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Q13613

- MTMR1_HUMAN

UniProt

Q13613 - MTMR1_HUMAN

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Protein

Myotubularin-related protein 1

Gene

MTMR1

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

Functioni

Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei438 – 4381Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei484 – 4841SubstrateBy similarity

GO - Molecular functioni

  1. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: InterPro

GO - Biological processi

  1. phosphatidylinositol biosynthetic process Source: Reactome
  2. phosphatidylinositol dephosphorylation Source: UniProtKB
  3. phospholipid metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 1
Alternative name(s):
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.641 Publication)
Gene namesi
Name:MTMR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7449. MTMR1.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665Myotubularin-related protein 1PRO_0000094932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13613.
PaxDbiQ13613.
PRIDEiQ13613.

PTM databases

PhosphoSiteiQ13613.

Expressioni

Gene expression databases

BgeeiQ13613.
CleanExiHS_MTMR1.
ExpressionAtlasiQ13613. baseline and differential.
GenevestigatoriQ13613.

Organism-specific databases

HPAiHPA018502.

Interactioni

Protein-protein interaction databases

BioGridi114306. 9 interactions.
STRINGi9606.ENSP00000359417.

Structurei

3D structure databases

ProteinModelPortaliQ13613.
SMRiQ13613. Positions 95-606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 16172GRAMAdd
BLAST
Domaini226 – 601376Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni351 – 3544Substrate bindingBy similarity
Regioni376 – 3772Substrate bindingBy similarity
Regioni438 – 4447Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 106Poly-Ala
Compositional biasi14 – 174Poly-Gly
Compositional biasi645 – 6484Poly-Ser

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322789.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiQ13613.
KOiK18081.
PhylomeDBiQ13613.
TreeFamiTF315197.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13613-1) [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
MDRPAAAAAA GCEGGGGPNP GPAGGRRPPR AAGGATAGSR QPSVETLDSP
60 70 80 90 100
TGSHVEWCKQ LIAATISSQI SGSVTSENVS RDYKALRDGN KLAQMEEAPL
110 120 130 140 150
FPGESIKAIV KDVMYICPFM GAVSGTLTVT DFKLYFKNVE RDPHFILDVP
160 170 180 190 200
LGVISRVEKI GAQSHGDNSC GIEIVCKDMR NLRLAYKQEE QSKLGIFENL
210 220 230 240 250
NKHAFPLSNG QALFAFSYKE KFPINGWKVY DPVSEYKRQG LPNESWKISK
260 270 280 290 300
INSNYEFCDT YPAIIVVPTS VKDDDLSKVA AFRAKGRVPV LSWIHPESQA
310 320 330 340 350
TITRCSQPLV GPNDKRCKED EKYLQTIMDA NAQSHKLIIF DARQNSVADT
360 370 380 390 400
NKTKGGGYES ESAYPNAELV FLEIHNIHVM RESLRKLKEI VYPSIDEARW
410 420 430 440 450
LSNVDGTHWL EYIRMLLAGA VRIADKIESG KTSVVVHCSD GWDRTAQLTS
460 470 480 490 500
LAMLMLDSYY RTIKGFETLV EKEWISFGHR FALRVGHGND NHADADRSPI
510 520 530 540 550
FLQFVDCVWQ MTRQFPSAFE FNELFLITIL DHLYSCLFGT FLCNCEQQRF
560 570 580 590 600
KEDVYTKTIS LWSYINSQLD EFSNPFFVNY ENHVLYPVAS LSHLELWVNY
610 620 630 640 650
YVRWNPRMRP QMPIHQNLKE LLAVRAELQK RVEGLQREVA TRAVSSSSER
660
GSSPSHSATS VHTSV
Length:665
Mass (Da):74,678
Last modified:July 19, 2003 - v4
Checksum:i12E766859F0DCA75
GO
Isoform 1A (identifier: Q13613-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     553-568: DVYTKTISLWSYINSQ → AWGAGTQRARGSLRSR
     569-665: Missing.

Show »
Length:568
Mass (Da):63,330
Checksum:iEA1F7406012707B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti541 – 5411F → L in CAA12271. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei553 – 56816DVYTK…YINSQ → AWGAGTQRARGSLRSR in isoform 1A. CuratedVSP_005169Add
BLAST
Alternative sequencei569 – 66597Missing in isoform 1A. CuratedVSP_005170Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF002223 Genomic DNA. No translation available.
CH471169 Genomic DNA. Translation: EAW99384.1.
CH471169 Genomic DNA. Translation: EAW99388.1.
AJ224979 mRNA. Translation: CAA12271.1.
AF057354 mRNA. Translation: AAD40368.1.
U58032 mRNA. Translation: AAC79117.1.
CCDSiCCDS14695.1. [Q13613-1]
RefSeqiNP_003819.1. NM_003828.2. [Q13613-1]
XP_006724918.1. XM_006724855.1. [Q13613-1]
UniGeneiHs.347187.

Genome annotation databases

EnsembliENST00000370390; ENSP00000359417; ENSG00000063601. [Q13613-1]
ENST00000485376; ENSP00000434105; ENSG00000063601. [Q13613-2]
GeneIDi8776.
KEGGihsa:8776.
UCSCiuc004fei.3. human. [Q13613-1]

Polymorphism databases

DMDMi33112667.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF002223 Genomic DNA. No translation available.
CH471169 Genomic DNA. Translation: EAW99384.1 .
CH471169 Genomic DNA. Translation: EAW99388.1 .
AJ224979 mRNA. Translation: CAA12271.1 .
AF057354 mRNA. Translation: AAD40368.1 .
U58032 mRNA. Translation: AAC79117.1 .
CCDSi CCDS14695.1. [Q13613-1 ]
RefSeqi NP_003819.1. NM_003828.2. [Q13613-1 ]
XP_006724918.1. XM_006724855.1. [Q13613-1 ]
UniGenei Hs.347187.

3D structure databases

ProteinModelPortali Q13613.
SMRi Q13613. Positions 95-606.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114306. 9 interactions.
STRINGi 9606.ENSP00000359417.

PTM databases

PhosphoSitei Q13613.

Polymorphism databases

DMDMi 33112667.

Proteomic databases

MaxQBi Q13613.
PaxDbi Q13613.
PRIDEi Q13613.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370390 ; ENSP00000359417 ; ENSG00000063601 . [Q13613-1 ]
ENST00000485376 ; ENSP00000434105 ; ENSG00000063601 . [Q13613-2 ]
GeneIDi 8776.
KEGGi hsa:8776.
UCSCi uc004fei.3. human. [Q13613-1 ]

Organism-specific databases

CTDi 8776.
GeneCardsi GC0XP149861.
H-InvDB HIX0017110.
HGNCi HGNC:7449. MTMR1.
HPAi HPA018502.
MIMi 300171. gene.
neXtProti NX_Q13613.
PharmGKBi PA31252.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322789.
GeneTreei ENSGT00760000118832.
HOGENOMi HOG000210598.
HOVERGENi HBG000220.
InParanoidi Q13613.
KOi K18081.
PhylomeDBi Q13613.
TreeFami TF315197.

Enzyme and pathway databases

Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

GeneWikii MTMR1.
GenomeRNAii 8776.
NextBioi 32908.
PROi Q13613.
SOURCEi Search...

Gene expression databases

Bgeei Q13613.
CleanExi HS_MTMR1.
ExpressionAtlasi Q13613. baseline and differential.
Genevestigatori Q13613.

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

« Hide 'large scale' publications
  1. "Genomic organization of a 225-kb region in Xq28 containing the gene for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)."
    Kioschis P., Wiemann S., Heiss N.S., Francis F., Goetz C., Poustka A., Taudien S., Platzer M., Wiehe T., Beckmann G., Weber J., Nordsiek G., Rosenthal A.
    Genomics 54:256-266(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Ancient genomic duplication within the myotubular myopathy locus (MTM1) in human Xq28."
    Kioschis P., Wiemann S., Francis F., Goetz C., Poustka A., Taudien S., Platzer M., Wiehe T., Beckmann G., Weber J., Nordsiek G., Rosenthal A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-665.
    Tissue: Brain.
  5. "Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human."
    Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N., Mandel J.-L.
    Hum. Mol. Genet. 7:1703-1712(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-610.
  6. "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] OF 404-535.
  7. "Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth disease."
    Kim S.A., Taylor G.S., Torgersen K.M., Dixon J.E.
    J. Biol. Chem. 277:4526-4531(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMTMR1_HUMAN
AccessioniPrimary (citable) accession number: Q13613
Secondary accession number(s): A0A024RC07
, Q9UBX6, Q9UEM0, Q9UQD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2003
Last modified: October 29, 2014
This is version 126 of the entry and version 4 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3