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Protein

Tyrosine-protein kinase Lyn

Gene

Lyn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B (By similarity). Phosphorylates LPXN on 'Tyr-72' (By similarity). Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation.By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

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/CD45.1 Publication

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: RGD
  3. gamma-tubulin binding Source: RGD
  4. glycosphingolipid binding Source: RGD
  5. integrin binding Source: RGD
  6. kinase activity Source: RGD
  7. non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  8. phosphoprotein binding Source: RGD
  9. platelet-derived growth factor receptor binding Source: RGD
  10. protein complex binding Source: RGD
  11. protein tyrosine kinase activity Source: RGD
  12. receptor binding Source: RGD
  13. ubiquitin protein ligase binding Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 5301.
ReactomeiREACT_277188. EPHB-mediated forward signaling.
REACT_278187. FCERI mediated NF-kB activation.
REACT_286909. Platelet Adhesion to exposed collagen.
REACT_289444. CD28 co-stimulation.
REACT_292219. FCGR activation.
REACT_296697. Fc epsilon receptor (FCERI) signaling.
REACT_297589. GPVI-mediated activation cascade.
REACT_302394. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_305922. CTLA4 inhibitory signaling.
REACT_313117. EPH-ephrin mediated repulsion of cells.
REACT_313573. Regulation of KIT signaling.
REACT_314415. Growth hormone receptor signaling.
REACT_320606. Regulation of signaling by CBL.
REACT_335137. Signaling by SCF-KIT.
REACT_335402. EPHA-mediated growth cone collapse.
REACT_340722. FCERI mediated Ca+2 mobilization.
REACT_341785. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_343260. Cell surface interactions at the vascular wall.
REACT_348379. EPH-Ephrin signaling.
REACT_353315. FCERI mediated MAPK activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Lyn (EC:2.7.10.2)
Alternative name(s):
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene namesi
Name:Lyn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi621017. Lyn.

Subcellular locationi

Cell membrane By similarity. Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Golgi apparatus By similarity
Note: Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity).By similarity

GO - Cellular componenti

  1. cell-cell adherens junction Source: RGD
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: Ensembl
  4. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  5. Golgi apparatus Source: UniProtKB-SubCell
  6. integrin alpha2-beta1 complex Source: RGD
  7. mast cell granule Source: GOC
  8. membrane Source: RGD
  9. membrane raft Source: RGD
  10. mitochondrial crista Source: RGD
  11. mitochondrial intermembrane space Source: RGD
  12. mitochondrial membrane Source: RGD
  13. nucleus Source: UniProtKB
  14. perinuclear region of cytoplasm Source: RGD
  15. plasma membrane Source: RGD
  16. postsynaptic density Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 512511Tyrosine-protein kinase LynPRO_0000088131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei30 – 301PhosphothreonineBy similarity
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei37 – 371PhosphothreonineBy similarity
Modified residuei193 – 1931PhosphotyrosineBy similarity
Modified residuei194 – 1941PhosphotyrosineBy similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei265 – 2651PhosphotyrosineBy similarity
Modified residuei306 – 3061PhosphotyrosineBy similarity
Modified residuei316 – 3161PhosphotyrosineBy similarity
Modified residuei397 – 3971Phosphotyrosine; by autocatalysis1 Publication
Modified residuei460 – 4601PhosphotyrosineBy similarity
Modified residuei473 – 4731PhosphotyrosineBy similarity
Modified residuei489 – 4891PhosphothreonineBy similarity
Modified residuei502 – 5021PhosphothreonineBy similarity
Modified residuei508 – 5081Phosphotyrosine; by autocatalysis, CSK and MATK1 Publication

Post-translational modificationi

Ubiquitinated. Ubiquitination is SH3-dependent (By similarity).By similarity
Phosphorylated on tyrosine residues in response to KIT signaling (By similarity). Autophosphorylated. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ07014.
PRIDEiQ07014.

PTM databases

PhosphoSiteiQ07014.

Expressioni

Tissue specificityi

Detected in spleen (at protein level). Expressed predominantly in B-lymphoid and myeloid cells.1 Publication

Gene expression databases

GenevestigatoriQ07014.

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 (By similarity). Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation (By similarity). Interacts with CD36.By similarity

Protein-protein interaction databases

BioGridi249512. 7 interactions.
IntActiQ07014. 3 interactions.
MINTiMINT-4564766.
STRINGi10116.ENSRNOP00000011130.

Structurei

3D structure databases

ProteinModelPortaliQ07014.
SMRiQ07014. Positions 67-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ07014.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ07014.
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. AlignAdd to basket

Isoform LYN A (identifier: Q07014-1) [UniParc]FASTAAdd to basket

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

« Hide

        10         20         30         40         50
MGCIKSKRKD NLNDDGVDMK TQPVRNTDRT IYVRDPTSNK QQRPVPESQL
60 70 80 90 100
LPGQRFQAKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLSSKRE GFIPSNYVAK VNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DYDPMHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSAQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGSKVL 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 RMPRMENCPD ELYDIMKMCW KESAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,660
Last modified:January 22, 2007 - v3
Checksum:iE03615E229CD43F1
GO
Isoform LYN B (identifier: Q07014-2) [UniParc]FASTAAdd to basket

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

Show »
Length:491
Mass (Da):56,133
Checksum:i6FFFB1609E015180
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311P → L in AAA20944 (PubMed:8125304).Curated
Sequence conflicti231 – 2311P → L in AAA20945 (PubMed:8125304).Curated
Sequence conflicti308 – 3081V → A in AAA20944 (PubMed:8125304).Curated
Sequence conflicti308 – 3081V → A in AAA20945 (PubMed:8125304).Curated
Sequence conflicti419 – 4191C → Y in AAA20944 (PubMed:8125304).Curated
Sequence conflicti419 – 4191C → Y in AAA20945 (PubMed:8125304).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 4521Missing in isoform LYN B. CuratedVSP_005004Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14951 mRNA. Translation: AAA41549.1.
L14782 mRNA. Translation: AAA20944.1.
L14823 mRNA. Translation: AAA20945.1.
AF000300 mRNA. Translation: AAB71344.1.
AF000301 mRNA. Translation: AAB71345.1.
AF000302 mRNA. Translation: AAB71346.1.
PIRiI56160.
PT0198.
RefSeqiNP_001104568.1. NM_001111098.1. [Q07014-2]
NP_110484.1. NM_030857.2. [Q07014-1]
XP_006237896.1. XM_006237834.2. [Q07014-1]
UniGeneiRn.4338.

Genome annotation databases

EnsembliENSRNOT00000011130; ENSRNOP00000011130; ENSRNOG00000008180. [Q07014-1]
GeneIDi81515.
KEGGirno:81515.
UCSCiRGD:621017. rat. [Q07014-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14951 mRNA. Translation: AAA41549.1.
L14782 mRNA. Translation: AAA20944.1.
L14823 mRNA. Translation: AAA20945.1.
AF000300 mRNA. Translation: AAB71344.1.
AF000301 mRNA. Translation: AAB71345.1.
AF000302 mRNA. Translation: AAB71346.1.
PIRiI56160.
PT0198.
RefSeqiNP_001104568.1. NM_001111098.1. [Q07014-2]
NP_110484.1. NM_030857.2. [Q07014-1]
XP_006237896.1. XM_006237834.2. [Q07014-1]
UniGeneiRn.4338.

3D structure databases

ProteinModelPortaliQ07014.
SMRiQ07014. Positions 67-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249512. 7 interactions.
IntActiQ07014. 3 interactions.
MINTiMINT-4564766.
STRINGi10116.ENSRNOP00000011130.

Chemistry

BindingDBiQ07014.
ChEMBLiCHEMBL4363.

PTM databases

PhosphoSiteiQ07014.

Proteomic databases

PaxDbiQ07014.
PRIDEiQ07014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011130; ENSRNOP00000011130; ENSRNOG00000008180. [Q07014-1]
GeneIDi81515.
KEGGirno:81515.
UCSCiRGD:621017. rat. [Q07014-1]

Organism-specific databases

CTDi4067.
RGDi621017. Lyn.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ07014.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ07014.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 5301.
ReactomeiREACT_277188. EPHB-mediated forward signaling.
REACT_278187. FCERI mediated NF-kB activation.
REACT_286909. Platelet Adhesion to exposed collagen.
REACT_289444. CD28 co-stimulation.
REACT_292219. FCGR activation.
REACT_296697. Fc epsilon receptor (FCERI) signaling.
REACT_297589. GPVI-mediated activation cascade.
REACT_302394. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_305922. CTLA4 inhibitory signaling.
REACT_313117. EPH-ephrin mediated repulsion of cells.
REACT_313573. Regulation of KIT signaling.
REACT_314415. Growth hormone receptor signaling.
REACT_320606. Regulation of signaling by CBL.
REACT_335137. Signaling by SCF-KIT.
REACT_335402. EPHA-mediated growth cone collapse.
REACT_340722. FCERI mediated Ca+2 mobilization.
REACT_341785. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_343260. Cell surface interactions at the vascular wall.
REACT_348379. EPH-Ephrin signaling.
REACT_353315. FCERI mediated MAPK activation.

Miscellaneous databases

NextBioi615007.
PROiQ07014.

Gene expression databases

GenevestigatoriQ07014.

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]
ProtoNetiSearch...

Publicationsi

  1. "Bacterially expressed rat p56lyn binds several proteins in rat basophilic leukemia cells including pp72, a tyrosine phosphorylated protein prominent in activated cells."
    Minoguchi K., Nishikata H., Siraganian R.P.
    J. Immunol. 150:222-222(1992)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE."
    Vonakis B.M., Chen H., Haleem-Smith H., Metzger H.
    J. Biol. Chem. 272:24072-24080(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Spontaneous autophosphorylation of Lyn tyrosine kinase at both its activation segment and C-terminal tail confers altered substrate specificity."
    Donella-Deana A., Cesaro L., Ruzzene M., Brunati A.M., Marin O., Pinna L.A.
    Biochemistry 37:1438-1446(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLYN_RAT
AccessioniPrimary (citable) accession number: Q07014
Secondary accession number(s): Q63320
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.