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Tyrosine-protein kinase SYK (EC 2.7.10.2) (Spleen tyrosine kinase) (p72Syk)

 KSYK_RAT                Reviewed;         629 AA.
Q64725;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 167.
RecName: Full=Tyrosine-protein kinase SYK;
EC=2.7.10.2;
AltName: Full=Spleen tyrosine kinase;
AltName: Full=p72Syk;
Name=Syk;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORMS SYKA
AND SYKB).
PubMed=7759516; DOI=10.1074/jbc.270.21.12659;
Rowley R.B., Bolen J.B., Fargnoli J.;
"Molecular cloning of rodent p72Syk. Evidence of alternative mRNA
splicing.";
J. Biol. Chem. 270:12659-12664(1995).
[2]
FUNCTION IN PHOSPHORYLATION OF HCLS1.
PubMed=8611520; DOI=10.1021/bi9528614;
Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.;
"SH2 domains mediate the sequential phosphorylation of HS1 protein by
p72syk and Src-related protein tyrosine kinases.";
Biochemistry 35:5327-5332(1996).
[3]
PHOSPHORYLATION AT TYR-317 BY LYN, AND PHOSPHORYLATION AT TYR-342 AND
TYR-346.
PubMed=12077122; DOI=10.1074/jbc.M201362200;
Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.;
"Regulation of signaling in B cells through the phosphorylation of Syk
on linker region tyrosines. A mechanism for negative signaling by the
Lyn tyrosine kinase.";
J. Biol. Chem. 277:31703-31714(2002).
-!- FUNCTION: Non-receptor tyrosine kinase which mediates signal
transduction downstream of a variety of transmembrane receptors
including classical immunoreceptors like the B-cell receptor
(BCR). Regulates several biological processes including innate and
adaptive immunity, cell adhesion, osteoclast maturation, platelet
activation and vascular development. Assembles into signaling
complexes with activated receptors at the plasma membrane via
interaction between its SH2 domains and the receptor tyrosine-
phosphorylated ITAM domains. The association with the receptor can
also be indirect and mediated by adapter proteins containing ITAM
or partial hemITAM domains. The phosphorylation of the ITAM
domains is generally mediated by SRC subfamily kinases upon
engagement of the receptor. More rarely signal transduction via
SYK could be ITAM-independent. Direct downstream effectors
phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and
BLNK. Initially identified as essential in B-cell receptor (BCR)
signaling, it is necessary for the maturation of B-cells most
probably at the pro-B to pre-B transition. Activated upon BCR
engagement, it phosphorylates and activates BLNK an adapter
linking the activated BCR to downstream signaling adapters and
effectors. It also phosphorylates and activates PLCG1 and the PKC
signaling pathway. It also phosphorylates BTK and regulates its
activity in B-cell antigen receptor (BCR)-coupled signaling. In
addition to its function downstream of BCR plays also a role in T-
cell receptor signaling. Plays also a crucial role in the innate
immune response to fungal, bacterial and viral pathogens. It is
for instance activated by the membrane lectin CLEC7A. Upon
stimulation by fungal proteins, CLEC7A together with SYK activates
immune cells inducing the production of ROS. Also activates the
inflammasome and NF-kappa-B-mediated transcription of chemokines
and cytokines in presence of pathogens. Regulates neutrophil
degranulation and phagocytosis through activation of the MAPK
signaling cascade. Also mediates the activation of dendritic cells
by cell necrosis stimuli. Also involved in mast cells activation.
Involved in interleukin-3/IL3-mediated signaling pathway in
basophils (By similarity). Also functions downstream of receptors
mediating cell adhesion. Relays for instance, integrin-mediated
neutrophils and macrophages activation and P-selectin
receptor/SELPG-mediated recruitment of leukocytes to inflammatory
loci. Plays also a role in non-immune processes. It is for
instance involved in vascular development where it may regulate
blood and lymphatic vascular separation. It is also required for
osteoclast development and function. Functions in the activation
of platelets by collagen, mediating PLCG2 phosphorylation and
activation. May be coupled to the collagen receptor by the ITAM
domain-containing FCER1G. Also activated by the membrane lectin
CLEC1B that is required for activation of platelets by
PDPN/podoplanin. Involved in platelet adhesion being activated by
ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances
production of the cytokine CXCL8/IL-8 via the NFKB pathway and may
thus have a role in the intestinal immune response (By
similarity). {ECO:0000250|UniProtKB:P48025,
ECO:0000269|PubMed:8611520}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ACTIVITY REGULATION: Autoinhibited. Intramolecular binding of the
interdomains A and B (also called linker region) to parts of the
catalytic domain keep the catalytic center in an inactive
conformation. The phosphorylation of the interdomains or the
binding of the SH2 domains with dually phosphorylated ITAM domains
on transmembrane proteins disrupt those intramolecular
interactions allowing the kinase domain to adopt an active
conformation. The phosphorylation of SYK and of the ITAM domains
which is responsible for SYK activation is essentially mediated by
SRC subfamily kinases, like LYN, upon transmembrane receptors
engagement. May also be negatively regulated by PTPN6 through
dephosphorylation. Downstream signaling adapters and intermediates
like BLNK or RHOH may mediate positive and/or negative feedback
regulation. Negatively regulated by CBL and CBLB through
ubiquitination and probable degradation (By similarity).
Phosphorylates SH3BP2 which in turn may regulate SYK through LYN
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with LYN; phosphorylates SYK. Interacts with
RHOH (phosphorylated); regulates mast cells activation. Interacts
with NFAM1 (phosphorylated); probably involved in BCR signaling.
Interacts with VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR
activation. Interacts with GAB2 (phosphorylated); probably
involved in IgE Fc receptor signaling. Interacts (via its SH2
domains) with CD79A (via its phosphorylated ITAM domain); the
interaction stimulates SYK autophosphorylation and activation.
Interacts (via SH2 domains) with FCER1G (via ITAM domain);
activates SYK and mediates neutrophils and macrophages integrin-
mediated activation. Interaction with FCER1G in basophils triggers
IL3-induced IL4 production (By similarity). Interacts with ITGB2
and FGR; involved in ITGB2 downstream signaling. Interacts with
ITGB3; upon activation by ITGB3 promotes platelet adhesion.
Interacts (via SH2 domains) with TYROBP (via ITAM domain);
involved in neutrophils and macrophages integrin-mediated
activation. Interacts with MSN and SELPLG; mediates the selectin-
dependent activation of SYK by SELPLG. Interacts with BLNK (via
SH2 domain). Interacts (via the second SH2 domain) with USP25 (via
C-terminus); phosphorylates USP25 and regulates USP25
intracellular levels. Interacts (via SH2 domains) with CLEC1B
(dimer). Interacts with CLEC7A; participates in leukocyte
activation in presence of fungal pathogens. Interacts
(phosphorylated) with SLA; may regulate SYK through CBL
recruitment. Interacts with YWHAG; attenuates BCR-induced membrane
translocation and activation of SYK (By similarity). Interacts
(via SH2 domains) with GCSAM; the interaction increases after B-
cell receptor stimulation, resulting in enhanced SYK
autophosphorylation and activity (By similarity). Interacts with
TNS2; leading to the phosphorylation of SYK (By similarity).
Interacts with FLNA (via filamin repeat 5); docks SYK to the
plasma membrane (By similarity). Interacts with CEACAM1;
lipopolysaccharide activated neutrophils induce phosphorylation of
SYK resulting in the formation of a complex including TLR4,
phosphorylated form of SYK and CEACAM1, which in turn, recruits
PTPN6 that dephosphorylates SYK, reducing the production of
reactive oxygen species (ROS) and lysosome disruption, leading to
a reduction of the inflammasome activity (By similarity).
Interacts (via SH2 domains) with CEACAM20 (phosphorylated form);
the interaction further enhances CEACAM20 phosphorylation (By
similarity). {ECO:0000250|UniProtKB:P43405,
ECO:0000250|UniProtKB:P48025}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}. Cytoplasm,
cytosol {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=SykB;
IsoId=Q64725-1; Sequence=Displayed;
Name=SykA;
IsoId=Q64725-2; Sequence=VSP_005011;
-!- DOMAIN: The SH2 domains mediate the interaction of SYK with the
phosphorylated ITAM domains of transmembrane proteins. Some
proteins like CLEC1B have a partial ITAM domain (also called
hemITAM) containing a single YxxL motif. The interaction with SYK
requires CLEC1B homodimerization (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated. Phosphorylated on tyrosine residues by
LYN following receptors engagement. Phosphorylation on Tyr-317
creates a binding site for CBL, an adapter protein that serves as
a negative regulator of BCR-stimulated calcium ion signaling (By
similarity). Phosphorylation at Tyr-342 creates a binding site for
VAV1 (By similarity). Phosphorylation on Tyr-342 and Tyr-346
enhances the phosphorylation and activation of phospholipase C-
gamma and the early phase of calcium ion mobilization via a
phosphoinositide 3-kinase-independent pathway (By similarity).
Phosphorylation on Ser-291 is very common, it peaks 5 minutes
after BCR stimulation, and creates a binding site for YWHAG (By
similarity). Phosphorylation at Tyr-624 creates a binding site for
BLNK (By similarity). Dephosphorylated by PTPN6 (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated by CBLB after BCR activation; which promotes
proteasomal degradation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SYK/ZAP-70 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U21684; AAA75167.1; -; mRNA.
EMBL; U21683; AAA75166.1; -; mRNA.
RefSeq; NP_036890.1; NM_012758.1. [Q64725-1]
UniGene; Rn.87407; -.
ProteinModelPortal; Q64725; -.
SMR; Q64725; -.
BioGrid; 247220; 2.
IntAct; Q64725; 1.
STRING; 10116.ENSRNOP00000016942; -.
BindingDB; Q64725; -.
ChEMBL; CHEMBL4364; -.
iPTMnet; Q64725; -.
PhosphoSitePlus; Q64725; -.
PaxDb; Q64725; -.
PRIDE; Q64725; -.
GeneID; 25155; -.
KEGG; rno:25155; -.
CTD; 6850; -.
RGD; 3796; Syk.
eggNOG; ENOG410IH0T; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000113264; -.
HOVERGEN; HBG001540; -.
InParanoid; Q64725; -.
KO; K05855; -.
PhylomeDB; Q64725; -.
BRENDA; 2.7.10.2; 5301.
PRO; PR:Q64725; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0071226; P:cellular response to molecule of fungal origin; ISS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0038156; P:interleukin-3-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0002366; P:leukocyte activation involved in immune response; ISS:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISS:UniProtKB.
GO; GO:0001945; P:lymph vessel development; ISS:UniProtKB.
GO; GO:0002281; P:macrophage activation involved in immune response; ISS:UniProtKB.
GO; GO:0002283; P:neutrophil activation involved in immune response; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IBA:GO_Central.
GO; GO:0045579; P:positive regulation of B cell differentiation; IBA:GO_Central.
GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0090237; P:regulation of arachidonic acid secretion; ISS:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; IDA:RGD.
GO; GO:0043313; P:regulation of neutrophil degranulation; ISS:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB.
GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0032928; P:regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0002554; P:serotonin secretion by platelet; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd09938; SH2_N-SH2_Zap70_Syk_like; 1.
Gene3D; 1.10.930.10; -; 1.
Gene3D; 3.30.505.10; -; 2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR035838; SYK/ZAP-70_N_SH2.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 2.
PIRSF; PIRSF000604; TyrPK_SYK; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF55550; SSF55550; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 2.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Angiogenesis; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Immunity;
Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; SH2 domain; Transferase;
Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 629 Tyrosine-protein kinase SYK.
/FTId=PRO_0000088167.
DOMAIN 14 106 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 167 258 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 365 625 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 371 379 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 107 166 Interdomain A. {ECO:0000250}.
REGION 259 364 Interdomain B. {ECO:0000250}.
ACT_SITE 488 488 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 396 396 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 27 27 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 46 46 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 130 130 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 255 255 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000250|UniProtKB:P48025}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 290 290 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 311 311 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 313 313 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 317 317 Phosphotyrosine; by LYN.
{ECO:0000269|PubMed:12077122}.
MOD_RES 339 339 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 342 342 Phosphotyrosine.
{ECO:0000269|PubMed:12077122}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 346 346 Phosphotyrosine.
{ECO:0000269|PubMed:12077122}.
MOD_RES 358 358 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 378 378 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 478 478 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 501 501 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 519 519 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 520 520 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 524 524 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 540 540 Phosphotyrosine.
{ECO:0000250|UniProtKB:P48025}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 576 576 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 623 623 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 624 624 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 625 625 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
VAR_SEQ 277 299 Missing (in isoform SykA). {ECO:0000305}.
/FTId=VSP_005011.
SEQUENCE 629 AA; 71529 MW; 81169A643EC6A6FE CRC64;
MAGNAVDNAN HLTYFFGNIT REEAEDYLVQ GGMTDGLYLL RQSRNYLGGF ALSVAHNRKA
HHYTIERELN GTYAISGGRA HASPADLCHY HSQEPEGLVC LLKKPFNRPP GVQPKTGPFE
DLKENLIREY VKQTWNLQGQ ALEQAIISQK PQLEKLIATT AHEKMPWFHG NISRDESEQT
VLIGSKTNGK FLIRARDNNG SFALCLLHEG KVLHYRIDRD KTGKLSIPEG KKFDTLWQLV
EHYSYKPDGL LRVLTVPCQK IGVQMGHPGS SNAHPVTWSP GGIISRIKSY SFPKPGHKKP
PPPQGSRPES TVSFNPYEPT GGAWGPDRGL QREALPMDTE VYESPYADPE EIRPKEVYLD
RKLLTLEDNE LGSGNFGTVK KGYYQMKKVV KTVAVKILKN EANDPALKDE LLAEANVMQQ
LDNPYIVRMI GICEAESWML VMEMAAWGPL NKYLQQNRHI KDKNIIELVH QVSMGMKYLE
ESNFVHRDLA ARNVLLVTQH YAKISDFGLS KALRADENYY KAQTHGKWPV KWYAPECINY
FKFSSKSDVW SFGVLMWEAF SYGQKPYRGM KGSEVTAMLE KGERMGCPPG CPREMYDLMF
LCWTYDVENR PGFAAVELRL RNYYYDVVN


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EIAAB13100 EK6,ELK,ELK,EPH tyrosine kinase 2,EPHB1,EPH-like kinase 6,Ephrin type-B receptor 1,EPHT2,hEK6,HEK6,Homo sapiens,Human,NET,NET,Neuronally-expressed EPH-related tyrosine kinase,Tyrosine-protein kinase r
U2227h CLIA kit BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38 96T


 

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