P25911 (LYN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Lyn

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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'. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 Ref.48 Ref.53 Ref.55 Ref.56
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.2 Ref.14 Ref.35 Ref.61
Enzyme 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. Ref.14 Ref.27 Ref.35 Ref.61
Subunit structure	Interacts with LIME1 and with CD79A upon activation of the B-cell receptor. Interacts with the B-cell receptor complex. Interacts with TGFB1I1. 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 (via SH3 domain) with PPP1R15A and PDE4A By similarity. Interacts with ADAM15 By similarity. Interacts with NDFIP2 and more weakly with NDFIP1 By similarity. Interacts with THEMIS2 (phosphorylated). Interacts with ABL1 By similarity. Interacts with FASLG and KIT. Interacts (via SH3 domain) with SCIMP (via proline-rich region) By similarity. Interacts with PTPN6/SHP-1. Interacts with HCLS1. Interacts with FCGR2. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts with HCLS1 By similarity. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with TEC. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN. Forms a multiprotein complex with LYN and HS1. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Ref.15 Ref.20 Ref.24 Ref.29 Ref.34 Ref.43 Ref.44 Ref.45 Ref.47 Ref.48 Ref.51 Ref.54
Subcellular location	Cell membrane By similarity. Nucleus By similarity. Cytoplasm By similarity. Cytoplasm › perinuclear 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.
Tissue specificity	Detected in bone marrow-derived monocytes (at protein level). Expressed predominantly in B-lymphoid and myeloid cells. Ref.2
Domain	The protein kinase domain plays an important role in its localization in the cell membrane By similarity.
Post-translational modification	Ubiquitinated by CBL, leading to its degradation. Ref.39 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. Ref.2 Ref.5 Ref.14 Ref.18 Ref.27 Ref.35 Ref.43 Ref.61
Disruption phenotype	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. Ref.11 Ref.12 Ref.16 Ref.18 Ref.26 Ref.33 Ref.42
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from mutant phenotype Ref.18. Source: UniProtKB B cell receptor signaling pathway Inferred from direct assay PubMed 7499277. Source: MGI Fc receptor mediated inhibitory signaling pathway Inferred from mutant phenotype Ref.43. Source: UniProtKB Fc receptor mediated stimulatory signaling pathway Inferred from mutant phenotype Ref.43. Source: UniProtKB cellular response to extracellular stimulus Inferred from electronic annotation. Source: Compara cellular response to heat Inferred from electronic annotation. Source: Compara cellular response to retinoic acid Inferred from electronic annotation. Source: Compara cytokine secretion Inferred from electronic annotation. Source: Compara dendritic cell differentiation Inferred from mutant phenotype Ref.42. Source: UniProtKB erythrocyte differentiation Inferred from mutant phenotype PubMed 10713104. Source: UniProtKB hemoglobin biosynthetic process Traceable author statement PubMed 10713104. Source: UniProtKB histamine secretion by mast cell Inferred from electronic annotation. Source: Compara innate immune response Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Inferred from direct assay PubMed 9000133. Source: MGI lipopolysaccharide-mediated signaling pathway Inferred from mutant phenotype Ref.56. Source: UniProtKB negative regulation of B cell proliferation Inferred from mutant phenotype Ref.18. Source: UniProtKB negative regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype Ref.40Ref.38. Source: UniProtKB negative regulation of MAP kinase activity Inferred from mutant phenotype Ref.18. Source: UniProtKB negative regulation of mast cell proliferation Inferred from mutant phenotype Ref.40. Source: UniProtKB negative regulation of myeloid leukocyte differentiation Inferred from mutant phenotype Ref.33. Source: UniProtKB negative regulation of toll-like receptor 2 signaling pathway Inferred from mutant phenotype Ref.56. Source: UniProtKB negative regulation of toll-like receptor 4 signaling pathway Inferred from mutant phenotype Ref.56. Source: UniProtKB neuron projection development Inferred from mutant phenotype PubMed 19118221. Source: MGI oligodendrocyte development Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.33. Source: UniProtKB platelet degranulation Inferred from mutant phenotype Ref.55. Source: UniProtKB positive regulation of Fc receptor mediated stimulatory signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from mutant phenotype Ref.32. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype PubMed 10713104Ref.32. Source: UniProtKB positive regulation of dendritic cell apoptotic process Inferred from mutant phenotype Ref.41. Source: UniProtKB positive regulation of glial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of mast cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of oligodendrocyte progenitor proliferation Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of stress-activated protein kinase signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of STAT protein Inferred from mutant phenotype PubMed 10713104. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.33. Source: UniProtKB regulation of B cell apoptotic process Inferred from mutant phenotype Ref.16. Source: UniProtKB regulation of B cell receptor signaling pathway Inferred from mutant phenotype Ref.33. Source: UniProtKB regulation of cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara regulation of cytokine secretion Inferred from mutant phenotype Ref.56. Source: UniProtKB regulation of erythrocyte differentiation Inferred from mutant phenotype Ref.26. Source: UniProtKB regulation of inflammatory response Inferred from mutant phenotype Ref.42. Source: UniProtKB regulation of mast cell degranulation Inferred from mutant phenotype Ref.43. Source: UniProtKB regulation of monocyte chemotaxis Inferred from electronic annotation. Source: Compara regulation of platelet aggregation Inferred from mutant phenotype Ref.55. Source: UniProtKB regulation of release of sequestered calcium ion into cytosol Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to carbohydrate stimulus Inferred from electronic annotation. Source: Compara response to hormone stimulus Inferred from direct assay PubMed 10713104. Source: UniProtKB response to insulin stimulus Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to sterol depletion Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara tolerance induction to self antigen Inferred from mutant phenotype Ref.18. Source: UniProtKB transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell alpha2-beta1 integrin complex Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome membrane raft Inferred from electronic annotation. Source: Compara mitochondrial crista Inferred from electronic annotation. Source: Compara mitochondrial intermembrane space Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 10713104. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.51. Source: MGI postsynaptic density Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW erythropoietin receptor binding Traceable author statement PubMed 10713104. Source: UniProtKB glycosphingolipid binding Inferred from electronic annotation. Source: Compara non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay Ref.33. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hcls1	P49710	10	EBI-643537,EBI-924601

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25911-1)

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.

Isoform 2 (identifier: P25911-2)

Also known as: LYN B; p53;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 512

512

Tyrosine-protein kinase Lyn

PRO_0000088130

Regions

Domain

63 – 123

61

SH3

Domain

129 – 226

98

SH2

Domain

247 – 501

255

Protein kinase

Nucleotide binding

253 – 261

9

ATP Probable

Sites

Active site

367

1

Proton acceptor By similarity

Binding site

275

1

ATP Probable

Amino acid modifications

Modified residue

6

1

Phosphoserine By similarity

Modified residue

19

1

Phosphoserine Ref.52

Modified residue

30

1

Phosphothreonine By similarity

Modified residue

32

1

Phosphotyrosine By similarity

Modified residue

37

1

Phosphothreonine By similarity

Modified residue

193

1

Phosphotyrosine Ref.49 Ref.50

Modified residue

194

1

Phosphotyrosine Ref.49 Ref.50

Modified residue

228

1

Phosphoserine By similarity

Modified residue

265

1

Phosphotyrosine By similarity

Modified residue

306

1

Phosphotyrosine By similarity

Modified residue

316

1

Phosphotyrosine By similarity

Modified residue

397

1

Phosphotyrosine; by autocatalysis Ref.27 Ref.43

Modified residue

460

1

Phosphotyrosine By similarity

Modified residue

473

1

Phosphotyrosine By similarity

Modified residue

489

1

Phosphothreonine By similarity

Modified residue

502

1

Phosphothreonine By similarity

Modified residue

508

1

Phosphotyrosine; by autocatalysis, CSK and MATK Ref.27 Ref.50 Ref.52

Lipidation

2

1

N-myristoyl glycine By similarity

Lipidation

3

1

S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence

25 – 45

21

Missing in isoform 2.

VSP_005003

Experimental info

Mutagenesis

508

1

Y → F: Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates. Ref.33 Ref.35

Sequence conflict

77

1

I → F in AAA39471. Ref.2

Sequence conflict

77

1

I → F in AAA39472. Ref.2

Sequence conflict

161

1

L → I in AAA39471. Ref.2

Sequence conflict

161

1

L → I in AAA39472. Ref.2

Sequence conflict

279

1

P → L in AAA39471. Ref.2

Sequence conflict

279

1

P → L in AAA39472. Ref.2

Sequence conflict

391

1

V → I in AAA39471. Ref.2

Sequence conflict

391

1

V → I in AAA39472. Ref.2

Sequence conflict

415

1

I → F in AAA40017. Ref.4

Sequence conflict

425

1

D → N in AAA39470. Ref.1

Sequence conflict

432

1

L → P in AAA40017. Ref.4

Secondary structure

1

.

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512

Helix Strand Turn

Details...

Helix

244 – 246

3

Beta strand

247 – 254

8

Beta strand

257 – 266

10

Turn

267 – 269

3

Beta strand

270 – 277

8

Helix

284 – 294

11

Beta strand

305 – 309

5

Beta strand

311 – 314

4

Beta strand

316 – 320

5

Helix

327 – 332

6

Helix

336 – 338

3

Helix

341 – 360

20

Helix

370 – 372

3

Beta strand

373 – 375

3

Beta strand

381 – 383

3

Helix

407 – 409

3

Helix

412 – 417

6

Helix

422 – 438

17

Helix

449 – 455

7

Helix

456 – 458

3

Helix

470 – 479

10

Helix

484 – 486

3

Helix

490 – 498

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LYN A) (p56) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: FDA1D21CC90C50EC	FASTA	512	58,812
	10 20 30 40 50 60 MGCIKSKRKD NLNDDEVDSK TQPVRNTDRT IYVRDPTSNK QQRPVPEFHL LPGQRFQTKD 70 80 90 100 110 120 PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLSSKRE GFIPSNYVAK 130 140 150 160 170 180 VNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DYDPMHGDVI 190 200 210 220 230 240 KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW 250 260 270 280 290 300 EIPRESIKLV KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD 310 320 330 340 350 360 KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ IAEGMAYIER 370 380 390 400 410 420 KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF 430 440 450 460 470 480 TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMSALSQGY RMPRMENCPD ELYDIMKMCW 490 500 510 KEKAEERPTF DYLQSVLDDF YTATEGQYQQ QP
	Isoform 2 (LYN B) (p53) [UniParc]. Checksum: 2C82015D510B1F59	FASTA	491	56,285
	10 20 30 40 50 60 MGCIKSKRKD NLNDDEVDSK TQPVPEFHLL PGQRFQTKDP EEQGDIVVAL YPYDGIHPDD 70 80 90 100 110 120 LSFKKGEKMK VLEEHGEWWK AKSLSSKREG FIPSNYVAKV NTLETEEWFF KDITRKDAER 130 140 150 160 170 180 QLLAPGNSAG AFLIRESETL KGSFSLSVRD YDPMHGDVIK HYKIRSLDNG GYYISPRITF 190 200 210 220 230 240 PCISDMIKHY QKQSDGLCRR LEKACISPKP QKPWDKDAWE IPRESIKLVK KLGAGQFGEV 250 260 270 280 290 300 WMGYYNNSTK VAVKTLKPGT MSVQAFLEEA NLMKTLQHDK LVRLYAVVTK EEPIYIITEF 310 320 330 340 350 360 MAKGSLLDFL KSDEGGKVLL PKLIDFSAQI AEGMAYIERK NYIHRDLRAA NVLVSESLMC 370 380 390 400 410 420 KIADFGLARV IEDNEYTARE GAKFPIKWTA PEAINFGCFT IKSDVWSFGI LLYEIVTYGK 430 440 450 460 470 480 IPYPGRTNAD VMSALSQGYR MPRMENCPDE LYDIMKMCWK EKAEERPTFD YLQSVLDDFY 490 TATEGQYQQQ P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 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]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193 AND TYR-194, MASS SPECTROMETRY. Tissue: Mast cell.
[50]	"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-193; TYR-194 AND TYR-508, MASS SPECTROMETRY. Tissue: Brain.
[51]	"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.
[52]	"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 AND TYR-508, MASS SPECTROMETRY. Tissue: Macrophage.
[53]	"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.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"Src-family kinases: rheostats of immune cell signaling." Lowell C.A. Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[60]	"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.
[61]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00230138.
IPI00649763.

PIR

A39719.

RefSeq

NP_001104566.1. NM_001111096.1.

UniGene

Mm.317331.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P25911.

SMR

P25911. Positions 64-512.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37806N.

IntAct

P25911. 7 interactions.

MINT

MINT-100482.

PTM databases

PhosphoSite

P25911.

Proteomic databases

PaxDb

P25911.

PRIDE

P25911.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000041377; ENSMUSP00000038838; ENSMUSG00000042228.
ENSMUST00000103010; ENSMUSP00000100075; ENSMUSG00000042228.

GeneID

17096.

KEGG

mmu:17096.

Organism-specific databases

CTD

4067.

MGI

MGI:96892. Lyn.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

InParanoid

P25911.

KO

K05854.

OMA

ISSMIKH.

OrthoDB

EOG4N04DP.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Reactome

REACT_107772. Immune System.
REACT_115202. Signal Transduction.

Gene expression databases

ArrayExpress

P25911.

Bgee

P25911.

Genevestigator

P25911.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2258.

EvolutionaryTrace

P25911.

NextBio

291240.

SOURCE

Search...

Entry information

Entry name

LYN_MOUSE

Accession

Primary (citable) accession number: P25911
Secondary accession number(s): Q62127

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 147 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program