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A0JMK5 (MTMR2_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:
Myotubularin-related protein 2

EC=3.1.3.-
Gene names
Name:mtmr2
ORF Names:si:dkey-110k5.3
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate By similarity.

Subunit structure

Homooligomer and heterooligomer By similarity.

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Note: Partly associated with membranes By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.

Contains 1 GRAM domain.

Contains 1 myotubularin phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   DomainCoiled coil
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-tyrosine dephosphorylation

Inferred from sequence or structural similarity. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: ZFIN

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Myotubularin-related protein 2
PRO_0000356230

Regions

Domain39 – 11678GRAM
Domain181 – 556376Myotubularin phosphatase
Region306 – 3094Substrate binding By similarity
Region331 – 3322Substrate binding By similarity
Region393 – 3997Substrate binding By similarity
Coiled coil569 – 60133 Potential

Sites

Active site3931Phosphocysteine intermediate By similarity
Binding site4391Substrate By similarity

Experimental info

Sequence conflict291V → L in AAI25913. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A0JMK5 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: A67ADEE5D7B27C1F

FASTA62071,109
        10         20         30         40         50         60 
MEESASVDSV ESLCSSTTTR SDRSSGPKVS DTELRSKGRP IEKMYKDPSK GELPLLPVEL 

        70         80         90        100        110        120 
VQESAKDVTY ICPFIGPIRG SLTVTNYRLF FRCTDREPVF GLDLPLGVLS RVEKIGAATG 

       130        140        150        160        170        180 
RGDVSYGLAC KDMRNLRFVH KEPDDSLKKS VFEVLMKFAF PVSNNMSLFA FEYKQVFPEN 

       190        200        210        220        230        240 
GWKVYDPLAE CKRQGLPNES WRISKLNDHY ELCDSYPATL VVPVTITDDE LRRVSSFRAK 

       250        260        270        280        290        300 
GRIPVLSWIH PESQAAVVRS SQPMVGQNGR RCKEDEKLLQ AIMDANAQSH KLFIFDARPS 

       310        320        330        340        350        360 
VNAAANKMKG GGFESEDAYQ NAELVFLDIH NIHVMRESLR KLKEVVYPNI EESHWLSNLE 

       370        380        390        400        410        420 
STHWLEHIKL ILAGALRIAD KVESGKTSVV VHCSDGWDRT AQLTSLALIM LDSHYRTIRG 

       430        440        450        460        470        480 
FQILVEKEWL SFGHRFQQRV GHGDKNHTDV DRSPIFLQFI DCVWQMTRQF PAAFEFNEYF 

       490        500        510        520        530        540 
LITILDHLYS CLFGTFLCNS EQQRLKEEIP KRTVSLWSFV NSQLEEFVNP LYVHYSSHVL 

       550        560        570        580        590        600 
FPTVGIRHLQ LWVSYYIRWN PRMRPQEPVH QRYKELLAKR AELQKRVEEL QREVSSRTAS 

       610        620 
SSSERAGSPT RSITPVQTFV 

« 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 (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL929305 Genomic DNA. Translation: CAQ13290.1.
BC125912 mRNA. Translation: AAI25913.1.
RefSeqNP_571446.1. NM_131371.1.
UniGeneDr.81275.

3D structure databases

ProteinModelPortalA0JMK5.
SMRA0JMK5. Positions 52-562.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000020004; ENSDARP00000007407; ENSDARG00000004616.
GeneID30644.
KEGGdre:30644.

Organism-specific databases

CTD8898.
ZFINZDB-GENE-990715-14. mtmr2.

Phylogenomic databases

eggNOGNOG322789.
GeneTreeENSGT00670000097670.
HOGENOMHOG000210598.
HOVERGENHBG000220.
InParanoidA0JMK5.
KOK18081.
OMAPENGWKV.
OrthoDBEOG7XDBF9.
PhylomeDBA0JMK5.
TreeFamTF315197.

Gene expression databases

BgeeA0JMK5.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTSM00568. GRAM. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20807001.
PROA0JMK5.

Entry information

Entry nameMTMR2_DANRE
AccessionPrimary (citable) accession number: A0JMK5
Secondary accession number(s): B0R0X3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: June 11, 2014
This is version 58 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