P52179 · MYOM1_HUMAN

  • Protein
    Myomesin-1
  • Gene
    MYOM1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentM band
Cellular Componentstriated muscle myosin thick filament
Molecular Functionidentical protein binding
Molecular Functionkinase binding
Molecular Functionprotein homodimerization activity
Molecular Functionstructural constituent of muscle
Biological Processextraocular skeletal muscle development
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of protein secretion
Biological Processprotein kinase A signaling
Biological Processsarcomere organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Myomesin-1
  • Alternative names
    • 190 kDa connectin-associated protein
    • 190 kDa titin-associated protein
    • Myomesin family member 1

Gene names

    • Name
      MYOM1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P52179
  • Secondary accessions
    • Q14BD6
    • Q6H969
    • Q6ZUU0

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_04722122in dbSNP:rs1791085
Natural variantVAR_047222181in dbSNP:rs1962519
Natural variantVAR_047223215in dbSNP:rs2230165
Natural variantVAR_047224341in dbSNP:rs8099021
Natural variantVAR_047225600in dbSNP:rs9807556
Natural variantVAR_047226960in dbSNP:rs1071600
Natural variantVAR_0472271408in dbSNP:rs3765623
Natural variantVAR_0472281453in dbSNP:rs16944397

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2,112 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue, disulfide bond.

TypeIDPosition(s)SourceDescription
ChainPRO_00000726841-1685UniProtMyomesin-1
Modified residue (large scale data)58PRIDEPhosphoserine
Modified residue (large scale data)65PRIDEPhosphoserine
Modified residue (large scale data)67PRIDEPhosphoserine
Modified residue (large scale data)69PRIDEPhosphoserine
Modified residue (large scale data)79PRIDEPhosphoserine
Modified residue113UniProtPhosphoserine
Modified residue (large scale data)113PRIDEPhosphoserine
Modified residue (large scale data)122PRIDEPhosphoserine
Modified residue (large scale data)125PRIDEPhosphoserine
Modified residue (large scale data)149PRIDEPhosphoserine
Modified residue (large scale data)152PRIDEPhosphothreonine
Modified residue (large scale data)184PRIDEPhosphoserine
Modified residue (large scale data)220PRIDEPhosphoserine
Modified residue (large scale data)236PRIDEPhosphoserine
Modified residue (large scale data)257PRIDEPhosphothreonine
Modified residue (large scale data)261PRIDEPhosphothreonine
Modified residue (large scale data)444PRIDEPhosphotyrosine
Modified residue (large scale data)451PRIDEPhosphoserine
Modified residue (large scale data)470PRIDEPhosphoserine
Modified residue (large scale data)694PRIDEPhosphoserine
Modified residue (large scale data)797PRIDEPhosphothreonine
Modified residue883UniProtPhosphoserine
Modified residue887UniProtPhosphoserine
Modified residue (large scale data)992PRIDEPhosphoserine
Modified residue (large scale data)996PRIDEPhosphotyrosine
Modified residue (large scale data)999PRIDEPhosphoserine
Modified residue (large scale data)1044PRIDEPhosphoserine
Modified residue1054UniProtPhosphoserine
Modified residue (large scale data)1054PRIDEPhosphoserine
Modified residue (large scale data)1065PRIDEPhosphoserine
Disulfide bond1160↔1210UniProt
Modified residue (large scale data)1177PRIDEPhosphoserine
Modified residue (large scale data)1178PRIDEPhosphothreonine
Modified residue (large scale data)1181PRIDEPhosphoserine
Modified residue (large scale data)1399PRIDEPhosphoserine
Modified residue (large scale data)1493PRIDEPhosphoserine
Modified residue (large scale data)1497PRIDEPhosphoserine
Modified residue (large scale data)1615PRIDEPhosphoserine
Modified residue (large scale data)1677PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Family & Domains

Features

Showing features for region, compositional bias, repeat, domain.

TypeIDPosition(s)Description
Region33-80Disordered
Compositional bias36-51Polar residues
Compositional bias63-80Polar residues
Compositional bias177-233Polar residues
Region177-244Disordered
Repeat182-1871
Region182-2176 X 6 AA tandem repeats
Repeat188-1932
Repeat194-1993
Repeat200-2054
Repeat206-2115
Repeat212-2176
Domain277-368Ig-like C2-type 1
Domain396-498Ig-like C2-type 2
Domain512-607Fibronectin type-III 1
Domain640-734Fibronectin type-III 2
Domain741-834Fibronectin type-III 3
Region840-938Disordered
Compositional bias880-907Polar residues
Domain933-1034Fibronectin type-III 4
Domain1041-1140Fibronectin type-III 5
Domain1132-1230Ig-like C2-type 3
Domain1358-1444Ig-like C2-type 4
Domain1573-1662Ig-like C2-type 5

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P52179-1

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.

