Q96Q04 · LMTK3_HUMAN
- ProteinSerine/threonine-protein kinase LMTK3
- GeneLMTK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1460 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein kinase which phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. May also regulate ESR1 levels indirectly via a PKC-AKT-FOXO3 pathway where it decreases the activity of PKC and the phosphorylation of AKT, thereby increasing binding of transcriptional activator FOXO3 to the ESR1 promoter and increasing ESR1 transcription (PubMed:21602804).
Involved in endocytic trafficking of N-methyl-D-aspartate receptors (NMDAR) in neurons (By similarity).
Involved in endocytic trafficking of N-methyl-D-aspartate receptors (NMDAR) in neurons (By similarity).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | dendrite | |
Cellular Component | Golgi membrane | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase LMTK3
- 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 accessionQ96Q04
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Note: Punctate pattern in cell projections.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 40-60 | Helical | ||||
Sequence: AVVLISCSGLLAFIFLLLTCL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057116 | 900 | in dbSNP:rs1643478 | |||
Sequence: V → L | ||||||
Natural variant | VAR_028943 | 929 | in dbSNP:rs1643478 | |||
Sequence: L → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,770 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-20 | UniProt | |||||
Sequence: MPAPGALILLAAVSASGCLA | |||||||
Chain | PRO_0000259460 | 21-1460 | UniProt | Serine/threonine-protein kinase LMTK3 | |||
Sequence: SPAHPDGFALGRAPLAPPYAVVLISCSGLLAFIFLLLTCLCCKRGDVGFKEFENPEGEDCSGEYTPPAEETSSSQSLPDVYILPLAEVSLPMPAPQPSHSDMTTPLGLSRQHLSYLQEIGSGWFGKVILGEIFSDYTPAQVVVKELRASAGPLEQRKFISEAQPYRSLQHPNVLQCLGLCVETLPFLLIMEFCQLGDLKRYLRAQRPPEGLSPELPPRDLRTLQRMGLEIARGLAHLHSHNYVHSDLALRNCLLTSDLTVRIGDYGLAHSNYKEDYYLTPERLWIPLRWAAPELLGELHGTFMVVDQSRESNIWSLGVTLWELFEFGAQPYRHLSDEEVLAFVVRQQHVKLARPRLKLPYADYWYDILQSCWRPPAQRPSASDLQLQLTYLLSERPPRPPPPPPPPRDGPFPWPWPPAHSAPRPGTLSSPFPLLDGFPGADPDDVLTVTESSRGLNLECLWEKARRGAGRGGGAPAWQPASAPPAPHANPSNPFYEALSTPSVLPVISARSPSVSSEYYIRLEEHGSPPEPLFPNDWDPLDPGVPAPQAPQAPSEVPQLVSETWASPLFPAPRPFPAQSSASGSFLLSGWDPEGRGAGETLAGDPAEVLGERGTAPWVEEEEEEEEGSSPGEDSSSLGGGPSRRGPLPCPLCSREGACSCLPLERGDAVAGWGGHPALGCPHPPEDDSSLRAERGSLADLPMAPPASAPPEFLDPLMGAAAPQYPGRGPPPAPPPPPPPPRAPADPAASPDPPSAVASPGSGLSSPGPKPGDSGYETETPFSPEGAFPGGGAAEEEGVPRPRAPPEPPDPGAPRPPPDPGPLPLPGPREKPTFVVQVSTEQLLMSLREDVTRNLLGEKGATARETGPRKAGRGPGNREKVPGLNRDPTVLGNGKQAPSLSLPVNGVTVLENGDQRAPGIEEKAAENGALGSPEREEKVLENGELTPPRREEKALENGELRSPEAGEKVLVNGGLTPPKSEDKVSENGGLRFPRNTERPPETGPWRAPGPWEKTPESWGPAPTIGEPAPETSLERAPAPSAVVSSRNGGETAPGPLGPAPKNGTLEPGTERRAPETGGAPRAPGAGRLDLGSGGRAPVGTGTAPGGGPGSGVDAKAGWVDNTRPQPPPPPLPPPPEAQPRRLEPAPPRARPEVAPEGEPGAPDSRAGGDTALSGDGDPPKPERKGPEMPRLFLDLGPPQGNSEQIKARLSRLSLALPPLTLTPFPGPGPRRPPWEGADAGAAGGEAGGAGAPGPAEEDGEDEDEDEEEDEEAAAPGAAAGPRGPGRARAAPVPVVVSSADADAARPLRGLLKSPRGADEPEDSELERKRKMVSFHGDVTVYLFDQETPTNELSVQAPPEGDTDPSTPPAPPTPPHPATPGDGFPSNDSGFGGSFEWAEDFPLLPPPGPPLCFSRFSVSPALETPGPPARAPDARPAGPVEN | |||||||
Modified residue | 232 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 490 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 531 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 535 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 981 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 1081 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1405 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with ESR1 (PubMed:21602804).
Interacts with AP-2 complex subunit alpha (By similarity).
Interacts with AP-2 complex subunit alpha (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96Q04 | ESR1 P03372 | 3 | EBI-720814, EBI-78473 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 75-95 | Disordered | ||||
Sequence: PEGEDCSGEYTPPAEETSSSQ | ||||||
Domain | 133-411 | Protein kinase | ||||
Sequence: LSYLQEIGSGWFGKVILGEIFSDYTPAQVVVKELRASAGPLEQRKFISEAQPYRSLQHPNVLQCLGLCVETLPFLLIMEFCQLGDLKRYLRAQRPPEGLSPELPPRDLRTLQRMGLEIARGLAHLHSHNYVHSDLALRNCLLTSDLTVRIGDYGLAHSNYKEDYYLTPERLWIPLRWAAPELLGELHGTFMVVDQSRESNIWSLGVTLWELFEFGAQPYRHLSDEEVLAFVVRQQHVKLARPRLKLPYADYWYDILQSCWRPPAQRPSASDLQLQLTYL | ||||||
Region | 413-456 | Disordered | ||||
Sequence: SERPPRPPPPPPPPRDGPFPWPWPPAHSAPRPGTLSSPFPLLDG | ||||||
Compositional bias | 414-443 | Pro residues | ||||
Sequence: ERPPRPPPPPPPPRDGPFPWPWPPAHSAPR | ||||||
Region | 486-513 | Disordered | ||||
Sequence: RGAGRGGGAPAWQPASAPPAPHANPSNP | ||||||
Region | 544-578 | Disordered | ||||
Sequence: EHGSPPEPLFPNDWDPLDPGVPAPQAPQAPSEVPQ | ||||||
Compositional bias | 552-572 | Pro residues | ||||
Sequence: LFPNDWDPLDPGVPAPQAPQA | ||||||
Region | 591-669 | Disordered | ||||
Sequence: APRPFPAQSSASGSFLLSGWDPEGRGAGETLAGDPAEVLGERGTAPWVEEEEEEEEGSSPGEDSSSLGGGPSRRGPLPC | ||||||
Region | 686-855 | Disordered | ||||
Sequence: GDAVAGWGGHPALGCPHPPEDDSSLRAERGSLADLPMAPPASAPPEFLDPLMGAAAPQYPGRGPPPAPPPPPPPPRAPADPAASPDPPSAVASPGSGLSSPGPKPGDSGYETETPFSPEGAFPGGGAAEEEGVPRPRAPPEPPDPGAPRPPPDPGPLPLPGPREKPTFVV | ||||||
Compositional bias | 744-773 | Pro residues | ||||
Sequence: YPGRGPPPAPPPPPPPPRAPADPAASPDPP | ||||||
Compositional bias | 823-848 | Pro residues | ||||
Sequence: APPEPPDPGAPRPPPDPGPLPLPGPR | ||||||
Region | 872-1349 | Disordered | ||||
Sequence: RNLLGEKGATARETGPRKAGRGPGNREKVPGLNRDPTVLGNGKQAPSLSLPVNGVTVLENGDQRAPGIEEKAAENGALGSPEREEKVLENGELTPPRREEKALENGELRSPEAGEKVLVNGGLTPPKSEDKVSENGGLRFPRNTERPPETGPWRAPGPWEKTPESWGPAPTIGEPAPETSLERAPAPSAVVSSRNGGETAPGPLGPAPKNGTLEPGTERRAPETGGAPRAPGAGRLDLGSGGRAPVGTGTAPGGGPGSGVDAKAGWVDNTRPQPPPPPLPPPPEAQPRRLEPAPPRARPEVAPEGEPGAPDSRAGGDTALSGDGDPPKPERKGPEMPRLFLDLGPPQGNSEQIKARLSRLSLALPPLTLTPFPGPGPRRPPWEGADAGAAGGEAGGAGAPGPAEEDGEDEDEDEEEDEEAAAPGAAAGPRGPGRARAAPVPVVVSSADADAARPLRGLLKSPRGADEPEDSELERKRK | ||||||
Compositional bias | 911-927 | Polar residues | ||||
Sequence: GNGKQAPSLSLPVNGVT | ||||||
Compositional bias | 947-982 | Basic and acidic residues | ||||
Sequence: GALGSPEREEKVLENGELTPPRREEKALENGELRSP | ||||||
Compositional bias | 1141-1172 | Pro residues | ||||
Sequence: TRPQPPPPPLPPPPEAQPRRLEPAPPRARPEV | ||||||
