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P25911

- LYN_MOUSE

UniProt

P25911 - LYN_MOUSE

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Protein

Tyrosine-protein kinase Lyn

Gene

Lyn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. 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.By similarity36 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.4 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

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 SU6656.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei275 – 2751ATPCurated
Active sitei367 – 3671Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi253 – 2619ATPCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. erythropoietin receptor binding Source: UniProtKB
  3. glycosphingolipid binding Source: Ensembl
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  5. protein complex binding Source: MGI
  6. protein kinase activity Source: MGI
  7. protein tyrosine kinase activity Source: UniProtKB
  8. SH3 domain binding Source: MGI

GO - Biological processi

  1. B cell homeostasis Source: UniProtKB
  2. B cell receptor signaling pathway Source: MGI
  3. cellular response to DNA damage stimulus Source: Ensembl
  4. cellular response to extracellular stimulus Source: Ensembl
  5. cellular response to heat Source: Ensembl
  6. cellular response to retinoic acid Source: Ensembl
  7. cytokine secretion Source: Ensembl
  8. dendritic cell differentiation Source: UniProtKB
  9. erythrocyte differentiation Source: UniProtKB
  10. Fc receptor mediated inhibitory signaling pathway Source: UniProtKB
  11. Fc receptor mediated stimulatory signaling pathway Source: UniProtKB
  12. hemoglobin biosynthetic process Source: UniProtKB
  13. hemopoiesis Source: UniProtKB
  14. histamine secretion by mast cell Source: Ensembl
  15. immune response-regulating cell surface receptor signaling pathway Source: UniProtKB
  16. innate immune response Source: UniProtKB-KW
  17. intracellular signal transduction Source: MGI
  18. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  19. negative regulation of B cell proliferation Source: UniProtKB
  20. negative regulation of cell proliferation Source: UniProtKB
  21. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  22. negative regulation of intracellular signal transduction Source: UniProtKB
  23. negative regulation of MAP kinase activity Source: UniProtKB
  24. negative regulation of mast cell proliferation Source: UniProtKB
  25. negative regulation of myeloid leukocyte differentiation Source: UniProtKB
  26. negative regulation of protein phosphorylation Source: UniProtKB
  27. negative regulation of toll-like receptor 2 signaling pathway Source: UniProtKB
  28. negative regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
  29. neuron projection development Source: MGI
  30. oligodendrocyte development Source: Ensembl
  31. peptidyl-tyrosine phosphorylation Source: UniProtKB
  32. platelet degranulation Source: UniProtKB
  33. positive regulation of B cell receptor signaling pathway Source: MGI
  34. positive regulation of cell migration Source: UniProtKB
  35. positive regulation of cell proliferation Source: UniProtKB
  36. positive regulation of dendritic cell apoptotic process Source: UniProtKB
  37. positive regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
  38. positive regulation of glial cell proliferation Source: Ensembl
  39. positive regulation of mast cell proliferation Source: Ensembl
  40. positive regulation of neuron projection development Source: Ensembl
  41. positive regulation of oligodendrocyte progenitor proliferation Source: Ensembl
  42. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  43. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  44. positive regulation of stress-activated protein kinase signaling cascade Source: Ensembl
  45. positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
  46. protein autophosphorylation Source: UniProtKB
  47. regulation of B cell apoptotic process Source: UniProtKB
  48. regulation of B cell receptor signaling pathway Source: UniProtKB
  49. regulation of cell adhesion mediated by integrin Source: Ensembl
  50. regulation of cytokine production Source: UniProtKB
  51. regulation of cytokine secretion Source: UniProtKB
  52. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  53. regulation of erythrocyte differentiation Source: UniProtKB
  54. regulation of inflammatory response Source: UniProtKB
  55. regulation of mast cell activation Source: UniProtKB
  56. regulation of mast cell degranulation Source: UniProtKB
  57. regulation of monocyte chemotaxis Source: Ensembl
  58. regulation of platelet aggregation Source: UniProtKB
  59. regulation of release of sequestered calcium ion into cytosol Source: MGI
  60. response to amino acid Source: Ensembl
  61. response to axon injury Source: Ensembl
  62. response to carbohydrate Source: Ensembl
  63. response to drug Source: Ensembl
  64. response to hormone Source: UniProtKB
  65. response to insulin Source: Ensembl
  66. response to organic cyclic compound Source: Ensembl
  67. response to sterol depletion Source: Ensembl
  68. response to toxic substance Source: Ensembl
  69. signal transduction Source: UniProtKB
  70. tolerance induction to self antigen Source: UniProtKB
  71. transmembrane receptor protein tyrosine kinase signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188204. Fc epsilon receptor (FCERI) signaling.
REACT_188530. FCERI mediated MAPK activation.
REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_198614. Growth hormone receptor signaling.
REACT_204081. CD28 co-stimulation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.
REACT_227425. Regulation of KIT signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.
REACT_261568. CTLA4 inhibitory signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Lyn (EC:2.7.10.2)
Alternative name(s):
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene namesi
Name:Lyn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:96892. Lyn.

