P07948 (LYN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Lyn
EC=2.7.10.2

Alternative name(s):
Lck/Yes-related novel protein tyrosine kinase
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn

Gene names

Name:	LYN
Synonyms:	JTK8

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. Mediates phosphorylation of the BCR-ABL fusion protein. 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.6 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.25 Ref.27 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Ref.38 Ref.45
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.7 Ref.8 Ref.19 Ref.20
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.9 Ref.29
Subunit structure	Interacts with TEC By similarity. 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 By similarity. 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 Epstein-Barr virus LMP2A. Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip). 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 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 ankyrin repeat region) with LYN (via SH3-domain) in an activation-independent status of LYN By similarity. Forms a multiprotein complex with LYN and HS1 By similarity. Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.42 Ref.43 Ref.46 Ref.48 Ref.57
Subcellular location	Cell membrane. Nucleus. Cytoplasm. Cytoplasm › perinuclear region. Golgi apparatus. 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 plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts. Ref.23 Ref.33 Ref.34 Ref.36
Tissue specificity	Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors. Ref.1 Ref.8
Domain	The protein kinase domain plays an important role in its localization in the cell membrane. Ref.23
Post-translational modification	Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent. Ref.29 Ref.46 Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. 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.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.33 Ref.34 Ref.38
Involvement in disease	Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells. Ref.33 Ref.35 Ref.38
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 Host-virus interaction Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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 sequence or structural similarity. Source: UniProtKB B cell receptor signaling pathway Inferred from electronic annotation. Source: Compara Fc receptor mediated inhibitory signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB Fc receptor mediated stimulatory signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB JAK-STAT cascade involved in growth hormone signaling pathway Traceable author statement. Source: Reactome T cell costimulation Traceable author statement. Source: Reactome 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 mutant phenotype PubMed 17910947. Source: BHF-UCL cytokine secretion Inferred from electronic annotation. Source: Compara dendritic cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB histamine secretion by mast cell Inferred from electronic annotation. Source: Compara innate immune response Inferred from electronic annotation. Source: UniProtKB-KW leukocyte migration Traceable author statement. Source: Reactome lipopolysaccharide-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of B cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of immune response Traceable author statement Ref.50. Source: UniProtKB negative regulation of mast cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of myeloid leukocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of toll-like receptor 2 signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of toll-like receptor 4 signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB neuron projection development Inferred from electronic annotation. Source: Compara oligodendrocyte development Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.7. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of Fc receptor mediated stimulatory signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cellular component movement Inferred from direct assay Ref.27. Source: UniProtKB positive regulation of dendritic cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of glial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of mast cell proliferation Inferred from mutant phenotype Ref.16. Source: UniProtKB positive regulation of neuron projection development Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL positive regulation of oligodendrocyte progenitor proliferation Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from electronic annotation. Source: Compara positive regulation of stress-activated protein kinase signaling cascade Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of tyrosine phosphorylation of STAT protein Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.7. Source: UniProtKB regulation of B cell apoptotic process Inferred from electronic annotation. Source: Compara regulation of B cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell adhesion mediated by integrin Inferred from mutant phenotype Ref.37. Source: UniProtKB regulation of cytokine production Inferred from sequence or structural similarity. Source: UniProtKB regulation of cytokine secretion Inferred from electronic annotation. Source: Compara regulation of erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of inflammatory response Inferred from electronic annotation. Source: Compara regulation of mast cell degranulation Inferred from sequence or structural similarity. Source: UniProtKB regulation of monocyte chemotaxis Inferred from mutant phenotype Ref.37. Source: UniProtKB regulation of platelet aggregation Inferred from sequence or structural similarity. Source: UniProtKB regulation of release of sequestered calcium ion into cytosol Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from direct assay Ref.18Ref.19. Source: UniProtKB 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 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 sequence or structural similarity. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay Ref.23PubMed 20605918. Source: UniProtKB alpha2-beta1 integrin complex Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome membrane raft Inferred from direct assay PubMed 11313396. Source: UniProtKB mitochondrial crista Inferred from electronic annotation. Source: Compara mitochondrial intermembrane space Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.36. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 20605918. Source: UniProtKB plasma membrane Inferred from direct assay Ref.23PubMed 20605918. Source: UniProtKB postsynaptic density Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycosphingolipid binding Inferred from electronic annotation. Source: Compara non-membrane spanning protein tyrosine kinase activity Traceable author statement. Source: Reactome receptor signaling protein tyrosine kinase activity Traceable author statement Ref.15. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O92972	2	EBI-79452,EBI-710506	From a different organism.
	P27958	5	EBI-79452,EBI-706378	From a different organism.
	Q9WMX2	3	EBI-79452,EBI-710918	From a different organism.
Arap3	Q8R5G7	2	EBI-79452,EBI-621463	From a different organism.
CD22	P20273	2	EBI-79452,EBI-78277
CD24	P25063	6	EBI-79452,EBI-6267018
CD37	P11049	5	EBI-79452,EBI-6139068
CDKN1B	P46527	2	EBI-79452,EBI-519280
GP6	Q9HCN6	2	EBI-79452,EBI-515278
ITGB1	P05556	4	EBI-79452,EBI-703066

Alternative products

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

Isoform 1 (identifier: P07948-1)

Also known as: LYN A; p56lyn;

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: P07948-2)

Also known as: LYN B; p53lyn;

The sequence of this isoform differs from the canonical sequence as follows:
     23-43: 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_0000088129

Regions

Domain

63 – 123

61

SH3

Domain

129 – 226

98

SH2

Domain

247 – 501

255

Protein kinase

Nucleotide binding

253 – 261

9

ATP By similarity

Sites

Active site

367

1

Proton acceptor By similarity

Binding site

275

1

ATP By similarity

Amino acid modifications

Modified residue

6

1

Phosphoserine

Modified residue

11

1

Phosphoserine Ref.40 Ref.44 Ref.55

Modified residue

13

1

Phosphoserine Ref.40 Ref.44 Ref.47 Ref.55

Modified residue

30

1

Phosphothreonine

Modified residue

32

1

Phosphotyrosine

Modified residue

37

1

Phosphothreonine

Modified residue

193

1

Phosphotyrosine

Modified residue

194

1

Phosphotyrosine

Modified residue

228

1

Phosphoserine Ref.44

Modified residue

265

1

Phosphotyrosine

Modified residue

306

1

Phosphotyrosine Ref.44

Modified residue

316

1

Phosphotyrosine Ref.44

Modified residue

397

1

Phosphotyrosine; by autocatalysis Ref.9 Ref.34

Modified residue

460

1

Phosphotyrosine Ref.38

Modified residue

473

1

Phosphotyrosine Ref.40 Ref.44

Modified residue

489

1

Phosphothreonine

Modified residue

502

1

Phosphothreonine

Modified residue

508

1

Phosphotyrosine; by autocatalysis, CSK and MATK Ref.9 Ref.11 Ref.26 Ref.34 Ref.40 Ref.44

Lipidation

2

1

N-myristoyl glycine Probable

Lipidation

3

1

S-palmitoyl cysteine Probable

Natural variations

Alternative sequence

23 – 43

21

Missing in isoform 2.

VSP_005002

Natural variant

385

1

D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.59

VAR_041737

Experimental info

Mutagenesis

2

1

G → A: Loss of localization to the cell membrane; when associated with A-3. Ref.36

Mutagenesis

3

1

C → A: Loss of localization to the cell membrane; when associated with A-2. Ref.36

Mutagenesis

275

1

K → A: Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus; when associated with A-2 and A-3. Ref.16 Ref.19 Ref.23 Ref.36

Mutagenesis

275

1

K → L or R: Loss of kinase activity. Ref.16 Ref.19 Ref.23 Ref.36

Mutagenesis

346

1

D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499. Ref.23

Mutagenesis

353

1

E → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499. Ref.23

Mutagenesis

397

1

Y → F: Strongly reduced kinase activity. Ref.29

Mutagenesis

498

1

D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499. Ref.23

Mutagenesis

499

1

D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498. Ref.23

Mutagenesis

508

1

Y → F: Abolishes autoinhibition and thereby increases kinase activity. Ref.29

Secondary structure

1

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512

Helix Strand Turn

Details...

Beta strand

66 – 72

7

Beta strand

78 – 80

3

Beta strand

89 – 95

7

Beta strand

97 – 104

8

Turn

105 – 107

3

Beta strand

110 – 114

5

Turn

115 – 117

3

Beta strand

118 – 120

3

Beta strand

259 – 262

4

Beta strand

265 – 269

5

Beta strand

273 – 275

3

Beta strand

284 – 286

3

Turn

287 – 289

3

Helix

290 – 293

4

Turn

294 – 297

4

Beta strand

306 – 309

4

Beta strand

311 – 314

4

Beta strand

316 – 319

4

Helix

327 – 330

4

Helix

334 – 338

5

Helix

341 – 360

20

Beta strand

372 – 375

4

Beta strand

381 – 383

3

Helix

407 – 409

3

Helix

412 – 416

5

Helix

422 – 437

16

Turn

449 – 451

3

Helix

452 – 457

6

Beta strand

466 – 468

3

Helix

470 – 477

8

Turn

478 – 480

3

Turn

484 – 486

3

Helix

490 – 502

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LYN A) (p56lyn) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 408D3D461204E378	FASTA	512	58,574
	10 20 30 40 50 60 MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL LPGQRFQTKD 70 80 90 100 110 120 PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLLTKKE GFIPSNYVAK 130 140 150 160 170 180 LNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DFDPVHGDVI 190 200 210 220 230 240 KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQADGLCR RLEKACISPK PQKPWDKDAW 250 260 270 280 290 300 EIPRESIKLV KRLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD 310 320 330 340 350 360 KLVRLYAVVT REEPIYIITE YMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ IAEGMAYIER 370 380 390 400 410 420 KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF 430 440 450 460 470 480 TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMTALSQGY RMPRVENCPD ELYDIMKMCW 490 500 510 KEKAEERPTF DYLQSVLDDF YTATEGQYQQ QP
	Isoform 2 (LYN B) (p53lyn) [UniParc]. Checksum: D74E4074D4B0C92A	FASTA	491	56,033
	10 20 30 40 50 60 MGCIKSKGKD SLSDDGVDLK TQPVPESQLL PGQRFQTKDP EEQGDIVVAL YPYDGIHPDD 70 80 90 100 110 120 LSFKKGEKMK VLEEHGEWWK AKSLLTKKEG FIPSNYVAKL NTLETEEWFF KDITRKDAER 130 140 150 160 170 180 QLLAPGNSAG AFLIRESETL KGSFSLSVRD FDPVHGDVIK HYKIRSLDNG GYYISPRITF 190 200 210 220 230 240 PCISDMIKHY QKQADGLCRR LEKACISPKP QKPWDKDAWE IPRESIKLVK RLGAGQFGEV 250 260 270 280 290 300 WMGYYNNSTK VAVKTLKPGT MSVQAFLEEA NLMKTLQHDK LVRLYAVVTR EEPIYIITEY 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 VMTALSQGYR MPRVENCPDE LYDIMKMCWK EKAEERPTFD YLQSVLDDFY 490 TATEGQYQQQ P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p56lck." Yamanashi Y., Fukushige S., Semba K., Sukegawa J., Miyajima N., Matsubara K., Yamamoto T., Toyoshima K. Mol. Cell. Biol. 7:237-243(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]	"The cDNAs encoding two forms of the LYN protein tyrosine kinase are expressed in rat mast cells and human myeloid cells." Rider L.G., Raben N., Miller L., Jelsema C. Gene 138:219-222(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[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).
[4]	"Putative tyrosine kinases expressed in K-562 human leukemia cells." Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K. Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
[5]	"Expression of the B cell-associated tyrosine kinase gene Lyn in primary neuroblastoma tumours and its modulation during the differentiation of neuroblastoma cell lines." Bielke W., Ziemiecki A., Kappos L., Miescher G.C. Biochem. Biophys. Res. Commun. 186:1403-1409(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
[6]	"CD19 is a substrate of the antigen receptor-associated protein tyrosine kinase in human B cells." Roifman C.M., Ke S. Biochem. Biophys. Res. Commun. 194:222-225(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CD19 PHOSPHORYLATION, INTERACTION WITH CD19.
[7]	"Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling." Yamanashi Y., Okada M., Semba T., Yamori T., Umemori H., Tsunasawa S., Toyoshima K., Kitamura D., Watanabe T., Yamamoto T. Proc. Natl. Acad. Sci. U.S.A. 90:3631-3635(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, INTERACTION WITH HCLS1.
[8]	"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn." Wang A.V., Scholl P.R., Geha R.S. J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION.
[9]	"Functional analysis of Csk in signal transduction through the B-cell antigen receptor." Hata A., Sabe H., Kurosaki T., Takata M., Hanafusa H. Mol. Cell. Biol. 14:7306-7313(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, ENZYME REGULATION.
[10]	"Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases." Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., Kieff E. Immunity 2:155-166(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
[11]	"Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets." Hirao A., Hamaguchi I., Suda T., Yamaguchi N. EMBO J. 16:2342-2351(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-508 BY MATK. Tissue: Platelet.
[12]	"Fc gamma receptor type IIb induced recruitment of inositol and protein phosphatases to the signal transductory complex of human B-cell." Sarmay G., Koncz G., Pecht I., Gergely J. Immunol. Lett. 57:159-164(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR2B.
[13]	"Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells." Linnekin D., DeBerry C.S., Mou S. J. Biol. Chem. 272:27450-27455(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIT, PHOSPHORYLATION.
[14]	"Functional interaction between SHPTP1 and the Lyn tyrosine kinase in the apoptotic response to DNA damage." Yoshida K., Kharbanda S., Kufe D. J. Biol. Chem. 274:34663-34668(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA DAMAGE RESPONSE; APOPTOSIS AND PHOSPHORYLATION OF PTPN6/SHPTP1, INTERACTION WITH PTPN6/SHPTP1.
[15]	"Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor." Gaul B.S., Harrison M.L., Geahlen R.L., Burton R.A., Post C.B. J. Biol. Chem. 275:16174-16182(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CD79A PHOSPHORYLATION, INTERACTION WITH CD79A.
[16]	"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 MAST CELL PROLIFERATION, MUTAGENESIS OF LYS-275.
[17]	"Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic AMP-specific phosphodiesterase PDE4A10." Rena G., Begg F., Ross A., MacKenzie C., McPhee I., Campbell L., Huston E., Sullivan M., Houslay M.D. Mol. Pharmacol. 59:996-1011(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDE4A. Tissue: Brain.
[18]	"Role for Lyn tyrosine kinase as a regulator of stress-activated protein kinase activity in response to DNA damage." Yoshida K., Weichselbaum R., Kharbanda S., Kufe D. Mol. Cell. Biol. 20:5370-5380(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"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: FUNCTION IN DNA DAMAGE RESPONSE; APOPTOSIS AND PHOSPHORYLATION OF PPP1R15A, INTERACTION WITH PPP1R15A, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-275.
[20]	"Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling." Liang X., Wisniewski D., Strife A., Shivakrupa R., Clarkson B., Resh M.D. J. Biol. Chem. 277:13732-13738(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATING KIT AND DOK1, CATALYTIC ACTIVITY, INTERACTION WITH KIT.
[21]	"DF3/MUC1 signaling in multiple myeloma cells is regulated by interleukin-7." Li Y., Chen W., Ren J., Yu W.H., Li Q., Yoshida K., Kufe D. Cancer Biol. Ther. 2:187-193(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MUC1.
[22]	"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 THPO-MEDIATED CELL PROLIFERATION.
[23]	"Trafficking of Lyn through the Golgi caveolin involves the charged residues on alphaE and alphaI helices in the kinase domain." Kasahara K., Nakayama Y., Ikeda K., Fukushima Y., Matsuda D., Horimoto S., Yamaguchi N. J. Cell Biol. 165:641-652(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LYS-275; ASP-346; GLU-353; ASP-498 AND ASP-499.
[24]	"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor." Roskoski R. Jr. Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[25]	"Thrombin-induced tyrosine phosphorylation of HS1 in human platelets is sequentially catalyzed by Syk and Lyn tyrosine kinases and associated with the cellular migration of the protein." Brunati A.M., Deana R., Folda A., Massimino M.L., Marin O., Ledro S., Pinna L.A., Donella-Deana A. J. Biol. Chem. 280:21029-21035(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HCLS1.
[26]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, MASS SPECTROMETRY.
[27]	"Integrin inhibition through Lyn-dependent cross talk from CXCR4 chemokine receptors in normal human CD34+ marrow cells." Nakata Y., Tomkowicz B., Gewirtz A.M., Ptasznik A. Blood 107:4234-4239(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[28]	"Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity." Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P., Wu J., Hochrein J.M., Engen J.R., Smithgall T.E. J. Biol. Chem. 281:30907-30916(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABL1.
[29]	"Csk-binding protein mediates sequential enzymatic down-regulation and degradation of Lyn in erythropoietin-stimulated cells." Ingley E., Schneider J.R., Payne C.J., McCarthy D.J., Harder K.W., Hibbs M.L., Klinken S.P. J. Biol. Chem. 281:31920-31929(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAG1, MUTAGENESIS OF TYR-397 AND TYR-508, ENZYME REGULATION, UBIQUITINATION.
[30]	"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.
[31]	"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.
[32]	"TOM1L1 is a Lyn substrate involved in FcepsilonRI signaling in mast cells." Zhang J., Suzuki K., Hitomi T., Siraganian R.P. J. Biol. Chem. 282:37669-37677(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOM1L1, FUNCTION IN TOM1L1 PHOSPHORYLATION.
[33]	"A critical role for Lyn in acute myeloid leukemia." Dos Santos C., Demur C., Bardet V., Prade-Houdellier N., Payrastre B., Recher C. Blood 111:2269-2279(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION AND SURVIVAL, PHOSPHORYLATION, SUBCELLULAR LOCATION, ROLE IN DISEASE.
