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Protein

[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial

Gene

Pdp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.By similarity

Catalytic activityi

[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi144 – 1441Magnesium 1By similarity
Metal bindingi144 – 1441Magnesium 2By similarity
Metal bindingi145 – 1451Magnesium 1; via carbonyl oxygenBy similarity
Metal bindingi418 – 4181Magnesium 2By similarity
Metal bindingi516 – 5161Magnesium 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (EC:3.1.3.43)
Short name:
PDP 1
Alternative name(s):
Protein phosphatase 2C
Pyruvate dehydrogenase phosphatase catalytic subunit 1
Short name:
PDPC 1
Gene namesi
Name:Pdp1
Synonyms:Ppm2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2685870. Pdp1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7171MitochondrionBy similarityAdd
BLAST
Chaini72 – 538467[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrialPRO_0000045808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ3UV70.
MaxQBiQ3UV70.
PaxDbiQ3UV70.
PRIDEiQ3UV70.

PTM databases

iPTMnetiQ3UV70.
PhosphoSiteiQ3UV70.

Expressioni

Gene expression databases

BgeeiQ3UV70.
ExpressionAtlasiQ3UV70. baseline and differential.
GenevisibleiQ3UV70. MM.

Interactioni

Subunit structurei

Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092766.

Structurei

3D structure databases

ProteinModelPortaliQ3UV70.
SMRiQ3UV70. Positions 80-538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 525417PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0700. Eukaryota.
COG0631. LUCA.
GeneTreeiENSGT00390000006874.
HOGENOMiHOG000220821.
HOVERGENiHBG008162.
InParanoidiQ3UV70.
KOiK01102.
PhylomeDBiQ3UV70.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 5 hits.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 3 hits.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3UV70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAPTQLFFP LVRNCELSRI YGTACYCHHK HLCCSPPYIP QNRLRYTPHP
60 70 80 90 100
AYATFCRPRE NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE
110 120 130 140 150
FDGKNVSSIL GFDSNQLPAN APIEDRRSAA TCLQTRGMLL GVFDGHAGCA
160 170 180 190 200
CSQAVSERLF YYIAVSLLPH ETLLEIENAV ESGRALLPIL QWHKHPNDYF
210 220 230 240 250
SKEASKLYFN SLRTYWQELI DLNTGESADI DVKEALINAF KRLDNDISLE
260 270 280 290 300
AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
310 320 330 340 350
EDGSWSAVTL SNDHNAQNER ELERLKLEHP KNEAKSVVKQ DRLLGLLMPF
360 370 380 390 400
RAFGDVKFKW SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE
410 420 430 440 450
VTYHRLRPQD KFLVLATDGL WETMHRQDVV RIVGEYLTGM HHQQPIAVGG
460 470 480 490 500
YKVTLGQMHG LLTERRAKMS SVFEDQNAAT HLIRHAVGNN EFGAVDHERL
510 520 530
SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ
Length:538
Mass (Da):61,180
Last modified:October 11, 2005 - v1
Checksum:iA32049DED0FC58EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK137550 mRNA. Translation: BAE23403.1.
CCDSiCCDS38694.1.
RefSeqiNP_001028625.1. NM_001033453.3.
NP_001091700.1. NM_001098230.1.
NP_001091701.1. NM_001098231.1.
NP_001277316.1. NM_001290387.1.
NP_001277320.1. NM_001290391.1.
UniGeneiMm.331489.

Genome annotation databases

EnsembliENSMUST00000056050; ENSMUSP00000050521; ENSMUSG00000049225.
ENSMUST00000108297; ENSMUSP00000103932; ENSMUSG00000049225.
GeneIDi381511.
KEGGimmu:381511.
UCSCiuc008sab.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK137550 mRNA. Translation: BAE23403.1.
CCDSiCCDS38694.1.
RefSeqiNP_001028625.1. NM_001033453.3.
NP_001091700.1. NM_001098230.1.
NP_001091701.1. NM_001098231.1.
NP_001277316.1. NM_001290387.1.
NP_001277320.1. NM_001290391.1.
UniGeneiMm.331489.

3D structure databases

ProteinModelPortaliQ3UV70.
SMRiQ3UV70. Positions 80-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092766.

PTM databases

iPTMnetiQ3UV70.
PhosphoSiteiQ3UV70.

Proteomic databases

EPDiQ3UV70.
MaxQBiQ3UV70.
PaxDbiQ3UV70.
PRIDEiQ3UV70.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056050; ENSMUSP00000050521; ENSMUSG00000049225.
ENSMUST00000108297; ENSMUSP00000103932; ENSMUSG00000049225.
GeneIDi381511.
KEGGimmu:381511.
UCSCiuc008sab.2. mouse.

Organism-specific databases

CTDi54704.
MGIiMGI:2685870. Pdp1.

Phylogenomic databases

eggNOGiKOG0700. Eukaryota.
COG0631. LUCA.
GeneTreeiENSGT00390000006874.
HOGENOMiHOG000220821.
HOVERGENiHBG008162.
InParanoidiQ3UV70.
KOiK01102.
PhylomeDBiQ3UV70.

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

PROiQ3UV70.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UV70.
ExpressionAtlasiQ3UV70. baseline and differential.
GenevisibleiQ3UV70. MM.

Family and domain databases

Gene3Di3.60.40.10. 2 hits.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 5 hits.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 3 hits.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Lung and Testis.

Entry informationi

Entry nameiPDP1_MOUSE
AccessioniPrimary (citable) accession number: Q3UV70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 11, 2005
Last modified: July 6, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.