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Q8BX10

- PGAM5_MOUSE

UniProt

Q8BX10 - PGAM5_MOUSE

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Protein
Serine/threonine-protein phosphatase PGAM5, mitochondrial
Gene
Pgam5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression By similarity. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB
  2. phosphatase activity Source: UniProtKB
  3. phosphoprotein phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. dephosphorylation Source: UniProtKB
  2. necroptotic process Source: UniProtKB
  3. positive regulation of GTPase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Necrosis

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PGAM5, mitochondrial (EC:3.1.3.16)
Alternative name(s):
Phosphoglycerate mutase family member 5
Gene namesi
Name:Pgam5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1919792. Pgam5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2923Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Serine/threonine-protein phosphatase PGAM5, mitochondrial
PRO_0000288783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791Phosphoserine By similarity
Modified residuei115 – 1151N6-acetyllysine By similarity
Modified residuei143 – 1431N6-acetyllysine By similarity
Modified residuei190 – 1901N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylated by the RIPK1/RIPK3 complex under necrotic conditions. This phosphorylation increases PGAM5 phosphatase activity By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BX10.
PaxDbiQ8BX10.
PRIDEiQ8BX10.

PTM databases

PhosphoSiteiQ8BX10.

Expressioni

Gene expression databases

BgeeiQ8BX10.
CleanExiMM_PGAM5.
GenevestigatoriQ8BX10.

Interactioni

Subunit structurei

Dimer. Forms a ternary complex with NFE2L2 and KEAP1. Interacts with BCL2L1 and MAP3K5 By similarity. Upon TNF-induced necrosis, forms in complex with RIPK1, RIPK3 and MLKL; the formation of this complex leads to PGAM5 phosphorylation By similarity. Interacts with DNM1L; this interaction leads to DNM1L dephosphorylation and activation and eventually to mitochondria fragmentation By similarity.

Protein-protein interaction databases

BioGridi215426. 1 interaction.
DIPiDIP-32064N.
IntActiQ8BX10. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BX10.
SMRiQ8BX10. Positions 88-288.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 816Interaction with KEAP1 By similarity

Domaini

The N-terminal 35 amino acids, including the potential transmembrane alpha-helix, function as a non-cleaved mitochondrial targeting sequence that targets the protein to the cytosolic side of the outer mitochondrial membrane By similarity.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71348.
GeneTreeiENSGT00390000004796.
HOGENOMiHOG000261217.
HOVERGENiHBG105576.
InParanoidiQ8BX10.
KOiK15637.
OMAiWLRMSLN.
OrthoDBiEOG7966H1.
PhylomeDBiQ8BX10.
TreeFamiTF314977.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BX10-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRGGGDADTR ATEPPAWTGA    50
RAGRGVWDTN WDRREPLSLI NLKKRNVESG EDELTSRLDH YKAKATRHIF 100
LIRHSQYHVD GSLEKDRTLT PLGREQAELT GLRLASLGLK FNKIVHSSMT 150
RAVETTDIIS KHLPGVSRVS TDLLREGAPI EPDPPVSHWK PEAVQYYEDG 200
ARIEAAFRNY IHRADARQEE DSYEIFICHA NVIRYIVCRA LQFPPEGWLR 250
LSLNNGSITH LVIRPNGRVA LRTLGDTGFM PPDKITRS 288
Length:288
Mass (Da):31,994
Last modified:March 1, 2003 - v1
Checksum:iB704CDF4E640F888
GO
Isoform 2 (identifier: Q8BX10-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-195: Missing.

