OSM
entrez
5008
canonical
uniprot
P13725
canonical
ensembl
ENSG00000099985
resolver
ensp
ENSP00000215781
resolver
ensp
ENSP00000383893
resolver
enst
ENST00000215781
resolver
enst
ENST00000403389
resolver
genesymbol
OSM
resolver
hgnc
HGNC:8506
resolver
uniprot
B5MCX1
resolver
uniprot
Q6FHP8
resolver
uniprot
Q9UCP6
resolver
uniprot_entry
B5MCX1_HUMAN
resolver
uniprot_entry
ONCM_HUMAN
resolver
uniprot_sec
Q6FHP8
resolver
uniprot_sec
Q9UCP6
resolver
amino_acid_sequence
MGVLLTQRTLLSLVLALLFPSMASMAAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPGAFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDLEKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQRKLEGCRFLHGYHRFMHSVGRVFSKWGESPNRSRRHSPHQALRKGVRRTRPSRKGKRLMTRGQLPR
uniprot
proteins
function
FUNCTION: Functions as a cytokine that uses both type I OSM receptor (heterodimers composed of LIFR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST) (PubMed:10997905, PubMed:39532904, PubMed:8999038). Functionally, regulates many processes including cell proliferation, cell differentiation, cytokine production (PubMed:10997905, PubMed:1542792, PubMed:1542793, PubMed:1717982, PubMed:2779549, PubMed:3540948). Mechanistically, low affinity ligand binding to IL6ST/gp130, induces heterodimerization with LIFR or OSMR, activating JAK tyrosine kinases (JAK1 or JAK2 and to a lesser extent TYK2) bound to their intracellular domains (PubMed:9188471). These kinases subsequently phosphorylate IL6ST/gp130 and LIFR or OSMR (PubMed:8999038). The tyrosine phosphorylated signaling receptors serve in turn as docking sites for recruitment and activation of STAT3 (PubMed:9188471). The type II OSM complex receptor is also able in addition to STAT3 to recruit STAT5B (PubMed:9188471). Moreover, the type II OSM complex receptor recruits SHC1 through OSMR in a JAK1 mediated phosphotyrosine-dependent manner, leading to SHC1 association with GRB2 and downstream activation of the Ras/Raf/MAPK pathway (PubMed:11016927). {ECO:0000269|PubMed:10997905, ECO:0000269|PubMed:11016927, ECO:0000269|PubMed:1542792, ECO:0000269|PubMed:1542793, ECO:0000269|PubMed:1717982, ECO:0000269|PubMed:2779549, ECO:0000269|PubMed:3540948, ECO:0000269|PubMed:39532904, ECO:0000269|PubMed:8999038, ECO:0000269|PubMed:9188471}.
uniprot
proteins
mass_dalton
28484
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="C->S: Inactive."; /evidence="ECO:0000269|PubMed:2026606"; MUTAGEN 192; /note="C->S: Inactive."; /evidence="ECO:0000269|PubMed:2026606"; MUTAGEN 201; /note="F->G: Inactive."; /evidence="ECO:0000269|PubMed:2026606"; MUTAGEN 209; /note="F->G: Inactive."; /evidence="ECO:0000269|PubMed:2026606"; MUTAGEN 220; /note="R->G: Inhibits propeptide cleavage."; /evidence="ECO:0000269|PubMed:2325640"; MUTAGEN 221; /note="R->G: Inhibits propeptide cleavage."; /evidence="ECO:0000269|PubMed:2325640
uniprot
proteins
post_translational_modification
PTM: Propeptide processing is not important for receptor binding activity but may be important for growth-inhibitory activity. {ECO:0000269|PubMed:2325640}.
uniprot
proteins
protein_family
LIF/OSM family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10997905
uniprot
proteins
pubmed
11016927
uniprot
proteins
pubmed
1542792
uniprot
proteins
pubmed
1542793
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1717982
uniprot
proteins
pubmed
2026606
uniprot
proteins
pubmed
2325640
uniprot
proteins
pubmed
2779549
uniprot
proteins
pubmed
3540948
uniprot
proteins
pubmed
39532904
uniprot
proteins
pubmed
8999038
uniprot
proteins
pubmed
9188471
uniprot
proteins
sequence_length
252
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:1542792, ECO:0000305|PubMed:3540948}.
uniprot
proteins