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Protein

Myosin light chain kinase, smooth muscle

Gene

Mylk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca2+ entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells.9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1515ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1607Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1492 – 1500ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • myosin light chain kinase activity Source: MGI
  • protein kinase activity Source: GO_Central

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.18 3474

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
Q6PDN3 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Myosin light chain kinase, smooth muscle (EC:2.7.11.18)
Short name:
MLCK
Short name:
smMLCK
Alternative name(s):
Kinase-related protein
Short name:
KRP
Telokin
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MylkImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:894806 Mylk

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice lacking isoform 1 show a reduced flow-mediated dilation of small mesenteric arteries but no significant changes in main cardiovascular function. Increased survival from burn. Prevention of epithelial MLC phosphorylation, tight junction disruption, protein leak, and diarrhea following T-cell activation.2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002339491 – 1941Myosin light chain kinase, smooth muscleAdd BLAST1941
ChainiPRO_00004037321 – 1934Myosin light chain kinase, smooth muscle, deglutamylated formAdd BLAST1934

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi177 ↔ 228PROSITE-ProRule annotation
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei226Phosphotyrosine; by ABL1By similarity1
Modified residuei295PhosphoserineBy similarity1
Modified residuei333PhosphoserineCombined sources1
Modified residuei355PhosphoserineCombined sources1
Disulfide bondi423 ↔ 475PROSITE-ProRule annotation
Modified residuei452Phosphotyrosine; by ABL1 and SRCBy similarity1
Disulfide bondi523 ↔ 571PROSITE-ProRule annotation
Disulfide bondi730 ↔ 793PROSITE-ProRule annotation
Modified residuei780Phosphotyrosine; by ABL1By similarity1
Modified residuei935PhosphoserineCombined sources1
Disulfide bondi1141 ↔ 1192PROSITE-ProRule annotation
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1471Phosphotyrosine; by ABL1By similarity1
Modified residuei1597Phosphotyrosine; by ABL1By similarity1
Modified residuei1657Phosphotyrosine; by ABL1By similarity1
Modified residuei1781PhosphoserineCombined sources1
Modified residuei1782PhosphoserineCombined sources1
Modified residuei1794PhosphoserineBy similarity1
Modified residuei1795PhosphoserineCombined sources1
Modified residuei1798PhosphoserineCombined sources1
Modified residuei1800PhosphothreonineCombined sources1
Modified residuei1801PhosphoserineCombined sources1
Disulfide bondi1852 ↔ 1904PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-452 promotes CTTN binding (By similarity).By similarity
The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (PubMed:21074048).1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6PDN3

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q6PDN3

PeptideAtlas

More...
PeptideAtlasi
Q6PDN3

PRoteomics IDEntifications database

More...
PRIDEi
Q6PDN3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6PDN3

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q6PDN3

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Smooth muscle isoform is expressed in all tissues with highest levels in bladder, uterus, vas deferens, colon, ileum, and tracheae. Isoform 1 is expressed in lung, bladder, and vas deferens. Telokin is expressed in smooth muscle cells of the gut, reproductive tract and urinary tract, including in uterus, vas deferens, bladder, colon, kidney, ureter and ovary. Telokin is also detected in the trachea.3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Isoform 1 is widely expressed at 14.5 dpc embryos with highest levels in some areas of the developing brain, the lower gastrointestinal tract, as well as certain blood vessels. Primary cultures of endothelial cells lose high level expression of smooth muscle isoform with increasing number of passages. Telokin is expressed in the embryonic gut from 11.5 dpc with highest level at 15.5 dpc. Also expressed in developing bronchi from 13.5 dpc. High levels in 15.5 dpc bladder, ureter, urethra and rectum. Telokin expression is induced in reproductive tract during postnatal development.2 Publications

Gene expression databases

CleanEx database of gene expression profiles

More...
CleanExi
MM_MYLK

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

All isoforms including Telokin bind calmodulin. Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 (By similarity). Interacts with SVIL and PTK2B/PYK2.By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Patz1Q9JMG93EBI-647412,EBI-647451

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q6PDN3, 21 interactors

Molecular INTeraction database

More...
MINTi
Q6PDN3

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000023538

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q6PDN3

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q6PDN3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini33 – 122Ig-like C2-type 1Sequence analysisAdd BLAST90
Domaini156 – 244Ig-like C2-type 2Sequence analysisAdd BLAST89
Domaini402 – 485Ig-like C2-type 3Sequence analysisAdd BLAST84
Domaini502 – 587Ig-like C2-type 4Sequence analysisAdd BLAST86
Domaini611 – 699Ig-like C2-type 5Sequence analysisAdd BLAST89
Domaini709 – 809Ig-like C2-type 6Sequence analysisAdd BLAST101
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati856 – 8831-1By similarityAdd BLAST28
Repeati884 – 9111-2By similarityAdd BLAST28
Repeati912 – 9391-3By similarityAdd BLAST28
Repeati940 – 9661-4By similarityAdd BLAST27
Repeati967 – 9851-5; truncatedAdd BLAST19
Repeati990 – 10022-1By similarityAdd BLAST13
Repeati1003 – 10142-2By similarityAdd BLAST12
Repeati1015 – 10262-3By similarityAdd BLAST12
Repeati1027 – 10382-4By similarityAdd BLAST12
Repeati1039 – 10492-5By similarityAdd BLAST11
Domaini1120 – 1208Ig-like C2-type 7Sequence analysisAdd BLAST89
Domaini1260 – 1348Ig-like C2-type 8Sequence analysisAdd BLAST89
Domaini1356 – 1449Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST94
Domaini1486 – 1741Protein kinasePROSITE-ProRule annotationAdd BLAST256
Domaini1831 – 1920Ig-like C2-type 9Sequence analysisAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni856 – 9855 X 28 AA approximate tandem repeatsAdd BLAST130
Regioni911 – 951Actin-binding (calcium/calmodulin-sensitive)By similarityAdd BLAST41
Regioni936 – 951Calmodulin-bindingBy similarityAdd BLAST16
Regioni990 – 10495 X 12 AA approximate tandem repeatsAdd BLAST60
Regioni1048 – 1482Actin-binding (calcium/calmodulin-insensitive)By similarityAdd BLAST435
Regioni1733 – 1796Calmodulin-bindingBy similarityAdd BLAST64

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1918 – 1941Glu-richSequence analysisAdd BLAST24

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0613 Eukaryota
ENOG410XQFD LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157879

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052551

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6PDN3

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063 FN3, 1 hit
cd14191 STKc_MLCK1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 10 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR015725 MLCK1_kinase_dom
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00041 fn3, 1 hit
PF07679 I-set, 9 hits
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00060 FN3, 1 hit
SM00409 IG, 9 hits
SM00408 IGc2, 9 hits
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 9 hits
SSF49265 SSF49265, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 1 hit
PS50835 IG_LIKE, 9 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 11 Publication (identifier: Q6PDN3-1) [UniParc]FASTAAdd to basket
Also known as: Non muscle isozyme1 Publication

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
MGDVKLFASS HMSKTSHSVD PSKVSSMPLT EAPAFILPPR NLCVKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRKG QAITNGGRFL LDCGVRGTFS LVIHTVREED
110 120 130 140 150
KGKYTCEASN GSGARQVTVE LTVEGNSMKK RDQPVLSKAS GFPGETRPSI
160 170 180 190 200
WGECPPKFAT KLGRAVVKEG QMWRFSCKIT GRPPPQVTWL KGNVPLQPSA
210 220 230 240 250
RVSMSEKNGM QILEIRGVTR DDLGVYTCMV VNGSGKASMS AELSIPGLDN
260 270 280 290 300
ASRLAVRGTK APSPDIRKEV TNGVSKDPET VAESKNCPSP QRSGSSARAT
310 320 330 340 350
NSHLKSPQEP KPKLCEDAPR KVPQSSILQK STSTITLQAL KVQPEARVPA
360 370 380 390 400
IGSFSPGEDR KSLAAPQQAT LPTRQSSLGG SVGNKFVTGN IPRESQREST
410 420 430 440 450
FPRFESQPQS QEVTEGQTVK FICEVSGIPK PDVGWFLEGI PVRRREGITE
460 470 480 490 500
VYEDGVSHHL CLLRARTRDS RKYSCTASNS LGQVSCSWSL LVDRPNLAQT
510 520 530 540 550
APSFSSVLKD SVVIEGQDFV LRCSVQGTPA PRVTWLLNGQ PIQFAHSICE
560 570 580 590 600
AGVAELHIQD ALPEDRGTYT CLAENAMGQV SCSATVTVQE KKGEGEREHR
610 620 630 640 650
LSPARSKPIA PIFLQGLSDL KVMDGSQVTM TVQVSGNPPP EVIWLHDGNE
660 670 680 690 700
IQESEDFHFE QKGGWHSLCI QEVFPEDTGT YTCEAWNSAG EVRTRAVLTV
710 720 730 740 750
QEPHDGTQPW FISKPRSVTA TLGQSVLISC AIAGDPFPTV HWLRDGRALS
760 770 780 790 800
KDSGHFELLQ NEDVFTLVLK NVQPWHAGQY EILLKNRVGE CSCQVSLMLH
810 820 830 840 850
NSPSRAPPRG REPASCEGLC GGGGVGAHGD GDRHGTLRPC WPARGQGWPE
860 870 880 890 900
EEDGEDVRGL LKRRVETRLH TEEAIRQQEV GQLDFRDLLG KKVSTKTVSE
910 920 930 940 950
DDLKDIPAEQ MDFRANLQRQ VKPKTISEEE RKVHSPQQVD FRSVLAKKGT
960 970 980 990 1000
PKTPVPEKAP PKAATPDFRS VLGGKKKSPS ENGGNSAEVL NVKAGESPTP
1010 1020 1030 1040 1050
AGDAQAIGAL KPVGNAKPAE TPKPIGNAKP TETLKPVGNT KPAETLKPIA
1060 1070 1080 1090 1100
NAQPSGSLKP VTNAQPAEPQ KPVGNAKSAE TSKPAGKEEV KEVKNDVNCK
1110 1120 1130 1140 1150
KGQVGATGNE KRPESQGSAP VFKEKLQDVH VAEGEKLLLQ CQVISDPPAT
1160 1170 1180 1190 1200
VTWSLNGKTL KTTKFIVLAQ EGSRFSVSIE KALPEDRGLY KCVAKNSAGQ
1210 1220 1230 1240 1250
AECSCQVTVD DAQTSENTKA PEMKSRRPKS SLPPVLGTES DATVKKKPAP
1260 1270 1280 1290 1300
KTPTKAAMPP QIIQFPEDQK VRAGEPVELF GKVAGTQPIT CKWMKFRKQI
1310 1320 1330 1340 1350
QESEHIKVEN GESGSKLTIL AARQEHCGCY TLVVENKLGS RQAQVNLTVV
1360 1370 1380 1390 1400
DKPDPPAGTP CASDIRSSSL TLSWYGSSYD GGSAVQSYNV EIWDTEDKVW
1410 1420 1430 1440 1450
KELATCRSTS FNVQDLLPDR EYKFRVRAVN VYGTSEPSQE SELTAVGEKP
1460 1470 1480 1490 1500
EEPKDEVEVS DDDEKEPEVD YRTVTVNTEQ KVSDVYDIEE RLGSGKFGQV
1510 1520 1530 1540 1550
FRLVEKKTGK IWAGKFFKAY SAKEKDNIRQ EISIMNCLHH PKLVQCVDAF
1560 1570 1580 1590 1600
EEKANIVMVL EIVSGGELFE RIIDEDFELT ERECIKYMRQ ISEGVEYIHK
1610 1620 1630 1640 1650
QGIVHLDLKP ENIMCVNKTG TRIKLIDFGL ARRLENAGSL KVLFGTPEFV
1660 1670 1680 1690 1700
APEVINYEPI GYATDMWSIG VICYILVSGL SPFMGDNDNE TLANVTSATW
1710 1720 1730 1740 1750
DFDDEAFDEI SDDAKDFISN LLKKDMKNRL DCTQCLQHPW LMKDTKNMEA
1760 1770 1780 1790 1800
KKLSKDRMKK YMARRKWQKT GNAVRAIGRL SSMAMISGLS GRKSSTGSPT
1810 1820 1830 1840 1850
SPINAEKLES EDDVSQAFLE AVAEEKPHVK PYFSKTIRDL EVVEGSAARF
1860 1870 1880 1890 1900
DCKIEGYPDP EVVWFKDDQS IRESRHFQID YDEDGNCSLI ISDVCGDDDA
1910 1920 1930 1940
KYTCKAVNSL GEATCTAELI VETMEEGEGE EGGEEEEEEE E
Length:1,941
Mass (Da):212,925
Last modified:May 2, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7FF12C60F1BDFFDD
GO
Isoform 21 Publication (identifier: Q6PDN3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1254: Missing.
     1255-1256: KA → MQ

