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Q8BKZ9

- ODPX_MOUSE

UniProt

Q8BKZ9 - ODPX_MOUSE

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Protein
Pyruvate dehydrogenase protein X component, mitochondrial
Gene
Pdhx
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex By similarity.

GO - Molecular functioni

  1. transferase activity, transferring acyl groups Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase protein X component, mitochondrial
Alternative name(s):
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
Lipoyl-containing pyruvate dehydrogenase complex component X
Gene namesi
Name:Pdhx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1351627. Pdhx.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Mitochondrion By similarity
Add
BLAST
Chaini54 – 501448Pyruvate dehydrogenase protein X component, mitochondrial
PRO_0000020485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-lipoyllysine By similarity
Modified residuei194 – 1941N6-acetyllysine By similarity
Modified residuei394 – 3941N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BKZ9.
PaxDbiQ8BKZ9.
PRIDEiQ8BKZ9.

2D gel databases

REPRODUCTION-2DPAGEIPI00222767.

PTM databases

PhosphoSiteiQ8BKZ9.

Expressioni

Gene expression databases

BgeeiQ8BKZ9.
CleanExiMM_PDHX.
GenevestigatoriQ8BKZ9.

Interactioni

Subunit structurei

Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) By similarity.

Protein-protein interaction databases

IntActiQ8BKZ9. 2 interactions.
MINTiMINT-1867323.
STRINGi10090.ENSMUSP00000011058.

Structurei

3D structure databases

ProteinModelPortaliQ8BKZ9.
SMRiQ8BKZ9. Positions 57-144, 183-224, 266-500.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 13175Lipoyl-binding
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 21432Interaction with DLD By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi150 – 17122Pro-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00740000115591.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiQ8BKZ9.
KOiK13997.
OMAiSWRLGCD.
OrthoDBiEOG7K3TKW.
PhylomeDBiQ8BKZ9.
TreeFamiTF332256.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BKZ9-1 [UniParc]FASTAAdd to Basket

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MAASWRLHCN QPLLRYLLGF SSRRSLGLAQ GAAAWPVDRG ASWRWFHSTQ    50
LLQADPIKVL MPSLSPTMEQ GNIVKWLRKE GEAVSAGDSL CEIETDKAVV 100
TLDANDDGIL AKIVVEEGAK NIQLGSLIAL MVEEGEDWKQ VEIPKDVSAP 150
PPVSKPPAPT QPSPQPQIPC PARKEHKGTA RFRLSPAARN ILEKHSLDAS 200
QGTATGPRGI FTKEDALKLV ELKQMGKITE SRPASAPPPS LSASVPPQAT 250
AGPSYPRPMT PPVSIPGQPN AAGTFTEIPA SNIRRVIAKR LTESKSTVPH 300
AYATADCDLG AVLKVRRDLV KDDIKVSVND FIIRAAAVTL KQMPGVNVTW 350
DGEGPKQLPS VDISVAVATD KGLITPIIKD AAAKGIQEIA DSVKVLSKKA 400
RDGKLMPEEY QGGSFSISNL GMFGIDEFAA VINPPQACIL AVGRFRPVLK 450
LTEDEEGNPQ LQQHQLITVT MSSDSRVVDD ELATRFLETF KANLENPMRL 500
G 501
Length:501
Mass (Da):53,999
Last modified:March 1, 2003 - v1
Checksum:i3FD1FA752EAC5092
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK047670 mRNA. Translation: BAC33120.1.
BC061231 mRNA. Translation: AAH61231.1.
CCDSiCCDS16473.1.
RefSeqiNP_780303.1. NM_175094.5.
UniGeneiMm.315011.

Genome annotation databases

EnsembliENSMUST00000011058; ENSMUSP00000011058; ENSMUSG00000010914.
GeneIDi27402.
KEGGimmu:27402.
UCSCiuc008lil.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK047670 mRNA. Translation: BAC33120.1 .
BC061231 mRNA. Translation: AAH61231.1 .
CCDSi CCDS16473.1.
RefSeqi NP_780303.1. NM_175094.5.
UniGenei Mm.315011.

3D structure databases

ProteinModelPortali Q8BKZ9.
SMRi Q8BKZ9. Positions 57-144, 183-224, 266-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BKZ9. 2 interactions.
MINTi MINT-1867323.
STRINGi 10090.ENSMUSP00000011058.

PTM databases

PhosphoSitei Q8BKZ9.

2D gel databases

REPRODUCTION-2DPAGE IPI00222767.

Proteomic databases

MaxQBi Q8BKZ9.
PaxDbi Q8BKZ9.
PRIDEi Q8BKZ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000011058 ; ENSMUSP00000011058 ; ENSMUSG00000010914 .
GeneIDi 27402.
KEGGi mmu:27402.
UCSCi uc008lil.3. mouse.

Organism-specific databases

CTDi 8050.
MGIi MGI:1351627. Pdhx.

Phylogenomic databases

eggNOGi COG0508.
GeneTreei ENSGT00740000115591.
HOGENOMi HOG000281566.
HOVERGENi HBG005063.
InParanoidi Q8BKZ9.
KOi K13997.
OMAi SWRLGCD.
OrthoDBi EOG7K3TKW.
PhylomeDBi Q8BKZ9.
TreeFami TF332256.

Enzyme and pathway databases

Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

ChiTaRSi PDHX. mouse.
NextBioi 305398.
PROi Q8BKZ9.
SOURCEi Search...

Gene expression databases

Bgeei Q8BKZ9.
CleanExi MM_PDHX.
Genevestigatori Q8BKZ9.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: Corpus striatum.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiODPX_MOUSE
AccessioniPrimary (citable) accession number: Q8BKZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 101 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

External Data

Dasty 3

Similar proteinsi