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Q13496

- MTM1_HUMAN

UniProt

Q13496 - MTM1_HUMAN

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Protein

Myotubularin

Gene

MTM1

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

Functioni

Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis.6 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.4 Publications
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.1 Publication

Enzyme regulationi

Allosterically activated by phosphatidylinositol 5-phosphate (PI5P).1 Publication

Kineticsi

  1. KM=39 µM for PI3P1 Publication
  2. KM=17 µM for PI(3,5)P21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei375 – 3751Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. intermediate filament binding Source: UniProtKB
  2. phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
  3. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  4. phosphatidylinositol binding Source: UniProtKB
  5. phosphoprotein phosphatase activity Source: UniProtKB
  6. protein tyrosine phosphatase activity Source: InterPro

GO - Biological processi

  1. endosome to lysosome transport Source: UniProtKB
  2. intermediate filament organization Source: UniProtKB
  3. mitochondrion distribution Source: UniProtKB
  4. mitochondrion morphogenesis Source: UniProtKB
  5. phosphatidylinositol biosynthetic process Source: Reactome
  6. phosphatidylinositol dephosphorylation Source: UniProtKB
  7. phospholipid metabolic process Source: Reactome
  8. protein dephosphorylation Source: UniProtKB
  9. protein transport Source: UniProtKB-KW
  10. regulation of vacuole organization Source: UniProtKB
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Lipid metabolism, Protein transport, Transport

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.
REACT_121025. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin
Alternative name(s):
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.951 Publication)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.644 Publications)
Gene namesi
Name:MTM1
Synonyms:CG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7448. MTM1.