[34]	"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts." Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C. Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT TYR-397 AND TYR-508, INTERACTION WITH PAG1 AND STAT3, SUBCELLULAR LOCATION.
[35]	"Lyn regulates BCR-ABL and Gab2 tyrosine phosphorylation and c-Cbl protein stability in imatinib-resistant chronic myelogenous leukemia cells." Wu J., Meng F., Lu H., Kong L., Bornmann W., Peng Z., Talpaz M., Donato N.J. Blood 111:3821-3829(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBL AND BCR-ABL, FUNCTION IN PHOSPHORYLATION OF BCR-ABL, ROLE IN DISEASE.
[36]	"Nuclear localization of Lyn tyrosine kinase mediated by inhibition of its kinase activity." Ikeda K., Nakayama Y., Togashi Y., Obata Y., Kuga T., Kasahara K., Fukumoto Y., Yamaguchi N. Exp. Cell Res. 314:3392-3404(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2; CYS-3 AND LYS-275.
[37]	"Monocyte migration and LFA-1-mediated attachment to brain microvascular endothelia is regulated by SDF-1 alpha through Lyn kinase." Malik M., Chen Y.-Y., Kienzle M.F., Tomkowicz B.E., Collman R.G., Ptasznik A. J. Immunol. 181:4632-4637(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ADHESION AND CELL MIGRATION.
[38]	"Association between imatinib-resistant BCR-ABL mutation-negative leukemia and persistent activation of LYN kinase." Wu J., Meng F., Kong L.Y., Peng Z., Ying Y., Bornmann W.G., Darnay B.G., Lamothe B., Sun H., Talpaz M., Donato N.J. J. Natl. Cancer Inst. 100:926-939(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-460, ROLE IN DISEASE.
[39]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[40]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; TYR-473 AND TYR-508, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[41]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[42]	"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening." Voss M., Lettau M., Janssen O. BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FASLG.
[43]	"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins." Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K. J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADAM15.
[44]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-228; TYR-306; TYR-316; TYR-473 AND TYR-508, MASS SPECTROMETRY.
[45]	"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems." Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B., Houtman J.C. J. Leukoc. Biol. 87:691-701(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
[46]	"Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2." Mund T., Pelham H.R. Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NDFIP1 AND NDFIP2, UBIQUITINATION.
[47]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[48]	"SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling." Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T. Mol. Cell. Biol. 31:4550-4562(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCIMP.
[49]	"Src-family kinases: rheostats of immune cell signaling." Lowell C.A. Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[50]	"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.
[51]	"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.
[52]	"The duplicitous nature of the Lyn tyrosine kinase in growth factor signaling." Hibbs M.L., Harder K.W. Growth Factors 24:137-149(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN GROWTH FACTOR SIGNALING.
[53]	"New insights on mast cell activation via the high affinity receptor for IgE." Rivera J., Fierro N.A., Olivera A., Suzuki R. Adv. Immunol. 98:85-120(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN MAST CELLS.
[54]	"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 ON ROLE IN MYELOID CELL FUNCTION AND SIGNALING.
[55]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, MASS SPECTROMETRY.
[56]	"Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck." Schweimer K., Hoffmann S., Bauer F., Friedrich U., Kardinal C., Feller S.M., Biesinger B., Sticht H. Biochemistry 41:5120-5130(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 61-123 IN COMPLEX WITH SAIMIRIINE HERPESVIRUS 2 TYROSINE KINASE INTERACTING PROTEIN.
[57]	"Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity." Bauer F., Schweimer K., Meiselbach H., Hoffmann S., Rosch P., Sticht H. Protein Sci. 14:2487-2498(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 61-122, INTERACTION WITH HERPESVIRUS TYROSINE KINASE INTERACTING PROTEIN.
[58]	"Structural basis for the inhibitor recognition of human Lyn kinase domain." Miyano N., Kinoshita T., Nakai R., Kirii Y., Yokota K., Tada T. Bioorg. Med. Chem. Lett. 19:6557-6560(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-512 IN COMPLEX WITH STAUROSPORINE.
[59]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-385.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16038 mRNA. Translation: AAA59540.1.
M79321 mRNA. Translation: AAB50019.1.
BC075001 mRNA. Translation: AAH75001.1.
BC075002 mRNA. Translation: AAH75002.1.
BC126456 mRNA. Translation: AAI26457.1.
BC126458 mRNA. Translation: AAI26459.1.

IPI

IPI00298625.
IPI00432416.

PIR

TVHULY. A26719.

RefSeq

NP_001104567.1. NM_001111097.2.
NP_002341.1. NM_002350.3.

UniGene

Hs.491767.
Hs.545418.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W1F	NMR	-	A	61-122	[»]
1WA7	NMR	-	A	61-123	[»]
3A4O	X-ray	3.00	X	233-512	[»]

ProteinModelPortal

P07948.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1056N.

IntAct

P07948. 31 interactions.

MINT

MINT-200655.

STRING

9606.ENSP00000376688.

PTM databases

PhosphoSite

P07948.

Polymorphism databases

DMDM

125480.

2D gel databases

REPRODUCTION-2DPAGE

P07948.

Proteomic databases

PaxDb

P07948.

PRIDE

P07948.

Protocols and materials databases

DNASU

4067.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000519728; ENSP00000428924; ENSG00000254087.
ENST00000520220; ENSP00000428424; ENSG00000254087.

GeneID

4067.

KEGG

hsa:4067.

UCSC

uc003xsk.4. human.
uc003xsl.4. human.

Organism-specific databases

CTD

4067.

GeneCards

GC08P056792.

HGNC

HGNC:6735. LYN.

HPA

CAB004492.
HPA001231.

MIM

165120. gene.

neXtProt

NX_P07948.

PharmGKB

PA30498.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

KO

K05854.

OMA

ISSMIKH.

OrthoDB

EOG4N04DP.

PhylomeDB

P07948.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
bcr_5pathway. BCR signaling pathway.
pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
epopathway. EPO signaling pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
glypican_1pathway. Glypican 1 network.
lysophospholipid_pathway. LPA receptor mediated events.
pdgfrbpathway. PDGFR-beta signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
ptp1bpathway. Signaling events mediated by PTP1B.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P07948.

Bgee

P07948.

CleanEx

HS_LYN.

Genevestigator

P07948.

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

BindingDB

P07948.

ChEMBL

CHEMBL3905.

ChiTaRS

LYN. human.

EvolutionaryTrace

P07948.

GenomeRNAi

4067.

NextBio

15944.

PMAP-CutDB

P07948.

SOURCE

Search...

Entry information

Entry name

LYN_HUMAN

Accession

Primary (citable) accession number: P07948
Secondary accession number(s): A0AVQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 169 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.