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Protein

Myotubularin-related protein 2

Gene

mtmr2

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.By similarity
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei393 – 3931Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei439 – 4391SubstrateBy similarity

GO - Molecular functioni

  1. phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
  2. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  3. protein tyrosine phosphatase activity Source: InterPro

GO - Biological processi

  1. phosphatidylinositol dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_277708. Synthesis of PIPs at the late endosome membrane.
REACT_299059. Synthesis of PIPs at the early endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 2
Alternative name(s):
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.95By similarity)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.64By similarity)
Gene namesi
Name:mtmr2
ORF Names:si:dkey-110k5.3
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 5

Organism-specific databases

ZFINiZDB-GENE-990715-14. mtmr2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. early endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Myotubularin-related protein 2PRO_0000356230Add
BLAST

Expressioni

Gene expression databases

BgeeiA0JMK5.

Interactioni

Subunit structurei

Homooligomer and heterooligomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliA0JMK5.
SMRiA0JMK5. Positions 52-562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 11678GRAMAdd
BLAST
Domaini181 – 556376Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni306 – 3094Substrate bindingBy similarity
Regioni331 – 3322Substrate bindingBy similarity
Regioni393 – 3997Substrate bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili569 – 60133Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 GRAM domain.Curated
Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiA0JMK5.
KOiK18081.
OMAiPENGWKV.
OrthoDBiEOG7XDBF9.
PhylomeDBiA0JMK5.
TreeFamiTF315197.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PfamiPF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0JMK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESASVDSV ESLCSSTTTR SDRSSGPKVS DTELRSKGRP IEKMYKDPSK
60 70 80 90 100
GELPLLPVEL VQESAKDVTY ICPFIGPIRG SLTVTNYRLF FRCTDREPVF
110 120 130 140 150
GLDLPLGVLS RVEKIGAATG RGDVSYGLAC KDMRNLRFVH KEPDDSLKKS
160 170 180 190 200
VFEVLMKFAF PVSNNMSLFA FEYKQVFPEN GWKVYDPLAE CKRQGLPNES
210 220 230 240 250
WRISKLNDHY ELCDSYPATL VVPVTITDDE LRRVSSFRAK GRIPVLSWIH
260 270 280 290 300
PESQAAVVRS SQPMVGQNGR RCKEDEKLLQ AIMDANAQSH KLFIFDARPS
310 320 330 340 350
VNAAANKMKG GGFESEDAYQ NAELVFLDIH NIHVMRESLR KLKEVVYPNI
360 370 380 390 400
EESHWLSNLE STHWLEHIKL ILAGALRIAD KVESGKTSVV VHCSDGWDRT
410 420 430 440 450
AQLTSLALIM LDSHYRTIRG FQILVEKEWL SFGHRFQQRV GHGDKNHTDV
460 470 480 490 500
DRSPIFLQFI DCVWQMTRQF PAAFEFNEYF LITILDHLYS CLFGTFLCNS
510 520 530 540 550
EQQRLKEEIP KRTVSLWSFV NSQLEEFVNP LYVHYSSHVL FPTVGIRHLQ
560 570 580 590 600
LWVSYYIRWN PRMRPQEPVH QRYKELLAKR AELQKRVEEL QREVSSRTAS
610 620
SSSERAGSPT RSITPVQTFV
Length:620
Mass (Da):71,109
Last modified:December 16, 2008 - v2
Checksum:iA67ADEE5D7B27C1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291V → L in AAI25913 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL929305 Genomic DNA. Translation: CAQ13290.1.
BC125912 mRNA. Translation: AAI25913.1.
RefSeqiNP_571446.1. NM_131371.1.
UniGeneiDr.81275.

Genome annotation databases

EnsembliENSDART00000020004; ENSDARP00000007407; ENSDARG00000004616.
GeneIDi30644.
KEGGidre:30644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL929305 Genomic DNA. Translation: CAQ13290.1.
BC125912 mRNA. Translation: AAI25913.1.
RefSeqiNP_571446.1. NM_131371.1.
UniGeneiDr.81275.

3D structure databases

ProteinModelPortaliA0JMK5.
SMRiA0JMK5. Positions 52-562.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000020004; ENSDARP00000007407; ENSDARG00000004616.
GeneIDi30644.
KEGGidre:30644.

Organism-specific databases

CTDi8898.
ZFINiZDB-GENE-990715-14. mtmr2.

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiA0JMK5.
KOiK18081.
OMAiPENGWKV.
OrthoDBiEOG7XDBF9.
PhylomeDBiA0JMK5.
TreeFamiTF315197.

Enzyme and pathway databases

ReactomeiREACT_277708. Synthesis of PIPs at the late endosome membrane.
REACT_299059. Synthesis of PIPs at the early endosome membrane.

Miscellaneous databases

NextBioi20807001.
PROiA0JMK5.

Gene expression databases

BgeeiA0JMK5.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PfamiPF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
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 (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiMTMR2_DANRE
AccessioniPrimary (citable) accession number: A0JMK5
Secondary accession number(s): B0R0X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: April 1, 2015
This is version 63 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.