  • Length
    1,685
  • Mass (Da)
    187,627
  • Last updated
    2008-11-04 v2
  • Checksum
    F0DBB25EB6323DF8
MSLPFYQRCHQHYDLSYRNKDVRSTVSHYQREKKRSAVYTQGSTAYSSRSSAAHRRESEAFRRASASSSQQQASQHALSSEVSRKAASAYDYGSSHGLTDSSLLLDDYSSKLSPKPKRAKHSLLSGEEKENLPSDYMVPIFSGRQKHVSGITDTEEERIKEAAAYIAQRNLLASEEGITTSKQSTASKQTTASKQSTASKQSTASKQSTASRQSTASRQSVVSKQATSALQQEETSEKKSRKVVIREKAERLSLRKTLEETETYHAKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSIAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINGCDFEDTAQYRASAMNVKGELSAYASVVVKRYKGEFDETRFHAGASTMPLSFGVTPYGYASRFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHFQPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVKCLEANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKMGIGFPSRVSEPVAALDPAEKARLKSRPSAPWTGQIIVTEEEPSEGIVPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTENWQRVNTELPVKSPRFALFDLAEGKSYCFRVRCSNSAGVGEPSEATEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESKDAKELVGYYIEASVAGSGKWEPCNNNPVKGSRFTCHGLVTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIGGGVSPDVCPALSDEPGGLTASRGRVHEASPPTFQKDALLGSKPNKPSLPSSSQNLGQTEVSKVSETVQEELTPPPQKAAPQGKSKSDPLKKKTDRAPPSPPCDITCLESFRDSMVLGWKQPDKIGGAEITGYYVNYREVIDGVPGKWREANVKAVSEEAYKISNLKENMVYQFQVAAMNMAGLGAPSAVSECFKCEEWTIAVPGPPHSLKCSEVRKDSLVLQWKPPVHSGRTPVTGYFVDLKEAKAKEDQWRGLNEAAIKNVYLKVRGLKEGVSYVFRVRAINQAGVGKPSDLAGPVVAETRPGTKEVVVNVDDDGVISLNFECDKMTPKSEFSWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGIYSCDVTDTDGIASSYLIDEEELKRLLALSHEHKFPTVPVKSELAVEILEKGQVRFWMQAEKLSGNAKVNYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQLQDGKATNHSTVVLVGDVFKKLQKEAEFQRQEWIRKQGPHFVEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKLVDEAFKELMMEVCKKIALSATDLKIQSTAEGIQLYSFVTYYVEDLKVNWSHNGSAIRYSDRVKTGVTGEQIWLQINEPTPNDKGKYVMELFDGKTGHQKTVDLSGQAYDEAYAEFQRLKQAAIAEKNRARVLGGLPDVVTIQEGKALNLTCNVWGDPPPEVSWLKNEKALASDDHCNLKFEAGRTAYFTINGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEEARMAALESLKGGKKAK

P52179-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
J3KRK2J3KRK2_HUMANMYOM1121

Sequence caution

The sequence CAA48833.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias36-51Polar residues
Compositional bias63-80Polar residues
Compositional bias177-233Polar residues
Sequence conflict247in Ref. 5; CAA48833
Sequence conflict442in Ref. 5; CAA48833
Sequence conflict599in Ref. 4; AAI16184
Sequence conflict601in Ref. 5; CAA48833
Sequence conflict615in Ref. 4; AAI16184
Sequence conflict616-625in Ref. 5; CAA48833
Sequence conflict776in Ref. 5; CAA48833
Sequence conflict793-794in Ref. 5; CAA48833
Alternative sequenceVSP_035663836-931in isoform 2
Compositional bias880-907Polar residues
Sequence conflict992in Ref. 5; CAA48833
Sequence conflict1001in Ref. 2; BAC86128
Sequence conflict1080in Ref. 5; CAA48833
Sequence conflict1141in Ref. 5; CAA48833
Sequence conflict1615-1616in Ref. 5; CAA48833
Sequence conflict1617in Ref. 2; BAC86128

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ621424
EMBL· GenBank· DDBJ
CAF18565.1
EMBL· GenBank· DDBJ
mRNA
AK125322
EMBL· GenBank· DDBJ
BAC86128.1
EMBL· GenBank· DDBJ
mRNA
AP005329
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AP005431
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC116183
EMBL· GenBank· DDBJ
AAI16184.1
EMBL· GenBank· DDBJ
mRNA
X69090
EMBL· GenBank· DDBJ
CAA48833.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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