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UniProtKB/Swiss-Prot entry Q9P2J9

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

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Entry information

Entry name

PDP2_HUMAN

Primary accession number

Q9P2J9

Secondary accession numbers

None

Integrated into Swiss-Prot on

January 24, 2001

Sequence was last modified on

January 24, 2001 (Sequence version 2)

Annotations were last modified on

November 25, 2008 (Entry version 70)

Name and origin of the protein

Protein name

[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial [Precursor]

Synonyms

PDP 2
EC 3.1.3.43
Pyruvate dehydrogenase phosphatase, catalytic subunit 2
PDPC 2

Gene name

	Name:	PDP2
	Synonyms:	KIAA1348

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

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

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1093/dnares/7.1.65; PubMed=10718198 [NCBI, ExPASy, EBI, Israel, Japan] Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; "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."; DNA Res. 7:65-73(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; 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).

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: Heterodimer of a catalytic subunit and a FAD protein of unknown function (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
SIMILARITY: Belongs to the PP2C family.

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

AB037769; BAA92586.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC028030; AAH28030.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_065837.1; -.

UniGene

Hs.654693

3D structure databases

ModBase

Q9P2J9.

PTM databases

PhosphoSite

Q9P2J9; -.

Organism-specific databases

Gene expression databases

ArrayExpress

Q9P2J9; -.

GermOnline

ENSG00000172840; Homo sapiens.

Ontologies

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:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese 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

Q9P2J9.

Genome annotation databases

Ensembl

ENSG00000172840; Homo sapiens. [Contig view]

GeneID

57546; -.

KEGG

hsa:57546; -.

Phylogenomic databases

HOGENOM

Q9P2J9; -.

HOVERGEN

Q9P2J9; -.

Other

NextBio

64003; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion; Protein phosphatase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 66`	`66`	`Mitochondrion (Potential).`
`CHAIN`	`67 529`	`463`	`[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial.`	`PRO_0000025421`
`METAL`	`141 141`		`Manganese 1 (By similarity).`
`METAL`	`141 141`		`Manganese 2 (By similarity).`
`METAL`	`142 142`		`Manganese 1; via carbonyl oxygen (By similarity).`
`METAL`	`412 412`		`Manganese 2 (By similarity).`

Sequence information

Length: 529 AA [This is the length of the unprocessed precursor]

Molecular weight: 59978 Da [This is the MW of the unprocessed precursor]

CRC64: 252CAEBCDAF61A5C [This is a checksum on the sequence]

        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

Q9P2J9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools