Q9Z2C5

PR
Gene name
Mtm1
Protein name
Myotubularin
Names
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase, Phosphatidylinositol-3-phosphate phosphatase
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:17772
EC number
3.1.3.64: Phosphoric monoester hydrolases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-63 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9Z2C5

Entry ID Method Resolution Chain Position Source
AF-Q9Z2C5-F1 Predicted AlphaFoldDB

36 variants for Q9Z2C5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389558080 3 S>F No EVA
rs3410505119 37 R>Q No EVA
rs233060719 43 L>P No EVA
rs3410659995 46 E>D No EVA
rs1134563859 97 G>V No EVA
rs1133542676 99 A>T No EVA
rs1134304703 100 T>I No EVA
rs3411240467 152 A>T No EVA
rs3409361874 153 F>I No EVA
rs3409361821 153 F>Y No EVA
rs3410819570 154 V>A No EVA
rs3410506508 156 E>K No EVA
rs3389577330 164 W>* No EVA
rs3389555222 183 W>* No EVA
rs3389555222 183 W>S No EVA
rs3389574773 196 E>G No EVA
rs31685040 218 T>M No EVA
rs3409811058 228 L>V No EVA
rs3410871738 286 V>L No EVA
rs3409276419 309 L>F No EVA
rs3412670577 313 N>K No EVA
rs3389529140 351 K>N No EVA
rs3389555198 375 C>R No EVA
rs3409361899 418 F>I No EVA
rs3410820887 426 D>V No EVA
rs3410506498 426 D>Y No EVA
rs3410765528 427 K>* No EVA
rs3410506509 427 K>N No EVA
rs3410506485 428 N>H No EVA
rs3389574756 437 I>N No EVA
rs3389541943 446 W>L No EVA
rs3389555166 461 G>C No EVA
rs3410765607 496 V>A No EVA
rs3389557029 511 N>D No EVA
rs3389558085 538 Y>C No EVA
rs3389518426 564 R>H No EVA

No associated diseases with Q9Z2C5

5 regional properties for Q9Z2C5

Type Name Position InterPro Accession
domain Tyrosine-specific protein phosphatases domain 386 - 433 IPR000387
domain Protein-tyrosine phosphatase, catalytic 365 - 513 IPR003595
domain GRAM domain 65 - 185 IPR004182
domain Myotubularin-like, phosphatase domain 192 - 580 IPR010569
active_site Protein-tyrosine phosphatase, active site 415 - 425 IPR016130

Functions

Description
EC Number 3.1.3.64 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Peripheral membrane protein
  • Cell projection, filopodium
  • Cell projection, ruffle
  • Late endosome
  • Cytoplasm, myofibril, sarcomere
  • 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 (By similarity)
  • In skeletal muscles, co-localizes with MTMR12 in the sarcomere (PubMed:23818870)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
I band A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
late endosome A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.

5 GO annotations of molecular function

Name Definition
intermediate filament binding Binding to an intermediate filament, a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of higher eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space.
phosphatidylinositol binding Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = a 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate + 2 H+.
phosphatidylinositol-3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.

19 GO annotations of biological process

Name Definition
autophagosome assembly The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm.
endosome to lysosome transport The directed movement of substances from endosomes to lysosomes.
intermediate filament organization Control of the spatial distribution of intermediate filaments; includes organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
mitochondrion distribution Any process that establishes the spatial arrangement of mitochondria between and within cells.
mitochondrion morphogenesis The process in which the anatomical structures of a mitochondrion are generated and organized.
muscle cell cellular homeostasis The cellular homeostatic process that preserves a muscle cell in a stable functional or structural state.
negative regulation of autophagosome assembly Any process that stops, prevents or reduces the frequency, rate or extent of autophagosome assembly.
negative regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
negative regulation of protein kinase B signaling Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
negative regulation of TOR signaling Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
positive regulation of skeletal muscle tissue growth Any process that activates, maintains or increases the rate of skeletal muscle growth.
proteasome-mediated ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
protein kinase B signaling A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase B (also called AKT), which occurs as a result of a single trigger reaction or compound.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
regulation of vacuole organization Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a vacuole.
skeletal muscle tissue growth The increase in size or mass of a skeletal muscle. This may be due to a change in the fiber number or size.
TOR signaling The series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A6QLT4 MTM1 Myotubularin Bos taurus (Bovine) PR
Q13496 MTM1 Myotubularin Homo sapiens (Human) PR
Q9Z2C4 Mtmr1 Myotubularin-related protein 1 Mus musculus (Mouse) PR
Q9Z2D1 Mtmr2 Myotubularin-related protein 2 Mus musculus (Mouse) PR
Q9Z2C9 Mtmr7 Myotubularin-related protein 7 Mus musculus (Mouse) PR
Q5EB32 mtm1 Myotubularin Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MASASASKYN SHSLENESIK KVSQDGVSQD VSETVPRLPG ELLITEKEVI YICPFNGPIK
70 80 90 100 110 120
GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDLRNLR
130 140 150 160 170 180
FALKQEGHSR RDMFEILVKH AFPLAHNLPL FAFVNEEKFN VDGWTVYNPV EEYRRQGLPN
190 200 210 220 230 240
HHWRISFINK CYELCETYPA LLVVPYRTSD DDLRRIATFR SRNRLPVLSW IHPENKMVIM
250 260 270 280 290 300
RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ TSKLMIYDAR PSVNAVANKA TGGGYESDDA
310 320 330 340 350 360
YQNSELSFLD IHNIHVMRES LKKVKDIVYP NIEESHWLSS LESTHWLEHI KLVLTGAIQV
370 380 390 400 410 420
ADQVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRTI EGFEILVQKE WISFGHKFAS
430 440 450 460 470 480
RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE GFLITVLDHL YSCRFGTFLF
490 500 510 520 530 540
NCDSARERQK LTERTVSLWS LINSNKDKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR
550 560 570 580 590 600
WNPRVKQQQP NPVEQRYMEL LALRDDYIKR LEELQLANSA KLADAPASTS SSSQMVPHVQ
THF