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Protein

Tyrosine-protein kinase Lyn

Gene

Lyn

Organism
Mus musculus (Mouse)
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. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation.By similarity36 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation4 Publications

Enzyme regulationi

Subject to autoinhibition, mediated by intramolecular interactions between the SH2 domain and the C-terminal phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508 inhibits kinase activity. Kinase activity is modulated by dephosphorylation by PTPRC/CD45. Inhibited by dasatinib, PP2, and SU6656.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei275ATPCurated1
Active sitei367Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi253 – 261ATPCurated9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • erythropoietin receptor binding Source: UniProtKB
  • glycosphingolipid binding Source: Ensembl
  • ion channel binding Source: MGI
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • protein complex binding Source: MGI
  • protein kinase activity Source: MGI
  • protein tyrosine kinase activity Source: UniProtKB
  • SH3 domain binding Source: MGI

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • B cell homeostasis Source: UniProtKB
  • B cell receptor signaling pathway Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to extracellular stimulus Source: Ensembl
  • cellular response to heat Source: Ensembl
  • cellular response to retinoic acid Source: MGI
  • central nervous system development Source: GO_Central
  • chemotaxis Source: GO_Central
  • cytokine secretion Source: Ensembl
  • dendritic cell differentiation Source: UniProtKB
  • erythrocyte differentiation Source: UniProtKB
  • Fc receptor mediated inhibitory signaling pathway Source: UniProtKB
  • Fc receptor mediated stimulatory signaling pathway Source: UniProtKB
  • hemoglobin biosynthetic process Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • histamine secretion by mast cell Source: Ensembl
  • immune response-regulating cell surface receptor signaling pathway Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • intracellular signal transduction Source: MGI
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • negative regulation of B cell proliferation Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • negative regulation of intracellular signal transduction Source: UniProtKB
  • negative regulation of MAP kinase activity Source: UniProtKB
  • negative regulation of mast cell proliferation Source: UniProtKB
  • negative regulation of myeloid leukocyte differentiation Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of toll-like receptor 2 signaling pathway Source: UniProtKB
  • negative regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
  • neuron projection development Source: MGI
  • oligodendrocyte development Source: Ensembl
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • platelet degranulation Source: UniProtKB
  • positive regulation of B cell receptor signaling pathway Source: MGI
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cellular component movement Source: MGI
  • positive regulation of dendritic cell apoptotic process Source: UniProtKB
  • positive regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
  • positive regulation of glial cell proliferation Source: Ensembl
  • positive regulation of mast cell proliferation Source: MGI
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of oligodendrocyte progenitor proliferation Source: Ensembl
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of stress-activated protein kinase signaling cascade Source: MGI
  • positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: MGI
  • regulation of B cell apoptotic process Source: UniProtKB
  • regulation of B cell receptor signaling pathway Source: UniProtKB
  • regulation of cell adhesion mediated by integrin Source: MGI
  • regulation of cytokine production Source: UniProtKB
  • regulation of cytokine secretion Source: UniProtKB
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of erythrocyte differentiation Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • regulation of mast cell activation Source: UniProtKB
  • regulation of mast cell degranulation Source: UniProtKB
  • regulation of monocyte chemotaxis Source: MGI
  • regulation of platelet aggregation Source: UniProtKB
  • regulation of release of sequestered calcium ion into cytosol Source: MGI
  • response to amino acid Source: Ensembl
  • response to axon injury Source: Ensembl
  • response to carbohydrate Source: Ensembl
  • response to drug Source: Ensembl
  • response to hormone Source: UniProtKB
  • response to insulin Source: Ensembl
  • response to organic cyclic compound Source: Ensembl
  • response to sterol depletion Source: Ensembl
  • response to toxic substance Source: Ensembl
  • signal transduction Source: UniProtKB
  • tolerance induction to self antigen Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-2454202. Fc epsilon receptor (FCERI) signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-389356. CD28 co-stimulation.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-5621575. CD209 (DC-SIGN) signaling.
R-MMU-75892. Platelet Adhesion to exposed collagen.
R-MMU-982772. Growth hormone receptor signaling.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Lyn (EC:2.7.10.2)
Alternative name(s):
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene namesi
Name:Lyn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:96892. Lyn.

Subcellular locationi

  • Cell membrane By similarity
  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity
  • Golgi apparatus By similarity
  • Membrane By similarity; Lipid-anchor 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi508Y → F: Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates. 2 Publications1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL2258.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000881302 – 512Tyrosine-protein kinase LynAdd BLAST511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Lipidationi3S-palmitoyl cysteineBy similarity1
Modified residuei19PhosphoserineCombined sources1
Modified residuei193PhosphotyrosineBy similarity1
Modified residuei228PhosphoserineBy similarity1
Modified residuei306PhosphotyrosineBy similarity1
Modified residuei316PhosphotyrosineBy similarity1
Modified residuei397Phosphotyrosine; by autocatalysisCombined sources2 Publications1
Modified residuei460PhosphotyrosineBy similarity1
Modified residuei473PhosphotyrosineBy similarity1
Modified residuei508Phosphotyrosine; by autocatalysis, CSK and MATKCombined sources1 Publication1

Post-translational modificationi

Ubiquitinated by CBL, leading to its degradation.1 Publication
Phosphorylated on tyrosine residues in response to KIT signaling (By similarity). Autophosphorylated. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.By similarity3 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP25911.
PeptideAtlasiP25911.
PRIDEiP25911.

PTM databases

iPTMnetiP25911.
PhosphoSitePlusiP25911.
SwissPalmiP25911.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000042228.
ExpressionAtlasiP25911. baseline and differential.
GenevisibleiP25911. MM.

Interactioni

Subunit structurei

Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation (By similarity). Interacts with CD36. Interacts with LYN (PubMed:22496641).By similarity18 Publications

Binary interactionsi

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

GO - Molecular functioni

  • erythropoietin receptor binding Source: UniProtKB
  • ion channel binding Source: MGI
  • protein complex binding Source: MGI
  • SH3 domain binding Source: MGI

Protein-protein interaction databases

BioGridi201256. 9 interactors.
DIPiDIP-37806N.
IntActiP25911. 13 interactors.
MINTiMINT-100482.
STRINGi10090.ENSMUSP00000038838.

Chemistry databases

BindingDBiP25911.

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi136 – 143Combined sources8
Beta strandi153 – 157Combined sources5
Beta strandi159 – 161Combined sources3
Beta strandi165 – 172Combined sources8
Beta strandi174 – 187Combined sources14
Beta strandi193 – 196Combined sources4
Beta strandi199 – 203Combined sources5
Helixi204 – 213Combined sources10
Beta strandi218 – 220Combined sources3
Helixi244 – 246Combined sources3
Beta strandi247 – 254Combined sources8
Beta strandi257 – 266Combined sources10
Turni267 – 269Combined sources3
Beta strandi270 – 277Combined sources8
Helixi284 – 294Combined sources11
Beta strandi305 – 309Combined sources5
Beta strandi311 – 314Combined sources4
Beta strandi316 – 320Combined sources5
Helixi327 – 332Combined sources6
Helixi336 – 338Combined sources3
Helixi341 – 360Combined sources20
Helixi370 – 372Combined sources3
Beta strandi373 – 375Combined sources3
Beta strandi381 – 383Combined sources3
Helixi407 – 409Combined sources3
Helixi412 – 417Combined sources6
Helixi422 – 438Combined sources17
Helixi449 – 455Combined sources7
Helixi456 – 458Combined sources3
Helixi470 – 479Combined sources10
Helixi484 – 486Combined sources3
Helixi490 – 498Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZV7X-ray2.50A239-512[»]
2ZV8X-ray2.70A239-512[»]
2ZV9X-ray2.76A239-512[»]
2ZVAX-ray2.60A239-512[»]
4TZIX-ray2.10A/B115-229[»]
ProteinModelPortaliP25911.
SMRiP25911.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25911.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 123SH3PROSITE-ProRule annotationAdd BLAST61
Domaini129 – 226SH2PROSITE-ProRule annotationAdd BLAST98
Domaini247 – 501Protein kinasePROSITE-ProRule annotationAdd BLAST255

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP25911.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG091G0D46.
PhylomeDBiP25911.
TreeFamiTF351634.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25911-1) [UniParc]FASTAAdd to basket
Also known as: LYN A, p56

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

« Hide

        10         20         30         40         50
MGCIKSKRKD NLNDDEVDSK TQPVRNTDRT IYVRDPTSNK QQRPVPEFHL
60 70 80 90 100
LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLSSKRE GFIPSNYVAK VNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DYDPMHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ
360 370 380 390 400
IAEGMAYIER KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR
410 420 430 440 450
EGAKFPIKWT APEAINFGCF TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA
460 470 480 490 500
DVMSALSQGY RMPRMENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,812
Last modified:January 23, 2007 - v4
Checksum:iFDA1D21CC90C50EC
GO
Isoform 2 (identifier: P25911-2) [UniParc]FASTAAdd to basket
Also known as: LYN B, p53

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti77I → F in AAA39471 (PubMed:2017160).Curated1
Sequence conflicti77I → F in AAA39472 (PubMed:2017160).Curated1
Sequence conflicti161L → I in AAA39471 (PubMed:2017160).Curated1
Sequence conflicti161L → I in AAA39472 (PubMed:2017160).Curated1
Sequence conflicti279P → L in AAA39471 (PubMed:2017160).Curated1
Sequence conflicti279P → L in AAA39472 (PubMed:2017160).Curated1
Sequence conflicti391V → I in AAA39471 (PubMed:2017160).Curated1
Sequence conflicti391V → I in AAA39472 (PubMed:2017160).Curated1
Sequence conflicti415I → F in AAA40017 (PubMed:2482828).Curated1
Sequence conflicti425D → N in AAA39470 (PubMed:1710766).Curated1
Sequence conflicti432L → P in AAA40017 (PubMed:2482828).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00500325 – 45Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZV7X-ray2.50A239-512[»]
2ZV8X-ray2.70A239-512[»]
2ZV9X-ray2.76A239-512[»]
2ZVAX-ray2.60A239-512[»]
4TZIX-ray2.10A/B115-229[»]
ProteinModelPortaliP25911.
SMRiP25911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201256. 9 interactors.
DIPiDIP-37806N.
IntActiP25911. 13 interactors.
MINTiMINT-100482.
STRINGi10090.ENSMUSP00000038838.

Chemistry databases

BindingDBiP25911.
ChEMBLiCHEMBL2258.

PTM databases

iPTMnetiP25911.
PhosphoSitePlusiP25911.
SwissPalmiP25911.

Proteomic databases

PaxDbiP25911.
PeptideAtlasiP25911.
PRIDEiP25911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4067.
MGIiMGI:96892. Lyn.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP25911.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG091G0D46.
PhylomeDBiP25911.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-2454202. Fc epsilon receptor (FCERI) signaling.
R-MMU-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-389356. CD28 co-stimulation.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-5621575. CD209 (DC-SIGN) signaling.
R-MMU-75892. Platelet Adhesion to exposed collagen.
R-MMU-982772. Growth hormone receptor signaling.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP25911.
PROiP25911.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000042228.
ExpressionAtlasiP25911. baseline and differential.
GenevisibleiP25911. MM.

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...

Entry informationi

Entry nameiLYN_MOUSE
AccessioniPrimary (citable) accession number: P25911
Secondary accession number(s): Q62127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 186 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.