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Q5R9S3

- MTM1_PONAB

UniProt

Q5R9S3 - MTM1_PONAB

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Protein

Myotubularin

Gene
MTM1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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 By similarity.

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei375 – 3751Phosphocysteine intermediate By similarity

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 dephosphorylation Source: UniProtKB
  6. protein dephosphorylation Source: UniProtKB
  7. protein transport Source: UniProtKB-KW
  8. regulation of vacuole organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin (EC:3.1.3.64)
Gene namesi
Name:MTM1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. filopodium Source: UniProtKB
  3. late endosome Source: UniProtKB
  4. plasma membrane Source: UniProtKB
  5. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603MyotubularinPRO_0000328656Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei495 – 4951Phosphothreonine By similarity
Modified residuei588 – 5881Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5R9S3.

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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5R9S3.
SMRiQ5R9S3. Positions 33-544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 9769GRAMAdd
BLAST
Domaini163 – 538376Myotubularin phosphataseAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 GRAM domain.

Phylogenomic databases

HOGENOMiHOG000210598.
HOVERGENiHBG000220.
KOiK01108.

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]

Sequencei

Sequence statusi: Complete.

Q5R9S3-1 [UniParc]FASTAAdd to Basket

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MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI    50
YICPFNGPIK GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT 100
SRGENSYGLD ITCKDMRNLR FALKQEGHSR RDMFEILTRY AFPLAHSLPL 150
FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRITFINK CYELCDTYPA 200
PLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV RCSQPLVGMS 250
GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA 300
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI 350
KLVLTGAIQV ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI 400
EGFEILVQKE WISFGHKFAS RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK 450
QFPTAFEFNE QFLIIILDHL YSCRFGTFLF NCESARERQK VTERTVSLWS 500
LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRIKQQQP 550
NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ 600
THF 603
Length:603
Mass (Da):69,900
Last modified:December 21, 2004 - v1
Checksum:iC4A50B462190D484
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859309 mRNA. Translation: CAH91487.1.
RefSeqiNP_001127425.1. NM_001133953.1.
UniGeneiPab.9382.

Genome annotation databases

GeneIDi100174495.
KEGGipon:100174495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859309 mRNA. Translation: CAH91487.1 .
RefSeqi NP_001127425.1. NM_001133953.1.
UniGenei Pab.9382.

3D structure databases

ProteinModelPortali Q5R9S3.
SMRi Q5R9S3. Positions 33-544.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R9S3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100174495.
KEGGi pon:100174495.

Organism-specific databases

CTDi 4534.

Phylogenomic databases

HOGENOMi HOG000210598.
HOVERGENi HBG000220.
KOi K01108.

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

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

Entry informationi

Entry nameiMTM1_PONAB
AccessioniPrimary (citable) accession number: Q5R9S3
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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