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P07948

- LYN_HUMAN

UniProt

P07948 - LYN_HUMAN

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Protein

Tyrosine-protein kinase Lyn

Gene

LYN

Organism
Homo sapiens (Human)
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. 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'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation.20 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 SU6656.2 Publications

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi253 – 2619ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. glycosphingolipid binding Source: Ensembl
  4. ion channel binding Source: BHF-UCL
  5. non-membrane spanning protein tyrosine kinase activity Source: Reactome
  6. protein tyrosine kinase activity Source: UniProtKB
  7. receptor signaling protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Host-virus interaction, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111133. Growth hormone receptor signaling.
REACT_111225. Regulation of KIT signaling.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_12519. PECAM1 interactions.
REACT_160274. FCGR activation.
REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_1695. GPVI-mediated activation cascade.
REACT_19183. CD28 co-stimulation.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23787. Regulation of signaling by CBL.
SignaLinkiP07948.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LYN
Synonyms:JTK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:6735. LYN.

Subcellular locationi

Cell membrane. Nucleus. Cytoplasm. Cytoplasmperinuclear 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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Loss of localization to the cell membrane; when associated with A-3. 1 Publication
Mutagenesisi3 – 31C → A: Loss of localization to the cell membrane; when associated with A-2. 1 Publication
Mutagenesisi275 – 2751K → 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. 4 Publications
Mutagenesisi275 – 2751K → L or R: Loss of kinase activity. 4 Publications
Mutagenesisi346 – 3461D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499. 1 Publication
Mutagenesisi353 – 3531E → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499. 1 Publication
Mutagenesisi397 – 3971Y → F: Strongly reduced kinase activity. 1 Publication
Mutagenesisi498 – 4981D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499. 1 Publication
Mutagenesisi499 – 4991D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498. 1 Publication
Mutagenesisi508 – 5081Y → F: Abolishes autoinhibition and thereby increases kinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA30498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 512511Tyrosine-protein kinase LynPRO_0000088129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Lipidationi3 – 31S-palmitoyl cysteineCurated
Modified residuei6 – 61Phosphoserine
Modified residuei11 – 111Phosphoserine3 Publications
Modified residuei13 – 131Phosphoserine4 Publications
Modified residuei30 – 301Phosphothreonine
Modified residuei32 – 321Phosphotyrosine
Modified residuei37 – 371Phosphothreonine
Modified residuei193 – 1931Phosphotyrosine1 Publication
Modified residuei194 – 1941Phosphotyrosine
Modified residuei228 – 2281Phosphoserine1 Publication
Modified residuei265 – 2651Phosphotyrosine
Modified residuei306 – 3061Phosphotyrosine1 Publication
Modified residuei316 – 3161Phosphotyrosine1 Publication
Modified residuei397 – 3971Phosphotyrosine; by autocatalysis2 Publications
Modified residuei460 – 4601Phosphotyrosine1 Publication
Modified residuei473 – 4731Phosphotyrosine2 Publications
Modified residuei489 – 4891Phosphothreonine
Modified residuei502 – 5021Phosphothreonine
Modified residuei508 – 5081Phosphotyrosine; by autocatalysis, CSK and MATK6 Publications

Post-translational modificationi

Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent.2 Publications
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.12 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP07948.
PaxDbiP07948.
PRIDEiP07948.

2D gel databases

REPRODUCTION-2DPAGEP07948.

PTM databases

PhosphoSiteiP07948.

Miscellaneous databases

PMAP-CutDBP07948.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiP07948.
CleanExiHS_LYN.
ExpressionAtlasiP07948. baseline and differential.
GenevestigatoriP07948.

Organism-specific databases

HPAiCAB004492.
HPA001231.