Subcellular locationi

Cell membrane By similarity. Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Golgi apparatus By similarity
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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. Golgi apparatus Source: UniProtKB-KW
  5. integrin alpha2-beta1 complex Source: Ensembl
  6. mast cell granule Source: GOC
  7. membrane raft Source: Ensembl
  8. mitochondrial crista Source: Ensembl
  9. mitochondrial intermembrane space Source: Ensembl
  10. nucleus Source: UniProtKB
  11. perinuclear region of cytoplasm Source: Ensembl
  12. plasma membrane Source: MGI
  13. postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype at birth. B-cell development in the bone marrow proceeds normally, but mice have reduced numbers of peripheral B-cells, with a greater proportion of immature cells and an increased turnover rate. Dendritic cells also have a more immature phenotype. Mice develop severe asthma upon exposure to airborne antigen. Mice display elevated levels of serum IgM. Aging mice display strongly increased levels of myeloid cells, severe extramedullary hematoipoiesis and tend to develop monocyte/macrophage tumors. After about 16 weeks, mice begin to develop splenomegaly and glomerulonephritis, and display autoimmune antibodies. Their B-cells are hypersensitive to stimulation of the B-cell receptor, and display enhanced activation of the MAP kinase signaling pathway. Mice do not display an allergic response upon IgE receptor engagement.7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi508 – 5081Y → F: Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates. 2 Publications

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 512511Tyrosine-protein kinase LynPRO_0000088130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei30 – 301PhosphothreonineBy similarity
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei37 – 371PhosphothreonineBy similarity
Modified residuei193 – 1931PhosphotyrosineBy similarity
Modified residuei194 – 1941PhosphotyrosineBy similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei265 – 2651PhosphotyrosineBy similarity
Modified residuei306 – 3061PhosphotyrosineBy similarity
Modified residuei316 – 3161PhosphotyrosineBy similarity
Modified residuei397 – 3971Phosphotyrosine; by autocatalysis3 Publications
Modified residuei460 – 4601PhosphotyrosineBy similarity
Modified residuei473 – 4731PhosphotyrosineBy similarity
Modified residuei489 – 4891PhosphothreonineBy similarity
Modified residuei502 – 5021PhosphothreonineBy similarity
Modified residuei508 – 5081Phosphotyrosine; by autocatalysis, CSK and MATK3 Publications

Post-translational modificationi

Ubiquitinated by CBL, leading to its degradation.1 Publication
Phosphorylated on tyrosine residues in response to KIT signaling (By similarity). Autophosphorylated. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.By similarity5 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25911.
PaxDbiP25911.
PRIDEiP25911.

PTM databases

PhosphoSiteiP25911.

Expressioni

Tissue specificityi

Detected in bone marrow-derived monocytes (at protein level). Expressed predominantly in B-lymphoid and myeloid cells.1 Publication

Gene expression databases

BgeeiP25911.
ExpressionAtlasiP25911. baseline and differential.
GenevestigatoriP25911.

Interactioni

Subunit structurei

Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation (By similarity). Interacts with CD36.By similarity17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hcls1P4971010EBI-643537,EBI-924601
Plcg2Q8CIH52EBI-643537,EBI-617954

Protein-protein interaction databases

BioGridi201256. 10 interactions.
DIPiDIP-37806N.
IntActiP25911. 13 interactions.
MINTiMINT-100482.

Structurei

Secondary structure

1
512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi244 – 2463Combined sources
Beta strandi247 – 2548Combined sources
Beta strandi257 – 26610Combined sources
Turni267 – 2693Combined sources
Beta strandi270 – 2778Combined sources
Helixi284 – 29411Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi311 – 3144Combined sources
Beta strandi316 – 3205Combined sources
Helixi327 – 3326Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 36020Combined sources
Helixi370 – 3723Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi381 – 3833Combined sources
Helixi407 – 4093Combined sources
Helixi412 – 4176Combined sources
Helixi422 – 43817Combined sources
Helixi449 – 4557Combined sources
Helixi456 – 4583Combined sources
Helixi470 – 47910Combined sources
Helixi484 – 4863Combined sources
Helixi490 – 4989Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZV7X-ray2.50A239-512[»]
2ZV8X-ray2.70A239-512[»]
2ZV9X-ray2.76A239-512[»]
2ZVAX-ray2.60A239-512[»]
ProteinModelPortaliP25911.
SMRiP25911. Positions 64-512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25911.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 12361SH3PROSITE-ProRule annotationAdd
BLAST
Domaini129 – 22698SH2PROSITE-ProRule annotationAdd
BLAST
Domaini247 – 501255Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain plays an important role in its localization in the cell membrane.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP25911.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG7GTT2V.
PhylomeDBiP25911.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P25911-1) [UniParc]FASTAAdd to Basket

Also known as: LYN A, p56

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGCIKSKRKD NLNDDEVDSK TQPVRNTDRT IYVRDPTSNK QQRPVPEFHL
60 70 80 90 100
LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLSSKRE GFIPSNYVAK VNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DYDPMHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ
360 370 380 390 400
IAEGMAYIER KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR
410 420 430 440 450
EGAKFPIKWT APEAINFGCF TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA
460 470 480 490 500
DVMSALSQGY RMPRMENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,812
Last modified:January 23, 2007 - v4
Checksum:iFDA1D21CC90C50EC
GO
Isoform 2 (identifier: P25911-2) [UniParc]FASTAAdd to Basket

Also known as: LYN B, p53

The sequence of this isoform differs from the canonical sequence as follows:
     25-45: Missing.

Show »
Length:491
Mass (Da):56,285
Checksum:i2C82015D510B1F59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771I → F in AAA39471. (PubMed:2017160)Curated
Sequence conflicti77 – 771I → F in AAA39472. (PubMed:2017160)Curated
Sequence conflicti161 – 1611L → I in AAA39471. (PubMed:2017160)Curated
Sequence conflicti161 – 1611L → I in AAA39472. (PubMed:2017160)Curated
Sequence conflicti279 – 2791P → L in AAA39471. (PubMed:2017160)Curated
Sequence conflicti279 – 2791P → L in AAA39472. (PubMed:2017160)Curated
Sequence conflicti391 – 3911V → I in AAA39471. (PubMed:2017160)Curated
Sequence conflicti391 – 3911V → I in AAA39472. (PubMed:2017160)Curated
Sequence conflicti415 – 4151I → F in AAA40017. (PubMed:2482828)Curated
Sequence conflicti425 – 4251D → N in AAA39470. (PubMed:1710766)Curated
Sequence conflicti432 – 4321L → P in AAA40017. (PubMed:2482828)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 4521Missing in isoform 2. 1 PublicationVSP_005003Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64608 mRNA. Translation: AAA39470.1.
M57696 mRNA. Translation: AAA39471.1.
M57697 mRNA. Translation: AAA39472.1.
BC031547 mRNA. Translation: AAH31547.1.
M33426 mRNA. Translation: AAA40017.1.
CCDSiCCDS17939.1. [P25911-2]
CCDS51109.1. [P25911-1]
PIRiA39719.
RefSeqiNP_001104566.1. NM_001111096.1. [P25911-1]
UniGeneiMm.317331.

Genome annotation databases

EnsembliENSMUST00000041377; ENSMUSP00000038838; ENSMUSG00000042228. [P25911-1]
ENSMUST00000103010; ENSMUSP00000100075; ENSMUSG00000042228. [P25911-2]
GeneIDi17096.
KEGGimmu:17096.
UCSCiuc008rwm.2. mouse. [P25911-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64608 mRNA. Translation: AAA39470.1 .
M57696 mRNA. Translation: AAA39471.1 .
M57697 mRNA. Translation: AAA39472.1 .
BC031547 mRNA. Translation: AAH31547.1 .
M33426 mRNA. Translation: AAA40017.1 .
CCDSi CCDS17939.1. [P25911-2 ]
CCDS51109.1. [P25911-1 ]
PIRi A39719.
RefSeqi NP_001104566.1. NM_001111096.1. [P25911-1 ]
UniGenei Mm.317331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZV7 X-ray 2.50 A 239-512 [» ]
2ZV8 X-ray 2.70 A 239-512 [» ]
2ZV9 X-ray 2.76 A 239-512 [» ]
2ZVA X-ray 2.60 A 239-512 [» ]
ProteinModelPortali P25911.
SMRi P25911. Positions 64-512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201256. 10 interactions.
DIPi DIP-37806N.
IntActi P25911. 13 interactions.
MINTi MINT-100482.

Chemistry

BindingDBi P25911.
ChEMBLi CHEMBL2258.

PTM databases

PhosphoSitei P25911.

Proteomic databases

MaxQBi P25911.
PaxDbi P25911.
PRIDEi P25911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041377 ; ENSMUSP00000038838 ; ENSMUSG00000042228 . [P25911-1 ]
ENSMUST00000103010 ; ENSMUSP00000100075 ; ENSMUSG00000042228 . [P25911-2 ]
GeneIDi 17096.
KEGGi mmu:17096.
UCSCi uc008rwm.2. mouse. [P25911-1 ]

Organism-specific databases

CTDi 4067.
MGIi MGI:96892. Lyn.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P25911.
KOi K05854.
OMAi WWRAKSL.
OrthoDBi EOG7GTT2V.
PhylomeDBi P25911.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188204. Fc epsilon receptor (FCERI) signaling.
REACT_188530. FCERI mediated MAPK activation.
REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_198614. Growth hormone receptor signaling.
REACT_204081. CD28 co-stimulation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.
REACT_227425. Regulation of KIT signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.
REACT_261568. CTLA4 inhibitory signaling.

Miscellaneous databases

EvolutionaryTracei P25911.
NextBioi 291240.
PROi P25911.
SOURCEi Search...

