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Q13614 (MTMR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myotubularin-related protein 2

EC=3.1.3.-
Gene names
Name:MTMR2
Synonyms:KIAA1073
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.9 Ref.15

Enzyme regulation

interaction with SBF1 increases phosphatase activity. Ref.9

Subunit structure

Homooligomer and heterooligomer. Interacts with SBF1 and SBF2. Ref.9 Ref.10

Subcellular location

Cytoplasm. Early endosome membrane; Peripheral membrane protein. Note: Partly associated with membranes. Ref.9 Ref.10 Ref.15

Domain

The coiled-coil domain mediates interaction with SBF2. Ref.17

Post-translational modification

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

Involvement in disease

Charcot-Marie-Tooth disease 4B1 (CMT4B1) [MIM:601382]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.18

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 BAA83025.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   DomainCoiled coil
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

dendritic spine maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

inositol phosphate dephosphorylation

Inferred from electronic annotation. Source: Ensembl

myelin assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of endocytosis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of myelination

Inferred from electronic annotation. Source: Ensembl

negative regulation of receptor catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of receptor internalization

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron development

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol dephosphorylation

Inferred from electronic annotation. Source: Ensembl

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of early endosome to late endosome transport

Inferred from sequence or structural similarity. Source: BHF-UCL

protein dephosphorylation

Non-traceable author statement Ref.6. Source: UniProtKB

protein tetramerization

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 12837694. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

dendrite

Inferred from sequence or structural similarity. Source: BHF-UCL

dendritic spine

Inferred from sequence or structural similarity. Source: BHF-UCL

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal postsynaptic density

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 12837694. Source: UniProtKB

synaptic membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic vesicle

Inferred from sequence or structural similarity. Source: BHF-UCL

vacuolar membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatidylinositol phosphate phosphatase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 12837694Ref.10. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: InterPro

protein tyrosine/serine/threonine phosphatase activity

Non-traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NEFLP071962EBI-475631,EBI-475646

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13614-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13614-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643Myotubularin-related protein 2
PRO_0000094934

Regions

Domain68 – 13972GRAM
Domain205 – 580376Myotubularin phosphatase
Region330 – 3334Substrate binding
Region355 – 3562Substrate binding
Region417 – 4237Substrate binding
Coiled coil593 – 62735 Ref.17
Compositional bias4 – 5350Ser-rich

Sites

Active site4171Phosphocysteine intermediate
Binding site4631Substrate

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue581Phosphoserine Ref.11 Ref.13 Ref.15

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_044933
Natural variant31K → T. Ref.1 Ref.5
Corresponds to variant rs3824874 [ dbSNP | Ensembl ].
VAR_047255
Natural variant2831R → W in CMT4B1. Ref.18
VAR_047947
Natural variant5451N → S.
Corresponds to variant rs558018 [ dbSNP | Ensembl ].
VAR_047256

Experimental info

Mutagenesis4171C → S: Loss of activity. Ref.16 Ref.17
Mutagenesis4191D → A: No effect. Ref.16
Mutagenesis4221D → A: Loss of activity. Ref.16
Mutagenesis6071L → Y: Reduces homodimerization and interaction with SBF1. Ref.9

Secondary structure

...................................................................................................... 643
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 4, 2008. Version 4.
Checksum: 10FD6508D0CDA719

FASTA64373,381
        10         20         30         40         50         60 
MEKSSSCESL GSQPAAARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI STSADNFSPD 

        70         80         90        100        110        120 
LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA VRGTLTVTNY RLYFKSMERD 

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

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

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

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

       370        380        390        400        410        420 
ESLRKLKEIV YPNIEETHWL 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 ENLPKRTVSL 

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

       610        620        630        640 
LAKRAELQKK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV 

« Hide

Isoform 2 [UniParc].

Checksum: DBC304269CEFC843
Show »

FASTA57165,959

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-3.
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-3.
Tissue: Uterus.
[6]"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 384-643 (ISOFORM 1).
[7]"A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast."
Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J., Klauck S.M., Poutska A., Dahl N.
Nat. Genet. 13:175-182(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 384-514 (ISOFORM 1).
[8]"Charcot-Marie-Tooth type 4B is caused by mutations in the gene encoding myotubularin-related protein-2."
Bolino A., Muglia M., Conforti F.L., LeGuern E., Salih M.A.M., Georgiou D.-M., Christodoulou K., Hausmanowa-Petrusewicz I., Mandich P., Schenone A., Gambardella A., Bono F., Quattrone A., Devoto M., Monaco A.P.
Nat. Genet. 25:17-19(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CMT4B1.
[9]"Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase."
Kim S.-A., Vacratsis P.O., Firestein R., Cleary M.L., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 100:4492-4497(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-607, INTERACTION WITH SBF1.
[10]"The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease."
Robinson F.L., Dixon J.E.
J. Biol. Chem. 280:31699-31707(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SBF2, SUBUNIT, SUBCELLULAR LOCATION.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Endosomal targeting of the phosphoinositide 3-phosphatase MTMR2 is regulated by an N-terminal phosphorylation site."
Franklin N.E., Taylor G.S., Vacratsis P.O.
J. Biol. Chem. 286:15841-15853(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-58.
[16]"Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome."
Begley M.J., Taylor G.S., Kim S.-A., Veine D.M., Dixon J.E., Stuckey J.A.
Mol. Cell 12:1391-1402(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT SER-417 IN COMPLEX WITH PHOSPHOINOSITIDE, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-417; ASP-419 AND ASP-422.
[17]"Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase."
Begley M.J., Taylor G.S., Brock M.A., Ghosh P., Woods V.L., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 103:927-932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 71-586 OF MUTANT SER-417 IN COMPLEX WITH PHOSPHOINOSITIDES, COILED-COIL DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-417.
[18]"A novel homozygous missense mutation in the myotubularin-related protein 2 gene associated with recessive Charcot-Marie-Tooth disease with irregularly folded myelin sheaths."
Nelis E., Erdem S., Tan E., Loefgren A., Ceuterick C., De Jonghe P., Van Broeckhoven C., Timmerman V., Topaloglu H.
Neuromuscul. Disord. 12:869-873(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMT4B1 TRP-283.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028996 mRNA. Translation: BAA83025.2. Different initiation.
AK302940 mRNA. Translation: BAG64098.1.
AP000870 Genomic DNA. No translation available.
AP001877 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66971.1.
BC052990 mRNA. Translation: AAH52990.1.
U58033 mRNA. Translation: AAC79118.1.
CCDSCCDS8305.1. [Q13614-1]
CCDS8306.1. [Q13614-2]
PIRT09497.
RefSeqNP_001230500.1. NM_001243571.1. [Q13614-2]
NP_057240.3. NM_016156.5. [Q13614-1]
NP_958435.1. NM_201278.2. [Q13614-2]
NP_958438.1. NM_201281.2. [Q13614-2]
XP_005274431.1. XM_005274374.1. [Q13614-2]
XP_005274432.1. XM_005274375.1. [Q13614-2]
XP_006718997.1. XM_006718934.1. [Q13614-2]
XP_006718998.1. XM_006718935.1. [Q13614-2]
XP_006718999.1. XM_006718936.1. [Q13614-2]
UniGeneHs.181326.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LW3X-ray2.30A1-643[»]
1M7RX-ray2.60A/B1-643[»]
1ZSQX-ray1.82A73-586[»]
1ZVRX-ray1.98A73-586[»]
ProteinModelPortalQ13614.
SMRQ13614. Positions 73-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114415. 13 interactions.
IntActQ13614. 5 interactions.
MINTMINT-6774021.
STRING9606.ENSP00000345752.

PTM databases

PhosphoSiteQ13614.

Polymorphism databases

DMDM212276520.

Proteomic databases

MaxQBQ13614.
PaxDbQ13614.
PRIDEQ13614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346299; ENSP00000345752; ENSG00000087053. [Q13614-1]
ENST00000352297; ENSP00000343737; ENSG00000087053. [Q13614-2]
ENST00000393223; ENSP00000376915; ENSG00000087053. [Q13614-2]
ENST00000409459; ENSP00000386882; ENSG00000087053. [Q13614-2]
GeneID8898.
KEGGhsa:8898.
UCSCuc001pfs.3. human. [Q13614-1]

Organism-specific databases

CTD8898.
GeneCardsGC11M095566.
GeneReviewsMTMR2.
HGNCHGNC:7450. MTMR2.
HPAHPA049831.
MIM601382. phenotype.
603557. gene.
neXtProtNX_Q13614.
Orphanet99955. Charcot-Marie-Tooth disease type 4B1.
PharmGKBPA31253.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322789.
HOGENOMHOG000210598.
HOVERGENHBG000220.
InParanoidQ13614.
KOK18081.
OMAPENGWKV.
OrthoDBEOG7XDBF9.
PhylomeDBQ13614.
TreeFamTF315197.

Enzyme and pathway databases

BRENDA3.1.3.64. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ13614.
BgeeQ13614.
CleanExHS_MTMR2.
GenevestigatorQ13614.

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

ChiTaRSMTMR2. human.
EvolutionaryTraceQ13614.
GeneWikiMTMR2.
GenomeRNAi8898.
NextBio33423.
PROQ13614.
SOURCESearch...

Entry information

Entry nameMTMR2_HUMAN
AccessionPrimary (citable) accession number: Q13614
Secondary accession number(s): A6NN98, Q9UPS9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 4, 2008
Last modified: July 9, 2014
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM