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Q502L2 (PGAM5_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PGAM5, mitochondrial

EC=3.1.3.16
Alternative name(s):
Phosphoglycerate mutase family member 5
Gene names
Name:pgam5
ORF Names:si:dkey-69p22.1, zgc:92057
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein By similarity.

Domain

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.

Post-translational modification

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

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
   Biological processNecrosis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprogrammed cell death

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Serine/threonine-protein phosphatase PGAM5, mitochondrial
PRO_0000288785

Regions

Transmembrane5 – 2723Helical; Potential

Experimental info

Sequence conflict821G → S in AAH95654. Ref.2
Sequence conflict891A → G in AAH85627. Ref.2
Sequence conflict921N → T in AAH95654. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q502L2 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: 798F3A77AEFF0078

FASTA28932,173
        10         20         30         40         50         60 
MSFRRALSLA CGFAGGSAVL VCAAVVADKN GYFGEGRRVT ETLAAVNAAH PPAWPTANGW 

        70         80         90        100        110        120 
DYNWDKREPS SMVNGKRKES TGENGSQDAE NNKPRATRHI FLIRHSQYNL KGDGDKERFL 

       130        140        150        160        170        180 
TPLGREQAEF TGQRLASFGL KYDTLIHSSM TRATETANII SKYLPGVELV SCDLLREGAP 

       190        200        210        220        230        240 
IEPVPPVTHW KPEAVQYHED GARIEAAFRR YIHRADAKQK EDSYEIIVCH ANVIRYFVCR 

       250        260        270        280 
ALQFPPEGWL RLGLNNGSIT WLTVRPSGRV SLRALGDSGF MPPDKLTRT 

« Hide

References

[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. expand/collapse author list , 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(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Olfactory epithelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR388061 Genomic DNA. Translation: CAM16277.1.
BC085627 mRNA. Translation: AAH85627.1.
BC095654 mRNA. Translation: AAH95654.1.
RefSeqNP_001007324.2. NM_001007323.2.
UniGeneDr.104263.

3D structure databases

ProteinModelPortalQ502L2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000051620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000051621; ENSDARP00000051620; ENSDARG00000035608.
GeneID492357.
KEGGdre:492357.

Organism-specific databases

CTD192111.
ZFINZDB-GENE-030131-683. pgam5.

Phylogenomic databases

eggNOGNOG71348.
GeneTreeENSGT00390000004796.
HOGENOMHOG000261217.
HOVERGENHBG105576.
InParanoidQ502L2.
KOK15637.
OMAWLRMSLN.
OrthoDBEOG7966H1.
PhylomeDBQ502L2.
TreeFamTF314977.

Gene expression databases

BgeeQ502L2.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
ProtoNetSearch...

Other

NextBio20864923.
PROQ502L2.

Entry information

Entry namePGAM5_DANRE
AccessionPrimary (citable) accession number: Q502L2
Secondary accession number(s): A2CEB1, Q5U3B2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: June 11, 2014
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families