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

 KSYK_MOUSE              Reviewed;         629 AA.
P48025;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
31-JAN-2018, entry version 184.
RecName: Full=Tyrosine-protein kinase SYK;
EC=2.7.10.2;
AltName: Full=Spleen tyrosine kinase;
Name=Syk; Synonyms=ptk72, Sykb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
PubMed=7477352; DOI=10.1038/378298a0;
Turner M., Mee P.J., Costello P.S., Williams O., Price A.A.,
Duddy L.P., Furlong M.T., Geahlen R.L., Tybulewicz V.L.;
"Perinatal lethality and blocked B-cell development in mice lacking
the tyrosine kinase Syk.";
Nature 378:298-302(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=7639745; DOI=10.1006/bbrc.1995.2126;
Flueck M., Zuercher G., Andres A., Ziemiecki A.;
"Molecular characterization of the murine syk protein tyrosine kinase
cDNA, transcripts and protein.";
Biochem. Biophys. Res. Commun. 213:273-281(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Richards J.D., Gold M.R., Hourihane S.L., Defranco A.L., Matsuuchi L.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION BY LYN.
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).
[5]
INTERACTION WITH CD79A.
PubMed=7538118; DOI=10.1074/jbc.270.19.11590;
Rowley R.B., Burkhardt A.L., Chao H.-G., Matsueda G.R., Bolen J.B.;
"Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated
Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and
autophosphorylation.";
J. Biol. Chem. 270:11590-11594(1995).
[6]
DISRUPTION PHENOTYPE.
PubMed=7477353; DOI=10.1038/378303a0;
Cheng A.M., Rowley B., Pao W., Hayday A., Bolen J.B., Pawson T.;
"Syk tyrosine kinase required for mouse viability and B-cell
development.";
Nature 378:303-306(1995).
[7]
FUNCTION IN ACTIVATION OF PLATELETS BY COLLAGEN, AND FUNCTION IN PLCG2
PHOSPHORYLATION.
PubMed=9171347; DOI=10.1093/emboj/16.9.2333;
Poole A., Gibbins J.M., Turner M., van Vugt M.J., van de Winkel J.G.,
Saito T., Tybulewicz V.L., Watson S.P.;
"The Fc receptor gamma-chain and the tyrosine kinase Syk are essential
for activation of mouse platelets by collagen.";
EMBO J. 16:2333-2341(1997).
[8]
FUNCTION IN INTEGRIN SIGNALING, PHOSPHORYLATION AT TYR-342; TYR-519
AND TYR-520, AND INTERACTION WITH ITGB2 AND FGR.
PubMed=11672534; DOI=10.1016/S1074-7613(01)00221-7;
Vines C.M., Potter J.W., Xu Y., Geahlen R.L., Costello P.S.,
Tybulewicz V.L., Lowell C.A., Chang P.W., Gresham H.D., Willman C.L.;
"Inhibition of beta 2 integrin receptor and Syk kinase signaling in
monocytes by the Src family kinase Fgr.";
Immunity 15:507-519(2001).
[9]
PHOSPHORYLATION AT TYR-317; 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).
[10]
FUNCTION IN INTEGRIN-MEDIATED PLATELET ADHESION.
PubMed=11940607; DOI=10.1083/jcb.200112113;
Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L.,
Brugge J.S., Lowell C.A., Shattil S.J.;
"Coordinate interactions of Csk, Src, and Syk kinases with
[alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton.";
J. Cell Biol. 157:265-275(2002).
[11]
UBIQUITINATION BY CBLB, AND ENZYME REGULATION.
PubMed=12771181; DOI=10.1084/jem.20021686;
Sohn H.W., Gu H., Pierce S.K.;
"Cbl-b negatively regulates B cell antigen receptor signaling in
mature B cells through ubiquitination of the tyrosine kinase Syk.";
J. Exp. Med. 197:1511-1524(2003).
[12]
FUNCTION IN VASCULAR DEVELOPMENT.
PubMed=12522250; DOI=10.1126/science.1079477;
Abtahian F., Guerriero A., Sebzda E., Lu M.M., Zhou R., Mocsai A.,
Myers E.E., Huang B., Jackson D.G., Ferrari V.A., Tybulewicz V.,
Lowell C.A., Lepore J.J., Koretzky G.A., Kahn M.L.;
"Regulation of blood and lymphatic vascular separation by signaling
proteins SLP-76 and Syk.";
Science 299:247-251(2003).
[13]
INTERACTION WITH NFAM1.
PubMed=15143214; DOI=10.1073/pnas.0401119101;
Ohtsuka M., Arase H., Takeuchi A., Yamasaki S., Shiina R., Suenaga T.,
Sakurai D., Yokosuka T., Arase N., Iwashima M., Kitamura T.,
Moriya H., Saito T.;
"NFAM1, an immunoreceptor tyrosine-based activation motif-bearing
molecule that regulates B cell development and signaling.";
Proc. Natl. Acad. Sci. U.S.A. 101:8126-8131(2004).
[14]
FUNCTION IN ROS PRODUCTION, AND FUNCTION IN RESPONSE TO FUNGAL
PATHOGEN.
PubMed=15956283; DOI=10.1182/blood-2005-03-1239;
Underhill D.M., Rossnagle E., Lowell C.A., Simmons R.M.;
"Dectin-1 activates Syk tyrosine kinase in a dynamic subset of
macrophages for reactive oxygen production.";
Blood 106:2543-2550(2005).
[15]
FUNCTION IN RESPONSE TO FUNGAL PATHOGEN, INTERACTION WITH CLEC7A, AND
SUBCELLULAR LOCATION.
PubMed=15845454; DOI=10.1016/j.immuni.2005.03.004;
Rogers N.C., Slack E.C., Edwards A.D., Nolte M.A., Schulz O.,
Schweighoffer E., Williams D.L., Gordon S., Tybulewicz V.L.,
Brown G.D., Reis e Sousa C.;
"Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern
recognition pathway for C type lectins.";
Immunity 22:507-517(2005).
[16]
FUNCTION IN ACTIVATION OF PLATELETS BY CLEC1B.
PubMed=16174766; DOI=10.1182/blood-2005-05-1994;
Suzuki-Inoue K., Fuller G.L.J., Garcia A., Eble J.A., Poehlmann S.,
Inoue O., Gartner T.K., Hughan S.C., Pearce A.C., Laing G.D.,
Theakston R.D.G., Schweighoffer E., Zitzmann N., Morita T.,
Tybulewicz V.L.J., Ozaki Y., Watson S.P.;
"A novel Syk-dependent mechanism of platelet activation by the C-type
lectin receptor CLEC-2.";
Blood 107:542-549(2006).
[17]
INTERACTION WITH GAB2.
PubMed=16456001; DOI=10.4049/jimmunol.176.4.2421;
Yu M., Lowell C.A., Neel B.G., Gu H.;
"Scaffolding adapter Grb2-associated binder 2 requires Syk to transmit
signals from FcepsilonRI.";
J. Immunol. 176:2421-2429(2006).
[18]
FUNCTION IN INTEGRIN-MEDIATED NEUTROPHIL ACTIVATION, INTERACTION WITH
FCER1G AND TYROBP, AND MUTAGENESIS OF ARG-41 AND ARG-194.
PubMed=17086186; DOI=10.1038/ni1407;
Mocsai A., Abram C.L., Jakus Z., Hu Y., Lanier L.L., Lowell C.A.;
"Integrin signaling in neutrophils and macrophages uses adaptors
containing immunoreceptor tyrosine-based activation motifs.";
Nat. Immunol. 7:1326-1333(2006).
[19]
FUNCTION IN OSTEOCLASTIC BONE RESORPTION.