Gene expression databases

Bgeei P25911.
ExpressionAtlasi P25911. baseline and differential.
Genevestigatori P25911.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alternatively spliced murine lyn mRNAs encode distinct proteins."
    Stanley E., Ralph S.J., McEwen S., Boulet I., Holtzman D.A., Lock P., Dunn A.R.
    Mol. Cell. Biol. 11:3399-3406(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
  2. "Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus."
    Yi T., Bolen J.B., Ihle J.N.
    Mol. Cell. Biol. 11:2391-2398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
    Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
    Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-432.
  5. "Association of B cell antigen receptor with protein tyrosine kinase Lyn."
    Yamanashi Y., Kakiuchi T., Mizuguchi J., Yamamoto T., Toyoshima K.
    Science 251:192-194(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH B CELL RECEPTOR, AUTOPHOSPHORYLATION.
  6. "Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity."
    Clark M.R., Johnson S.A., Cambier J.C.
    EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD79A.
  7. "B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn."
    Law D.A., Chan V.W., Datta S.K., DeFranco A.L.
    Curr. Biol. 3:645-657(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD79A AND CD79B, FUNCTION IN PHOSPHORYLATION OF CD79A AND CD79B.
  8. "Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling."
    Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T., Yamamoto T., Yamamura H.
    J. Exp. Med. 179:1725-1729(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYK PHOSPHORYLATION.
  9. "Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha."
    Pleiman C.M., Abrams C., Gauen L.T., Bedzyk W., Jongstra J., Shaw A.S., Cambier J.C.
    Proc. Natl. Acad. Sci. U.S.A. 91:4268-4272(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD79A.
  10. "Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit."
    Pleiman C.M., Hertz W.M., Cambier J.C.
    Science 263:1609-1612(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PIK3R1 ACTIVATION, INTERACTION WITH PIK3R1.
  11. "Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease."
    Hibbs M.L., Tarlinton D.M., Armes J., Grail D., Hodgson G., Maglitto R., Stacker S.A., Dunn A.R.
    Cell 83:301-311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  12. "Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice."
    Nishizumi H., Taniuchi I., Yamanashi Y., Kitamura D., Ilic D., Mori S., Watanabe T., Yamamoto T.
    Immunity 3:549-560(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B CELLS AND IN PHOSPHORYLATION OF CBL AND HCLS1.
  13. "Tyrosine phosphorylation and translocation of the c-cbl protein after activation of tyrosine kinase signaling pathways."
    Tanaka S., Neff L., Baron R., Levy J.B.
    J. Biol. Chem. 270:14347-14351(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL.
  14. "Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase."
    Sotirellis N., Johnson T.M., Hibbs M.L., Stanley I.J., Stanley E., Dunn A.R., Cheng H.C.
    J. Biol. Chem. 270:29773-29780(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION.
  15. "Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase."
    Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.
    FASEB J. 10:637-642(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TEC PHOSPHORYLATION, INTERACTION WITH TEC.
  16. "Altered antigen receptor signaling and impaired Fas-mediated apoptosis of B cells in Lyn-deficient mice."
    Wang J., Koizumi T., Watanabe T.
    J. Exp. Med. 184:831-838(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  17. "Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases."
    Rawlings D.J., Scharenberg A.M., Park H., Wahl M.I., Lin S., Kato R.M., Fluckiger A.C., Witte O.N., Kinet J.P.
    Science 271:822-825(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BTK.
  18. "Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation."
    Chan V.W., Meng F., Soriano P., DeFranco A.L., Lowell C.A.
    Immunity 7:69-81(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, ALTERNATIVE SPLICING, PHOSPHORYLATION.
  19. "Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells."
    Nishizumi H., Yamamoto T.
    J. Immunol. 158:2350-2355(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAST CELLS AND IN SIGNALING DOWN-STREAM OF FCER1.
  20. "Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway."
    Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.
    Blood 91:3734-3745(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPOR AND JAK2, FUNCTION.
  21. "Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes."
    Chan V.W., Lowell C.A., DeFranco A.L.
    Curr. Biol. 8:545-553(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION AND ACTIVATION OF MAPK1/ERK2; MAPK8/JNK1 AND MAPK9/JNK2.
  22. "Inhibition of the B cell by CD22: a requirement for Lyn."
    Smith K.G., Tarlinton D.M., Doody G.M., Hibbs M.L., Fearon D.T.
    J. Exp. Med. 187:807-811(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CD22 PHOSPHORYLATION.
  23. "A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals."
    Nishizumi H., Horikawa K., Mlinaric-Rascan I., Yamamoto T.
    J. Exp. Med. 187:1343-1348(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION.
  24. "Fc epsilon receptor I-associated lyn-dependent phosphorylation of Fc gamma receptor IIB during negative regulation of mast cell activation."
    Malbec O., Fong D.C., Turner M., Tybulewicz V.L., Cambier J.C., Fridman W.H., Daeron M.
    J. Immunol. 160:1647-1658(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FCGR2 PHOSPHORYLATION, INTERACTION WITH FCGR2.
  25. "The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1 upon tyrosine phosphorylation."
    Adachi T., Flaswinkel H., Yakura H., Reth M., Tsubata T.
    J. Immunol. 160:4662-4665(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CD72 PHOSPHORYLATION.
  26. "Regulation of B-1 cell activation and its autoantibody production by Lyn kinase-regulated signallings."
    Ochi H., Takeshita H., Suda T., Nisitani S., Honjo T., Watanabe T.
    Immunology 98:595-603(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN ERYTHROPOIESIS.
  27. "CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells."
    Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H.
    J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, DEPHOSPHORYLATION BY PTPRC/CD45, ENZYME REGULATION.
  28. "Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1."
    Maeda A., Scharenberg A.M., Tsukada S., Bolen J.B., Kinet J.P., Kurosaki T.
    Oncogene 18:2291-2297(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LILRB3/PIR-B.
  29. "Association of Lyn tyrosine kinase to the GM-CSF and IL-3 receptor common betac subunit and role of Src tyrosine kinases in DNA synthesis and anti-apoptosis."
    Dahl M.E., Arai K.I., Watanabe S.
    Genes Cells 5:143-153(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CSF2RB, INTERACTION WITH CSF2RB.
  30. "Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling."
    Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H., Yamamoto T., Baltimore D.
    Genes Dev. 14:11-16(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DOK1.
  31. "Negative regulation of B cell receptor-mediated signaling in B-1 cells through CD5 and Ly49 co-receptors via Lyn kinase activity."
    Ochi H., Watanabe T.
    Int. Immunol. 12:1417-1423(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CD5 PHOSPHORYLATION.
  32. "Lyn is required for normal stem cell factor-induced proliferation and chemotaxis of primary hematopoietic cells."
    O'Laughlin-Bunner B., Radosevic N., Taylor M.L., Shivakrupa R., DeBerry C., Metcalfe D.D., Zhou M., Lowell C., Linnekin D.
    Blood 98:343-350(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION AND MIGRATION IN RESPONSE TO KITLG.
  33. "Gain- and loss-of-function Lyn mutant mice define a critical inhibitory role for Lyn in the myeloid lineage."
    Harder K.W., Parsons L.M., Armes J., Evans N., Kountouri N., Clark R., Quilici C., Grail D., Hodgson G.S., Dunn A.R., Hibbs M.L.
    Immunity 15:603-615(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF SIRPA; PTPN6/SHP-1; PTPN11/SHP-2 AND INPP5D/SHIP-1, MUTAGENESIS OF TYR-508.
  34. "Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis."
    Grishin A.V., Azhipa O., Semenov I., Corey S.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R15A.
  35. "Sustained activation of Lyn tyrosine kinase in vivo leads to autoimmunity."
    Hibbs M.L., Harder K.W., Armes J., Kountouri N., Quilici C., Casagranda F., Dunn A.R., Tarlinton D.M.
    J. Exp. Med. 196:1593-1604(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF IMMUNE RESPONSE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF TYR-508.
  36. "Regulation of signaling in B cells through the phosphorylation of Syk on linker region tyrosines. A mechanism for negative signaling by the Lyn tyrosine kinase."
    Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.
    J. Biol. Chem. 277:31703-31714(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATING SYK.
  37. "The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling."
    Pereira S., Lowell C.
    J. Immunol. 171:1319-1327(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  38. "Lyn tyrosine kinase regulates thrombopoietin-induced proliferation of hematopoietic cell lines and primary megakaryocytic progenitors."
    Lannutti B.J., Drachman J.G.
    Blood 103:3736-3743(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DOWN-REGULATION OF THPO-MEDIATED CELL PROLIFERATION AND IN DOWN-REGULATION OF MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
  39. "Differential regulation of the B cell receptor-mediated signaling by the E3 ubiquitin ligase Cbl."
    Shao Y., Yang C., Elly C., Liu Y.C.
    J. Biol. Chem. 279:43646-43653(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  40. "The Src kinase Lyn is a negative regulator of mast cell proliferation."
    Hernandez-Hansen V., Mackay G.A., Lowell C.A., Wilson B.S., Oliver J.M.
    J. Leukoc. Biol. 75:143-151(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAST CELL PROLIFERATION AND IN DOWN-REGULATION OF AKT1; MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
  41. "The Lyn tyrosine kinase differentially regulates dendritic cell generation and maturation."
    Chu C.L., Lowell C.A.
    J. Immunol. 175:2880-2889(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NEGATIVE REGULATOR OF DENDRITIC CELL DIFFERENTIATION; PROLIFERATION AND SURVIVAL.
  42. "Lyn-deficient mice develop severe, persistent asthma: Lyn is a critical negative regulator of Th2 immunity."
    Beavitt S.J., Harder K.W., Kemp J.M., Jones J., Quilici C., Casagranda F., Lam E., Turner D., Brennan S., Sly P.D., Tarlinton D.M., Anderson G.P., Hibbs M.L.
    J. Immunol. 175:1867-1875(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MATURATION OF DENDRITIC CELLS AND IN INFLAMMATORY RESPONSE.
  43. "Positive and negative regulation of mast cell activation by Lyn via the FcepsilonRI."
    Xiao W., Nishimoto H., Hong H., Kitaura J., Nunomura S., Maeda-Yamamoto M., Kawakami Y., Lowell C.A., Ra C., Kawakami T.
    J. Immunol. 175:6885-6892(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FCER1 SIGNALING; PHOSPHORYLATION OF SYK; MS4A2/FCER1B; INPP5D/SHIP AND PTPN6/SHP-1; ACTIVATION OF AKT1; MAPK1/ERK2 AND MAPK3/ERK1, PHOSPHORYLATION AT TYR-397, INTERACTION WITH MS4A2/FCER1B.
  44. "LIME acts as a transmembrane adapter mediating BCR-dependent B-cell activation."
    Ahn E., Lee H., Yun Y.
    Blood 107:1521-1527(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1, FUNCTION IN PHOSPHORYLATION OF LIME1.
  45. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
    Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
    Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT3.
  46. "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
    Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
    J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  47. "Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets."
    Rathore V.B., Okada M., Newman P.J., Newman D.K.
    Biochem. J. 403:275-281(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  48. "Leupaxin negatively regulates B cell receptor signaling."
    Chew V., Lam K.P.
    J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LPXN, INTERACTION WITH LPXN.
  49. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  50. "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
    Samuels A.L., Klinken S.P., Ingley E.
    Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD54.
  51. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; TYR-397 AND TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  52. "Erythropoietin down-regulates stem cell factor receptor (Kit) expression in the leukemic proerythroblast: role of Lyn kinase."
    Kosmider O., Buet D., Gallais I., Denis N., Moreau-Gachelin F.
    PLoS ONE 4:E5721-E5721(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  53. "Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
    Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
    PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THEMIS2.
  54. "An important role of the SRC family kinase Lyn in stimulating platelet granule secretion."
    Li Z., Zhang G., Liu J., Stojanovic A., Ruan C., Lowell C.A., Du X.
    J. Biol. Chem. 285:12559-12570(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET GRANULE SECRETION AND PLATELET AGGREGATION.
  55. "Activation of murine macrophages via TLR2 and TLR4 is negatively regulated by a Lyn/PI3K module and promoted by SHIP1."
    Keck S., Freudenberg M., Huber M.
    J. Immunol. 184:5809-5818(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DOWN-REGULATION OF TLR2 AND TLR4 SIGNALING; CYTOKINE RELEASE AND THE INFLAMMATORY RESPONSE TO LIPOPOLYSACCHARIDE.
  56. "Src-family kinases in B-cell development and signaling."
    Gauld S.B., Cambier J.C.
    Oncogene 23:8001-8006(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN B CELLS.
  57. "Lyn tyrosine kinase: accentuating the positive and the negative."
    Xu Y., Harder K.W., Huntington N.D., Hibbs M.L., Tarlinton D.M.
    Immunity 22:9-18(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN B CELLS.
  58. "Src-family kinases: rheostats of immune cell signaling."
    Lowell C.A.
    Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  59. "Multiple roles of Lyn kinase in myeloid cell signaling and function."
    Scapini P., Pereira S., Zhang H., Lowell C.A.
    Immunol. Rev. 228:23-40(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  60. "Crystal structures of the Lyn protein tyrosine kinase domain in its Apo- and inhibitor-bound state."
    Williams N.K., Lucet I.S., Klinken S.P., Ingley E., Rossjohn J.
    J. Biol. Chem. 284:284-291(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 239-512 IN COMPLEXES WITH DASATINIB; PP2 AND AMP-PNP, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiLYN_MOUSE
AccessioniPrimary (citable) accession number: P25911
Secondary accession number(s): Q62127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3