Subcellular locationi

Cytoplasm 2 Publications. Cell membrane; Peripheral membrane protein 1 Publication. Cell projectionfilopodium 1 Publication. Cell projectionruffle 1 Publication. Late endosome 1 Publication
Note: Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles. Predominantly located in the cytoplasm following interaction with MTMR12. Recruited to the late endosome following EGF stimulation.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. filopodium Source: UniProtKB
  5. late endosome Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopathy, centronuclear, X-linked (CNMX) [MIM:310400]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.12 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471Missing in CNMX. 1 Publication
VAR_006386
Natural varianti49 – 491V → F in CNMX; greatly reduced binding to PI(3,5)P2; does not translocate to the late endosome following EGF stimulation; shows normal EGFR degradation. 1 Publication
VAR_018227
Natural varianti68 – 681Y → D in CNMX. 1 Publication
VAR_018228
Natural varianti69 – 691R → C in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2. 3 Publications
VAR_006387
Natural varianti69 – 691R → P in CNMX. 1 Publication
VAR_018229
Natural varianti69 – 691R → S in CNMX; severe. 1 Publication
VAR_018230
Natural varianti70 – 701L → F in CNMX; mild; reduced binding to PI(3,5)P2. 2 Publications
VAR_006388
Natural varianti87 – 871L → P in CNMX; mild; reduced binding to PI(3,5)P2. 1 Publication
VAR_006389
Natural varianti157 – 1571E → K in CNMX. 1 Publication
VAR_018231
Natural varianti179 – 1791P → S in CNMX; mild. 2 Publications
VAR_009217
Natural varianti180 – 1801N → K in CNMX; very mild. 1 Publication
VAR_018232
Natural varianti184 – 1841R → G in CNMX; severe; loss of activity; abolishes interaction with DES. 1 Publication
VAR_006390
Natural varianti184 – 1841R → L in CNMX; reduced activity and response to PI5P. 1 Publication
VAR_018233
Natural varianti186 – 1861T → I in CNMX. 1 Publication
VAR_018234
Natural varianti189 – 1891N → S in CNMX. 1 Publication
VAR_006391
Natural varianti197 – 1971T → I in CNMX. 1 Publication
VAR_018235
Natural varianti198 – 1981Y → N in CNMX; severe. 1 Publication
VAR_006392
Natural varianti199 – 1991P → S in CNMX. 1 Publication
VAR_018236
Natural varianti202 – 2021L → S in CNMX; severe. 1 Publication
VAR_018237
Natural varianti205 – 2051P → L in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES. 4 Publications
VAR_006393
Natural varianti225 – 2251I → T in CNMX; mild. 2 Publications
VAR_009218
Natural varianti226 – 2261P → T in CNMX. 1 Publication
VAR_018238
Natural varianti227 – 2271V → M in CNMX. 1 Publication
VAR_018239
Natural varianti228 – 2281L → P in CNMX. 1 Publication
VAR_018240
Natural varianti229 – 2291S → P in CNMX; mild. 1 Publication
VAR_006394
Natural varianti230 – 2301W → C in CNMX. 2 Publications
VAR_018241
Natural varianti232 – 2321H → R in CNMX. 1 Publication
VAR_018242
Natural varianti241 – 2411R → C in CNMX; mild to moderate; abolishes interaction with DES. 5 Publications
VAR_006395
Natural varianti241 – 2411R → L in CNMX; severe; loss of activity. 1 Publication
VAR_006396
Natural varianti264 – 2641I → S in CNMX; severe. 1 Publication
VAR_009219
Natural varianti279 – 2791A → G in CNMX. 1 Publication
VAR_018243
Natural varianti294 – 2941Missing in CNMX; mild. 1 Publication
VAR_009220
Natural varianti317 – 3171M → R in CNMX; mild. 1 Publication
VAR_006397
Natural varianti346 – 3461W → C in CNMX; mild. 1 Publication
VAR_018244
Natural varianti346 – 3461W → S in CNMX.
VAR_018245
Natural varianti364 – 3641V → G in CNMX. 1 Publication
VAR_018246
Natural varianti374 – 3741H → D in CNMX.
VAR_018247
Natural varianti376 – 3761S → N in CNMX; dramatic decrease in phosphatase activity. 1 Publication
VAR_006398
Natural varianti378 – 3781G → E in CNMX. 1 Publication
VAR_018248
Natural varianti378 – 3781G → R in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation. 4 Publications
VAR_006399
Natural varianti387 – 3871S → Y in CNMX. 1 Publication
VAR_068846
Natural varianti389 – 3891A → D in CNMX; severe. 1 Publication
VAR_018249
Natural varianti391 – 3911L → P in CNMX. 1 Publication
VAR_018250
Natural varianti397 – 3971Y → C in CNMX; severe; dramatic decrease in phosphatase activity. 4 Publications
VAR_006400
Natural varianti402 – 4021G → A in CNMX; mild. 1 Publication
VAR_006401
Natural varianti402 – 4021G → R in CNMX. 3 Publications
VAR_018251
Natural varianti402 – 4021G → V in CNMX. 1 Publication
VAR_018252
Natural varianti404 – 4041E → K in CNMX; mild. 2 Publications
VAR_006402
Natural varianti406 – 4061L → P in CNMX; severe. 1 Publication
VAR_006403
Natural varianti411 – 4111W → C in CNMX.
VAR_018253
Natural varianti420 – 4201S → SFIQ in CNMX; severe.
VAR_009221
Natural varianti421 – 4211R → Q in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES. 4 Publications
VAR_006404
Natural varianti421 – 4211R → RFIQ in CNMX; severe.
VAR_006405
Natural varianti431 – 4311D → N in CNMX. 1 Publication
VAR_006406
Natural varianti433 – 4331D → N in CNMX. 1 Publication
VAR_006407
Natural varianti444 – 4441C → Y in CNMX. 1 Publication
VAR_018254
Natural varianti469 – 4691H → P in CNMX; loss of activity. 2 Publications
VAR_006408
Natural varianti470 – 4701L → P in CNMX; severe. 1 Publication
VAR_018255
Natural varianti481 – 4811N → Y in CNMX; mild. 1 Publication
VAR_018256
Natural varianti499 – 4991W → R in CNMX; mild. 1 Publication
VAR_006409
Natural varianti510 – 5101K → N in CNMX; severe. 1 Publication
VAR_009222

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141K → A: Reduced response to PI5P. 1 Publication
Mutagenesisi181 – 1811H → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
Mutagenesisi206 – 2061Y → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
Mutagenesisi209 – 2091S → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
Mutagenesisi220 – 2201R → A: Loss of activity. 1 Publication
Mutagenesisi255 – 2551K → A: Disrupts interaction with DES. 1 Publication
Mutagenesisi257 – 2571D → A: No effect on subcellular location. 1 Publication
Mutagenesisi269 – 2691K → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
Mutagenesisi278 – 2781D → A: Localizes to plasma membrane extensions. Does not affect interaction with DES. 3 Publications
Mutagenesisi375 – 3751C → A: No effect on subcellular location. 5 Publications
Mutagenesisi375 – 3751C → S: Lacks activity toward PI3P. Does not affect interaction with DES. 5 Publications
Mutagenesisi377 – 3771D → A: No effect on subcellular location. 2 Publications
Mutagenesisi380 – 3801D → A: Does not affect interaction with DES. 3 Publications
Mutagenesisi394 – 3941D → A: Produces an unstable protein. 1 Publication
Mutagenesisi410 – 4101E → A: Produces an unstable protein. 1 Publication
Mutagenesisi420 – 4201S → D: Does not affect interaction with DES. 1 Publication
Mutagenesisi443 – 4431D → A: Produces an unstable protein. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi310400. phenotype.
Orphaneti596. X-linked centronuclear myopathy.
PharmGKBiPA31251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603MyotubularinPRO_0000094930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei495 – 4951Phosphothreonine1 Publication
Modified residuei588 – 5881Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13496.
PaxDbiQ13496.
PRIDEiQ13496.

PTM databases

PhosphoSiteiQ13496.

Expressioni

Gene expression databases

BgeeiQ13496.
CleanExiHS_MTM1.
ExpressionAtlasiQ13496. baseline and differential.
GenevestigatoriQ13496.

Organism-specific databases

HPAiHPA010008.
HPA010665.

Interactioni

Subunit structurei

Interacts with MTMR12; the interaction modulates MTM1 intracellular localization. Interacts with KMT2A/MLL1 (via SET domain). Interacts with DES in skeletal muscle but not in cardiac muscle. Interacts with SPEG.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIN1O004996EBI-2864109,EBI-719094
DESP1766113EBI-2864109,EBI-1055572
DesP310014EBI-2864109,EBI-298565From a different organism.
MTMR12Q9C0I14EBI-2864109,EBI-2829520

Protein-protein interaction databases

BioGridi110630. 3 interactions.
IntActiQ13496. 6 interactions.
STRINGi9606.ENSP00000359423.

Structurei

3D structure databases

ProteinModelPortaliQ13496.
SMRiQ13496. Positions 33-543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 9769GRAMAdd
BLAST
Domaini163 – 538376Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Domaini

The GRAM domain mediates binding to PI(3,5)P2 and, with lower affinity, to other phosphoinositides.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiQ13496.
KOiK01108.
OMAiQGLPNHH.
PhylomeDBiQ13496.
TreeFamiTF315197.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
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: Q13496-1) [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
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI
60 70 80 90 100
YICPFNGPIK GRVYITNYRL YLRSLETDSS LILDVPLGVI SRIEKMGGAT
110 120 130 140 150
SRGENSYGLD ITCKDMRNLR FALKQEGHSR RDMFEILTRY AFPLAHSLPL
160 170 180 190 200
FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRITFINK CYELCDTYPA
210 220 230 240 250
LLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV RCSQPLVGMS
260 270 280 290 300
GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA
310 320 330 340 350
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI
360 370 380 390 400
KLVLTGAIQV ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI
410 420 430 440 450
EGFEILVQKE WISFGHKFAS RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK
460 470 480 490 500
QFPTAFEFNE QFLIIILDHL YSCRFGTFLF NCESARERQK VTERTVSLWS
510 520 530 540 550
LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRIKQQQP
560 570 580 590 600
NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ

THF
Length:603
Mass (Da):69,932
Last modified:July 15, 1998 - v2
Checksum:iBE9770F2471957C0
GO
Isoform 2 (identifier: Q13496-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-114: Missing.

Note: No experimental confirmation available.

Show »
Length:566
Mass (Da):66,053
Checksum:i237719B8DEB99D1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101E → K in AAH30779. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471Missing in CNMX. 1 Publication
VAR_006386
Natural varianti49 – 491V → F in CNMX; greatly reduced binding to PI(3,5)P2; does not translocate to the late endosome following EGF stimulation; shows normal EGFR degradation. 1 Publication
VAR_018227
Natural varianti68 – 681Y → D in CNMX. 1 Publication
VAR_018228
Natural varianti69 – 691R → C in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2. 3 Publications
VAR_006387
Natural varianti69 – 691R → P in CNMX. 1 Publication
VAR_018229
Natural varianti69 – 691R → S in CNMX; severe. 1 Publication
VAR_018230
Natural varianti70 – 701L → F in CNMX; mild; reduced binding to PI(3,5)P2. 2 Publications
VAR_006388
Natural varianti87 – 871L → P in CNMX; mild; reduced binding to PI(3,5)P2. 1 Publication
VAR_006389
Natural varianti157 – 1571E → K in CNMX. 1 Publication
VAR_018231
Natural varianti179 – 1791P → S in CNMX; mild. 2 Publications
VAR_009217
Natural varianti180 – 1801N → K in CNMX; very mild. 1 Publication
VAR_018232
Natural varianti184 – 1841R → G in CNMX; severe; loss of activity; abolishes interaction with DES. 1 Publication
VAR_006390
Natural varianti184 – 1841R → L in CNMX; reduced activity and response to PI5P. 1 Publication
VAR_018233
Natural varianti186 – 1861T → I in CNMX. 1 Publication
VAR_018234
Natural varianti189 – 1891N → S in CNMX. 1 Publication
VAR_006391
Natural varianti197 – 1971T → I in CNMX. 1 Publication
VAR_018235
Natural varianti198 – 1981Y → N in CNMX; severe. 1 Publication
VAR_006392
Natural varianti199 – 1991P → S in CNMX. 1 Publication
VAR_018236
Natural varianti202 – 2021L → S in CNMX; severe. 1 Publication
VAR_018237
Natural varianti205 – 2051P → L in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES. 4 Publications
VAR_006393
Natural varianti225 – 2251I → T in CNMX; mild. 2 Publications
VAR_009218
Natural varianti226 – 2261P → T in CNMX. 1 Publication
VAR_018238
Natural varianti227 – 2271V → M in CNMX. 1 Publication
VAR_018239
Natural varianti228 – 2281L → P in CNMX. 1 Publication
VAR_018240
Natural varianti229 – 2291S → P in CNMX; mild. 1 Publication
VAR_006394
Natural varianti230 – 2301W → C in CNMX. 2 Publications
VAR_018241
Natural varianti232 – 2321H → R in CNMX. 1 Publication
VAR_018242
Natural varianti241 – 2411R → C in CNMX; mild to moderate; abolishes interaction with DES. 5 Publications
VAR_006395
Natural varianti241 – 2411R → L in CNMX; severe; loss of activity. 1 Publication
VAR_006396
Natural varianti264 – 2641I → S in CNMX; severe. 1 Publication
VAR_009219
Natural varianti279 – 2791A → G in CNMX. 1 Publication
VAR_018243
Natural varianti294 – 2941Missing in CNMX; mild. 1 Publication
VAR_009220
Natural varianti317 – 3171M → R in CNMX; mild. 1 Publication
VAR_006397
Natural varianti346 – 3461W → C in CNMX; mild. 1 Publication
VAR_018244
Natural varianti346 – 3461W → S in CNMX.
VAR_018245
Natural varianti364 – 3641V → G in CNMX. 1 Publication
VAR_018246
Natural varianti374 – 3741H → D in CNMX.
VAR_018247
Natural varianti376 – 3761S → N in CNMX; dramatic decrease in phosphatase activity. 1 Publication
VAR_006398
Natural varianti378 – 3781G → E in CNMX. 1 Publication
VAR_018248
Natural varianti378 – 3781G → R in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation. 4 Publications
VAR_006399
Natural varianti387 – 3871S → Y in CNMX. 1 Publication
VAR_068846
Natural varianti389 – 3891A → D in CNMX; severe. 1 Publication
VAR_018249
Natural varianti391 – 3911L → P in CNMX. 1 Publication
VAR_018250
Natural varianti397 – 3971Y → C in CNMX; severe; dramatic decrease in phosphatase activity. 4 Publications
VAR_006400
Natural varianti402 – 4021G → A in CNMX; mild. 1 Publication
VAR_006401
Natural varianti402 – 4021G → R in CNMX. 3 Publications
VAR_018251
Natural varianti402 – 4021G → V in CNMX. 1 Publication
VAR_018252
Natural varianti404 – 4041E → K in CNMX; mild. 2 Publications
VAR_006402
Natural varianti406 – 4061L → P in CNMX; severe. 1 Publication
VAR_006403
Natural varianti411 – 4111W → C in CNMX.
VAR_018253
Natural varianti420 – 4201S → SFIQ in CNMX; severe.
VAR_009221
Natural varianti421 – 4211R → Q in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES. 4 Publications
VAR_006404
Natural varianti421 – 4211R → RFIQ in CNMX; severe.
VAR_006405
Natural varianti431 – 4311D → N in CNMX. 1 Publication
VAR_006406
Natural varianti433 – 4331D → N in CNMX. 1 Publication
VAR_006407
Natural varianti444 – 4441C → Y in CNMX. 1 Publication
VAR_018254
Natural varianti469 – 4691H → P in CNMX; loss of activity. 2 Publications
VAR_006408
Natural varianti470 – 4701L → P in CNMX; severe. 1 Publication
VAR_018255
Natural varianti481 – 4811N → Y in CNMX; mild. 1 Publication
VAR_018256
Natural varianti499 – 4991W → R in CNMX; mild. 1 Publication
VAR_006409
Natural varianti510 – 5101K → N in CNMX; severe. 1 Publication
VAR_009222

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 11437Missing in isoform 2. 1 PublicationVSP_056208Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46024 mRNA. Translation: AAC51682.1.
AF020676
, AF020664, AF020665, AF020666, AF020667, AF020668, AF020669, AF020670, AF020671, AF020672, AF020673, AF020674, AF020675 Genomic DNA. Translation: AAC12865.1.
AK297021 mRNA. Translation: BAH12477.1.
AC109994 Genomic DNA. No translation available.
AF002223 Genomic DNA. No translation available.
CH471169 Genomic DNA. Translation: EAW99377.1.
BC030779 mRNA. Translation: AAH30779.1.
CCDSiCCDS14694.1. [Q13496-1]
RefSeqiNP_000243.1. NM_000252.2.
XP_005274744.1. XM_005274687.1.
UniGeneiHs.655056.

Genome annotation databases

EnsembliENST00000370396; ENSP00000359423; ENSG00000171100. [Q13496-1]
GeneIDi4534.
KEGGihsa:4534.
UCSCiuc004fef.4. human. [Q13496-1]

Polymorphism databases

DMDMi2851537.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Leiden Muscular Dystrophy pages, Myotubularin 1 (MTM1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46024 mRNA. Translation: AAC51682.1 .
AF020676
, AF020664 , AF020665 , AF020666 , AF020667 , AF020668 , AF020669 , AF020670 , AF020671 , AF020672 , AF020673 , AF020674 , AF020675 Genomic DNA. Translation: AAC12865.1 .
AK297021 mRNA. Translation: BAH12477.1 .
AC109994 Genomic DNA. No translation available.
AF002223 Genomic DNA. No translation available.
CH471169 Genomic DNA. Translation: EAW99377.1 .
BC030779 mRNA. Translation: AAH30779.1 .
CCDSi CCDS14694.1. [Q13496-1 ]
RefSeqi NP_000243.1. NM_000252.2.
XP_005274744.1. XM_005274687.1.
UniGenei Hs.655056.

3D structure databases

ProteinModelPortali Q13496.
SMRi Q13496. Positions 33-543.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110630. 3 interactions.
IntActi Q13496. 6 interactions.
STRINGi 9606.ENSP00000359423.

PTM databases

PhosphoSitei Q13496.

Polymorphism databases

DMDMi 2851537.

Proteomic databases

MaxQBi Q13496.
PaxDbi Q13496.
PRIDEi Q13496.

