EKS-MUM-00400
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-MUM-00400
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
TK/Src443.16.6E-133226476251
StatusReviewed
Ensembl ProteinENSMUSP00000100075
UniProt AccessionP25911; Q62127;
Protein NameTyrosine-protein kinase Lyn
Protein Synonyms/Alias V-yes-1 Yamaguchi sarcoma viral related oncogene homolog; p53Lyn; p56Lyn;
Gene NameLyn
Gene Synonyms/Alias Lyn;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSMUSG00000042228ENSMUSP00000038838ENSMUST00000041377
ENSMUSG00000042228ENSMUSP00000100075ENSMUST00000103010
OrganismMus musculus
Functional DescriptionNon-receptor tyrosine-protein kinase that transmitssignals 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'.
Protein Length491
Protein Sequence
(FASTA)
MGCIKSKRKD NLNDDEVDSK TQPVPEFHLL PGQRFQTKDP EEQGDIVVAL YPYDGIHPDD 60
LSFKKGEKMK VLEEHGEWWK AKSLSSKREG FIPSNYVAKV NTLETEEWFF KDITRKDAER 120
QLLAPGNSAG AFLIRESETL KGSFSLSVRD YDPMHGDVIK HYKIRSLDNG GYYISPRITF 180
PCISDMIKHY QKQSDGLCRR LEKACISPKP QKPWDKDAWE IPRESIKLVK KLGAGQFGEV 240
WMGYYNNSTK VAVKTLKPGT MSVQAFLEEA NLMKTLQHDK LVRLYAVVTK EEPIYIITEF 300
MAKGSLLDFL KSDEGGKVLL PKLIDFSAQI AEGMAYIERK NYIHRDLRAA NVLVSESLMC 360
KIADFGLARV IEDNEYTARE GAKFPIKWTA PEAINFGCFT IKSDVWSFGI LLYEIVTYGK 420
IPYPGRTNAD VMSALSQGYR MPRMENCPDE LYDIMKMCWK EKAEERPTFD YLQSVLDDFY 480
TATEGQYQQQ P 491
Nucleotide Sequence
(FASTA)
ATGGGATGTA TTAAATCAAA AAGGAAAGAC AATCTCAATG ACGATGAAGT AGATTCGAAG 60
ACTCAACCAG TTCCTGAATT TCATCTTTTA CCAGGACAGA GATTTCAAAC AAAAGATCCA 120
GAGGAACAAG GTGACATTGT GGTGGCCTTA TACCCTTATG ATGGCATCCA CCCAGATGAC 180
TTGTCCTTCA AGAAAGGAGA AAAGATGAAA GTTCTAGAAG AGCATGGGGA ATGGTGGAAA 240
GCTAAGTCCC TTTCATCAAA GAGAGAAGGC TTCATCCCCA GCAACTACGT GGCCAAGGTC 300
AACACCTTAG AAACTGAAGA GTGGTTCTTC AAGGACATAA CAAGGAAAGA TGCAGAGCGA 360
CAGCTTCTGG CACCAGGGAA CAGTGCAGGA GCTTTCCTTA TCAGAGAAAG CGAAACTTTA 420
AAGGGAAGCT TCTCTCTTTC TGTCAGAGAT TATGACCCTA TGCATGGTGA TGTCATTAAG 480
CACTACAAAA TTAGAAGTCT GGACAATGGT GGCTATTACA TCTCTCCTCG CATCACTTTT 540
CCCTGCATCA GTGACATGAT TAAGCATTAC CAAAAGCAGT CTGATGGTCT ATGCAGAAGA 600
CTGGAGAAGG CATGCATCAG TCCCAAACCT CAGAAGCCAT GGGATAAAGA TGCCTGGGAG 660
ATCCCCCGGG AGTCCATTAA GTTGGTGAAA AAGCTTGGCG CAGGGCAGTT TGGGGAAGTC 720
TGGATGGGTT ACTATAACAA CAGCACAAAG GTGGCTGTGA AGACCCTCAA GCCCGGCACC 780
ATGTCTGTGC AGGCATTCCT GGAAGAGGCC AACCTCATGA AGACCTTGCA ACATGACAAG 840
CTAGTGCGGC TGTACGCTGT GGTCACCAAG GAGGAGCCCA TCTACATCAT CACCGAGTTC 900
ATGGCTAAGG GTAGTTTGCT GGATTTCCTC AAGAGTGATG AAGGTGGCAA GGTGCTGCTG 960
CCCAAGCTCA TTGACTTCTC GGCCCAGATT GCAGAAGGCA TGGCGTACAT CGAGCGGAAG 1020
AACTACATCC ACCGTGATCT GCGAGCTGCT AACGTCCTGG TCTCTGAGTC ACTCATGTGC 1080
AAGATTGCAG ACTTTGGCCT CGCGAGAGTC ATCGAAGATA ACGAGTACAC AGCAAGGGAA 1140
GGTGCGAAGT TCCCTATCAA GTGGACAGCT CCAGAGGCCA TCAACTTCGG CTGCTTCACT 1200
ATCAAATCTG ACGTGTGGTC CTTCGGAATT CTCCTGTATG AGATTGTCAC CTATGGGAAG 1260
ATTCCCTACC CAGGGAGAAC CAACGCAGAT GTGATGAGCG CACTGTCACA GGGATATCGA 1320
ATGCCACGCA TGGAGAACTG CCCAGATGAG CTCTATGACA TCATGAAAAT GTGTTGGAAA 1380
GAAAAGGCAG AGGAGAGGCC AACTTTTGAC TACTTACAGA GTGTCCTGGA TGACTTCTAT 1440
ACAGCCACAG AAGGGCAGTA TCAGCAGCAA CCGTAG 1476
Domain Profile
S: 1     lklvkklGeGqfGevwlgkwkgsvkvavktlkegtlspeafleeaqilkklrheklvkly  60
         +klvkklG+GqfGevw+g++++s+kvavktlk+gt+s +afleea+++k+l+h+klv+ly
Q: 226   IKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLY  285
         689*********************************************************
S: 61    avvseeePiyivtelmakGslldflkeeegkklklpklvdlaaqvaeGmayleeknlihr  120
         avv++eePiyi+te+makGslldflk++eg k+ lpkl+d++aq+aeGmay+e+kn+ihr
Q: 286   AVVTKEEPIYIITEFMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHR  345
         ************************************************************
S: 121   dlaarnvlvgeslvvkvadfGlarlieddeytakegaklPikWtaPeaiklgkftiksdv  180
         dl+a+nvlv+esl++k+adfGlar+ied+eyta+egak+PikWtaPeai++g+ftiksdv
Q: 346   DLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDV  405
         ************************************************************
S: 181   WsfGillteivtkGkvPypGmtneevleqvergyrlprpeecpeelyelllecwkkdpee  240
         WsfGill+eivt+Gk+PypG tn++v++++++gyr+pr+e+cp+ely+++++cwk+++ee
Q: 406   WSFGILLYEIVTYGKIPYPGRTNADVMSALSQGYRMPRMENCPDELYDIMKMCWKEKAEE  465
         ************************************************************
S: 241   rPtfetlqevl  251
         rPtf++lq+vl
Q: 466   RPTFDYLQSVL  476
         ********986
Domain Sequence
(FASTA)
IKLVKKLGAG QFGEVWMGYY NNSTKVAVKT LKPGTMSVQA FLEEANLMKT LQHDKLVRLY 60
AVVTKEEPIY IITEFMAKGS LLDFLKSDEG GKVLLPKLID FSAQIAEGMA YIERKNYIHR 120
DLRAANVLVS ESLMCKIADF GLARVIEDNE YTAREGAKFP IKWTAPEAIN FGCFTIKSDV 180
WSFGILLYEI VTYGKIPYPG RTNADVMSAL SQGYRMPRME NCPDELYDIM KMCWKEKAEE 240
RPTFDYLQSV L 251
Keyword3D-structure; Adaptive immunity; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Golgi apparatus; Immunity; Inflammatory response; Innate immunity; Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Danio rerio"; ?>Equus caballus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Monodelphis domestica"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Tarsius syrichta"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00342
EKS-ANC-00358
EKS-BOT-00368
EKS-CAJ-00372
EKS-CAF-00369
EKS-CAP-00401
EKS-DAR-00748
EKS-EQC-00359
EKS-GAM-00222
EKS-GAG-00312
EKS-GAA-00452
EKS-GOG-00359
EKS-HOS-00374
EKS-ICT-00348
EKS-LAC-00384
EKS-LOA-00377
EKS-MAM-00368
EKS-MOD-00359
EKS-MUP-00362
EKS-MYL-00366
EKS-NOL-00336
EKS-ORN-00477
EKS-ORA-00322
EKS-ORC-00346
EKS-ORL-00439
EKS-OTG-00372
EKS-PAT-00348
EKS-PES-00327
EKS-POA-00358
EKS-RAN-00382
EKS-SAH-00338
EKS-SUS-00327
EKS-TAG-00441
EKS-TAS-00040
EKS-TEN-00466
EKS-XET-00488
EKS-XIM-00465
Gene Ontology
GO:0034666; C:alpha2-beta1 integrin complex
GO:0005829; C:cytosol
GO:0005794; C:Golgi apparatus
GO:0045121; C:membrane raft
GO:0030061; C:mitochondrial crista
GO:0005758; C:mitochondrial intermembrane space
GO:0005634; C:nucleus
GO:0048471; C:perinuclear region of cytoplasm
GO:0005886; C:plasma membrane
GO:0014069; C:postsynaptic density
GO:0005524; F:ATP binding
GO:0005128; F:erythropoietin receptor binding
GO:0043208; F:glycosphingolipid binding
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity
GO:0004713; F:protein tyrosine kinase activity
GO:0001782; P:B cell homeostasis
GO:0050853; P:B cell receptor signaling pathway
GO:0034605; P:cellular response to heat
GO:0071300; P:cellular response to retinoic acid
GO:0050663; P:cytokine secretion
GO:0097028; P:dendritic cell differentiation
GO:0030218; P:erythrocyte differentiation
GO:0002774; P:Fc receptor mediated inhibitory signaling pathway
GO:0002431; P:Fc receptor mediated stimulatory signaling pathway
GO:0042541; P:hemoglobin biosynthetic process
GO:0002553; P:histamine secretion by mast cell
GO:0045087; P:innate immune response
GO:0035556; P:intracellular signal transduction
GO:0031663; P:lipopolysaccharide-mediated signaling pathway
GO:0030889; P:negative regulation of B cell proliferation
GO:0070373; P:negative regulation of ERK1 and ERK2 cascade
GO:0043407; P:negative regulation of MAP kinase activity
GO:0070667; P:negative regulation of mast cell proliferation
GO:0002762; P:negative regulation of myeloid leukocyte differentiation
GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway
GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway
GO:0031175; P:neuron projection development
GO:0014003; P:oligodendrocyte development
GO:0018108; P:peptidyl-tyrosine phosphorylation
GO:0002576; P:platelet degranulation
GO:0030335; P:positive regulation of cell migration
GO:0008284; P:positive regulation of cell proliferation
GO:2000670; P:positive regulation of dendritic cell apoptotic process
GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway
GO:0060252; P:positive regulation of glial cell proliferation
GO:0070668; P:positive regulation of mast cell proliferation
GO:0010976; P:positive regulation of neuron projection development
GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation
GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity
GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade
GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein
GO:0046777; P:protein autophosphorylation
GO:0002902; P:regulation of B cell apoptotic process
GO:0050855; P:regulation of B cell receptor signaling pathway
GO:0033628; P:regulation of cell adhesion mediated by integrin
GO:0050707; P:regulation of cytokine secretion
GO:0045646; P:regulation of erythrocyte differentiation
GO:0050727; P:regulation of inflammatory response
GO:0043304; P:regulation of mast cell degranulation
GO:0090025; P:regulation of monocyte chemotaxis
GO:0090330; P:regulation of platelet aggregation
GO:0051279; P:regulation of release of sequestered calcium ion into cytosol
GO:0043200; P:response to amino acid stimulus
GO:0048678; P:response to axon injury
GO:0009743; P:response to carbohydrate stimulus
GO:0006974; P:response to DNA damage stimulus
GO:0009725; P:response to hormone stimulus
GO:0032868; P:response to insulin stimulus
GO:0014070; P:response to organic cyclic compound
GO:0006991; P:response to sterol depletion
GO:0009636; P:response to toxin
GO:0002513; P:tolerance induction to self antigen
GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway
KEGG
mmu:17096;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
IPR000980; SH2.
IPR001452; SH3_domain.
IPR008266; Tyr_kinase_AS.
IPR020635; Tyr_kinase_cat_dom.
Pfam
PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
SMARTs
SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
Prosites
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
Prints
PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
Created Date20-Feb-2013