LTK
entrez
4058
canonical
uniprot
P29376
canonical
ensembl
ENSG00000062524
resolver
ensp
ENSP00000263800
resolver
ensp
ENSP00000347293
resolver
ensp
ENSP00000392196
resolver
ensp
ENSP00000458111
resolver
ensp
ENSP00000567526
resolver
ensp
ENSP00000567527
resolver
genesymbol
LTK
resolver
genesymbol_syn
TYK1
resolver
hgnc
HGNC:6721
resolver
uniprot
A6NNJ8
resolver
uniprot
B4DL89
resolver
uniprot
E9PFX4
resolver
uniprot_entry
LTK_HUMAN
resolver
uniprot_sec
A6NNJ8
resolver
uniprot_sec
B4DL89
resolver
uniprot_sec
E9PFX4
resolver
activity_regulation
ACTIVITY REGULATION: Activated by ligand-binding, leading to homodimerization and autophosphorylation. {ECO:0000250|UniProtKB:Q9UM73}.
uniprot
proteins
amino_acid_sequence
MGCWGQLLVWFGAAGAILCSSPGSQETFLRSSPLPLASPSPRDPKVSAPPSILEPASPLNSPGTEGSWLFSTCGASGRHGPTQTQCDGAYAGTSVVVTVGAAGQLRGVQLWRVPGPGQYLISAYGAAGGKGAKNHLSRAHGVFVSAIFSLGLGESLYILVGQQGEDACPGGSPESQLVCLGESRAVEEHAAMDGSEGVPGSRRWAGGGGGGGGATYVFRVRAGELEPLLVAAGGGGRAYLRPRDRGRTQASPEKLENRSEAPGSGGRGGAAGGGGGWTSRAPSPQAGRSLQEGAEGGQGCSEAWATLGWAAAGGFGGGGGACTAGGGGGGYRGGDASETDNLWADGEDGVSFIHPSSELFLQPLAVTENHGEVEIRRHLNCSHCPLRDCQWQAELQLAECLCPEGMELAVDNVTCMDLHKPPGPLVLMVAVVATSTLSLLMVCGVLILVKQKKWQGLQEMRLPSPELELSKLRTSAIRTAPNPYYCQVGLGPAQSWPLPPGVTEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQYCTQDPDVLNSLLPMELGPTPEEEGTSGLGNRSLECLRPPQPQELSPEKLKSWGGSPLGPWLSSGLKPLKSRGLQPQNLWNPTYRS
uniprot
proteins
disease_involvement
DISEASE: Note=Genetic variations in LTK that cause up-regulation of the PI3K pathway may possibly contribute to susceptibility to abnormal proliferation of self-reactive B-cells and, therefore, to systemic lupus erythematosus (SLE) (PubMed:14695357). SLE is a chronic, inflammatory and often febrile multisystemic disorder of connective tissue, thought to represent a failure of the regulatory mechanisms of the autoimmune system (PubMed:14695357). {ECO:0000269|PubMed:14695357}.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Receptor with a tyrosine-protein kinase activity (PubMed:10445845, PubMed:20548102, PubMed:30061385). Following activation by ALKAL1 or ALKAL2 ligands at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:30061385, PubMed:34646012). Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activated protein kinase (MAPK) pathway (PubMed:20548102). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity). The exact function of this protein is not known; studies with chimeric proteins demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival (PubMed:18849880, PubMed:9223670). Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport (PubMed:20548102). {ECO:0000250|UniProtKB:Q9UM73, ECO:0000269|PubMed:10445845, ECO:0000269|PubMed:18849880, ECO:0000269|PubMed:20548102, ECO:0000269|PubMed:30061385, ECO:0000269|PubMed:34646012, ECO:0000269|PubMed:9223670}.
uniprot
proteins
mass_dalton
91681
uniprot
proteins
mutagenesis
MUTAGEN 241; /note="R->A: Abolished homodimerization following interaction with ALKAL1."; /evidence="ECO:0000269|PubMed:34646012"; MUTAGEN 544; /note="K->M: Loss of interaction with PLCG1, PI3-kinase subunit p85, Ras GTPase-activating protein and RAF1."; /evidence="ECO:0000269|PubMed:8084603"; MUTAGEN 750; /note="G->E: Increases autophosphorylation and interaction with PI3-kinase subunit p85 (demonstrated with chimeric EGFR-LTK)."; /evidence="ECO:0000269|PubMed:14695357"; MUTAGEN 753; /note="Y->F: Abolishes interaction with PI3-kinase subunit p85, impairs PI3 kinase activity and leads to apoptosis (demonstrated with chimeric EGFR-LTK)."; /evidence="ECO:0000269|PubMed:9223670"; MUTAGEN 862; /note="Y->F: Impairs phosphorylation of CBLC (demonstrated with chimeric EGFR-LTK)."; /evidence="ECO:0000269|PubMed:9223670
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. {ECO:0000269|PubMed:14695357}.
uniprot
proteins
protein_family
Insulin receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10445845
uniprot
proteins
pubmed
14695357
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1655406
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18849880
uniprot
proteins
pubmed
19815557
uniprot
proteins
pubmed
20548102
uniprot
proteins
pubmed
2156206
uniprot
proteins
pubmed
2320375
uniprot
proteins
pubmed
30061385
uniprot
proteins
pubmed
34646012
uniprot
proteins
pubmed
7685902
uniprot
proteins
pubmed
8084603
uniprot
proteins
pubmed
9223670
uniprot
proteins
sequence_length
864
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34646012}; Single-pass type I membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 425..449; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins