Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9P0J1 (PDP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P0J1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9P0J1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCVCPGPRRIGIPVRSSSLPLFSDAM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7171Mitochondrion By similarity
Chain72 – 537466[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
PRO_0000025419

Sites

Metal binding1441Magnesium 1 By similarity
Metal binding1441Magnesium 2 By similarity
Metal binding1451Magnesium 1; via carbonyl oxygen By similarity
Metal binding4181Magnesium 2 By similarity
Metal binding5161Magnesium 1 By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine Ref.6

Natural variations

Alternative sequence11M → MCVCPGPRRIGIPVRSSSLP LFSDAM in isoform 2.
VSP_046869
Natural variant2841Missing in PDP deficiency; low activity. Ref.7
VAR_029882

Experimental info

Sequence conflict105 – 11612NVSSI…FDSNQ → MSVLSLDLTAIK in AAF67480. Ref.1
Sequence conflict1511C → W in AAF67480. Ref.1
Sequence conflict1651V → G in AAF67480. Ref.1
Sequence conflict1681L → V in AAF67480. Ref.1
Sequence conflict5371E → EK in AAF67480. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2005. Version 3.
Checksum: 818B0064CA7961A0

FASTA53761,054
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2A29F37D7121A093
Show »

FASTA56263,695

References

« Hide '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. expand/collapse author list , 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] (ISOFORM 1).
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. 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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-101 (ISOFORM 2).
Tissue: Amygdala and Fetal brain.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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] (ISOFORM 1).
Tissue: Testis.
[6]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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.
DA769567 mRNA. No translation available.
AC084346 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91704.1.
BC047619 mRNA. Translation: AAH47619.1.
BC098343 mRNA. Translation: AAH98343.1.
CCDSCCDS55262.1. [Q9P0J1-2]
CCDS6259.1. [Q9P0J1-1]
RefSeqNP_001155251.1. NM_001161779.1. [Q9P0J1-2]
NP_001155252.1. NM_001161780.1. [Q9P0J1-2]
NP_001155253.1. NM_001161781.1. [Q9P0J1-1]
NP_060914.2. NM_018444.3. [Q9P0J1-1]
UniGeneHs.22265.

3D structure databases

ProteinModelPortalQ9P0J1.
SMRQ9P0J1. Positions 80-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120103. 2 interactions.
IntActQ9P0J1. 2 interactions.
MINTMINT-4831562.
STRING9606.ENSP00000297598.

PTM databases

PhosphoSiteQ9P0J1.

Polymorphism databases

DMDM78099789.

Proteomic databases

MaxQBQ9P0J1.
PaxDbQ9P0J1.
PRIDEQ9P0J1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297598; ENSP00000297598; ENSG00000164951. [Q9P0J1-1]
ENST00000396200; ENSP00000379503; ENSG00000164951. [Q9P0J1-2]
ENST00000517764; ENSP00000430380; ENSG00000164951. [Q9P0J1-1]
ENST00000520728; ENSP00000428317; ENSG00000164951. [Q9P0J1-1]
GeneID54704.
KEGGhsa:54704.
UCSCuc003yge.3. human. [Q9P0J1-1]

Organism-specific databases

CTD54704.
GeneCardsGC08P094870.
HGNCHGNC:9279. PDP1.
HPAHPA018483.
HPA019081.
HPA021152.
MIM605993. gene.
608782. phenotype.
neXtProtNX_Q9P0J1.
Orphanet79246. Pyruvate dehydrogenase phosphatase deficiency.
PharmGKBPA33607.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000220821.
HOVERGENHBG008162.
InParanoidQ9P0J1.
KOK01102.
OMAHNAQNER.
OrthoDBEOG7KQ219.
PhylomeDBQ9P0J1.
TreeFamTF313505.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9P0J1.
BgeeQ9P0J1.
CleanExHS_PPM2C.
GenevestigatorQ9P0J1.

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

ChiTaRSPDP1. human.
GeneWikiPyruvate_dehydrogenase_phosphatase.
GenomeRNAi54704.
NextBio35535205.
PROQ9P0J1.
SOURCESearch...

Entry information

Entry namePDP1_HUMAN
AccessionPrimary (citable) accession number: Q9P0J1
Secondary accession number(s): B3KX71, J3KPU0, Q5U5K1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 25, 2005
Last modified: July 9, 2014
This is version 127 of the entry and version 3 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 entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM