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Q9Z2D1 (MTMR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Binds phosphatidylinositol 4-phosphate, hosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Ref.5

Enzyme regulation

interaction with SBF1 increases phosphatase activity By similarity.

Subunit structure

Homooligomer and heterooligomer. Interacts with SBF1 and SBF2 By similarity. Ref.6

Subcellular location

Cytoplasm. Early endosome membrane; Peripheral membrane protein By similarity. Note: Partly associated with membranes. Ref.6

Tissue specificity

Detected in fetal forebrain, dorsal root ganglia, trigeminal ganglia, kidney, adrenal gland and lung. Detected in adult dorsal root ganglia, neurons of the central nervous system, motor neurons, cell soma and neurites of sensory neurons, olfactory bulb, cerebellum and hippocampus. Ref.5

Post-translational modification

Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures 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.

Sequence caution

The sequence AAC80002.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Endosome
Membrane
   DomainCoiled coil
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdendritic spine maintenance

Inferred from electronic annotation. Source: Ensembl

dephosphorylation

Inferred from direct assay PubMed 16399794. Source: MGI

inositol phosphate dephosphorylation

Inferred from direct assay PubMed 16399794. Source: MGI

myelin assembly

Inferred from mutant phenotype PubMed 22028665. Source: MGI

negative regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

negative regulation of myelination

Inferred from genetic interaction PubMed 22028665. Source: MGI

negative regulation of receptor catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of receptor internalization

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from genetic interaction PubMed 22028665. Source: MGI

phosphatidylinositol dephosphorylation

Inferred from direct assay PubMed 16399794. Source: MGI

phosphatidylinositol metabolic process

Inferred from mutant phenotype PubMed 22028665. Source: MGI

positive regulation of early endosome to late endosome transport

Inferred from electronic annotation. Source: Ensembl

protein tetramerization

Inferred from physical interaction PubMed 16399794. Source: MGI

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 12837694PubMed 16399794. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal postsynaptic density

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

synaptic membrane

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

vacuolar membrane

Inferred from direct assay PubMed 16399794. Source: MGI

   Molecular_functionphosphatidylinositol phosphate phosphatase activity

Inferred from mutant phenotype PubMed 22028665. Source: MGI

protein homodimerization activity

Inferred from physical interaction PubMed 16399794. Source: MGI

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643Myotubularin-related protein 2
PRO_0000094935

Regions

Domain68 – 13972GRAM
Domain205 – 580376Myotubularin phosphatase
Region330 – 3334Substrate binding By similarity
Region355 – 3562Substrate binding By similarity
Region417 – 4237Substrate binding By similarity
Coiled coil593 – 62735 By similarity
Compositional bias4 – 5350Ser-rich

Sites

Active site4171Phosphocysteine intermediate
Binding site4631Substrate By similarity

Amino acid modifications

Modified residue61Phosphoserine Ref.7
Modified residue581Phosphoserine By similarity

Experimental info

Mutagenesis1031G → E: Severely impaired interaction with membranes and strongly reduced catalytic activity. Ref.5 Ref.6
Mutagenesis4171C → A: Loss of activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9Z2D1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: FD4E43867CBB9864

FASTA64373,232
        10         20         30         40         50         60 
MEKSSSCESL GAQLPAARLP SEDSLSSAST SHSENSVHTK SASAISSDSI STSADNFSPD 

        70         80         90        100        110        120 
LRVLREANKL AEMEEPALLP GENIKDMAKD VTYICPFTGA VRGTLTVTSY RLYFKSMERD 

       130        140        150        160        170        180 
PPFVLDASLG VISRVEKIGG ASSRGENSYG LETVCKDIRN LRFAHKPEGR TRRSIFENLM 

       190        200        210        220        230        240 
KYAFPVSNGL PLFAFEYKEV FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY 

       250        260        270        280        290        300 
PALLVVPANI PDEELKRVAS FRSRGRIPVL SWIHPESQAT VTRCSQPMVG VSGKRSKEDE 

       310        320        330        340        350        360 
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF LDIHNIHVMR 

       370        380        390        400        410        420 
ESLRKLKEIV YPTIEETHWL SNLESTHWLE HIKLILAGAL RIADKVESGK TSVVVHCSDG 

       430        440        450        460        470        480 
WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE KEWLSFGHRF QLRVGHGDKN HADADRSPVF 

       490        500        510        520        530        540 
LQFIDCVWQM TRQFPTAFEF NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKKTVSL 

       550        560        570        580        590        600 
WSYINSQLED FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHSRYKEL 

       610        620        630        640 
LAKRAELQRK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization and expression analysis of Mtmr2, mouse homolog of MTMR2, the myotubularin-related 2 gene, mutated in CMT4B."
Bolino A., Marigo V., Loader J., Romio L., Leoni A., Di Duca M., Cinti R., Feltri M.L., Wrabetz L., Ravazzolo R., Monaco A.P.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human."
Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N., Mandel J.-L.
Hum. Mol. Genet. 7:1703-1712(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-225.
[5]"Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1."
Berger P., Bonneick S., Willi S., Wymann M., Suter U.
Hum. Mol. Genet. 11:1569-1579(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-103, TISSUE SPECIFICITY.
[6]"Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module."
Berger P., Schaffitzel C., Berger I., Ban N., Suter U.
Proc. Natl. Acad. Sci. U.S.A. 100:12177-12182(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-103 AND CYS-417, SUBUNIT.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY055832 mRNA. Translation: AAL14198.1.
CT010488 Genomic DNA. Translation: CAX15666.1.
CH466522 Genomic DNA. Translation: EDL24975.1.
AF073880 mRNA. Translation: AAC80002.1. Different initiation.
CCDSCCDS22818.3.
RefSeqNP_076347.3. NM_023858.3.
UniGeneMm.210405.

3D structure databases

ProteinModelPortalQ9Z2D1.
SMRQ9Z2D1. Positions 73-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid218525. 1 interaction.

PTM databases

PhosphoSiteQ9Z2D1.

Proteomic databases

MaxQBQ9Z2D1.
PaxDbQ9Z2D1.
PRIDEQ9Z2D1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034396; ENSMUSP00000034396; ENSMUSG00000031918.
GeneID77116.
KEGGmmu:77116.
UCSCuc009odz.2. mouse.

Organism-specific databases

CTD8898.
MGIMGI:1924366. Mtmr2.

Phylogenomic databases

eggNOGNOG322789.
GeneTreeENSGT00670000097670.
HOGENOMHOG000210598.
HOVERGENHBG000220.
InParanoidQ9Z2D1.
KOK18081.
OMAPENGWKV.
OrthoDBEOG7XDBF9.
TreeFamTF315197.

Gene expression databases

BgeeQ9Z2D1.
CleanExMM_MTMR2.
GenevestigatorQ9Z2D1.

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

NextBio346504.
PROQ9Z2D1.
SOURCESearch...

Entry information

Entry nameMTMR2_MOUSE
AccessionPrimary (citable) accession number: Q9Z2D1
Secondary accession number(s): B8JJF4, Q8VHA7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 108 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot