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Q9UBF9

- MYOTI_HUMAN

UniProt

Q9UBF9 - MYOTI_HUMAN

Protein

Myotilin

Gene

MYOT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural constituent of muscle Source: ProtInc

    GO - Biological processi

    1. muscle contraction Source: ProtInc

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotilin
    Alternative name(s):
    57 kDa cytoskeletal protein
    Myofibrillar titin-like Ig domains protein
    Titin immunoglobulin domain protein
    Gene namesi
    Name:MYOT
    Synonyms:TTID
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:12399. MYOT.

    Subcellular locationi

    Cell membranesarcolemma. Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line
    Note: Sarcomeric, also localized to the sarcolemma. Colocalizes with MYOZ1 at the Z-lines in skeletal muscle.

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. sarcolemma Source: UniProtKB-SubCell
    3. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Limb-girdle muscular dystrophy 1A (LGMD1A) [MIM:159000]: An autosomal dominant degenerative myopathy with onset within a mean age of 28 years. Characterized by progressive skeletal muscle weakness of the hip and shoulder girdles, later progressing to include distal weakness, as well as a distinctive dysarthric pattern of speech. Affected muscle exhibits disorganization and streaming of the Z-line.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551S → F in LGMD1A and MFM3. 2 Publications
    VAR_021569
    Natural varianti57 – 571T → I in LGMD1A; does not abolish interaction with ACTN1. 1 Publication
    Corresponds to variant rs28937597 [ dbSNP | Ensembl ].
    VAR_021570
    Myopathy, myofibrillar, 3 (MFM3) [MIM:609200]: A neuromuscular disorder characterized by progressive skeletal muscle weakness greater distally than proximally, tight heel cords, hyporeflexia, cardiomyopathy and peripheral neuropathy in some patients. Affected muscle exhibits disorganization and streaming of the Z-line, presence of large hyaline structures, excessive accumulation of myotilin and other ectopically expressed proteins and prominent congophilic deposits.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551S → F in LGMD1A and MFM3. 2 Publications
    VAR_021569
    Natural varianti60 – 601S → C in MFM3. 1 Publication
    VAR_021571
    Natural varianti60 – 601S → F in MFM3. 1 Publication
    VAR_021572
    Natural varianti95 – 951S → I in MFM3. 1 Publication
    VAR_021573
    Spheroid body myopathy (SBM) [MIM:182920]: Autosomal dominant form of myofibrillar myopathy (MFM), characterized by slowly progressing proximal muscle weakness and dysarthric nasal speech. There is no evidence of cardiomyopathy. Muscle biopsy shows spheroid bodies within the type I muscle fibers.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391S → F in SBM. 1 Publication
    VAR_029532

    Keywords - Diseasei

    Disease mutation, Limb-girdle muscular dystrophy, Myofibrillar myopathy

    Organism-specific databases

    MIMi159000. phenotype.
    182920. phenotype.
    609200. phenotype.
    Orphaneti266. Autosomal dominant limb-girdle muscular dystrophy type 1A.
    98911. Distal myotilinopathy.
    268129. Spheroid body myopathy.
    PharmGKBiPA37064.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498MyotilinPRO_0000072687Add
    BLAST

    Proteomic databases

    PaxDbiQ9UBF9.
    PRIDEiQ9UBF9.

    PTM databases

    PhosphoSiteiQ9UBF9.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle (at protein level). Expressed in skeletal muscle, heart, bone marrow and thyroid gland.2 Publications

    Gene expression databases

    ArrayExpressiQ9UBF9.
    BgeeiQ9UBF9.
    CleanExiHS_MYOT.
    GenevestigatoriQ9UBF9.

    Organism-specific databases

    HPAiHPA037733.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with ACTA1, ACTN1, FLNA, FLNB, FLNC and MYOZ2. Interacts with the C-terminal region of MYOZ1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLNCQ143156EBI-296701,EBI-489954

    Protein-protein interaction databases

    BioGridi114878. 10 interactions.
    IntActiQ9UBF9. 7 interactions.
    STRINGi9606.ENSP00000239926.

    Structurei

    Secondary structure

    1
    498
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi249 – 2513
    Beta strandi259 – 2624
    Beta strandi267 – 2726
    Beta strandi274 – 2774
    Beta strandi280 – 2856
    Beta strandi288 – 2903
    Beta strandi294 – 2963
    Beta strandi298 – 3014
    Turni302 – 3043
    Beta strandi305 – 3128
    Helixi315 – 3173
    Beta strandi319 – 3279
    Beta strandi330 – 34112
    Beta strandi351 – 3533
    Beta strandi358 – 3614
    Beta strandi364 – 3729
    Beta strandi379 – 3846
    Beta strandi396 – 4005
    Beta strandi405 – 4139
    Helixi415 – 4173
    Beta strandi419 – 4279
    Beta strandi430 – 44112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KDGNMR-A249-344[»]
    2KKQNMR-A344-449[»]
    ProteinModelPortaliQ9UBF9.
    SMRiQ9UBF9. Positions 249-449.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBF9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini250 – 33586Ig-like C2-type 1Add
    BLAST
    Domaini349 – 44193Ig-like C2-type 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 15072Necessary for interaction with ACTN1Add
    BLAST
    Regioni215 – 498284Necessary for interaction with ACTA1Add
    BLAST
    Regioni215 – 493279Necessary for interaction with FLNCAdd
    BLAST

    Sequence similaritiesi

    Belongs to the myotilin/palladin family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiNOG147321.
    HOGENOMiHOG000028074.
    HOVERGENiHBG066530.
    InParanoidiQ9UBF9.
    OMAiDSVKLEC.
    PhylomeDBiQ9UBF9.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    [Graphical view]
    PfamiPF07679. I-set. 2 hits.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBF9-1) [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

    MFNYERPKHF IQSQNPCGSR LQPPGPETSS FSSQTKQSSI IIQPRQCTEQ    50
    RFSASSTLSS HITMSSSAFP ASPKQHAGSN PGQRVTTTYN QSPASFLSSI 100
    LPSQPDYNSS KIPSAMDSNY QQSSAGQPIN AKPSQTANAK PIPRTPDHEI 150
    QGSKEALIQD LERKLKCKDT LLHNGNQRLT YEEKMARRLL GPQNAAAVFQ 200
    AQDDSGAQDS QQHNSEHARL QVPTSQVRSR STSRGDVNDQ DAIQEKFYPP 250
    RFIQVPENMS IDEGRFCRMD FKVSGLPAPD VSWYLNGRTV QSDDLHKMIV 300
    SEKGLHSLIF EVVRASDAGA YACVAKNRAG EATFTVQLDV LAKEHKRAPM 350
    FIYKPQSKKV LEGDSVKLEC QISAIPPPKL FWKRNNEMVQ FNTDRISLYQ 400
    DNTGRVTLLI KDVNKKDAGW YTVSAVNEAG VTTCNTRLDV TARPNQTLPA 450
    PKQLRVRPTF SKYLALNGKG LNVKQAFNPE GEFQRLAAQS GLYESEEL 498
    Length:498
    Mass (Da):55,395
    Last modified:November 2, 2010 - v2
    Checksum:i7F226DD43A0C611B
    GO
    Isoform 2 (identifier: Q9UBF9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-184: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:314
    Mass (Da):35,147
    Checksum:iF4B4033F166A94D2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331S → I in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035520
    Natural varianti39 – 391S → F in SBM. 1 Publication
    VAR_029532
    Natural varianti50 – 501Q → R.
    Corresponds to variant rs34717730 [ dbSNP | Ensembl ].
    VAR_049914
    Natural varianti55 – 551S → F in LGMD1A and MFM3. 2 Publications
    VAR_021569
    Natural varianti57 – 571T → I in LGMD1A; does not abolish interaction with ACTN1. 1 Publication
    Corresponds to variant rs28937597 [ dbSNP | Ensembl ].
    VAR_021570
    Natural varianti60 – 601S → C in MFM3. 1 Publication
    VAR_021571
    Natural varianti60 – 601S → F in MFM3. 1 Publication
    VAR_021572
    Natural varianti74 – 741K → Q.3 Publications
    Corresponds to variant rs41431944 [ dbSNP | Ensembl ].
    VAR_029533
    Natural varianti95 – 951S → I in MFM3. 1 Publication
    VAR_021573

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 184184Missing in isoform 2. 1 PublicationVSP_041450Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF133820 mRNA. Translation: AAD29051.2.
    AF144477 mRNA. Translation: AAD44754.1.
    AK300088 mRNA. Translation: BAG61891.1.
    AC106791 Genomic DNA. No translation available.
    BC005376 mRNA. Translation: AAH05376.1.
    CCDSiCCDS4194.1. [Q9UBF9-1]
    CCDS47268.1. [Q9UBF9-2]
    RefSeqiNP_001129412.1. NM_001135940.1. [Q9UBF9-2]
    NP_006781.1. NM_006790.2.
    UniGeneiHs.84665.

    Genome annotation databases

    EnsembliENST00000239926; ENSP00000239926; ENSG00000120729. [Q9UBF9-1]
    ENST00000421631; ENSP00000391185; ENSG00000120729. [Q9UBF9-2]
    GeneIDi9499.
    KEGGihsa:9499.
    UCSCiuc003lbv.3. human. [Q9UBF9-1]

    Polymorphism databases

    DMDMi311033402.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF133820 mRNA. Translation: AAD29051.2 .
    AF144477 mRNA. Translation: AAD44754.1 .
    AK300088 mRNA. Translation: BAG61891.1 .
    AC106791 Genomic DNA. No translation available.
    BC005376 mRNA. Translation: AAH05376.1 .
    CCDSi CCDS4194.1. [Q9UBF9-1 ]
    CCDS47268.1. [Q9UBF9-2 ]
    RefSeqi NP_001129412.1. NM_001135940.1. [Q9UBF9-2 ]
    NP_006781.1. NM_006790.2.
    UniGenei Hs.84665.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KDG NMR - A 249-344 [» ]
    2KKQ NMR - A 344-449 [» ]
    ProteinModelPortali Q9UBF9.
    SMRi Q9UBF9. Positions 249-449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114878. 10 interactions.
    IntActi Q9UBF9. 7 interactions.
    STRINGi 9606.ENSP00000239926.

    PTM databases

    PhosphoSitei Q9UBF9.

    Polymorphism databases

    DMDMi 311033402.

    Proteomic databases

    PaxDbi Q9UBF9.
    PRIDEi Q9UBF9.

    Protocols and materials databases

    DNASUi 9499.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000239926 ; ENSP00000239926 ; ENSG00000120729 . [Q9UBF9-1 ]
    ENST00000421631 ; ENSP00000391185 ; ENSG00000120729 . [Q9UBF9-2 ]
    GeneIDi 9499.
    KEGGi hsa:9499.
    UCSCi uc003lbv.3. human. [Q9UBF9-1 ]

    Organism-specific databases

    CTDi 9499.
    GeneCardsi GC05P137203.
    GeneReviewsi MYOT.
    HGNCi HGNC:12399. MYOT.
    HPAi HPA037733.
    MIMi 159000. phenotype.
    182920. phenotype.
    604103. gene.
    609200. phenotype.
    neXtProti NX_Q9UBF9.
    Orphaneti 266. Autosomal dominant limb-girdle muscular dystrophy type 1A.
    98911. Distal myotilinopathy.
    268129. Spheroid body myopathy.
    PharmGKBi PA37064.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147321.
    HOGENOMi HOG000028074.
    HOVERGENi HBG066530.
    InParanoidi Q9UBF9.
    OMAi DSVKLEC.
    PhylomeDBi Q9UBF9.

    Miscellaneous databases

    ChiTaRSi MYOT. human.
    EvolutionaryTracei Q9UBF9.
    GeneWikii Myotilin.
    GenomeRNAii 9499.
    NextBioi 35590.
    PROi Q9UBF9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBF9.
    Bgeei Q9UBF9.
    CleanExi HS_MYOT.
    Genevestigatori Q9UBF9.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    [Graphical view ]
    Pfami PF07679. I-set. 2 hits.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TTID: a novel gene at 5q31 encoding a protein with titin-like features."
      Godley L.A., Lai F., Liu J., Zhao N., Le Beau M.M.
      Genomics 60:226-233(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT GLN-74.
      Tissue: Bone marrow.
    2. "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy."
      Salmikangas P., Mykkaenen O.M., Groenholm M., Heiska L., Kere J., Carpen O.
      Hum. Mol. Genet. 8:1329-1336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, INTERACTION WITH ACTN1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT GLN-74.
      Tissue: Skeletal muscle.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Pericardium.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-74.
      Tissue: Liver.
    6. "Indications for a novel muscular dystrophy pathway: gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin."
      van der Ven P.F.M., Wiesner S., Salmikangas P., Auerbach D., Himmel M., Kempa S., Hayess K., Pacholsky D., Taivainen A., Schroeder R., Carpen O., Fuerst D.O.
      J. Cell Biol. 151:235-248(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNC.
    7. "Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly."
      Salmikangas P., van der Ven P.F.M., Lalowski M., Taivainen A., Zhao F., Suila H., Schroeder R., Lappalainen P., Fuerst D.O., Carpen O.
      Hum. Mol. Genet. 12:189-203(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MYOFIBRIL ASSEMBLY AND STABILITY, SUBUNIT, INTERACTION WITH ACTA1.
    8. "The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins."
      Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L.
      J. Cell Sci. 118:3739-3749(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNA; FLNB; FLNC; MYOZ1 AND MYOZ2, SUBCELLULAR LOCATION.
    9. "Solution structure of the first immunoglobulin domain of human myotilin."
      Heikkinen O., Permi P., Koskela H., Carpen O., Ylaenne J., Kilpelaeinen I.
      J. Biomol. NMR 44:107-112(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 249-344.
    10. "Solution NMR structure of the Ig-like C2-type 2 domain of human myotilin. Northeast structural genomics target HR3158."
      Northeast structural genomics consortium (NESG)
      Submitted (JUL-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 344-449.
    11. Cited for: VARIANT LGMD1A ILE-57, INTERACTION WITH ACTN1.
    12. Cited for: VARIANT LGMD1A PHE-55.
    13. "Mutations in myotilin cause myofibrillar myopathy."
      Selcen D., Engel A.G.
      Neurology 62:1363-1371(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MFM3 PHE-55; CYS-60; PHE-60 AND ILE-95.
    14. Erratum
      Selcen D., Engel A.G.
      Neurology 63:405-405(2004)
    15. Cited for: VARIANT SBM PHE-39.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-33.

    Entry informationi

    Entry nameiMYOTI_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBF9
    Secondary accession number(s): A0A4R6, B4DT79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3