Protocols and materials databases

DNASUi 4534.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370396 ; ENSP00000359423 ; ENSG00000171100 . [Q13496-1 ]
GeneIDi 4534.
KEGGi hsa:4534.
UCSCi uc004fef.4. human. [Q13496-1 ]

Organism-specific databases

CTDi 4534.
GeneCardsi GC0XP149738.
GeneReviewsi MTM1.
HGNCi HGNC:7448. MTM1.
HPAi HPA010008.
HPA010665.
MIMi 300415. gene.
310400. phenotype.
neXtProti NX_Q13496.
Orphaneti 596. X-linked centronuclear myopathy.
PharmGKBi PA31251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322789.
GeneTreei ENSGT00760000118832.
HOGENOMi HOG000210598.
HOVERGENi HBG000220.
InParanoidi Q13496.
KOi K01108.
OMAi QGLPNHH.
PhylomeDBi Q13496.
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.
REACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSi MTM1. human.
GeneWikii Myotubularin_1.
GenomeRNAii 4534.
NextBioi 17492.
PROi Q13496.
SOURCEi Search...

Gene expression databases

Bgeei Q13496.
CleanExi HS_MTM1.
ExpressionAtlasi Q13496. baseline and differential.
Genevestigatori Q13496.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
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. "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] (ISOFORM 1).
  2. "Genomic organization of the MTM1 gene implicated in X-linked myotubular myopathy."
    Laporte J., Guiraud-Chaumeil C., Tanner S.M., Blondeau F., Hu L.J., Vicaire S., Liechti-Gallati S., Mandel J.-L.
    Eur. J. Hum. Genet. 6:325-330(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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: Umbilical cord blood.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Tissue: Testis.
  7. "Association of SET domain and myotubularin-related proteins modulates growth control."
    Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.
    Nat. Genet. 18:331-337(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KMT2A/MLL1.
  8. Cited for: REVIEW ON VARIANTS CNMX.
  9. "Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway."
    Blondeau F., Laporte J., Bodin S., Superti-Furga G., Payrastre B., Mandel J.L.
    Hum. Mol. Genet. 9:2223-2229(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-278; CYS-375; ASP-377; ASP-380; ASP-394; GLU-410 AND ASP-443.
  10. "Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate."
    Taylor G.S., Maehama T., Dixon J.E.
    Proc. Natl. Acad. Sci. U.S.A. 97:8910-8915(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS LEU-205; LEU-241; ASN-376; ARG-378 AND CYS-397, MUTAGENESIS OF CYS-375.
  11. "The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles."
    Laporte J., Blondeau F., Gansmuller A., Lutz Y., Vonesch J.L., Mandel J.L.
    J. Cell Sci. 115:3105-3117(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-257; ASP-278; CYS-375; ASP-377 AND ASP-380.
  12. "Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases."
    Schaletzky J., Dove S.K., Short B., Lorenzo O., Clague M.J., Barr F.A.
    Curr. Biol. 13:504-509(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, CHARACTERIZATION OF VARIANTS CYS-69; GLY-184; LEU-241; GLN-421 AND PRO-469, MUTAGENESIS OF LYS-114; ARG-220 AND CYS-375.
  13. "Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP."
    Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L., Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INTERACTION WITH MTMR12, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction."
    Tsujita K., Itoh T., Ijuin T., Yamamoto A., Shisheva A., Laporte J., Takenawa T.
    J. Biol. Chem. 279:13817-13824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, ROLE OF GRAM DOMAIN, CHARACTERIZATION OF VARIANTS PHE-49; CYS-69; PHE-70 AND PRO-87.
  15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle."
    Hnia K., Tronchere H., Tomczak K.K., Amoasii L., Schultz P., Beggs A.H., Payrastre B., Mandel J.L., Laporte J.
    J. Clin. Invest. 121:70-85(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DES, CHARACTERIZATION OF VARIANTS GLY-184; LEU-205; CYS-241 AND GLN-421, MUTAGENESIS OF HIS-181; TYR-206; SER-209; LYS-255; LYS-269; ASP-278; CYS-375; ASP-380 AND SER-420.
