A0A8I5QKL9 · A0A8I5QKL9_HUMAN
- ProteinMyosin light chain kinase, smooth muscle
- GeneMYLK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1660 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 1239 | ATP (UniProtKB | ChEBI) | |||
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | protein kinase activity | |
Biological Process | muscle structure development | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyosin light chain kinase, smooth muscle
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A8I5QKL9
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Modified residue (large scale data) | 357 | PRIDE | Phosphotyrosine | |||
Modified residue (large scale data) | 693 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 837 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 897 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1083 | PRIDE | Phosphothreonine | |||
Modified residue (large scale data) | 1184 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1316 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1363 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1505 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1506 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1514 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1518 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1519 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1520 | PRIDE | Phosphothreonine | |||
Modified residue (large scale data) | 1522 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1524 | PRIDE | Phosphothreonine | |||
Modified residue (large scale data) | 1525 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1534 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1539 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1594 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1598 | PRIDE | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 33-122 | Ig-like | |||
Domain | 161-249 | Ig-like | |||
Domain | 260-345 | Ig-like | |||
Domain | 366-457 | Ig-like | |||
Domain | 467-554 | Ig-like | |||
Region | 678-844 | Disordered | |||
Compositional bias | 681-695 | Basic and acidic residues | |||
Compositional bias | 741-768 | Polar residues | |||
Compositional bias | 804-834 | Basic and acidic residues | |||
Domain | 844-932 | Ig-like | |||
Region | 938-983 | Disordered | |||
Domain | 984-1072 | Ig-like | |||
Domain | 1080-1172 | Fibronectin type-III | |||
Region | 1159-1192 | Disordered | |||
Domain | 1210-1465 | Protein kinase | |||
Compositional bias | 1513-1529 | Polar residues | |||
Region | 1513-1533 | Disordered | |||
Domain | 1555-1644 | Ig-like | |||
Sequence similarities
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,660
- Mass (Da)182,972
- Last updated2022-05-25 v1
- Checksum549531FFE71C6A13
Computationally mapped potential isoform sequences
There are 20 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q15746 | MYLK_HUMAN | MYLK | 1914 | ||
A0A8I5QKW8 | A0A8I5QKW8_HUMAN | MYLK | 690 | ||
A0A8I5QJT9 | A0A8I5QJT9_HUMAN | MYLK | 625 | ||
A0A8I5QJW9 | A0A8I5QJW9_HUMAN | MYLK | 720 | ||
A0A8J9G5A3 | A0A8J9G5A3_HUMAN | MYLK | 82 | ||
F8WBL7 | F8WBL7_HUMAN | MYLK | 70 | ||
D6R9C2 | D6R9C2_HUMAN | MYLK | 229 | ||
A0A8I5KS78 | A0A8I5KS78_HUMAN | MYLK | 76 | ||
A0A8I5KQY6 | A0A8I5KQY6_HUMAN | MYLK | 251 | ||
A0A8I5KTQ1 | A0A8I5KTQ1_HUMAN | MYLK | 713 | ||
A0A8I5KU53 | A0A8I5KU53_HUMAN | MYLK | 1924 | ||
A0A8I5KUP2 | A0A8I5KUP2_HUMAN | MYLK | 953 | ||
A0A8I5KUH4 | A0A8I5KUH4_HUMAN | MYLK | 476 | ||
A0A8I5KUB2 | A0A8I5KUB2_HUMAN | MYLK | 924 | ||
A0A8I5KVV3 | A0A8I5KVV3_HUMAN | MYLK | 31 | ||
A0A8I5KYA1 | A0A8I5KYA1_HUMAN | MYLK | 83 | ||
A0A8I5KYB9 | A0A8I5KYB9_HUMAN | MYLK | 59 | ||
A0A8I5KYZ0 | A0A8I5KYZ0_HUMAN | MYLK | 462 | ||
A0A8I5KZ33 | A0A8I5KZ33_HUMAN | MYLK | 47 | ||
A0A8I5KXG8 | A0A8I5KXG8_HUMAN | MYLK | 442 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 681-695 | Basic and acidic residues | |||
Compositional bias | 741-768 | Polar residues | |||
Compositional bias | 804-834 | Basic and acidic residues | |||
Compositional bias | 1513-1529 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC020634 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC023165 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC117381 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |