
CONFLICT   523   523        Q -> K (in Ref. 2; AAB01380). 
CONFLICT   526   526        T -> M (in Ref. 2; AAB01380). 
CONFLICT   538   538        A -> E (in Ref. 2; AAB01380). 
CONFLICT   541   541        R -> S (in Ref. 2; AAB01380). 
CONFLICT   548   548        D -> N (in Ref. 2; AAB01380). 
CONFLICT   558   558        S -> P (in Ref. 2; AAB01380). 
CONFLICT   561   561        E -> A (in Ref. 2; AAB01380). 
CONFLICT   571   571        D -> N (in Ref. 2; AAB01380). 
HELIX   16    20  5      
TURN   22    24  3      
HELIX   27    29  3      
HELIX   32    37  6      
TURN   41    43  3      
HELIX   51    64  14      
HELIX   68    81  14      
HELIX   83    91  9      
TURN   95    97  3      
HELIX   98   101  4      
HELIX   105   111  7      
HELIX   113   116  4      
STRAND   122   126  5      
HELIX   127   129  3      
HELIX   133   137  5      
STRAND   147   151  5      
TURN   157   159  3      
HELIX   163   167  5      
HELIX   168   181  14      
HELIX   185   187  3      
STRAND   188   194  7      
HELIX   200   204  5      
HELIX   218   236  19      
STRAND   241   244  4      
HELIX   249   259  11      
TURN   260   262  3      
STRAND   263   267  5      
TURN   268   270  3      
HELIX   271   288  18      
HELIX   292   294  3      
STRAND   297   301  5      
HELIX   304   320  17      
HELIX   324   328  5      
STRAND   331   335  5      
HELIX   351   354  4      
HELIX   364   371  8      
STRAND   374   378  5      
HELIX   388   397  10      
STRAND   402   405  4      
HELIX   410   412  3      
HELIX   417   423  7      
TURN   424   426  3      
STRAND   429   434  6      
HELIX   454   456  3      
HELIX   458   468  11      
HELIX   475   487  13      
HELIX   491   495  5      
HELIX   503   505  3      
HELIX   506   523  18      
HELIX   536   542  7      
Sequence information
Length: 572 AA [This is the length of the unprocessed precursor] Molecular weight: 64150 Da [This is the MW of the unprocessed precursor] CRC64: EA4C8CB36F6C619C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEPEAPRRRH THQRGYLLTR NPHLNKDLAF TLEERQQLNI HGLLPPSFNS QEIQVLRVVK 

        70         80         90        100        110        120 
NFEHLNSDFD RYLLLMDLQD RNEKLFYRVL TSDIEKFMPI VYTPTVGLAC QQYSLVFRKP 

       130        140        150        160        170        180 
RGLFITIHDR GHIASVLNAW PEDVIKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC 

       190        200        210        220        230        240 
GGMNPQECLP VILDVGTENE ELLKDPLYIG LRQRRVRGSE YDDFLDEFME AVSSKYGMNC 

       250        260        270        280        290        300 
LIQFEDFANV NAFRLLNKYR NQYCTFNDDI QGTASVAVAG LLAALRITKN KLSDQTILFQ 

       310        320        330        340        350        360 
GAGEAALGIA HLIVMALEKE GLPKEKAIKK IWLVDSKGLI VKGRASLTQE KEKFAHEHEE 

       370        380        390        400        410        420 
MKNLEAIVQE IKPTALIGVA AIGGAFSEQI LKDMAAFNER PIIFALSNPT SKAECSAEQC 

       430        440        450        460        470        480 
YKITKGRAIF ASGSPFDPVT LPNGQTLYPG QGNNSYVFPG VALGVVACGL RQITDNIFLT 

       490        500        510        520        530        540 
TAEVIAQQVS DKHLEEGRLY PPLNTIRDVS LKIAEKIVKD AYQEKTATVY PEPQNKEAFV 

       550        560        570 
RSQMYSTDYD QILPDCYSWP EEVQKIQTKV DQ 

P48163 in FASTA format

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