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Protein

Serine/threonine-protein phosphatase PGAM5, mitochondrial

Gene

Pgam5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.By similarity1 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
  4. protein complex binding Source: MGI

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 – 2923HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: UniProtKB-SubCell
  3. mitochondrion Source: MGI
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, mitochondrialPRO_0000288783Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8BX10.
SMRiQ8BX10. Positions 88-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 816Interaction with KEAP1By 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.
OMAiEIIVCHA.
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. AlignAdd to basket

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

        10         20         30         40         50
MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRGGGDADTR ATEPPAWTGA
60 70 80 90 100
RAGRGVWDTN WDRREPLSLI NLKKRNVESG EDELTSRLDH YKAKATRHIF
110 120 130 140 150
LIRHSQYHVD GSLEKDRTLT PLGREQAELT GLRLASLGLK FNKIVHSSMT
160 170 180 190 200
RAVETTDIIS KHLPGVSRVS TDLLREGAPI EPDPPVSHWK PEAVQYYEDG
210 220 230 240 250
ARIEAAFRNY IHRADARQEE DSYEIFICHA NVIRYIVCRA LQFPPEGWLR
260 270 280
LSLNNGSITH LVIRPNGRVA LRTLGDTGFM PPDKITRS
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461A → V in BAE26984 (PubMed:16141072).Curated
Sequence conflicti102 – 1021I → M in BAC28763 (PubMed:16141072).Curated
Sequence conflicti144 – 1441I → V in BAB28067 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 1951Missing in isoform 2. 2 PublicationsVSP_025762

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ8BX10.
SMRiQ8BX10. Positions 88-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2331071.

PTM databases

PhosphoSiteiQ8BX10.

Proteomic databases

MaxQBiQ8BX10.
PaxDbiQ8BX10.
PRIDEiQ8BX10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi192111.
MGIiMGI:1919792. Pgam5.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiPgam5. mouse.
NextBioi336451.
PROiQ8BX10.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BX10.
CleanExiMM_PGAM5.
GenevestigatoriQ8BX10.

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.
ProtoNetiSearch...

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: March 4, 2015
This is version 90 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

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 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.