Note: Might be produced by alternative promoter usage and alternative splicing. No experimental confirmation available.
Show »
Length:687
Mass (Da):77,433
Checksum:iDCCF826A8ABA42B5
GO
Isoform 3 (identifier: Q6PDN3-3) [UniParc]FASTAAdd to basket
Also known as: Smooth muscle isozyme

The sequence of this isoform differs from the canonical sequence as follows:
     1-910: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:1,031
Mass (Da):113,703
Checksum:iD9435CF18C0E4337
GO
Isoform 4 (identifier: Q6PDN3-4) [UniParc]FASTAAdd to basket
Also known as: Telokin

The sequence of this isoform differs from the canonical sequence as follows:
     1-1782: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:159
Mass (Da):17,529
Checksum:i7EFDC75F450F3B6D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1B1A8B1B1A8_MOUSE
Myosin light chain kinase, smooth m...
Mylk
1,950Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH58610 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAO85807 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti173W → G (PubMed:11832329).Curated1
Sequence conflicti173W → G (PubMed:11472067).Curated1
Sequence conflicti252S → A in AAK53241 (PubMed:11472067).Curated1
Sequence conflicti471 – 472RK → GR (PubMed:11832329).Curated2
Sequence conflicti471 – 472RK → GR (PubMed:11472067).Curated2
Sequence conflicti478S → T in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti482G → A in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti666 – 667HS → TP in AAO85807 (PubMed:11832329).Curated2
Sequence conflicti677D → S in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti749 – 750LS → SP in AAO85807 (PubMed:11832329).Curated2
Sequence conflicti1004A → G in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1038G → A in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1106A → R in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1174 – 1181RFSVSIEK → TFLCLHRE in AAO85807 (PubMed:11832329).Curated8
Sequence conflicti1210D → A in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1289I → T in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1340Missing in BAE36678 (PubMed:16141072).Curated1
Sequence conflicti1409T → H in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1657Y → H in AAH58610 (PubMed:15489334).Curated1
Sequence conflicti1661G → R in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1678S → R in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1706A → E in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1732 – 1735CTQC → STHG in AAO85807 (PubMed:11832329).Curated4
Sequence conflicti1825E → K in AAO85807 (PubMed:11832329).Curated1
Sequence conflicti1888S → T in AAG34169 (PubMed:11121372).Curated1
Sequence conflicti1941Missing in AAH58610 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0188481 – 1782Missing in isoform 4. 1 PublicationAdd BLAST1782
Alternative sequenceiVSP_0520021 – 1254Missing in isoform 2. 1 PublicationAdd BLAST1254
Alternative sequenceiVSP_0188471 – 910Missing in isoform 3. 1 PublicationAdd BLAST910
Alternative sequenceiVSP_0520031255 – 1256KA → MQ in isoform 2. 1 Publication2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY237727 mRNA Translation: AAO85808.1
AF314149 mRNA Translation: AAG34169.1
AY237726 mRNA Translation: AAO85807.1 Different initiation.
AK162008 mRNA Translation: BAE36678.1
BC034209 mRNA Translation: AAH34209.1
BC045197 mRNA Translation: AAH45197.1
BC058610 mRNA Translation: AAH58610.2 Different initiation.
AF335470 Genomic DNA Translation: AAK53241.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.33360

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000231589; ENSMUSP00000156149; ENSMUSG00000022836 [Q6PDN3-4]

UCSC genome browser

More...
UCSCi
uc007zbe.1 mouse [Q6PDN3-1]
uc007zbh.1 mouse [Q6PDN3-4]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237727 mRNA Translation: AAO85808.1
AF314149 mRNA Translation: AAG34169.1
AY237726 mRNA Translation: AAO85807.1 Different initiation.
AK162008 mRNA Translation: BAE36678.1
BC034209 mRNA Translation: AAH34209.1
BC045197 mRNA Translation: AAH45197.1
BC058610 mRNA Translation: AAH58610.2 Different initiation.
AF335470 Genomic DNA Translation: AAK53241.1
UniGeneiMm.33360

3D structure databases

ProteinModelPortaliQ6PDN3
SMRiQ6PDN3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6PDN3, 21 interactors
MINTiQ6PDN3
STRINGi10090.ENSMUSP00000023538

Protein family/group databases

MoonDBiQ6PDN3 Predicted

PTM databases

iPTMnetiQ6PDN3
PhosphoSitePlusiQ6PDN3

Proteomic databases

jPOSTiQ6PDN3
PaxDbiQ6PDN3
PeptideAtlasiQ6PDN3
PRIDEiQ6PDN3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000231589; ENSMUSP00000156149; ENSMUSG00000022836 [Q6PDN3-4]
UCSCiuc007zbe.1 mouse [Q6PDN3-1]
uc007zbh.1 mouse [Q6PDN3-4]

Organism-specific databases

MGIiMGI:894806 Mylk

Phylogenomic databases

eggNOGiKOG0613 Eukaryota
ENOG410XQFD LUCA
GeneTreeiENSGT00940000157879
HOVERGENiHBG052551
InParanoidiQ6PDN3

Enzyme and pathway databases

BRENDAi2.7.11.18 3474

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Mylk mouse

Protein Ontology

More...
PROi
PR:Q6PDN3

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

CleanExiMM_MYLK

Family and domain databases

CDDicd00063 FN3, 1 hit
cd14191 STKc_MLCK1, 1 hit
Gene3Di2.60.40.10, 10 hits
InterProiView protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR015725 MLCK1_kinase_dom
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00041 fn3, 1 hit
PF07679 I-set, 9 hits
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00060 FN3, 1 hit
SM00409 IG, 9 hits
SM00408 IGc2, 9 hits
SM00220 S_TKc, 1 hit
SUPFAMiSSF48726 SSF48726, 9 hits
SSF49265 SSF49265, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50853 FN3, 1 hit
PS50835 IG_LIKE, 9 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMYLK_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6PDN3
Secondary accession number(s): Q3TSJ7
, Q80UX0, Q80YN7, Q80YN8, Q8K026, Q924D2, Q9ERD3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: January 16, 2019
This is version 133 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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