MTMR5_HUMAN
ID MTMR5_HUMAN Reviewed; 1868 AA.
AC O95248; A0A024R4Z9; A6PVG9; G5E933; O60228; Q5JXD8; Q5PPM2; Q96GR9; Q9UGB8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Myotubularin-related protein 5;
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 5 {ECO:0000305};
DE AltName: Full=SET-binding factor 1;
DE Short=Sbf1;
GN Name=SBF1; Synonyms=MTMR5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 939-1867 (ISOFORM 1).
RC TISSUE=Muscle, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 239-1868 (ISOFORM 1), FUNCTION, LACK OF
RP CATALYTIC ACTIVITY, AND INTERACTION WITH KMT2A/MLL1.
RC TISSUE=Lymphoblast;
RX PubMed=9537414; DOI=10.1038/ng0498-331;
RA Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.;
RT "Association of SET domain and myotubularin-related proteins modulates
RT growth control.";
RL Nat. Genet. 18:331-337(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1363-1603.
RX PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA Mandel J.-L.;
RT "Characterization of the myotubularin dual specificity phosphatase gene
RT family from yeast to human.";
RL Hum. Mol. Genet. 7:1703-1712(1998).
RN [6]
RP INTERACTION WITH SUV39H1.
RX PubMed=10848615; DOI=10.1128/mcb.20.13.4900-4909.2000;
RA Firestein R., Cui X., Huie P., Cleary M.L.;
RT "Set domain-dependent regulation of transcriptional silencing and growth
RT control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9.";
RL Mol. Cell. Biol. 20:4900-4909(2000).
RN [7]
RP FUNCTION, INTERACTION WITH MTMR2, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DOMAIN.
RX PubMed=12668758; DOI=10.1073/pnas.0431052100;
RA Kim S.-A., Vacratsis P.O., Firestein R., Cleary M.L., Dixon J.E.;
RT "Regulation of myotubularin-related (MTMR)2 phosphatidylinositol
RT phosphatase by MTMR5, a catalytically inactive phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4492-4497(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121; THR-1138 AND SER-1747,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP VARIANTS CMT4B3 VAL-418 AND ALA-1565.
RX PubMed=23749797; DOI=10.1212/wnl.0b013e31829a3421;
RA Nakhro K., Park J.M., Hong Y.B., Park J.H., Nam S.H., Yoon B.R., Yoo J.H.,
RA Koo H., Jung S.C., Kim H.L., Kim J.Y., Choi K.G., Choi B.O., Chung K.W.;
RT "SET binding factor 1 (SBF1) mutation causes Charcot-Marie-Tooth disease
RT type 4B3.";
RL Neurology 81:165-173(2013).
CC -!- FUNCTION: Acts as an adapter for the phosphatase MTMR2 to regulate
CC MTMR2 catalytic activity and subcellular location (PubMed:12668758).
CC May function as a guanine nucleotide exchange factor (GEF) activating
CC RAB28 (PubMed:20937701). Promotes the exchange of GDP to GTP,
CC converting inactive GDP-bound Rab proteins into their active GTP-bound
CC form (PubMed:20937701). Inhibits myoblast differentiation in vitro and
CC induces oncogenic transformation in fibroblasts (PubMed:9537414).
CC {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701,
CC ECO:0000269|PubMed:9537414}.
CC -!- SUBUNIT: Heterodimer with lipid phosphatase MTMR2 (PubMed:12668758).
CC Interacts with KMT2A/MLL1 (via SET domain) (PubMed:9537414). Interacts
CC with SUV39H1 (PubMed:10848615). {ECO:0000269|PubMed:10848615,
CC ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:9537414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12668758,
CC ECO:0000269|PubMed:20937701}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12668758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95248-1; Sequence=Displayed;
CC Name=4;
CC IsoId=O95248-4; Sequence=VSP_015158;
CC Name=5;
CC IsoId=O95248-5; Sequence=VSP_059427, VSP_015158;
CC -!- DOMAIN: The C-terminal domain mediates interaction with MTMR2.
CC {ECO:0000269|PubMed:12668758}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 4B3 (CMT4B3) [MIM:615284]: A
CC recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder
CC of the peripheral nervous system, characterized by progressive weakness
CC and atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are
CC characterized by severely reduced nerve conduction velocities (less
CC than 38 m/sec), segmental demyelination and remyelination with onion
CC bulb formations on nerve biopsy, slowly progressive distal muscle
CC atrophy and weakness, absent deep tendon reflexes, and hollow feet. By
CC convention autosomal recessive forms of demyelinating Charcot-Marie-
CC Tooth disease are designated CMT4. {ECO:0000269|PubMed:23749797}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 1422 in the dsPTPase catalytic loop and does not have phosphatase
CC activity (PubMed:9537414). The pocket is however sufficiently preserved
CC to bind phosphorylated substrates, and maybe protect them from
CC phosphatases. {ECO:0000269|PubMed:9537414, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39675.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL096767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73536.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73538.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73539.1; -; Genomic_DNA.
DR EMBL; BC009268; AAH09268.2; -; mRNA.
DR EMBL; BC087612; AAH87612.1; -; mRNA.
DR EMBL; U93181; AAC39675.1; ALT_FRAME; mRNA.
DR EMBL; AF072929; AAC78842.1; -; mRNA.
DR CCDS; CCDS14091.2; -. [O95248-5]
DR RefSeq; NP_002963.2; NM_002972.3. [O95248-5]
DR AlphaFoldDB; O95248; -.
DR SMR; O95248; -.
DR BioGRID; 112212; 168.
DR IntAct; O95248; 36.
DR MINT; O95248; -.
DR STRING; 9606.ENSP00000370196; -.
DR DEPOD; SBF1; -.
DR iPTMnet; O95248; -.
DR PhosphoSitePlus; O95248; -.
DR BioMuta; SBF1; -.
DR EPD; O95248; -.
DR jPOST; O95248; -.
DR MassIVE; O95248; -.
DR MaxQB; O95248; -.
DR PaxDb; O95248; -.
DR PeptideAtlas; O95248; -.
DR PRIDE; O95248; -.
DR ProteomicsDB; 33814; -.
DR ProteomicsDB; 50743; -. [O95248-1]
DR ProteomicsDB; 50744; -. [O95248-4]
DR Antibodypedia; 28572; 85 antibodies from 15 providers.
DR DNASU; 6305; -.
DR Ensembl; ENST00000380817.8; ENSP00000370196.2; ENSG00000100241.22. [O95248-5]
DR Ensembl; ENST00000684986.1; ENSP00000509117.1; ENSG00000100241.22. [O95248-4]
DR Ensembl; ENST00000689129.1; ENSP00000510414.1; ENSG00000100241.22. [O95248-1]
DR GeneID; 6305; -.
DR KEGG; hsa:6305; -.
DR MANE-Select; ENST00000380817.8; ENSP00000370196.2; NM_002972.4; NP_002963.2. [O95248-5]
DR UCSC; uc003blh.5; human. [O95248-1]
DR UCSC; uc062flz.1; human.
DR CTD; 6305; -.
DR DisGeNET; 6305; -.
DR GeneCards; SBF1; -.
DR GeneReviews; SBF1; -.
DR HGNC; HGNC:10542; SBF1.
DR HPA; ENSG00000100241; Low tissue specificity.
DR MalaCards; SBF1; -.
DR MIM; 603560; gene.
DR MIM; 615284; phenotype.
DR neXtProt; NX_O95248; -.
DR OpenTargets; ENSG00000100241; -.
DR Orphanet; 363981; Charcot-Marie-Tooth disease type 4B3.
DR PharmGKB; PA34953; -.
DR VEuPathDB; HostDB:ENSG00000100241; -.
DR eggNOG; KOG1090; Eukaryota.
DR eggNOG; KOG2080; Eukaryota.
DR GeneTree; ENSGT00940000155263; -.
DR InParanoid; O95248; -.
DR OMA; GFSSTHM; -.
DR OrthoDB; 45015at2759; -.
DR PhylomeDB; O95248; -.
DR TreeFam; TF318583; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; O95248; -.
DR Reactome; R-HSA-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; O95248; -.
DR BioGRID-ORCS; 6305; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; SBF1; human.
DR GeneWiki; SBF1; -.
DR GenomeRNAi; 6305; -.
DR Pharos; O95248; Tbio.
DR PRO; PR:O95248; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95248; protein.
DR Bgee; ENSG00000100241; Expressed in left testis and 191 other tissues.
DR ExpressionAtlas; O95248; baseline and differential.
DR Genevisible; O95248; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; TAS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR030574; MTMR5.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022096; SBF1/SBF2.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR PANTHER; PTHR10807:SF43; PTHR10807:SF43; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF12335; SBF2; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Charcot-Marie-Tooth disease; Cytoplasm;
KW Disease variant; Guanine-nucleotide releasing factor; Methylation;
KW Neurodegeneration; Neuropathy; Phosphoprotein; Reference proteome.
FT CHAIN 1..1868
FT /note="Myotubularin-related protein 5"
FT /id="PRO_0000094938"
FT DOMAIN 7..185
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 204..337
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 339..440
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 881..969
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 1121..1597
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT DOMAIN 1762..1866
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 91..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1223
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 93
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_059427"
FT VAR_SEQ 1276
FT /note="H -> HVPSPRARVTTLSNPMAASASRRTAPR (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_015158"
FT VARIANT 418
FT /note="M -> V (in CMT4B3; dbSNP:rs587776986)"
FT /evidence="ECO:0000269|PubMed:23749797"
FT /id="VAR_070046"
FT VARIANT 1565
FT /note="T -> A (in CMT4B3; dbSNP:rs200488568)"
FT /evidence="ECO:0000269|PubMed:23749797"
FT /id="VAR_070047"
FT CONFLICT 597
FT /note="A -> V (in Ref. 4; AAC39675)"
FT /evidence="ECO:0000305"
FT CONFLICT 1173
FT /note="P -> R (in Ref. 4; AAC39675)"
FT /evidence="ECO:0000305"
FT CONFLICT 1377
FT /note="A -> P (in Ref. 5; AAC78842)"
FT /evidence="ECO:0000305"
FT CONFLICT 1557
FT /note="Y -> H (in Ref. 5; AAC78842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1868 AA; 208443 MW; E2C80DF9FB94AF1C CRC64;
MARLADYFVL VAFGPHPRGS GEGQGQILQR FPEKDWEDNP FPQGIELFCQ PSGWQLCPER
NPPTFFVAVL TDINSERHYC ACLTFWEPAE PSQQETTRVE DATEREEEGD EGGQTHLSPT
APAPSAQLFA PKTLVLVSRL DHTEVFRNSL GLIYAIHVEG LNVCLENVIG NLLTCTVPLA
GGSQRTISLG AGDRQVIQTP LADSLPVSRC SVALLFRQLG ITNVLSLFCA ALTEHKVLFL
SRSYQRLADA CRGLLALLFP LRYSFTYVPI LPAQLLEVLS TPTPFIIGVN AAFQAETQEL
LDVIVADLDG GTVTIPECVH IPPLPEPLQS QTHSVLSMVL DPELELADLA FPPPTTSTSS
LKMQDKELRA VFLRLFAQLL QGYRWCLHVV RIHPEPVIRF HKAAFLGQRG LVEDDFLMKV
LEGMAFAGFV SERGVPYRPT DLFDELVAHE VARMRADENH PQRVLRHVQE LAEQLYKNEN
PYPAVAMHKV QRPGESSHLR RVPRPFPRLD EGTVQWIVDQ AAAKMQGAPP AVKAERRTTV
PSGPPMTAIL ERCSGLHVNS ARRLEVVRNC ISYVFEGKML EAKKLLPAVL RALKGRAARR
CLAQELHLHV QQNRAVLDHQ QFDFVVRMMN CCLQDCTSLD EHGIAAALLP LVTAFCRKLS
PGVTQFAYSC VQEHVVWSTP QFWEAMFYGD VQTHIRALYL EPTEDLAPAQ EVGEAPSQED
ERSALDVASE QRRLWPTLSR EKQQELVQKE ESTVFSQAIH YANRMSYLLL PLDSSKSRLL
RERAGLGDLE SASNSLVTNS MAGSVAESYD TESGFEDAET CDVAGAVVRF INRFVDKVCT
ESGVTSDHLK GLHVMVPDIV QMHIETLEAV QRESRRLPPI QKPKLLRPRL LPGEECVLDG
LRVYLLPDGR EEGAGGSAGG PALLPAEGAV FLTTYRVIFT GMPTDPLVGE QVVVRSFPVA
ALTKEKRISV QTPVDQLLQD GLQLRSCTFQ LLKMAFDEEV GSDSAELFRK QLHKLRYPPD
IRATFAFTLG SAHTPGRPPR VTKDKGPSLR TLSRNLVKNA KKTIGRQHVT RKKYNPPSWE
HRGQPPPEDQ EDEISVSEEL EPSTLTPSSA LKPSDRMTMS SLVERACCRD YQRLGLGTLS
SSLSRAKSEP FRISPVNRMY AICRSYPGLL IVPQSVQDNA LQRVSRCYRQ NRFPVVCWRS
GRSKAVLLRS GGLHGKGVVG LFKAQNAPSP GQSQADSSSL EQEKYLQAVV SSMPRYADAS
GRNTLSGFSS AHMGSHGKWG SVRTSGRSSG LGTDVGSRLA GRDALAPPQA NGGPPDPGFL
RPQRAALYIL GDKAQLKGVR SDPLQQWELV PIEVFEARQV KASFKKLLKA CVPGCPAAEP
SPASFLRSLE DSEWLIQIHK LLQVSVLVVE LLDSGSSVLV GLEDGWDITT QVVSLVQLLS
DPFYRTLEGF RLLVEKEWLS FGHRFSHRGA HTLAGQSSGF TPVFLQFLDC VHQVHLQFPM
EFEFSQFYLK FLGYHHVSRR FRTFLLDSDY ERIELGLLYE EKGERRGQVP CRSVWEYVDR
LSKRTPVFHN YMYAPEDAEV LRPYSNVSNL KVWDFYTEET LAEGPPYDWE LAQGPPEPPE
EERSDGGAPQ SRRRVVWPCY DSCPRAQPDA ISRLLEELQR LETELGQPAE RWKDTWDRVK
AAQRLEGRPD GRGTPSSLLV STAPHHRRSL GVYLQEGPVG STLSLSLDSD QSSGSTTSGS
RQAARRSTST LYSQFQTAES ENRSYEGTLY KKGAFMKPWK ARWFVLDKTK HQLRYYDHRV
DTECKGVIDL AEVEAVAPGT PTMGAPKTVD EKAFFDVKTT RRVYNFCAQD VPSAQQWVDR
IQSCLSDA
