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Protein

Tyrosine-protein kinase Lyn

Gene

LYN

Organism
Homo sapiens (Human)
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. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation.20 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.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 SU6656.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei275ATPPROSITE-ProRule annotation1
Active sitei367Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi253 – 261ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • glycosphingolipid binding Source: Ensembl
  • ion channel binding Source: BHF-UCL
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • protein tyrosine kinase activity Source: UniProtKB
  • receptor binding Source: GO_Central
  • receptor signaling protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07443-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-2029481. FCGR activation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2682334. EPH-Ephrin signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-389356. CD28 co-stimulation.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-5621480. Dectin-2 family.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-75892. Platelet Adhesion to exposed collagen.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-982772. Growth hormone receptor signaling.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP07948.
SIGNORiP07948.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Lyn (EC:2.7.10.2)
Alternative name(s):
Lck/Yes-related novel protein tyrosine kinase
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene namesi
Name:LYN
Synonyms:JTK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:6735. LYN.

Subcellular locationi

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

  • Note: Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts.

GO - Cellular componenti

  • cell-cell adherens junction Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • Golgi apparatus Source: UniProtKB
  • integrin alpha2-beta1 complex Source: Ensembl
  • mast cell granule Source: GOC
  • membrane raft Source: UniProtKB
  • mitochondrial crista Source: Ensembl
  • mitochondrial intermembrane space Source: Ensembl
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Loss of localization to the cell membrane; when associated with A-3. 1 Publication1
Mutagenesisi3C → A: Loss of localization to the cell membrane; when associated with A-2. 1 Publication1
Mutagenesisi275K → A: Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus; when associated with A-2 and A-3. 4 Publications1
Mutagenesisi275K → L or R: Loss of kinase activity. 4 Publications1
Mutagenesisi346D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499. 1 Publication1
Mutagenesisi353E → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499. 1 Publication1
Mutagenesisi397Y → F: Strongly reduced kinase activity. 1 Publication1
Mutagenesisi498D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499. 1 Publication1
Mutagenesisi499D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498. 1 Publication1
Mutagenesisi508Y → F: Abolishes autoinhibition and thereby increases kinase activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi4067.
OpenTargetsiENSG00000254087.
PharmGKBiPA30498.

Chemistry databases

ChEMBLiCHEMBL3905.
DrugBankiDB06616. Bosutinib.
DB09079. Nintedanib.
DB08901. Ponatinib.
GuidetoPHARMACOLOGYi2060.

Polymorphism and mutation databases

BioMutaiLYN.
DMDMi125480.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000881292 – 512Tyrosine-protein kinase LynAdd BLAST511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1 Publication1
Lipidationi3S-palmitoyl cysteineCurated1
Modified residuei11PhosphoserineCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei193Phosphotyrosine1 Publication1
Modified residuei228PhosphoserineCombined sources1
Modified residuei306PhosphotyrosineCombined sources1
Modified residuei316PhosphotyrosineCombined sources1
Modified residuei397Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei460Phosphotyrosine1 Publication1
Modified residuei473PhosphotyrosineCombined sources1
Modified residuei508Phosphotyrosine; by autocatalysis, CSK and MATKCombined sources3 Publications1

Post-translational modificationi

Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent.2 Publications
Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.7 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP07948.
MaxQBiP07948.
PaxDbiP07948.
PeptideAtlasiP07948.
PRIDEiP07948.

2D gel databases

REPRODUCTION-2DPAGEP07948.

PTM databases

iPTMnetiP07948.
PhosphoSitePlusiP07948.
SwissPalmiP07948.

Miscellaneous databases

PMAP-CutDBP07948.

Expressioni

Tissue specificityi

Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors.2 Publications

Gene expression databases

BgeeiENSG00000254087.
CleanExiHS_LYN.
ExpressionAtlasiP07948. baseline and differential.
GenevisibleiP07948. HS.

Organism-specific databases

HPAiCAB004492.
HPA001231.

Interactioni

Subunit structurei

Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts with Epstein-Barr virus LMP2A. Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip). Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation. Interacts with CD36. Interacts with LYN (By similarity).By similarity29 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
O929722EBI-79452,EBI-710506From a different organism.
P225753EBI-79452,EBI-866709From a different organism.
P279584EBI-79452,EBI-706378From a different organism.
Q9WMX23EBI-79452,EBI-710918From a different organism.
ARP102755EBI-79452,EBI-608057
Arap3Q8R5G72EBI-79452,EBI-621463From a different organism.
CD22P202732EBI-79452,EBI-78277
CD24P250636EBI-79452,EBI-6267018
CD37P110495EBI-79452,EBI-6139068
CDKN1BP465272EBI-79452,EBI-519280
EGFRP005336EBI-79452,EBI-297353
GAB1Q134807EBI-79452,EBI-517684
GP6Q9HCN62EBI-79452,EBI-515278
ITGB1P055564EBI-79452,EBI-703066
KITP107217EBI-79452,EBI-1379503
MCM7P339935EBI-6895930,EBI-355924
METP085812EBI-79452,EBI-1039152
PAG1Q9NWQ816EBI-79452,EBI-2828115
RACK1P632442EBI-79452,EBI-296739
SRCP129312EBI-79452,EBI-621482

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • ion channel binding Source: BHF-UCL
  • receptor binding Source: GO_Central

Protein-protein interaction databases

BioGridi110245. 191 interactors.
DIPiDIP-1056N.
IntActiP07948. 70 interactors.
MINTiMINT-200655.
STRINGi9606.ENSP00000428924.

Chemistry databases

BindingDBiP07948.

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi66 – 72Combined sources7
Beta strandi78 – 80Combined sources3
Beta strandi89 – 95Combined sources7
Beta strandi97 – 104Combined sources8
Turni105 – 107Combined sources3
Beta strandi110 – 114Combined sources5
Turni115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi259 – 262Combined sources4
Beta strandi265 – 269Combined sources5
Beta strandi273 – 275Combined sources3
Beta strandi284 – 286Combined sources3
Turni287 – 289Combined sources3
Helixi290 – 293Combined sources4
Turni294 – 297Combined sources4
Beta strandi306 – 309Combined sources4
Beta strandi311 – 314Combined sources4
Beta strandi316 – 319Combined sources4
Helixi327 – 330Combined sources4
Helixi334 – 338Combined sources5
Helixi341 – 360Combined sources20
Beta strandi372 – 375Combined sources4
Beta strandi381 – 383Combined sources3
Helixi407 – 409Combined sources3
Helixi412 – 416Combined sources5
Helixi422 – 437Combined sources16
Turni449 – 451Combined sources3
Helixi452 – 457Combined sources6
Beta strandi466 – 468Combined sources3
Helixi470 – 477Combined sources8
Turni478 – 480Combined sources3
Turni484 – 486Combined sources3
Helixi490 – 502Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
ProteinModelPortaliP07948.
SMRiP07948.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07948.

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.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP07948.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG091G0D46.
PhylomeDBiP07948.
TreeFamiTF351634.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: P07948-1) [UniParc]FASTAAdd to basket
Also known as: LYN A, p56lyn

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

« Hide

        10         20         30         40         50
MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL
60 70 80 90 100
LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLLTKKE GFIPSNYVAK LNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DFDPVHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQADGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KRLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT REEPIYIITE YMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ
360 370 380 390 400
IAEGMAYIER KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR
410 420 430 440 450
EGAKFPIKWT APEAINFGCF TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA
460 470 480 490 500
DVMTALSQGY RMPRVENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,574
Last modified:January 23, 2007 - v3
Checksum:i408D3D461204E378
GO
Isoform 2 (identifier: P07948-2) [UniParc]FASTAAdd to basket
Also known as: LYN B, p53lyn

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

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041737385D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00500223 – 43Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16038 mRNA. Translation: AAA59540.1.
M79321 mRNA. Translation: AAB50019.1.
BC075001 mRNA. Translation: AAH75001.1.
BC075002 mRNA. Translation: AAH75002.1.
BC126456 mRNA. Translation: AAI26457.1.
BC126458 mRNA. Translation: AAI26459.1.
CCDSiCCDS47859.1. [P07948-2]
CCDS6162.1. [P07948-1]
PIRiA26719. TVHULY.
RefSeqiNP_001104567.1. NM_001111097.2. [P07948-2]
NP_002341.1. NM_002350.3. [P07948-1]
XP_016868905.1. XM_017013416.1. [P07948-2]
UniGeneiHs.491767.
Hs.545418.

Genome annotation databases

EnsembliENST00000519728; ENSP00000428924; ENSG00000254087. [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087. [P07948-2]
GeneIDi4067.
KEGGihsa:4067.
UCSCiuc003xsk.5. human. [P07948-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16038 mRNA. Translation: AAA59540.1.
M79321 mRNA. Translation: AAB50019.1.
BC075001 mRNA. Translation: AAH75001.1.
BC075002 mRNA. Translation: AAH75002.1.
BC126456 mRNA. Translation: AAI26457.1.
BC126458 mRNA. Translation: AAI26459.1.
CCDSiCCDS47859.1. [P07948-2]
CCDS6162.1. [P07948-1]
PIRiA26719. TVHULY.
RefSeqiNP_001104567.1. NM_001111097.2. [P07948-2]
NP_002341.1. NM_002350.3. [P07948-1]
XP_016868905.1. XM_017013416.1. [P07948-2]
UniGeneiHs.491767.
Hs.545418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
ProteinModelPortaliP07948.
SMRiP07948.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110245. 191 interactors.
DIPiDIP-1056N.
IntActiP07948. 70 interactors.
MINTiMINT-200655.
STRINGi9606.ENSP00000428924.

Chemistry databases

BindingDBiP07948.
ChEMBLiCHEMBL3905.
DrugBankiDB06616. Bosutinib.
DB09079. Nintedanib.
DB08901. Ponatinib.
GuidetoPHARMACOLOGYi2060.

PTM databases

iPTMnetiP07948.
PhosphoSitePlusiP07948.
SwissPalmiP07948.

Polymorphism and mutation databases

BioMutaiLYN.
DMDMi125480.

2D gel databases

REPRODUCTION-2DPAGEP07948.

Proteomic databases

EPDiP07948.
MaxQBiP07948.
PaxDbiP07948.
PeptideAtlasiP07948.
PRIDEiP07948.

Protocols and materials databases

DNASUi4067.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000519728; ENSP00000428924; ENSG00000254087. [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087. [P07948-2]
GeneIDi4067.
KEGGihsa:4067.
UCSCiuc003xsk.5. human. [P07948-1]

Organism-specific databases

CTDi4067.
DisGeNETi4067.
GeneCardsiLYN.
HGNCiHGNC:6735. LYN.
HPAiCAB004492.
HPA001231.
MIMi165120. gene.
neXtProtiNX_P07948.
OpenTargetsiENSG00000254087.
PharmGKBiPA30498.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP07948.
KOiK05854.
OMAiWWRAKSL.
OrthoDBiEOG091G0D46.
PhylomeDBiP07948.
TreeFamiTF351634.

Enzyme and pathway databases

BioCyciZFISH:HS07443-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-2029481. FCGR activation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2682334. EPH-Ephrin signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-389356. CD28 co-stimulation.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-5621480. Dectin-2 family.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-75892. Platelet Adhesion to exposed collagen.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-982772. Growth hormone receptor signaling.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP07948.
SIGNORiP07948.

Miscellaneous databases

ChiTaRSiLYN. human.
EvolutionaryTraceiP07948.
GeneWikiiLYN.
GenomeRNAii4067.
PMAP-CutDBP07948.
PROiP07948.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000254087.
CleanExiHS_LYN.
ExpressionAtlasiP07948. baseline and differential.
GenevisibleiP07948. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P07948
Secondary accession number(s): A0AVQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 210 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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.