Show »
Length:287
Mass (Da):31,866
Checksum:iEF709F19D24DBBD6
GO

Sequence cautioni

The sequence BAB28067.1 differs from that shown. Reason: Frameshift at positions 52 and 66.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 1951Missing in isoform 2.
VSP_025762

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461A → V in BAE26984. 1 Publication
Sequence conflicti102 – 1021I → M in BAC28763. 1 Publication
Sequence conflicti144 – 1441I → V in BAB28067. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK012159 mRNA. Translation: BAB28067.1. Frameshift.
AK034588 mRNA. Translation: BAC28763.1.
AK049246 mRNA. Translation: BAC33634.1.
AK146216 mRNA. Translation: BAE26984.1.
AK169643 mRNA. Translation: BAE41272.1.
BC052179 mRNA. Translation: AAH52179.1.
BC138924 mRNA. Translation: AAI38925.1.
BC138925 mRNA. Translation: AAI38926.1.
CCDSiCCDS19523.1. [Q8BX10-2]
CCDS51606.1. [Q8BX10-1]
RefSeqiNP_001157010.1. NM_001163538.1. [Q8BX10-1]
NP_082549.2. NM_028273.3. [Q8BX10-2]
UniGeneiMm.61682.

Genome annotation databases

EnsembliENSMUST00000059229; ENSMUSP00000057760; ENSMUSG00000029500. [Q8BX10-2]
ENSMUST00000112505; ENSMUSP00000108124; ENSMUSG00000029500. [Q8BX10-1]
GeneIDi72542.
KEGGimmu:72542.
UCSCiuc008yqh.2. mouse. [Q8BX10-2]
uc008yqi.2. mouse. [Q8BX10-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK012159 mRNA. Translation: BAB28067.1 . Frameshift.
AK034588 mRNA. Translation: BAC28763.1 .
AK049246 mRNA. Translation: BAC33634.1 .
AK146216 mRNA. Translation: BAE26984.1 .
AK169643 mRNA. Translation: BAE41272.1 .
BC052179 mRNA. Translation: AAH52179.1 .
BC138924 mRNA. Translation: AAI38925.1 .
BC138925 mRNA. Translation: AAI38926.1 .
CCDSi CCDS19523.1. [Q8BX10-2 ]
CCDS51606.1. [Q8BX10-1 ]
RefSeqi NP_001157010.1. NM_001163538.1. [Q8BX10-1 ]
NP_082549.2. NM_028273.3. [Q8BX10-2 ]
UniGenei Mm.61682.

3D structure databases

ProteinModelPortali Q8BX10.
SMRi Q8BX10. Positions 88-288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 215426. 1 interaction.
DIPi DIP-32064N.
IntActi Q8BX10. 3 interactions.

Chemistry

ChEMBLi CHEMBL2331071.

PTM databases

PhosphoSitei Q8BX10.

Proteomic databases

MaxQBi Q8BX10.
PaxDbi Q8BX10.
PRIDEi Q8BX10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000059229 ; ENSMUSP00000057760 ; ENSMUSG00000029500 . [Q8BX10-2 ]
ENSMUST00000112505 ; ENSMUSP00000108124 ; ENSMUSG00000029500 . [Q8BX10-1 ]
GeneIDi 72542.
KEGGi mmu:72542.
UCSCi uc008yqh.2. mouse. [Q8BX10-2 ]
uc008yqi.2. mouse. [Q8BX10-1 ]

Organism-specific databases

CTDi 192111.
MGIi MGI:1919792. Pgam5.

Phylogenomic databases

eggNOGi NOG71348.
GeneTreei ENSGT00390000004796.
HOGENOMi HOG000261217.
HOVERGENi HBG105576.
InParanoidi Q8BX10.
KOi K15637.
OMAi WLRMSLN.
OrthoDBi EOG7966H1.
PhylomeDBi Q8BX10.
TreeFami TF314977.

Miscellaneous databases

ChiTaRSi Pgam5. mouse.
NextBioi 336451.
PROi Q8BX10.
SOURCEi Search...

Gene expression databases

Bgeei Q8BX10.
CleanExi MM_PGAM5.
Genevestigatori Q8BX10.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J, DBA/2 and NOD.
    Tissue: Thymus.
  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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-288 (ISOFORM 1).
    Tissue: Brain and Embryo.
  3. "The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways."
    Wang Z., Jiang H., Chen S., Du F., Wang X.
    Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPGAM5_MOUSE
AccessioniPrimary (citable) accession number: Q8BX10
Secondary accession number(s): B2RSM6
, Q3UK19, Q80VY8, Q8BM78, Q9CZU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 85 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