  20. Cited for: INTERACTION WITH SPEG.
  21. "Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy."
    de Gouyon B.M., Zhao W., Laporte J., Mandel J.-L., Metzenberg A., Herman G.E.
    Hum. Mol. Genet. 6:1499-1504(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CNMX CYS-69; GLY-184; ASN-198; LEU-241; ARG-317; CYS-397; LYS-404; PRO-406; GLN-421 AND ARG-499.
  22. Cited for: VARIANTS CNMX CYS-69; PHE-70; PRO-87; SER-189; LEU-205; PRO-229; CYS-241; ASN-376; ARG-378; CYS-397; ALA-402; GLN-421; ASN-431; ASN-433 AND PRO-469.
  23. "MTM1 gene mutations in Japanese patients with the severe infantile form of myotubular myopathy."
    Nishino I., Minami N., Kobayashi O., Ikezawa M., Goto Y., Arahata K., Nonaka I.
    Neuromuscul. Disord. 8:453-458(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CNMX VAL-402.
  24. "Germline mosaicism in X-linked myotubular myopathy."
    Haene B.G., Rogers R.C., Schwartz C.E.
    Clin. Genet. 56:77-81(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CNMX GLU-378.
  25. "Identification of novel mutations in the MTM1 gene causing severe and mild forms of X-linked myotubular myopathy."
    Buj-Bello A., Biancalana V., Moutou C., Laporte J., Mandel J.-L.
    Hum. Mutat. 14:320-325(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CNMX SER-179; THR-225; CYS-241; SER-264; GLY-294 DEL; ARG-378 AND ASN-510.
  26. "Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients."
    Tanner S.M., Schneider V., Thomas N.S.T., Clarke A., Lazarou L., Liechti-Gallati S.
    Neuromuscul. Disord. 9:41-49(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CNMX LEU-205; THR-225; CYS-230; ARG-232; CYS-241; ARG-402 AND TYR-444.
  27. "Characterization of mutations in fifty North American patients with X-linked myotubular myopathy."
    Herman G.E., Kopacz K., Zhao W., Mills P.L., Metzenberg A., Das S.
    Hum. Mutat. 19:114-121(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CNMX PHE-49; CYS-69; SER-179; ILE-186; LEU-205; MET-227; PRO-228; CYS-241; GLY-279; ARG-378; PRO-391; CYS-397; ARG-402 AND GLN-421.
  28. "Rapid scanning of myotubularin (MTM1) gene by denaturing high-performance liquid chromatography (DHPLC)."
    Flex E., De Luca A., D'Apice M.R., Buccino A., Dallapiccola B., Novelli G.
    Neuromuscul. Disord. 12:501-505(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CNMX ILE-197; SER-199; ARG-378 AND ARG-402.
  29. "X-linked myotubular myopathy in a family with three adult survivors."
    Yu S., Manson J., White S., Bourne A., Waddy H., Davis M., Haan E.
    Clin. Genet. 64:148-152(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CNMX LYS-157.
  30. "Characterisation of mutations in 77 patients with X-linked myotubular myopathy, including a family with a very mild phenotype."
    Biancalana V., Caron O., Gallati S., Baas F., Kress W., Novelli G., D'Apice M.R., Lagier-Tourenne C., Buj-Bello A., Romero N.B., Mandel J.-L.
    Hum. Genet. 112:135-142(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CNMX LYS-47 DEL; ASP-68; PRO-69; SER-69; PHE-70; LYS-180; LEU-184; SER-202; LEU-205; THR-226; CYS-230; CYS-241; CYS-346; GLY-364; ASP-389; CYS-397; GLN-421; PRO-469; PRO-470 AND TYR-481.
  31. "Extreme phenotypic variability in a German family with X-linked myotubular myopathy associated with E404K mutation in MTM1."
    Hoffjan S., Thiels C., Vorgerd M., Neuen-Jacob E., Epplen J.T., Kress W.
    Neuromuscul. Disord. 16:749-753(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CNMX LYS-404.
  32. "X-linked myotubular myopathy with a novel MTM1 mutation in a Taiwanese child."
    Chang C.Y., Lin S.P., Lin H.Y., Chuang C.K., Ho C.S., Su Y.N.
    J. Formos. Med. Assoc. 107:965-970(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CNMX TYR-387.

Entry informationi

Entry nameiMTM1_HUMAN
AccessioniPrimary (citable) accession number: Q13496
Secondary accession number(s): A6NDB1
, B7Z491, F2Z330, Q8NEL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: October 29, 2014
This is version 138 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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