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Q13614

- MTMR2_HUMAN

UniProt

Q13614 - MTMR2_HUMAN

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Protein

Myotubularin-related protein 2

Gene

MTMR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.2 Publications
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.1 Publication

Enzyme regulationi

Interaction with SBF1 increases phosphatase activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei417 – 4171Phosphocysteine intermediate
Binding sitei463 – 4631Substrate

GO - Molecular functioni

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

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. dendritic spine maintenance Source: BHF-UCL
  3. inositol phosphate dephosphorylation Source: Ensembl
  4. myelin assembly Source: Ensembl
  5. negative regulation of endocytosis Source: BHF-UCL
  6. negative regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  7. negative regulation of myelination Source: Ensembl
  8. negative regulation of receptor catabolic process Source: BHF-UCL
  9. negative regulation of receptor internalization Source: BHF-UCL
  10. neuron development Source: Ensembl
  11. phosphatidylinositol biosynthetic process Source: Reactome
  12. phosphatidylinositol dephosphorylation Source: UniProtKB
  13. phospholipid metabolic process Source: Reactome
  14. positive regulation of early endosome to late endosome transport Source: BHF-UCL
  15. protein dephosphorylation Source: UniProtKB
  16. protein tetramerization Source: Ensembl
  17. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.3.64. 2681.
ReactomeiREACT_120756. Synthesis of PIPs at the early endosome membrane.
REACT_120918. Synthesis of PIPs at the late endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 2
Alternative name(s):
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.951 Publication)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.642 Publications)
Gene namesi
Name:MTMR2
Synonyms:KIAA1073
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7450. MTMR2.

Subcellular locationi

Cytoplasm 2 Publications. Early endosome membrane 1 Publication; Peripheral membrane protein 1 Publication
Note: Partly associated with membranes.2 PublicationsCurated

GO - Cellular componenti

  1. axon Source: BHF-UCL
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. dendrite Source: BHF-UCL
  5. dendritic spine Source: BHF-UCL
  6. endosome Source: UniProtKB-KW
  7. neuronal postsynaptic density Source: BHF-UCL
  8. nucleus Source: UniProtKB
  9. synaptic membrane Source: BHF-UCL
  10. synaptic vesicle Source: BHF-UCL
  11. vacuolar membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

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 CMT4.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti283 – 2831R → W in CMT4B1. 1 Publication
VAR_047947

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi417 – 4171C → S: Loss of activity. 2 Publications
Mutagenesisi419 – 4191D → A: No effect. 1 Publication
Mutagenesisi422 – 4221D → A: Loss of activity. 1 Publication
Mutagenesisi607 – 6071L → Y: Reduces homodimerization and interaction with SBF1. 1 Publication

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi601382. phenotype.
Orphaneti99955. Charcot-Marie-Tooth disease type 4B1.
PharmGKBiPA31253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643Myotubularin-related protein 2PRO_0000094934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei58 – 581Phosphoserine3 Publications

Post-translational modificationi

Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13614.
PaxDbiQ13614.
PRIDEiQ13614.

PTM databases

PhosphoSiteiQ13614.

Expressioni

Gene expression databases

BgeeiQ13614.
CleanExiHS_MTMR2.
ExpressionAtlasiQ13614. baseline and differential.
GenevestigatoriQ13614.

Organism-specific databases

HPAiHPA049831.

Interactioni

Subunit structurei

Homooligomer and heterooligomer. Interacts with SBF1 and SBF2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NEFLP071962EBI-475631,EBI-475646

Protein-protein interaction databases

BioGridi114415. 13 interactions.
IntActiQ13614. 5 interactions.
MINTiMINT-6774021.
STRINGi9606.ENSP00000345752.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi84 – 9512
Turni96 – 983
Beta strandi99 – 12123
Beta strandi123 – 1286
Helixi129 – 1313
Beta strandi132 – 1387
Beta strandi145 – 1473
Beta strandi149 – 1557
Turni156 – 1583
Beta strandi159 – 1646
Helixi167 – 1693
Helixi172 – 18211
Turni185 – 1895
Helixi193 – 1953
Helixi205 – 2073
Helixi211 – 2177
Beta strandi223 – 2286
Turni230 – 2334
Beta strandi234 – 2363
Beta strandi242 – 2476
Helixi252 – 26110
Helixi263 – 2653
Beta strandi269 – 2735
Turni275 – 2773
Beta strandi280 – 2845
Turni290 – 2934
Helixi297 – 30913
Beta strandi310 – 3123
Beta strandi314 – 3207
Helixi324 – 33310
Turni340 – 3423
Beta strandi346 – 3505
Helixi356 – 37015
Helixi376 – 3783
Helixi379 – 3868
Helixi388 – 40720
Beta strandi413 – 4164
Beta strandi418 – 4225
Helixi423 – 43513
Helixi437 – 4404
Helixi442 – 45211
Turni453 – 4575
Helixi460 – 4645
Turni465 – 4673
Helixi479 – 49315
Turni495 – 4973
Helixi502 – 51413
Beta strandi516 – 5183
Beta strandi522 – 5243
Helixi525 – 5306
Helixi533 – 5364
Helixi540 – 5456
Helixi548 – 5514
Turni554 – 5574
Beta strandi560 – 5623
Turni570 – 5723
Helixi577 – 5804

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LW3X-ray2.30A1-643[»]
1M7RX-ray2.60A/B1-643[»]
1ZSQX-ray1.82A73-586[»]
1ZVRX-ray1.98A73-586[»]
ProteinModelPortaliQ13614.
SMRiQ13614. Positions 73-585.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13614.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 13972GRAMAdd
BLAST
Domaini205 – 580376Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni330 – 3334Substrate binding
Regioni355 – 3562Substrate binding
Regioni417 – 4237Substrate binding

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili593 – 627351 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 5350Ser-richAdd
BLAST

Domaini

The coiled-coil domain mediates interaction with SBF2.

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.
InParanoidiQ13614.
KOiK18081.
OMAiPENGWKV.
OrthoDBiEOG7XDBF9.
PhylomeDBiQ13614.
TreeFamiTF315197.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR004182. 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]
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13614-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEKSSSCESL GSQPAAARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI
60 70 80 90 100
STSADNFSPD LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA
110 120 130 140 150
VRGTLTVTNY RLYFKSMERD PPFVLDASLG VINRVEKIGG ASSRGENSYG
160 170 180 190 200
LETVCKDIRN LRFAHKPEGR TRRSIFENLM KYAFPVSNNL PLFAFEYKEV
210 220 230 240 250
FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY PALLVVPANI
260 270 280 290 300
PDEELKRVAS FRSRGRIPVL SWIHPESQAT ITRCSQPMVG VSGKRSKEDE
310 320 330 340 350
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF
360 370 380 390 400
LDIHNIHVMR ESLRKLKEIV YPNIEETHWL SNLESTHWLE HIKLILAGAL
410 420 430 440 450
RIADKVESGK TSVVVHCSDG WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE
460 470 480 490 500
KEWLSFGHRF QLRVGHGDKN HADADRSPVF LQFIDCVWQM TRQFPTAFEF
510 520 530 540 550
NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKRTVSL WSYINSQLED
560 570 580 590 600
FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHNRYKEL
610 620 630 640
LAKRAELQKK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV
Length:643
Mass (Da):73,381
Last modified:November 4, 2008 - v4
Checksum:i10FD6508D0CDA719
GO
Isoform 2 (identifier: Q13614-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.

Show »
Length:571
Mass (Da):65,959
Checksum:iDBC304269CEFC843
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31K → T.2 Publications
Corresponds to variant rs3824874 [ dbSNP | Ensembl ].
VAR_047255
Natural varianti283 – 2831R → W in CMT4B1. 1 Publication
VAR_047947
Natural varianti545 – 5451N → S.
Corresponds to variant rs558018 [ dbSNP | Ensembl ].
VAR_047256

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_044933Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS8305.1. [Q13614-1]
CCDS8306.1. [Q13614-2]
PIRiT09497.
RefSeqiNP_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]
UniGeneiHs.181326.

Genome annotation databases

EnsembliENST00000346299; ENSP00000345752; ENSG00000087053. [Q13614-1]
ENST00000352297; ENSP00000343737; ENSG00000087053. [Q13614-2]
ENST00000393223; ENSP00000376915; ENSG00000087053. [Q13614-2]
ENST00000409459; ENSP00000386882; ENSG00000087053. [Q13614-2]
GeneIDi8898.
KEGGihsa:8898.
UCSCiuc001pfs.3. human. [Q13614-1]

Polymorphism databases

DMDMi212276520.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Inherited peripheral neuropathies mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS8305.1. [Q13614-1 ]
CCDS8306.1. [Q13614-2 ]
PIRi T09497.
RefSeqi NP_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 ]
UniGenei Hs.181326.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q13614.
SMRi Q13614. Positions 73-585.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114415. 13 interactions.
IntActi Q13614. 5 interactions.
MINTi MINT-6774021.
STRINGi 9606.ENSP00000345752.

PTM databases

PhosphoSitei Q13614.

Polymorphism databases

DMDMi 212276520.

Proteomic databases

MaxQBi Q13614.
PaxDbi Q13614.
PRIDEi Q13614.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346299 ; ENSP00000345752 ; ENSG00000087053 . [Q13614-1 ]
ENST00000352297 ; ENSP00000343737 ; ENSG00000087053 . [Q13614-2 ]
ENST00000393223 ; ENSP00000376915 ; ENSG00000087053 . [Q13614-2 ]
ENST00000409459 ; ENSP00000386882 ; ENSG00000087053 . [Q13614-2 ]
GeneIDi 8898.
KEGGi hsa:8898.
UCSCi uc001pfs.3. human. [Q13614-1 ]

Organism-specific databases

CTDi 8898.
GeneCardsi GC11M095566.
GeneReviewsi MTMR2.
HGNCi HGNC:7450. MTMR2.
HPAi HPA049831.
MIMi 601382. phenotype.
603557. gene.
neXtProti NX_Q13614.
Orphaneti 99955. Charcot-Marie-Tooth disease type 4B1.
PharmGKBi PA31253.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322789.
GeneTreei ENSGT00760000118832.
HOGENOMi HOG000210598.
HOVERGENi HBG000220.
InParanoidi Q13614.
KOi K18081.
OMAi PENGWKV.
OrthoDBi EOG7XDBF9.
PhylomeDBi Q13614.
TreeFami TF315197.

Enzyme and pathway databases

BRENDAi 3.1.3.64. 2681.
Reactomei REACT_120756. Synthesis of PIPs at the early endosome membrane.
REACT_120918. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

ChiTaRSi MTMR2. human.
EvolutionaryTracei Q13614.
GeneWikii MTMR2.
GenomeRNAii 8898.
NextBioi 33423.
PROi Q13614.
SOURCEi Search...

Gene expression databases

Bgeei Q13614.
CleanExi HS_MTMR2.
ExpressionAtlasi Q13614. baseline and differential.
Genevestigatori Q13614.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR004182. 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 ]
Pfami PF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view ]
SMARTi SM00568. GRAM. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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. Cited for: INVOLVEMENT IN CMT4B1.
  9. "Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth disease."
    Kim S.A., Taylor G.S., Torgersen K.M., Dixon J.E.
    J. Biol. Chem. 277:4526-4531(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  10. "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, CATALYTIC ACTIVITY, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-607, INTERACTION WITH SBF1.
  11. "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.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.

Entry informationi

Entry nameiMTMR2_HUMAN
AccessioniPrimary (citable) accession number: Q13614
Secondary accession number(s): A6NN98, Q9UPS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 4, 2008
Last modified: October 29, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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