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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).By similarity

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.By similarity
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.By similarity

Enzyme regulationi

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

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 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

Lipid metabolism, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin
Alternative name(s):
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.95By similarity)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.64By similarity)
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 By similarity; 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).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 – 4951PhosphothreonineBy similarity
Modified residuei588 – 5881PhosphoserineBy 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). Interacts with SPEG (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5R9S3.
SMRiQ5R9S3. Positions 33-544.
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.By similarity

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiQ5R9S3.
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

« Hide

        10         20         30         40         50
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI
60 70 80 90 100
YICPFNGPIK GRVYITNYRL YLRSLETDSA 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
PLVVPYRASD 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):69,900
Last modified:December 21, 2004 - v1
Checksum:iC4A50B462190D484
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q5R9S3.
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: October 29, 2014
This is version 56 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