Compositional bias | 1274-1292 | Acidic residues | ||||
Sequence: AEEDGEDEDEDEEEDEEAA | ||||||
Compositional bias | 1331-1349 | Basic and acidic residues | ||||
Sequence: KSPRGADEPEDSELERKRK | ||||||
Region | 1361-1460 | Disordered | ||||
Sequence: LFDQETPTNELSVQAPPEGDTDPSTPPAPPTPPHPATPGDGFPSNDSGFGGSFEWAEDFPLLPPPGPPLCFSRFSVSPALETPGPPARAPDARPAGPVEN | ||||||
Compositional bias | 1362-1379 | Polar residues | ||||
Sequence: FDQETPTNELSVQAPPEG | ||||||
Compositional bias | 1380-1399 | Pro residues | ||||
Sequence: DTDPSTPPAPPTPPHPATPG |
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,460
- Mass (Da)153,661
- Last updated2006-10-31 v2
- ChecksumFF99FBFD873C73D3
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F9ZH67 | A0A5F9ZH67_HUMAN | LMTK3 | 1215 | ||
A0A5F9ZHT0 | A0A5F9ZHT0_HUMAN | LMTK3 | 68 | ||
A0A3B3IRV9 | A0A3B3IRV9_HUMAN | LMTK3 | 154 | ||
A0A3B3ISL5 | A0A3B3ISL5_HUMAN | LMTK3 | 1486 | ||
A0A3B3ITQ7 | A0A3B3ITQ7_HUMAN | LMTK3 | 650 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 414-443 | Pro residues | ||||
Sequence: ERPPRPPPPPPPPRDGPFPWPWPPAHSAPR | ||||||
Compositional bias | 552-572 | Pro residues | ||||
Sequence: LFPNDWDPLDPGVPAPQAPQA | ||||||
Compositional bias | 744-773 | Pro residues | ||||
Sequence: YPGRGPPPAPPPPPPPPRAPADPAASPDPP | ||||||
Sequence conflict | 774 | in Ref. 3; AAH36690 | ||||
Sequence: S → A | ||||||
Compositional bias | 823-848 | Pro residues | ||||
Sequence: APPEPPDPGAPRPPPDPGPLPLPGPR | ||||||
Compositional bias | 911-927 | Polar residues | ||||
Sequence: GNGKQAPSLSLPVNGVT | ||||||
Compositional bias | 947-982 | Basic and acidic residues | ||||
Sequence: GALGSPEREEKVLENGELTPPRREEKALENGELRSP | ||||||
Compositional bias | 1141-1172 | Pro residues | ||||
Sequence: TRPQPPPPPLPPPPEAQPRRLEPAPPRARPEV | ||||||
Compositional bias | 1274-1292 | Acidic residues | ||||
Sequence: AEEDGEDEDEDEEEDEEAA | ||||||
Compositional bias | 1331-1349 | Basic and acidic residues | ||||
Sequence: KSPRGADEPEDSELERKRK | ||||||
Compositional bias | 1362-1379 | Polar residues | ||||
Sequence: FDQETPTNELSVQAPPEG | ||||||
Compositional bias | 1380-1399 | Pro residues | ||||
Sequence: DTDPSTPPAPPTPPHPATPG | ||||||
Sequence conflict | 1398 | in Ref. 3; AAH36690 | ||||
Sequence: P → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB067470 EMBL· GenBank· DDBJ | BAB67776.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC008403 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC036690 EMBL· GenBank· DDBJ | AAH36690.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |