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Q07014 (LYN_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Lyn
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. 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.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.4

Enzyme regulation

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

Subunit structure

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.

Subcellular location

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.

Tissue specificity

Detected in spleen (at protein level). Expressed predominantly in B-lymphoid and myeloid cells. Ref.4

Domain

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

Post-translational modification

Ubiquitinated. Ubiquitination is SH3-dependent 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. Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

B cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

Fc receptor mediated inhibitory signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

Fc receptor mediated stimulatory signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic nuclear changes

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to extracellular stimulus

Inferred from expression pattern PubMed 17845203. Source: RGD

cellular response to heat

Inferred from expression pattern PubMed 12372808. Source: RGD

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cytokine secretion

Inferred from mutant phenotype PubMed 16177098. Source: RGD

dendritic cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

histamine secretion by mast cell

Inferred from mutant phenotype PubMed 16177098. Source: RGD

immune response-regulating cell surface receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mast cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myeloid leukocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of toll-like receptor 2 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of toll-like receptor 4 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte development

Inferred from expression pattern PubMed 15504915. Source: RGD

platelet degranulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from mutant phenotype PubMed 16177098. Source: RGD

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dendritic cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glial cell proliferation

Inferred from direct assay PubMed 15504915. Source: RGD

positive regulation of mast cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of oligodendrocyte progenitor proliferation

Inferred from mutant phenotype PubMed 15504915. Source: RGD

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphorylation

Inferred from mutant phenotype PubMed 16177098. Source: RGD

positive regulation of stress-activated protein kinase signaling cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of STAT protein

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

regulation of erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

regulation of mast cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mast cell degranulation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of monocyte chemotaxis

Inferred from electronic annotation. Source: Ensembl

regulation of platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 16177098. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 16529858. Source: RGD

response to axon injury

Inferred from expression pattern PubMed 17918263. Source: RGD

response to carbohydrate

Inferred from expression pattern PubMed 10330413. Source: RGD

response to drug

Inferred from expression pattern PubMed 17039281. Source: RGD

response to hormone

Inferred from sequence or structural similarity. Source: UniProtKB

response to insulin

Inferred from expression pattern PubMed 12089355. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 15287886PubMed 17265464. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 16713446. Source: RGD

response to sterol depletion

Inferred from expression pattern PubMed 10330413. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 16529858. Source: RGD

tolerance induction to self antigen

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

alpha2-beta1 integrin complex

Inferred from direct assay PubMed 18234883. Source: RGD

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

mast cell granule

Inferred from mutant phenotype PubMed 16177098. Source: GOC

membrane

Inferred from direct assay PubMed 16177098. Source: RGD

membrane raft

Inferred from direct assay PubMed 18326662. Source: RGD

mitochondrial crista

Inferred from direct assay PubMed 12007793. Source: RGD

mitochondrial intermembrane space

Inferred from direct assay PubMed 12007793. Source: RGD

mitochondrial membrane

Inferred from direct assay PubMed 12007793. Source: RGD

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 18579528. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 14529711. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction PubMed 14529711PubMed 18579528PubMed 8190127PubMed 8757630PubMed 9692543. Source: RGD

glycosphingolipid binding

Inferred from physical interaction PubMed 8106508. Source: RGD

integrin binding

Inferred from direct assay PubMed 15504915. Source: RGD

kinase activity

Traceable author statement PubMed 12007793. Source: RGD

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoprotein binding

Inferred from physical interaction PubMed 8910399. Source: RGD

platelet-derived growth factor receptor binding

Inferred from physical interaction PubMed 15504915. Source: RGD

protein binding

Inferred from physical interaction PubMed 18579528. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 17579026PubMed 18234883. Source: RGD

protein tyrosine kinase activity

Inferred from direct assay PubMed 12007793. Source: RGD

receptor binding

Inferred from physical interaction PubMed 11591756PubMed 11714805PubMed 16177098PubMed 8870703. Source: RGD

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 14531861. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform LYN A (identifier: Q07014-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform LYN B (identifier: Q07014-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 512511Tyrosine-protein kinase Lyn
PRO_0000088131

Regions

Domain63 – 12361SH3
Domain129 – 22698SH2
Domain247 – 501255Protein kinase
Nucleotide binding253 – 2619ATP By similarity

Sites

Active site3671Proton acceptor By similarity
Binding site2751ATP By similarity

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue301Phosphothreonine By similarity
Modified residue321Phosphotyrosine By similarity
Modified residue371Phosphothreonine By similarity
Modified residue1931Phosphotyrosine By similarity
Modified residue1941Phosphotyrosine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2651Phosphotyrosine By similarity
Modified residue3061Phosphotyrosine By similarity
Modified residue3161Phosphotyrosine By similarity
Modified residue3971Phosphotyrosine; by autocatalysis Ref.4
Modified residue4601Phosphotyrosine By similarity
Modified residue4731Phosphotyrosine By similarity
Modified residue4891Phosphothreonine By similarity
Modified residue5021Phosphothreonine By similarity
Modified residue5081Phosphotyrosine; by autocatalysis, CSK and MATK Ref.4
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence25 – 4521Missing in isoform LYN B.
VSP_005004

Experimental info

Sequence conflict2311P → L in AAA20944. Ref.2
Sequence conflict2311P → L in AAA20945. Ref.2
Sequence conflict3081V → A in AAA20944. Ref.2
Sequence conflict3081V → A in AAA20945. Ref.2
Sequence conflict4191C → Y in AAA20944. Ref.2
Sequence conflict4191C → Y in AAA20945. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform LYN A [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E03615E229CD43F1

FASTA51258,660
        10         20         30         40         50         60 
MGCIKSKRKD NLNDDGVDMK TQPVRNTDRT IYVRDPTSNK QQRPVPESQL LPGQRFQAKD 

        70         80         90        100        110        120 
PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLSSKRE GFIPSNYVAK 

       130        140        150        160        170        180 
VNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DYDPMHGDVI 

       190        200        210        220        230        240 
KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW 

       250        260        270        280        290        300 
EIPRESIKLV KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSAQAFLEE ANLMKTLQHD 

       310        320        330        340        350        360 
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGSKVL LPKLIDFSAQ IAEGMAYIER 

       370        380        390        400        410        420 
KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF 

       430        440        450        460        470        480 
TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMTALSQGY RMPRMENCPD ELYDIMKMCW 

       490        500        510 
KESAEERPTF DYLQSVLDDF YTATEGQYQQ QP 

« Hide

Isoform LYN B [UniParc].

Checksum: 6FFFB1609E015180
Show »

FASTA49156,133

References

[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(1993)
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(1994) [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(1997) [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(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI56160.
PT0198.
RefSeqNP_001104568.1. NM_001111098.1. [Q07014-2]
NP_110484.1. NM_030857.2. [Q07014-1]
XP_006237896.1. XM_006237834.1. [Q07014-1]
UniGeneRn.4338.

3D structure databases

ProteinModelPortalQ07014.
SMRQ07014. Positions 67-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249512. 7 interactions.
IntActQ07014. 3 interactions.
MINTMINT-4564766.
STRING10116.ENSRNOP00000011130.

Chemistry

BindingDBQ07014.
ChEMBLCHEMBL4363.

PTM databases

PhosphoSiteQ07014.

Proteomic databases

PaxDbQ07014.
PRIDEQ07014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000011130; ENSRNOP00000011130; ENSRNOG00000008180. [Q07014-1]
GeneID81515.
KEGGrno:81515.
UCSCRGD:621017. rat. [Q07014-1]

Organism-specific databases

CTD4067.
RGD621017. Lyn.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087866.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ07014.
KOK05854.
OMAWWRAKSL.
OrthoDBEOG7GTT2V.
PhylomeDBQ07014.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.
ReactomeREACT_227097. Immune System.

Gene expression databases

GenevestigatorQ07014.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

NextBio615007.
PROQ07014.

Entry information

Entry nameLYN_RAT
AccessionPrimary (citable) accession number: Q07014
Secondary accession number(s): Q63320
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families