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Q5R9S3 (MTM1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.

Enzyme regulation

Allosterically activated by phosphatidylinositol 5-phosphate (PI5P) By similarity.

Subunit structure

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 By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. Late endosome By similarity. 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 By similarity.

Domain

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

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.

Contains 1 GRAM domain.

Contains 1 myotubularin phosphatase domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Endosome
Membrane
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendosome to lysosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament organization

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion distribution

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of vacuole organization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from sequence or structural similarity. Source: UniProtKB

late endosome

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionintermediate filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Myotubularin
PRO_0000328656

Regions

Domain29 – 9769GRAM
Domain163 – 538376Myotubularin phosphatase

Sites

Active site3751Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue4951Phosphothreonine By similarity
Modified residue5881Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R9S3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: C4A50B462190D484

FASTA60369,900
        10         20         30         40         50         60 
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI YICPFNGPIK 

        70         80         90        100        110        120 
GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDMRNLR 

       130        140        150        160        170        180 
FALKQEGHSR RDMFEILTRY AFPLAHSLPL FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN 

       190        200        210        220        230        240 
HHWRITFINK CYELCDTYPA PLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV 

       250        260        270        280        290        300 
RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA 

       310        320        330        340        350        360 
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV 

       370        380        390        400        410        420 
ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS 

       430        440        450        460        470        480 
RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE QFLIIILDHL YSCRFGTFLF 

       490        500        510        520        530        540 
NCESARERQK VTERTVSLWS LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR 

       550        560        570        580        590        600 
WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ 


THF 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859309 mRNA. Translation: CAH91487.1.
RefSeqNP_001127425.1. NM_001133953.1.
UniGenePab.9382.

3D structure databases

ProteinModelPortalQ5R9S3.
SMRQ5R9S3. Positions 33-544.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R9S3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174495.
KEGGpon:100174495.

Organism-specific databases

CTD4534.

Phylogenomic databases

HOGENOMHOG000210598.
HOVERGENHBG000220.
KOK01108.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR004182. GRAM.
IPR010569. Myotubularin-like_Pase_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF02893. GRAM. 1 hit.
PF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTSM00568. GRAM. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTM1_PONAB
AccessionPrimary (citable) accession number: Q5R9S3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families