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UniProtKB/Swiss-Prot entry Q9P0J1

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

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Entry information
Entry name PDP1_HUMAN
Primary accession number Q9P0J1
Secondary accession number Q5U5K1
Integrated into Swiss-Prot on January 24, 2001
Sequence was last modified on October 25, 2005 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 68)
Name and origin of the protein
Protein name [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial [Precursor]
Synonyms PDP 1
EC 3.1.3.43
Pyruvate dehydrogenase phosphatase, catalytic subunit 1
PDPC 1
Protein phosphatase 2C
Gene name
Name: PDP1
Synonyms: PDP, PPM2C
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 [LARGE SCALE MRNA].
TISSUE=Adrenal gland;
DOI=10.1073/pnas.160270997; PubMed=10931946 [NCBI, ExPASy, EBI, Israel, Japan]
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[3]
 VARIANT PDP DEFICIENCY LEU-284 DEL, AND CHARACTERIZATION OF VARIANT PDP DEFICIENCY LEU-284 DEL.
DOI=10.1210/jc.2005-0123; PubMed=15855260 [NCBI, ExPASy, EBI, Israel, Japan]
Maj M.C., MacKay N., Levandovskiy V., Addis J., Baumgartner E.R., Baumgartner M.R., Robinson B.H., Cameron J.M.;
"Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation.";
J. Clin. Endocrinol. Metab. 90:4101-4107(2005).
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
AF155661; AAF67480.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047619; AAH47619.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC098343; AAH98343.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060914.2; -.
UniGene Hs.22265
3D structure databases
ModBase Q9P0J1.
PTM databases
PhosphoSite Q9P0J1; -.
Organism-specific databases
H-InvDB HIX0007649; -.
HGNC HGNC:9279; PPM2C.
GenAtlas PDP1.
HPA HPA018483; -.
HPA019081; -.
MIM 605993; gene. [NCBI / EBI]
608782; phenotype. [NCBI / EBI]
PharmGKB PA33607; -.
GeneCards Q9P0J1.
Gene expression databases
ArrayExpress Q9P0J1; -.
CleanEx HS_PPM2C; -.
GermOnline ENSG00000164951; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008287; Cellular component: protein serine/threonine phosphatase complex (inferred from electronic annotation from InterPro).
GO:0004741; Molecular function: [pyruvate dehydrogenase (lipoamide)] phosphatase activity (inferred from electronic annotation from EC).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004722; Molecular function: protein serine/threonine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0006470; Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR015655; PP2C.
IPR001932; PP2C-related.
IPR000222; PP2C_Mn2_Asp60_BS.
IPR014045; PP2C_N.
Graphical view of domain structure.
Gene3D G3DSA:3.60.40.10; PP2C-related; 1.
PANTHER PTHR13832; PP2C; 1.
Pfam PF00481; PP2C; 1.
Pfam graphical view of domain structure.
SMART SM00331; PP2C_SIG; 1.
SM00332; PP2Cc; 1.
SMART graphical view of domain structure.
PROSITE PS01032; PP2C; 1.
ProtoNet Q9P0J1.
Genome annotation databases
Ensembl ENSG00000164951; Homo sapiens. [Contig view]
GeneID 54704; -.
KEGG hsa:54704; -.
Phylogenomic databases
HOVERGEN Q9P0J1; -.
Other
NextBio 57261; -.
SOURCE PDP1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Disease mutation; Hydrolase; Magnesium; Metal-binding; Mitochondrion; Protein phosphatase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    71  71     Mitochondrion (By similarity). 
CHAIN   72   537  466     [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial. PRO_0000025419
METAL   144   144        Magnesium 1 (By similarity). 
METAL   144   144        Magnesium 2 (By similarity). 
METAL   145   145        Magnesium 1; via carbonyl oxygen (By similarity). 
METAL   418   418        Magnesium 2 (By similarity). 
VARIANT   284   284  1     Missing (in PDP deficiency; low activity). VAR_029882
CONFLICT   105   116        NVSSILGFDSNQ -> MSVLSLDLTAIK (in Ref. 1; AAF67480). 
CONFLICT   151   151        C -> W (in Ref. 1; AAF67480). 
CONFLICT   165   165        V -> G (in Ref. 1; AAF67480). 
CONFLICT   168   168        L -> V (in Ref. 1; AAF67480). 
CONFLICT   537   537        E -> EK (in Ref. 1; AAF67480). 
Sequence information
Length: 537 AA [This is the length of the unprocessed precursor] Molecular weight: 61054 Da [This is the MW of the unprocessed precursor] CRC64: 818B0064CA7961A0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSSSYIP QSRLRYTPHP AYATFCRPKE 

        70         80         90        100        110        120 
NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNQLPAN 

       130        140        150        160        170        180 
APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV 

       190        200        210        220        230        240 
ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF 

       250        260        270        280        290        300 
KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE 

       310        320        330        340        350        360 
EDGSWSAVTL SNDHNAQNER ELERLKLEHP KSEAKSVVKQ DRLLGLLMPF RAFGDVKFKW 

       370        380        390        400        410        420 
SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL 

       430        440        450        460        470        480 
WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRTKMS SVFEDQNAAT 

       490        500        510        520        530 
HLIRHAVGNN EFGTVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQE
Q9P0J1 in FASTA format

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