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Protein

Serine/threonine-protein phosphatase PGAM5, mitochondrial

Gene

pgam5

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics (By similarity). May be a central mediator for programmed necrosis (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. programmed cell death Source: UniProtKB-KW
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
ORF Names:si:dkey-69p22.1, zgc:92057
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 5

Organism-specific databases

ZFINiZDB-GENE-030131-683. pgam5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2723HelicalSequence AnalysisAdd
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 – 289289Serine/threonine-protein phosphatase PGAM5, mitochondrialPRO_0000288785Add
BLAST

Post-translational modificationi

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

Expressioni

Gene expression databases

BgeeiQ502L2.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000051620.

Structurei

3D structure databases

ProteinModelPortaliQ502L2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.
InParanoidiQ502L2.
KOiK15637.
OMAiEIIVCHA.
OrthoDBiEOG7966H1.
PhylomeDBiQ502L2.
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.

Sequencei

Sequence statusi: Complete.

Q502L2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRRALSLA CGFAGGSAVL VCAAVVADKN GYFGEGRRVT ETLAAVNAAH
60 70 80 90 100
PPAWPTANGW DYNWDKREPS SMVNGKRKES TGENGSQDAE NNKPRATRHI
110 120 130 140 150
FLIRHSQYNL KGDGDKERFL TPLGREQAEF TGQRLASFGL KYDTLIHSSM
160 170 180 190 200
TRATETANII SKYLPGVELV SCDLLREGAP IEPVPPVTHW KPEAVQYHED
210 220 230 240 250
GARIEAAFRR YIHRADAKQK EDSYEIIVCH ANVIRYFVCR ALQFPPEGWL
260 270 280
RLGLNNGSIT WLTVRPSGRV SLRALGDSGF MPPDKLTRT
Length:289
Mass (Da):32,173
Last modified:May 28, 2007 - v2
Checksum:i798F3A77AEFF0078
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821G → S in AAH95654 (Ref. 2) Curated
Sequence conflicti89 – 891A → G in AAH85627 (Ref. 2) Curated
Sequence conflicti92 – 921N → T in AAH95654 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR388061 Genomic DNA. Translation: CAM16277.1.
BC085627 mRNA. Translation: AAH85627.1.
BC095654 mRNA. Translation: AAH95654.1.
RefSeqiNP_001007324.2. NM_001007323.2.
UniGeneiDr.104263.

Genome annotation databases

EnsembliENSDART00000051621; ENSDARP00000051620; ENSDARG00000035608.
GeneIDi492357.
KEGGidre:492357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR388061 Genomic DNA. Translation: CAM16277.1.
BC085627 mRNA. Translation: AAH85627.1.
BC095654 mRNA. Translation: AAH95654.1.
RefSeqiNP_001007324.2. NM_001007323.2.
UniGeneiDr.104263.

3D structure databases

ProteinModelPortaliQ502L2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000051620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000051621; ENSDARP00000051620; ENSDARG00000035608.
GeneIDi492357.
KEGGidre:492357.

Organism-specific databases

CTDi192111.
ZFINiZDB-GENE-030131-683. pgam5.

Phylogenomic databases

eggNOGiNOG71348.
GeneTreeiENSGT00390000004796.
HOGENOMiHOG000261217.
HOVERGENiHBG105576.
InParanoidiQ502L2.
KOiK15637.
OMAiEIIVCHA.
OrthoDBiEOG7966H1.
PhylomeDBiQ502L2.
TreeFamiTF314977.

Miscellaneous databases

NextBioi20864923.
PROiQ502L2.

Gene expression databases

BgeeiQ502L2.

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

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.

Entry informationi

Entry nameiPGAM5_DANRE
AccessioniPrimary (citable) accession number: Q502L2
Secondary accession number(s): A2CEB1, Q5U3B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 28, 2007
Last sequence update: May 28, 2007
Last modified: January 6, 2015
This is version 58 of the entry and version 2 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. 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.