Lyn
entrez
17096
canonical
uniprot
P25911
canonical
ensembl
ENSMUSG00000042228
resolver
ensp
ENSMUSP00000038838
resolver
ensp
ENSMUSP00000100075
resolver
ensp
ENSMUSP00000234345
resolver
genesymbol
Lyn
resolver
uniprot
Q3TCS3
resolver
uniprot
Q3U6Q5
resolver
uniprot
Q62127
resolver
uniprot
Q8CEI0
resolver
uniprot_entry
LYN_MOUSE
resolver
uniprot_entry
Q3TCS3_MOUSE
resolver
uniprot_entry
Q3U6Q5_MOUSE
resolver
uniprot_entry
Q8CEI0_MOUSE
resolver
uniprot_sec
Q62127
resolver
activity_regulation
ACTIVITY REGULATION: Subject to autoinhibition, mediated by intramolecular interactions between the SH2 domain and the C-terminal phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508 inhibits kinase activity. Kinase activity is modulated by dephosphorylation by PTPRC/CD45. Inhibited by dasatinib, PP2, and SU6656. {ECO:0000269|PubMed:10415030, ECO:0000269|PubMed:12486102, ECO:0000269|PubMed:18984583, ECO:0000269|PubMed:8530369}.
uniprot
proteins
amino_acid_sequence
MGCIKSKRKDNLNDDEVDSKTQPVRNTDRTIYVRDPTSNKQQRPVPEFHLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLSSKREGFIPSNYVAKVNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDYDPMHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQSDGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEFMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMSALSQGYRMPRMENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Involved in the regulation of endothelial activation, neutrophil adhesion and transendothelial migration (By similarity). Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, MS4A2/FCER1B, SYK and TEC. Phosphorylates PIRB at Tyr-794 and Tyr-824, which is required for PIRB interaction with PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10327049). Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (PubMed:28098138). Phosphorylates CLNK (PubMed:12681493). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By similarity). {ECO:0000250|UniProtKB:P07948, ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10594694, ECO:0000269|PubMed:10640270, ECO:0000269|PubMed:10672044, ECO:0000269|PubMed:11007759, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11672542, ECO:0000269|PubMed:12077122, ECO:0000269|PubMed:12681493, ECO:0000269|PubMed:12874221, ECO:0000269|PubMed:14525964, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:16034130, ECO:0000269|PubMed:16116174, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:19492092, ECO:0000269|PubMed:20189992, ECO:0000269|PubMed:20385881, ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:7513017, ECO:0000269|PubMed:7584145, ECO:0000269|PubMed:7585947, ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8629002, ECO:0000269|PubMed:9036984, ECO:0000269|PubMed:9064343, ECO:0000269|PubMed:9252121, ECO:0000269|PubMed:9469421, ECO:0000269|PubMed:9480991, ECO:0000269|PubMed:9547345, ECO:0000269|PubMed:9573010, ECO:0000269|PubMed:9590210, ECO:0000269|PubMed:9601638}.
uniprot
proteins
mass_dalton
58812
uniprot
proteins
mutagenesis
MUTAGEN 508; /note="Y->F: Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates."; /evidence="ECO:0000269|PubMed:11672542, ECO:0000269|PubMed:12486102
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by CBL, leading to its degradation. {ECO:0000269|PubMed:15304502}.; PTM: Autophosphorylated (By similarity). Phosphorylated on tyrosine residues in response to KIT signaling (By similarity). Phosphorylation at Tyr-397 is required for optimal activity (PubMed:16272347). Phosphorylation at Tyr-508 inhibits kinase activity (By similarity). Phosphorylated at Tyr-508 by CSK (By similarity). Dephosphorylated by PTPRC/CD45 (PubMed:10415030). Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A (PubMed:9252121). Phosphorylated in response to ITGB1 in B-cells (By similarity). {ECO:0000250|UniProtKB:P07948, ECO:0000269|PubMed:10415030, ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:9252121}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SRC subfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10327049
uniprot
proteins
pubmed
10415030
uniprot
proteins
pubmed
10594694
uniprot
proteins
pubmed
10640270
uniprot
proteins
pubmed
10672044
uniprot
proteins
pubmed
11007759
uniprot
proteins
pubmed
11435302
uniprot
proteins
pubmed
11517336
uniprot
proteins
pubmed
11672542
uniprot
proteins
pubmed
12077122
uniprot
proteins
pubmed
12486102
uniprot
proteins
pubmed
12681493
uniprot
proteins
pubmed
12874221
uniprot
proteins
pubmed
14525964
uniprot
proteins
pubmed
14726379
uniprot
proteins
pubmed
15220000
uniprot
proteins
pubmed
15304502
uniprot
proteins
pubmed
15335855
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15489917
uniprot
proteins
pubmed
15664155
uniprot
proteins
pubmed
16034130
uniprot
proteins
pubmed
16116174
uniprot
proteins
pubmed
16249387
uniprot
proteins
pubmed
16272347
uniprot
proteins
pubmed
16684964
uniprot
proteins
pubmed
16731527
uniprot
proteins
pubmed
1702903
uniprot
proteins
pubmed
1710766
uniprot
proteins
pubmed
17233630
uniprot
proteins
pubmed
17640867
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
18984583
uniprot
proteins
pubmed
19064729
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19290919
uniprot
proteins
pubmed
19492092
uniprot
proteins
pubmed
2017160
uniprot
proteins
pubmed
20189992
uniprot
proteins
pubmed
20385881
uniprot
proteins
pubmed
20644716
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22496641
uniprot
proteins
pubmed
2482828
uniprot
proteins
pubmed
28098138
uniprot
proteins
pubmed
7513017
uniprot
proteins
pubmed
7584145
uniprot
proteins
pubmed
7585947
uniprot
proteins
pubmed
7782294
uniprot
proteins
pubmed
8128248
uniprot
proteins
pubmed
8168489
uniprot
proteins
pubmed
8183901
uniprot
proteins
pubmed
8530369
uniprot
proteins
pubmed
8621063
uniprot
proteins
pubmed
8629002
uniprot
proteins
pubmed
9036984
uniprot
proteins
pubmed
9064343
uniprot
proteins
pubmed
9252121
uniprot
proteins
pubmed
9469421
uniprot
proteins
pubmed
9480991
uniprot
proteins
pubmed
9547345
uniprot
proteins
pubmed
9573010
uniprot
proteins
pubmed
9590210
uniprot
proteins
pubmed
9601638
uniprot
proteins
sequence_length
512
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P07948}; Lipid-anchor {ECO:0000250|UniProtKB:P07948}. Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). {ECO:0000250}.
uniprot
proteins