Q13614 (MTMR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myotubularin-related protein 2
EC=3.1.3.-

Gene names

Name:	MTMR2
Synonyms:	KIAA1073

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	643 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
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.14
Domain	The coiled-coil domain mediates interaction with SBF2. Ref.16
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.17
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 component	Cytoplasm Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Domain	Coiled coil
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dendritic spine maintenance Inferred from sequence or structural similarity. Source: BHF-UCL inositol phosphate dephosphorylation Inferred from electronic annotation. Source: Compara myelin assembly Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome phosphatidylinositol dephosphorylation Inferred from electronic annotation. Source: Compara positive regulation of early endosome to late endosome transport Inferred from sequence or structural similarity. Source: BHF-UCL protein tetramerization Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	axon Inferred from sequence or structural similarity. Source: BHF-UCL cytosol Inferred from sequence or structural similarity. Source: BHF-UCL early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 12837694. Source: UniProtKB postsynaptic density Inferred from sequence or structural similarity. Source: BHF-UCL 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: Compara
Molecular_function	phosphatidylinositol phosphate phosphatase activity Inferred from electronic annotation. Source: Compara 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
NEFL	P07196	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 643

643

Myotubularin-related protein 2

PRO_0000094934

Regions

Domain

68 – 139

72

GRAM

Domain

205 – 580

376

Myotubularin phosphatase

Region

330 – 333

4

Substrate binding

Region

355 – 356

2

Substrate binding

Region

417 – 423

7

Substrate binding

Coiled coil

593 – 627

35

Ref.16

Compositional bias

4 – 53

50

Ser-rich

Sites

Active site

417

1

Phosphocysteine intermediate

Binding site

463

1

Substrate

Amino acid modifications

Modified residue

58

1

Phosphoserine Ref.11 Ref.12 Ref.14

Natural variations

Alternative sequence

1 – 72

72

Missing in isoform 2.

VSP_044933

Natural variant

3

1

K → T. Ref.1 Ref.5
Corresponds to variant rs3824874 [ dbSNP | Ensembl ].

VAR_047255

Natural variant

283

1

R → W in CMT4B1. Ref.17

VAR_047947

Natural variant

545

1

N → S.
Corresponds to variant rs558018 [ dbSNP | Ensembl ].

VAR_047256

Experimental info

Mutagenesis

417

1

C → S: Loss of activity. Ref.15 Ref.16

Mutagenesis

419

1

D → A: No effect. Ref.15

Mutagenesis

422

1

D → A: Loss of activity. Ref.15

Mutagenesis

607

1

L → Y: Reduces homodimerization and interaction with SBF1. Ref.9

Secondary structure

1

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643

Helix Strand Turn

Details...

Beta strand

84 – 95

12

Turn

96 – 98

3

Beta strand

99 – 121

23

Beta strand

123 – 128

6

Helix

129 – 131

3

Beta strand

132 – 138

7

Beta strand

145 – 147

3

Beta strand

149 – 155

7

Turn

156 – 158

3

Beta strand

159 – 164

6

Helix

167 – 169

3

Helix

172 – 182

11

Turn

185 – 189

5

Helix

193 – 195

3

Helix

205 – 207

3

Helix

211 – 217

7

Beta strand

223 – 228

6

Turn

230 – 233

4

Beta strand

234 – 236

3

Beta strand

242 – 247

6

Helix

252 – 261

10

Helix

263 – 265

3

Beta strand

269 – 273

5

Turn

275 – 277

3

Beta strand

280 – 284

5

Turn

290 – 293

4

Helix

297 – 309

13

Beta strand

310 – 312

3

Beta strand

314 – 320

7

Helix

324 – 333

10

Turn

340 – 342

3

Beta strand

346 – 350

5

Helix

356 – 370

15

Helix

376 – 378

3

Helix

379 – 386

8

Helix

388 – 407

20

Beta strand

413 – 416

4

Beta strand

418 – 422

5

Helix

423 – 435

13

Helix

437 – 440

4

Helix

442 – 452

11

Turn

453 – 457

5

Helix

460 – 464

5

Turn

465 – 467

3

Helix

479 – 493

15

Turn

495 – 497

3

Helix

502 – 514

13

Beta strand

516 – 518

3

Beta strand

522 – 524

3

Helix

525 – 530

6

Helix

533 – 536

4

Helix

540 – 545

6

Helix

548 – 551

4

Turn

554 – 557

4

Beta strand

560 – 562

3

Turn

570 – 572

3

Helix

577 – 580

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 4, 2008. Version 4. Checksum: 10FD6508D0CDA719	FASTA	643	73,381
	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
	Isoform 2 [UniParc]. Checksum: DBC304269CEFC843	FASTA	571	65,959
	10 20 30 40 50 60 MEEPPLLPGE NIKDMAKDVT YICPFTGAVR GTLTVTNYRL YFKSMERDPP FVLDASLGVI 70 80 90 100 110 120 NRVEKIGGAS SRGENSYGLE TVCKDIRNLR FAHKPEGRTR RSIFENLMKY AFPVSNNLPL 130 140 150 160 170 180 FAFEYKEVFP ENGWKLYDPL LEYRRQGIPN ESWRITKINE RYELCDTYPA LLVVPANIPD 190 200 210 220 230 240 EELKRVASFR SRGRIPVLSW IHPESQATIT RCSQPMVGVS GKRSKEDEKY LQAIMDSNAQ 250 260 270 280 290 300 SHKIFIFDAR PSVNAVANKA KGGGYESEDA YQNAELVFLD IHNIHVMRES LRKLKEIVYP 310 320 330 340 350 360 NIEETHWLSN LESTHWLEHI KLILAGALRI ADKVESGKTS VVVHCSDGWD RTAQLTSLAM 370 380 390 400 410 420 LMLDGYYRTI RGFEVLVEKE WLSFGHRFQL RVGHGDKNHA DADRSPVFLQ FIDCVWQMTR 430 440 450 460 470 480 QFPTAFEFNE YFLITILDHL YSCLFGTFLC NSEQQRGKEN LPKRTVSLWS YINSQLEDFT 490 500 510 520 530 540 NPLYGSYSNH VLYPVASMRH LELWVGYYIR WNPRMKPQEP IHNRYKELLA KRAELQKKVE 550 560 570 ELQREISNRS TSSSERASSP AQCVTPVQTV V

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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.
[14]	"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.
[15]	"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, MASS SPECTROMETRY, MUTAGENESIS OF CYS-417; ASP-419 AND ASP-422.
[16]	"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, MASS SPECTROMETRY, MUTAGENESIS OF CYS-417.
[17]	"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.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

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.

IPI

IPI00014307.
IPI00398737.

PIR

T09497.

RefSeq

NP_001230500.1. NM_001243571.1.
NP_057240.3. NM_016156.5.
NP_958435.1. NM_201278.2.
NP_958438.1. NM_201281.2.

UniGene

Hs.181326.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LW3	X-ray	2.30	A	1-643	[»]
1M7R	X-ray	2.60	A/B	1-643	[»]
1ZSQ	X-ray	1.82	A	73-586	[»]
1ZVR	X-ray	1.98	A	73-586	[»]

ProteinModelPortal

Q13614.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13614. 4 interactions.

MINT

MINT-6774021.

STRING

9606.ENSP00000345752.

PTM databases

PhosphoSite

Q13614.

Polymorphism databases

DMDM

212276520.

Proteomic databases

PaxDb

Q13614.

PRIDE

Q13614.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346299; ENSP00000345752; ENSG00000087053.
ENST00000352297; ENSP00000343737; ENSG00000087053.
ENST00000393223; ENSP00000376915; ENSG00000087053.
ENST00000409459; ENSP00000386882; ENSG00000087053.

GeneID

8898.

KEGG

hsa:8898.

UCSC

uc001pfs.3. human.

Organism-specific databases

CTD

8898.

GeneCards

GC11M095566.

HGNC

HGNC:7450. MTMR2.

MIM

601382. phenotype.
603557. gene.

neXtProt

NX_Q13614.

Orphanet

99955. Charcot-Marie-Tooth disease type 4B1.

PharmGKB

PA31253.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

NOG322789.

HOGENOM

HOG000210598.

HOVERGEN

HBG000220.

InParanoid

Q13614.

KO

K01112.

OMA

PENGWKV.

OrthoDB

EOG4GMTWP.

PhylomeDB

Q13614.

Enzyme and pathway databases

BRENDA

3.1.3.64. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q13614.

Bgee

Q13614.

CleanEx

HS_MTMR2.

Genevestigator

Q13614.

GermOnline

ENSG00000087053. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR004182. GRAM.
IPR010569. Myotub-related.
IPR017906. Myotubularin_phosphatase_dom.
IPR011993. PH_like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

Pfam

PF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]

SMART

SM00568. GRAM. 1 hit.
[Graphical view]

PROSITE

PS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

MTMR2. human.

EvolutionaryTrace

Q13614.

GenomeRNAi

8898.

NextBio

33423.

SOURCE

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Entry information

Entry name

MTMR2_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 138 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.