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Tyrosine-protein kinase SYK (EC 2.7.10.2) (Spleen tyrosine kinase) [Cleaved into: 72 kDa tyrosine-protein kinase SYK; 40 kDa tyrosine-protein kinase SYK]

 KSYK_PIG                Reviewed;         628 AA.
Q00655;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
18-JUL-2018, entry version 148.
RecName: Full=Tyrosine-protein kinase SYK;
EC=2.7.10.2;
AltName: Full=Spleen tyrosine kinase;
Contains:
RecName: Full=72 kDa tyrosine-protein kinase SYK;
Contains:
RecName: Full=40 kDa tyrosine-protein kinase SYK;
Name=SYK;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 313-333; 346-354
AND 369-379.
TISSUE=Spleen;
PubMed=1874735;
Taniguchi T., Kobayashi T., Kondo J., Takahashi K., Nakamura H.,
Suzuki J., Nagai K., Yamada T., Nakamura S., Yamamura H.;
"Molecular cloning of a porcine gene syk that encodes a 72-kDa
protein-tyrosine kinase showing high susceptibility to proteolysis.";
J. Biol. Chem. 266:15790-15796(1991).
[2]
PHOSPHORYLATION BY LYN, INTERACTION WITH LYN, AND AUTOPHOSPHORYLATION.
PubMed=7513017; DOI=10.1084/jem.179.5.1725;
Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T.,
Yamamoto T., Yamamura H.;
"Syk activation by the Src-family tyrosine kinase in the B cell
receptor signaling.";
J. Exp. Med. 179:1725-1729(1994).
[3]
FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH VAV1,
MUTAGENESIS OF TYR-341 AND TYR-345, AND PHOSPHORYLATION AT TYR-341.
PubMed=8986718; DOI=10.1016/S1074-7613(00)80273-3;
Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.;
"Functional and physical interactions of Syk family kinases with the
Vav proto-oncogene product.";
Immunity 5:591-604(1996).
[4]
FUNCTION IN PHOSPHORYLATION OF BTK.
PubMed=11226282; DOI=10.1073/pnas.051626198;
Baba Y., Hashimoto S., Matsushita M., Watanabe D., Kishimoto T.,
Kurosaki T., Tsukada S.;
"BLNK mediates Syk-dependent Btk activation.";
Proc. Natl. Acad. Sci. U.S.A. 98:2582-2586(2001).
[5]
FUNCTION IN PHOSPHORYLATION OF SH3BP2, MUTAGENESIS OF LYS-395, AND
ENZYME REGULATION.
PubMed=12709437; DOI=10.1074/jbc.M301201200;
Maeno K., Sada K., Kyo S., Miah S.M., Kawauchi-Kamata K., Qu X.,
Shi Y., Yamamura H.;
"Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3
domains of Lyn protein-tyrosine kinase.";
J. Biol. Chem. 278:24912-24920(2003).
[6]
ENZYME REGULATION.
PubMed=17936247; DOI=10.1016/j.bbrc.2007.09.100;
Adachi T., Wienands J., Tsubata T., Kurosaki T.;
"Interdomain A is crucial for ITAM-dependent and -independent
regulation of Syk.";
Biochem. Biophys. Res. Commun. 364:111-117(2007).
-!- 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:11226282, ECO:0000269|PubMed:12709437,
ECO:0000269|PubMed:8986718}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME 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 (By similarity). May also be negatively regulated by
PTPN6 through dephosphorylation (By similarity). Downstream
signaling adapters and intermediates like BLNK or RHOH may mediate
positive and/or negative feedback regulation (By similarity).
Negatively regulated by CBL and CBLB through ubiquitination and
probable degradation (By similarity). Phosphorylates SH3BP2 which
in turn may regulate SYK through LYN. {ECO:0000250,
ECO:0000269|PubMed:12709437, ECO:0000269|PubMed:17936247}.
-!- SUBUNIT: Interacts with LYN; phosphorylates SYK. Interacts with
RHOH (phosphorylated); regulates mast cells activation (By
similarity). Interacts with NFAM1 (phosphorylated); probably
involved in BCR signaling (By similarity). Interacts with VAV1
(via SH2 domain); phosphorylates VAV1 upon BCR activation.
Interacts with GAB2 (phosphorylated); probably involved in IgE Fc
receptor signaling (By similarity). Interacts (via its SH2
domains) with CD79A (via its phosphorylated ITAM domain); the
interaction stimulates SYK autophosphorylation and activation (By
similarity). Interacts (via SH2 domains) with FCER1G (via ITAM
domain); activates SYK and mediates neutrophils and macrophages
integrin-mediated activation (By similarity). Interaction with
FCER1G in basophils triggers IL3-induced IL4 production (By
similarity). Interacts with ITGB2 and FGR; involved in ITGB2
downstream signaling (By similarity). Interacts with ITGB3; upon
activation by ITGB3 promotes platelet adhesion (By similarity).
Interacts (via SH2 domains) with TYROBP (via ITAM domain);
involved in neutrophils and macrophages integrin-mediated
activation (By similarity). Interacts with MSN and SELPLG;
mediates the selectin-dependent activation of SYK by SELPLG (By
similarity). Interacts with BLNK (via SH2 domain) (By similarity).
Interacts (via the second SH2 domain) with USP25 (via C-terminus);
phosphorylates USP25 and regulates USP25 intracellular levels (By
similarity). Interacts (via SH2 domains) with CLEC1B (dimer) (By
similarity). Interacts with CLEC7A; participates in leukocyte
activation in presence of fungal pathogens (By similarity).
Interacts (phosphorylated) with SLA; may regulate SYK through CBL
recruitment (By similarity). 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
CEACAM1; lipopolysaccharide activated neutrophils induce
phosphorylation of SYK resulting in the formation of a complex
including TLR4 and the 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, which in turn, reduces the activity of the
inflammasome (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: 72 kDa tyrosine-protein kinase SYK: Cell
membrane {ECO:0000305}. Cytoplasm, cytosol. Note=Mainly associated
with membranes.
-!- SUBCELLULAR LOCATION: 40 kDa tyrosine-protein kinase SYK: Cell
membrane {ECO:0000305}. Cytoplasm, cytosol. Note=Equally
distributed between membranes and cytosol.
-!- TISSUE SPECIFICITY: Spleen and with lesser amounts in thymus.
-!- 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-316
creates a binding site for CBL, an adapter protein that serves as
a negative regulator of BCR-stimulated calcium ion signaling.
Phosphorylation at Tyr-341 creates a binding site for VAV1 (By
similarity). Phosphorylation on Tyr-341 and Tyr-345 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-290 is very common, it peaks 5 minutes after BCR stimulation,
and creates a binding site for YWHAG (By similarity).
Phosphorylation at Tyr-623 creates a binding site for BLNK (By
similarity). Dephosphorylated by PTPN6 (By similarity).
{ECO:0000250}.
-!- PTM: Shows high susceptibility to proteolysis.
-!- 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; M73237; AAA31112.1; -; mRNA.
PIR; A40802; A40802.
RefSeq; NP_001098422.1; NM_001104952.1.
UniGene; Ssc.55112; -.
ProteinModelPortal; Q00655; -.
SMR; Q00655; -.
IntAct; Q00655; 1.
MINT; Q00655; -.
iPTMnet; Q00655; -.
PaxDb; Q00655; -.
PRIDE; Q00655; -.
GeneID; 100125540; -.
KEGG; ssc:100125540; -.
CTD; 6850; -.
eggNOG; ENOG410JR52; Eukaryota.
eggNOG; ENOG4111TV9; LUCA.
HOGENOM; HOG000113264; -.
HOVERGEN; HBG001540; -.
InParanoid; Q00655; -.
KO; K05855; -.
BRENDA; 2.7.10.2; 6170.
Proteomes; UP000008227; 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:0005102; F:signaling receptor binding; IBA:GO_Central.
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:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IBA:GO_Central.
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: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; 3.
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; Angiogenesis; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing; Immunity;
Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; SH2 domain; Transferase;
Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 628 72 kDa tyrosine-protein kinase SYK.
/FTId=PRO_0000024468.
CHAIN 313 628 40 kDa tyrosine-protein kinase SYK.
/FTId=PRO_0000024469.
DOMAIN 10 102 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 163 253 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 364 624 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 370 378 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 103 162 Interdomain A. {ECO:0000250}.
REGION 254 363 Interdomain B. {ECO:0000250}.
ACT_SITE 487 487 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 395 395 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 23 23 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 42 42 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 126 126 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 250 250 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 289 289 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 316 316 Phosphotyrosine; by LYN.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 338 338 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 341 341 Phosphotyrosine.
{ECO:0000269|PubMed:8986718}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 345 345 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 357 357 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 377 377 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 477 477 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 500 500 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 518 518 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 519 519 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 523 523 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 539 539 Phosphotyrosine.
{ECO:0000250|UniProtKB:P48025}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 622 622 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 623 623 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 624 624 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MUTAGEN 341 341 Y->F: Alters interaction with VAV1.
{ECO:0000269|PubMed:8986718}.
MUTAGEN 345 345 Y->F: Moderately alters interaction with
VAV1. {ECO:0000269|PubMed:8986718}.
MUTAGEN 395 395 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:12709437}.
SEQUENCE 628 AA; 71620 MW; D7C0CEF7EBBEBC1E CRC64;
MADSANHLPF FFGQITREEA EDYLVQGGMS DGLYLLRQSR NYLGGFALSV AYDRKAHHYT
IERELNGTYA ISGGRTHGSP AELCHYHSQE LDGLVCLLKN PFNRPPGVQP KTGPFEDLKE
NLIREYVKQT WNLQGQALEQ AIISQKPQLE KLIATTAHEK MPWFHGKISR DESEQIVLIG
SKTNGKFLIR ARDNGSYALG LLHEGKVLHY RIDKDKTGKL SIPGGKNFDT LWQLVEHYSY
KSDGLLRVLT VPCQKIGGQT GNDSFRPQLP SAHPATWSAG GIISRIKSYS FPKPGHRKAS
SPQGNRPESL VSYNPYESDR GPWANEREAQ REALPMDTEV YESPYADPEE IRPKEVYLDR
KLLTLEDKEL GSGNFGTVKK GYYQMKKVVK TVAVKILKNE ANDPALKDEL LAEANVMQQL
DNPYIVRMIG ICEAESWMLV MEMAELGPLN KYLQQNRHVK DKNIIELVHQ VSMGMKYLEE
CNFVHRDLAA RNVLLVTQHY AKISDFGLSK ALRADENYYK AQTHGKWPVK WYAPECINYY
KFSSKSDVWS FGVLMWEAFS YGQKPYRGMK GSEVSAMLEK GERMGCPPGC PREMYELMTL
CWTYDVENRP GFVAVELRLR NYYYDVVN


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EIAAB33009 Chicken,Gallus gallus,Inactive tyrosine-protein kinase 7,Kinase-like protein,KLG,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
EIAAB44680 BYK,DTK,Homo sapiens,Human,RSE,SKY,TYRO3,Tyrosine-protein kinase byk,Tyrosine-protein kinase DTK,Tyrosine-protein kinase receptor TYRO3,Tyrosine-protein kinase RSE,Tyrosine-protein kinase SKY
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
U2227h CLIA 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
E2227h ELISA 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
E2227h ELISA 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
E2227h 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
18-661-15209 Tyrosine-protein kinase BTK - EC 2.7.10.2; Bruton tyrosine kinase; Agammaglobulinaemia tyrosine kinase; ATK; B cell progenitor kinase; BPK Polyclonal 0.1 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.001 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.02 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.01 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.005 mg
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
EIAAB14370 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,FAK2,Focal adhesion kinase 2,Homo sapiens,Human,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,PTK2B,PY
EIAAB14369 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,Fak2,Focal adhesion kinase 2,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,Ptk2b,Pyk2,Rat,Rattus norve


 

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