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 with Epstein-Barr virus LMP2A. Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip). Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation. Interacts with CD36.29 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
O929722EBI-79452,EBI-710506From a different organism.
P225753EBI-79452,EBI-866709From a different organism.
P279585EBI-79452,EBI-706378From a different organism.
Q9WMX23EBI-79452,EBI-710918From a different organism.
ARP102755EBI-79452,EBI-608057
Arap3Q8R5G72EBI-79452,EBI-621463From a different organism.
CD22P202732EBI-79452,EBI-78277
CD24P250636EBI-79452,EBI-6267018
CD37P110495EBI-79452,EBI-6139068
CDKN1BP465272EBI-79452,EBI-519280
EGFRP005336EBI-79452,EBI-297353
GAB1Q134807EBI-79452,EBI-517684
GNB2L1P632442EBI-79452,EBI-296739
GP6Q9HCN62EBI-79452,EBI-515278
ITGB1P055564EBI-79452,EBI-703066
KITP107217EBI-79452,EBI-1379503
MCM7P339935EBI-6895930,EBI-355924
METP085812EBI-79452,EBI-1039152
PAG1Q9NWQ83EBI-79452,EBI-2828115

Protein-protein interaction databases

BioGridi110245. 175 interactions.
DIPiDIP-1056N.
IntActiP07948. 51 interactions.
MINTiMINT-200655.
STRINGi9606.ENSP00000376688.

Structurei

Secondary structure

1
512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 727
Beta strandi78 – 803
Beta strandi89 – 957
Beta strandi97 – 1048
Turni105 – 1073
Beta strandi110 – 1145
Turni115 – 1173
Beta strandi118 – 1203
Beta strandi259 – 2624
Beta strandi265 – 2695
Beta strandi273 – 2753
Beta strandi284 – 2863
Turni287 – 2893
Helixi290 – 2934
Turni294 – 2974
Beta strandi306 – 3094
Beta strandi311 – 3144
Beta strandi316 – 3194
Helixi327 – 3304
Helixi334 – 3385
Helixi341 – 36020
Beta strandi372 – 3754
Beta strandi381 – 3833
Helixi407 – 4093
Helixi412 – 4165
Helixi422 – 43716
Turni449 – 4513
Helixi452 – 4576
Beta strandi466 – 4683
Helixi470 – 4778
Turni478 – 4803
Turni484 – 4863
Helixi490 – 50213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
ProteinModelPortaliP07948.
SMRiP07948. Positions 64-512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07948.

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.1 Publication

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.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP07948.
KOiK05854.
OMAiWWRAKSL.
PhylomeDBiP07948.
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: P07948) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL
60 70 80 90 100
LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLLTKKE GFIPSNYVAK LNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DFDPVHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQADGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KRLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT REEPIYIITE YMAKGSLLDF 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
DVMTALSQGY RMPRVENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,574
Last modified:January 23, 2007 - v3
Checksum:i408D3D461204E378
GO
Isoform 2 (identifier: P07948-2) [UniParc]FASTAAdd to Basket

Also known as: LYN B, p53lyn

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

Show »
Length:491
Mass (Da):56,033
Checksum:iD74E4074D4B0C92A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti385 – 3851D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
VAR_041737

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei23 – 4321Missing in isoform 2. 1 PublicationVSP_005002Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS47859.1. [P07948-2]
CCDS6162.1. [P07948-1]
PIRiA26719. TVHULY.
RefSeqiNP_001104567.1. NM_001111097.2. [P07948-2]
NP_002341.1. NM_002350.3. [P07948-1]
XP_005251290.1. XM_005251233.2. [P07948-1]
UniGeneiHs.491767.
Hs.545418.

Genome annotation databases

EnsembliENST00000519728; ENSP00000428924; ENSG00000254087. [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087. [P07948-2]
GeneIDi4067.
KEGGihsa:4067.
UCSCiuc003xsk.4. human. [P07948-1]
uc003xsl.4. human. [P07948-2]

Polymorphism databases

DMDMi125480.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS47859.1. [P07948-2 ]
CCDS6162.1. [P07948-1 ]
PIRi A26719. TVHULY.
RefSeqi NP_001104567.1. NM_001111097.2. [P07948-2 ]
NP_002341.1. NM_002350.3. [P07948-1 ]
XP_005251290.1. XM_005251233.2. [P07948-1 ]
UniGenei Hs.491767.
Hs.545418.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W1F NMR - A 61-123 [» ]
1WA7 NMR - A 61-123 [» ]
3A4O X-ray 3.00 X 233-512 [» ]
ProteinModelPortali P07948.
SMRi P07948. Positions 64-512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110245. 175 interactions.
DIPi DIP-1056N.
IntActi P07948. 51 interactions.
MINTi MINT-200655.
STRINGi 9606.ENSP00000376688.

Chemistry

BindingDBi P07948.
ChEMBLi CHEMBL2363074.
DrugBanki DB06616. Bosutinib.
DB08901. Ponatinib.
GuidetoPHARMACOLOGYi 2060.

PTM databases

PhosphoSitei P07948.

Polymorphism databases

DMDMi 125480.

2D gel databases

REPRODUCTION-2DPAGE P07948.

Proteomic databases

MaxQBi P07948.
PaxDbi P07948.
PRIDEi P07948.

Protocols and materials databases

DNASUi 4067.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000519728 ; ENSP00000428924 ; ENSG00000254087 . [P07948-1 ]
ENST00000520220 ; ENSP00000428424 ; ENSG00000254087 . [P07948-2 ]
GeneIDi 4067.
KEGGi hsa:4067.
UCSCi uc003xsk.4. human. [P07948-1 ]
uc003xsl.4. human. [P07948-2 ]

Organism-specific databases

CTDi 4067.
GeneCardsi GC08P056792.
HGNCi HGNC:6735. LYN.
HPAi CAB004492.
HPA001231.
MIMi 165120. gene.
neXtProti NX_P07948.
PharmGKBi PA30498.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P07948.
KOi K05854.
OMAi WWRAKSL.
PhylomeDBi P07948.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_111133. Growth hormone receptor signaling.
REACT_111225. Regulation of KIT signaling.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_12519. PECAM1 interactions.
REACT_160274. FCGR activation.
REACT_163701. FCERI mediated MAPK activation.
REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163936. Fc epsilon receptor (FCERI) signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_1695. GPVI-mediated activation cascade.
REACT_19183. CD28 co-stimulation.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23787. Regulation of signaling by CBL.
SignaLinki P07948.

Miscellaneous databases

ChiTaRSi LYN. human.
EvolutionaryTracei P07948.
GeneWikii LYN.
GenomeRNAii 4067.
NextBioi 15944.
PMAP-CutDB P07948.
PROi P07948.
SOURCEi Search...

Gene expression databases

Bgeei P07948.
CleanExi HS_LYN.
ExpressionAtlasi P07948. baseline and differential.
Genevestigatori P07948.

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. "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. 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. Cited for: INTERACTION WITH CBLC.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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 PHOSPHORYLATION OF KIT AND DOK1, CATALYTIC ACTIVITY, INTERACTION WITH KIT.
  22. "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.
  23. "Identification of UNC119 as a novel activator of SRC-type tyrosine kinases."
    Cen O., Gorska M.M., Stafford S.J., Sur S., Alam R.
    J. Biol. Chem. 278:8837-8845(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC119.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. "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.
  34. "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.
  35. Cited for: FUNCTION IN CELL PROLIFERATION AND SURVIVAL, PHOSPHORYLATION, SUBCELLULAR LOCATION, ROLE IN DISEASE.
  36. "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.
  37. "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.
  38. "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, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; CYS-3 AND LYS-275.
  39. "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.
  40. "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-193 AND TYR-460, ROLE IN DISEASE.
  41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  42. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  44. "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.
  45. "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.
  46. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-228; TYR-306; TYR-316; TYR-473 AND TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  47. "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.
  48. "CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer."
    Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.
    Nat. Immunol. 11:155-161(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LTR4 AND LTR6 HETERODIMERIZATION, INTERACTION WITH CD36.
  49. "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.
  50. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  51. "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.
  52. "Src-family kinases: rheostats of immune cell signaling."
    Lowell C.A.
    Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  53. "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.
  54. "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.
  55. "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.
  56. "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.
  57. "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: ROLE IN MYELOID CELL FUNCTION, SIGNALING.
  58. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  59. "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.
  60. "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.
  61. "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.
  62. "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.

Entry informationi

Entry nameiLYN_HUMAN
AccessioniPrimary (citable) accession number: P07948
Secondary accession number(s): A0AVQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3