Reviewed, UniProtKB/Swiss-Prot Q9P2J9 (PDP2_HUMAN)

Names and origin

Protein names

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

Gene names

Name:	PDP2
Synonyms:	KIAA1348

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	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 subunit and a FAD protein of unknown function By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese 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 magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese 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 – 66	66	Mitochondrion Potential
	Chain	67 – 529	463	[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial		PRO_0000025421
Sites
	Metal binding	141	1	Manganese 1 By similarity
	Metal binding	141	1	Manganese 2 By similarity
	Metal binding	142	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	412	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9P2J9-1 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 252CAEBCDAF61A5C	FASTA	529	59,978
	10 20 30 40 50 60 MSSTVSYWIL NSTRNSIATL QGGRRLYSRY VSNRNKLKWR LFSRVPPTLN SSPCGGFTLC 70 80 90 100 110 120 KAYRHTSTEE DDFHLQLSPE QINEVLRAGE TTHKILDLES RVPNSVLRFE SNQLAANSPV 130 140 150 160 170 180 EDRRGVASCL QTNGLMFGIF DGHGGHACAQ AVSERLFYYV AVSLMSHQTL EHMEGAMESM 190 200 210 220 230 240 KPLLPILHWL KHPGDSIYKD VTSVHLDHLR VYWQELLDLH MEMGLSIEEA LMYSFQRLDS 250 260 270 280 290 300 DISLEIQAPL EDEVTRNLSL QVAFSGATAC MAHVDGIHLH VANAGDCRAI LGVQEDNGMW 310 320 330 340 350 360 SCLPLTRDHN AWNQAELSRL KREHPESEDR TIIMEDRLLG VLIPCRAFGD VQLKWSKELQ 370 380 390 400 410 420 RSILERGFNT EALNIYQFTP PHYYTPPYLT AEPEVTYHRL RPQDKFLVLA SDGLWDMLSN 430 440 450 460 470 480 EDVVRLVVGH LAEADWHKTD LAQRPANLGL MQSLLLQRKA SGLHEADQNA ATRLIRHAIG 490 500 510 520 NNEYGEMEAE RLAAMLTLPE DLARMYRDDI TVTVVYFNSE SIGAYYKGG

References

[1]	"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed: 10718198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[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: Brain.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB037769 mRNA. Translation: BAA92586.1. Different initiation. BC028030 mRNA. Translation: AAH28030.1.
IPI	IPI00002251.
RefSeq	NP_065837.1.
UniGene	Hs.654693
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9P2J9.
Genome annotation databases
Ensembl	ENSG00000172840. Homo sapiens. [Contig view]
GeneID	57546.
KEGG	hsa:57546.
Organism-specific databases
GeneCards	GC16P065471.
HUGE	Search...
Phylogenomic databases
HOGENOM	Q9P2J9.
HOVERGEN	Q9P2J9.
OMA	Q9P2J9. LRVYWQE.
Enzyme and pathway databases
BRENDA	3.1.3.43. 247.
Reactome	REACT_1505. Integration of energy metabolism.
Gene expression databases
ArrayExpress	Q9P2J9.
Bgee	Q9P2J9.
GermOnline	ENSG00000172840. 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	64003.

Entry information

Entry name

PDP2_HUMAN

Accession

Primary (citable) accession number: Q9P2J9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 24, 2001
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)