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Q13613 (MTMR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myotubularin-related protein 1

EC=3.1.3.-
Gene names
Name:MTMR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipid phosphatase that acts on phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate. Ref.6

Subunit structure

Interacts with MTMR12. Ref.6

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.6.

Sequence similarities

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

Contains 1 GRAM domain.

Contains 1 myotubularin phosphatase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13613-1)

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.
Isoform 1A (identifier: Q13613-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Myotubularin-related protein 1
PRO_0000094932

Regions

Domain90 – 16172GRAM
Domain226 – 601376Myotubularin phosphatase
Region351 – 3544Substrate binding By similarity
Region376 – 3772Substrate binding By similarity
Region438 – 4447Substrate binding By similarity
Compositional bias5 – 106Poly-Ala
Compositional bias14 – 174Poly-Gly
Compositional bias645 – 6484Poly-Ser

Sites

Active site4381Phosphocysteine intermediate By similarity
Binding site4841Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9

Natural variations

Alternative sequence553 – 56816DVYTK…YINSQ → AWGAGTQRARGSLRSR in isoform 1A.
VSP_005169
Alternative sequence569 – 66597Missing in isoform 1A.
VSP_005170

Experimental info

Sequence conflict5411F → L in CAA12271. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2003. Version 4.
Checksum: 12E766859F0DCA75

FASTA66574,678
        10         20         30         40         50         60 
MDRPAAAAAA GCEGGGGPNP GPAGGRRPPR AAGGATAGSR QPSVETLDSP TGSHVEWCKQ 

        70         80         90        100        110        120 
LIAATISSQI SGSVTSENVS RDYKALRDGN KLAQMEEAPL FPGESIKAIV KDVMYICPFM 

       130        140        150        160        170        180 
GAVSGTLTVT DFKLYFKNVE RDPHFILDVP LGVISRVEKI GAQSHGDNSC GIEIVCKDMR 

       190        200        210        220        230        240 
NLRLAYKQEE QSKLGIFENL NKHAFPLSNG QALFAFSYKE KFPINGWKVY DPVSEYKRQG 

       250        260        270        280        290        300 
LPNESWKISK INSNYEFCDT YPAIIVVPTS VKDDDLSKVA AFRAKGRVPV LSWIHPESQA 

       310        320        330        340        350        360 
TITRCSQPLV GPNDKRCKED EKYLQTIMDA NAQSHKLIIF DARQNSVADT NKTKGGGYES 

       370        380        390        400        410        420 
ESAYPNAELV FLEIHNIHVM RESLRKLKEI VYPSIDEARW LSNVDGTHWL EYIRMLLAGA 

       430        440        450        460        470        480 
VRIADKIESG KTSVVVHCSD GWDRTAQLTS LAMLMLDSYY RTIKGFETLV EKEWISFGHR 

       490        500        510        520        530        540 
FALRVGHGND NHADADRSPI FLQFVDCVWQ MTRQFPSAFE FNELFLITIL DHLYSCLFGT 

       550        560        570        580        590        600 
FLCNCEQQRF KEDVYTKTIS LWSYINSQLD EFSNPFFVNY ENHVLYPVAS LSHLELWVNY 

       610        620        630        640        650        660 
YVRWNPRMRP QMPIHQNLKE LLAVRAELQK RVEGLQREVA TRAVSSSSER GSSPSHSATS 


VHTSV 

« Hide

Isoform 1A [UniParc].

Checksum: EA1F7406012707B6
Show »

FASTA56863,330

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.
[4]"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.
[5]"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.
[6]"Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP."
Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L., Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.
Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MTMR12.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF002223 Genomic DNA. No translation available.
AJ224979 mRNA. Translation: CAA12271.1.
AF057354 mRNA. Translation: AAD40368.1.
U58032 mRNA. Translation: AAC79117.1.
CCDSCCDS14695.1. [Q13613-1]
RefSeqNP_003819.1. NM_003828.2. [Q13613-1]
XP_006724918.1. XM_006724855.1. [Q13613-1]
UniGeneHs.347187.

3D structure databases

ProteinModelPortalQ13613.
SMRQ13613. Positions 95-606.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114306. 2 interactions.
STRING9606.ENSP00000359417.

PTM databases

PhosphoSiteQ13613.

Polymorphism databases

DMDM33112667.

Proteomic databases

MaxQBQ13613.
PaxDbQ13613.
PRIDEQ13613.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370390; ENSP00000359417; ENSG00000063601. [Q13613-1]
ENST00000451863; ENSP00000387446; ENSG00000063601. [Q13613-2]
ENST00000485376; ENSP00000434105; ENSG00000063601. [Q13613-2]
ENST00000544228; ENSP00000440534; ENSG00000063601. [Q13613-1]
ENST00000594143; ENSP00000472612; ENSG00000269759. [Q13613-1]
ENST00000596801; ENSP00000470456; ENSG00000269759. [Q13613-2]
ENST00000598665; ENSP00000470030; ENSG00000269759. [Q13613-2]
ENST00000602010; ENSP00000471922; ENSG00000269759. [Q13613-1]
GeneID8776.
KEGGhsa:8776.
UCSCuc004fei.3. human. [Q13613-1]

Organism-specific databases

CTD8776.
GeneCardsGC0XP149861.
H-InvDBHIX0017110.
HGNCHGNC:7449. MTMR1.
HPAHPA018502.
MIM300171. gene.
neXtProtNX_Q13613.
PharmGKBPA31252.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322789.
HOGENOMHOG000210598.
HOVERGENHBG000220.
InParanoidQ13613.
KOK18081.
PhylomeDBQ13613.
TreeFamTF315197.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ13613.
BgeeQ13613.
CleanExHS_MTMR1.
GenevestigatorQ13613.

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...

Other

GeneWikiMTMR1.
GenomeRNAi8776.
NextBio32908.
PROQ13613.
SOURCESearch...

Entry information

Entry nameMTMR1_HUMAN
AccessionPrimary (citable) accession number: Q13613
Secondary accession number(s): Q9UBX6, Q9UEM0, Q9UQD5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2003
Last modified: July 9, 2014
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM