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Q9P2J9 (PDP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence caution

The sequence BAA92586.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6666Mitochondrion Potential
Chain67 – 529463[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial
PRO_0000025421

Sites

Metal binding1411Manganese 1 By similarity
Metal binding1411Manganese 2 By similarity
Metal binding1421Manganese 1; via carbonyl oxygen By similarity
Metal binding4121Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P2J9 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 252CAEBCDAF61A5C

FASTA52959,978
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[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. expand/collapse author list , 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: Testis.
[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. expand/collapse author list , 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: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB037769 mRNA. Translation: BAA92586.1. Different initiation.
AK292539 mRNA. Translation: BAF85228.1.
CH471092 Genomic DNA. Translation: EAW83048.1.
BC028030 mRNA. Translation: AAH28030.1.
RefSeqNP_065837.1. NM_020786.2.
XP_005256121.1. XM_005256064.2.
XP_005256122.1. XM_005256065.2.
XP_005256123.1. XM_005256066.2.
XP_005256124.1. XM_005256067.2.
XP_005256125.1. XM_005256068.2.
UniGeneHs.632214.

3D structure databases

ProteinModelPortalQ9P2J9.
SMRQ9P2J9. Positions 79-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121604. 2 interactions.
STRING9606.ENSP00000309548.

PTM databases

PhosphoSiteQ9P2J9.

Polymorphism databases

DMDM12585321.

Proteomic databases

PaxDbQ9P2J9.
PRIDEQ9P2J9.

Protocols and materials databases

DNASU57546.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311765; ENSP00000309548; ENSG00000172840.
GeneID57546.
KEGGhsa:57546.
UCSCuc002eqk.2. human.

Organism-specific databases

CTD57546.
GeneCardsGC16P066914.
HGNCHGNC:30263. PDP2.
HPAHPA019950.
MIM615499. gene.
neXtProtNX_Q9P2J9.
PharmGKBPA165450460.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000220821.
HOVERGENHBG008162.
InParanoidQ9P2J9.
KOK01102.
OMAKPEVTYH.
PhylomeDBQ9P2J9.
TreeFamTF313505.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9P2J9.
BgeeQ9P2J9.
GenevestigatorQ9P2J9.

Family and domain databases

Gene3D3.60.40.10. 2 hits.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 3 hits.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi57546.
NextBio64003.
PROQ9P2J9.
SOURCESearch...

Entry information

Entry namePDP2_HUMAN
AccessionPrimary (citable) accession number: Q9P2J9
Secondary accession number(s): A8K924
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM