Q9P0J1 (PDP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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):
Protein phosphatase 2C
Pyruvate dehydrogenase phosphatase catalytic subunit 1
Short name=PDPC 1

Gene names

Name:	PDP1
Synonyms:	PDP, PPM2C

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	Pyruvate dehydrogenase phosphatase deficiency (PDP deficiency) [MIM:608782]: Results in lactic acidosis leading to neurological dysfunction. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the PP2C family.
Sequence caution	The sequence AAF67480.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Ligand	Calcium Magnesium Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-threonine dephosphorylation Inferred from direct assay PubMed 20801214. Source: UniProtKB pyruvate metabolic process Traceable author statement. Source: Reactome regulation of acetyl-CoA biosynthetic process from pyruvate Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	[pyruvate dehydrogenase (lipoamide)] phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 20801214. Source: UniProtKB
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
	Metal binding	516	1	Magnesium 1 By similarity
Amino acid modifications
	Modified residue	202	1	N6-acetyllysine Ref.5
Natural variations
	Natural variant	284	1	Missing in PDP deficiency; low activity. Ref.6		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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adrenal gland.
[2]	"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]. Tissue: Amygdala.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Testis.
[5]	"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-202, MASS SPECTROMETRY.
[6]	"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] [Europe PMC] [Abstract] Cited for: VARIANT PDP DEFICIENCY LEU-284 DEL, CHARACTERIZATION OF VARIANT PDP DEFICIENCY LEU-284 DEL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF155661 mRNA. Translation: AAF67480.1. Different initiation. AK126862 mRNA. Translation: BAG54383.1. CH471060 Genomic DNA. Translation: EAW91704.1. BC047619 mRNA. Translation: AAH47619.1. BC098343 mRNA. Translation: AAH98343.1.
IPI	IPI00218971.
RefSeq	NP_001155251.1. NM_001161779.1. NP_001155252.1. NM_001161780.1. NP_001155253.1. NM_001161781.1. NP_060914.2. NM_018444.3.
UniGene	Hs.22265.
3D structure databases
ProteinModelPortal	Q9P0J1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P0J1. 1 interaction.
STRING	9606.ENSP00000297598.
PTM databases
PhosphoSite	Q9P0J1.
Polymorphism databases
DMDM	78099789.
Proteomic databases
PaxDb	Q9P0J1.
PRIDE	Q9P0J1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297598; ENSP00000297598; ENSG00000164951. ENST00000517764; ENSP00000430380; ENSG00000164951. ENST00000520728; ENSP00000428317; ENSG00000164951.
GeneID	54704.
KEGG	hsa:54704.
UCSC	uc003yge.3. human.
Organism-specific databases
CTD	54704.
GeneCards	GC08P094870.
HGNC	HGNC:9279. PDP1.
HPA	HPA018483. HPA019081. HPA021152.
MIM	605993. gene. 608782. phenotype.
neXtProt	NX_Q9P0J1.
Orphanet	79246. Pyruvate dehydrogenase phosphatase deficiency.
PharmGKB	PA33607.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000220821.
HOVERGEN	HBG008162.
InParanoid	Q9P0J1.
KO	K01102.
OrthoDB	EOG4XD3QP.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9P0J1.
Bgee	Q9P0J1.
CleanEx	HS_PPM2C.
Genevestigator	Q9P0J1.
GermOnline	ENSG00000164951. Homo sapiens.
Family and domain databases
Gene3D	3.60.40.10. 2 hits.
InterPro	IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PDP1. human.
GenomeRNAi	54704.
NextBio	57261.
SOURCE	Search...

Entry information

Entry name

PDP1_HUMAN

Accession

Primary (citable) accession number: Q9P0J1
Secondary accession number(s): B3KX71, Q5U5K1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.