Reviewed, UniProtKB/Swiss-Prot Q9P0J1 (PDP1_HUMAN)

Names and origin

Protein names

Recommended name:
    [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
      Short name=PDP 1
    EC=3.1.3.43
Alternative name(s):
    Pyruvate dehydrogenase phosphatase, catalytic subunit 1
      Short name=PDPC 1
    Protein phosphatase 2C

Gene names

Name:	PDP1
Synonyms:	PDP, PPM2C

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex By similarity.
Catalytic activity	[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Subunit structure	Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Involvement in disease	Defects in PDP1 are the cause of pyruvate dehydrogenase phosphatase deficiency (PDP deficiency) [MIM:608782]. PDP deficiency results in lactic acidosis leading to neurological dysfunction.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Ligand	Calcium Magnesium Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell protein serine/threonine phosphatase complex Inferred from electronic annotation. Source: InterPro
Molecular function	[pyruvate dehydrogenase (lipoamide)] phosphatase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 71	71	Mitochondrion By similarity
	Chain	72 – 537	466	[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial		PRO_0000025419
Sites
	Metal binding	144	1	Magnesium 1 By similarity
	Metal binding	144	1	Magnesium 2 By similarity
	Metal binding	145	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	418	1	Magnesium 2 By similarity
Natural variations
	Natural variant	284	1	Missing in PDP deficiency; low activity.		VAR_029882
Experimental info
	Sequence conflict	105 – 116	12	NVSSI…FDSNQ → MSVLSLDLTAIK in AAF67480. Ref.1
	Sequence conflict	151	1	C → W in AAF67480. Ref.1
	Sequence conflict	165	1	V → G in AAF67480. Ref.1
	Sequence conflict	168	1	L → V in AAF67480. Ref.1
	Sequence conflict	537	1	E → EK in AAF67480. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9P0J1-1 [UniParc]. Last modified October 25, 2005. Version 3. Checksum: 818B0064CA7961A0	FASTA	537	61,054
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." 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. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	"Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation." Maj M.C., MacKay N., Levandovskiy V., Addis J., Baumgartner E.R., Baumgartner M.R., Robinson B.H., Cameron J.M. J. Clin. Endocrinol. Metab. 90:4101-4107(2005) [PubMed: 15855260] [Abstract] Cited for: VARIANT PDP DEFICIENCY LEU-284 DEL, CHARACTERIZATION OF VARIANT PDP DEFICIENCY LEU-284 DEL.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF155661 mRNA. Translation: AAF67480.1. Different initiation. BC047619 mRNA. Translation: AAH47619.1. BC098343 mRNA. Translation: AAH98343.1.
IPI	IPI00218971.
RefSeq	NP_060914.2.
UniGene	Hs.22265
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q9P0J1.
Proteomic databases
PRIDE	Q9P0J1.
Genome annotation databases
Ensembl	ENSG00000164951. Homo sapiens. [Contig view]
GeneID	54704.
KEGG	hsa:54704.
Organism-specific databases
GeneCards	GC08P094998.
H-InvDB	HIX0007649.
HGNC	HGNC:9279. PPM2C.
HPA	HPA018483. HPA019081.
MIM	605993. gene. 608782. phenotype.
PharmGKB	PA33607.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9P0J1.
Enzyme and pathway databases
BRENDA	3.1.3.43. 247.
Reactome	REACT_1505. Integration of energy metabolism.
Gene expression databases
ArrayExpress	Q9P0J1.
Bgee	Q9P0J1.
CleanEx	HS_PPM2C.
GermOnline	ENSG00000164951. Homo sapiens.
Family and domain databases
InterPro	IPR015655. PP2C. IPR001932. PP2C-related. IPR000222. PP2C_Mn2_Asp60_BS. IPR014045. PP2C_N. [Graphical view]
Gene3D	G3DSA:3.60.40.10. PP2C-related. 1 hit.
PANTHER	PTHR13832. PP2C. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	57261.
SOURCE	Search...

Entry information

Entry name

PDP1_HUMAN

Accession

Primary (citable) accession number: Q9P0J1
Secondary accession number(s): Q5U5K1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	October 25, 2005
Last modified:	June 16, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)