PubMed=17353363; DOI=10.1083/jcb.200611083;
Zou W., Kitaura H., Reeve J., Long F., Tybulewicz V.L., Shattil S.J.,
Ginsberg M.H., Ross F.P., Teitelbaum S.L.;
"Syk, c-Src, the alphavbeta3 integrin, and ITAM immunoreceptors, in
concert, regulate osteoclastic bone resorption.";
J. Cell Biol. 176:877-888(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-313; TYR-317;
TYR-342; TYR-346; TYR-519; TYR-520; TYR-540; TYR-623 AND TYR-624, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[21]
INTERACTION WITH BLNK.
PubMed=18369315; DOI=10.1038/emboj.2008.62;
Kulathu Y., Hobeika E., Turchinovich G., Reth M.;
"The kinase Syk as an adaptor controlling sustained calcium signalling
and B-cell development.";
EMBO J. 27:1333-1344(2008).
[22]
FUNCTION IN RESPONSE TO BACTERIA.
PubMed=19797524; DOI=10.1182/blood-2009-05-220806;
Van Ziffle J.A., Lowell C.A.;
"Neutrophil-specific deletion of Syk kinase results in reduced host
defense to bacterial infection.";
Blood 114:4871-4882(2009).
[23]
FUNCTION IN MAST CELL ACTIVATION, INTERACTION WITH RHOH, AND ENZYME
REGULATION.
PubMed=19124738; DOI=10.4049/jimmunol.182.2.957;
Oda H., Fujimoto M., Patrick M.S., Chida D., Sato Y., Azuma Y.,
Aoki H., Abe T., Suzuki H., Shirai M.;
"RhoH plays critical roles in Fc epsilon RI-dependent signal
transduction in mast cells.";
J. Immunol. 182:957-962(2009).
[24]
FUNCTION IN RESPONSE TO FUNGAL PATHOGEN, FUNCTION IN INFLAMMASOME
ACTIVATION, AND FUNCTION IN REGULATION OF TRANSCRIPTION.
PubMed=19339971; DOI=10.1038/nature07965;
Gross O., Poeck H., Bscheider M., Dostert C., Hannesschlaeger N.,
Endres S., Hartmann G., Tardivel A., Schweighoffer E., Tybulewicz V.,
Mocsai A., Tschopp J., Ruland J.;
"Syk kinase signalling couples to the Nlrp3 inflammasome for anti-
fungal host defence.";
Nature 459:433-436(2009).
[25]
FUNCTION IN IMMUNE SYSTEM STIMULATION BY CELL NECROSIS.
PubMed=19219027; DOI=10.1038/nature07750;
Sancho D., Joffre O.P., Keller A.M., Rogers N.C., Martinez D.,
Hernanz-Falcon P., Rosewell I., Reis e Sousa C.;
"Identification of a dendritic cell receptor that couples sensing of
necrosis to immunity.";
Nature 458:899-903(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[27]
INTERACTION WITH CEACAM1.
PubMed=22496641; DOI=10.1371/journal.ppat.1002597;
Lu R., Pan H., Shively J.E.;
"CEACAM1 negatively regulates IL-1beta production in LPS activated
neutrophils by recruiting SHP-1 to a SYK-TLR4-CEACAM1 complex.";
PLoS Pathog. 8:E1002597-E1002597(2012).
[28]
FUNCTION, AND INTERACTION WITH CEACAM20.
PubMed=26195794; DOI=10.1073/pnas.1510167112;
Murata Y., Kotani T., Supriatna Y., Kitamura Y., Imada S.,
Kawahara K., Nishio M., Daniwijaya E.W., Sadakata H., Kusakari S.,
Mori M., Kanazawa Y., Saito Y., Okawa K., Takeda-Morishita M.,
Okazawa H., Ohnishi H., Azuma T., Suzuki A., Matozaki T.;
"Protein tyrosine phosphatase SAP-1 protects against colitis through
regulation of CEACAM20 in the intestinal epithelium.";
Proc. Natl. Acad. Sci. U.S.A. 112:E4264-E4271(2015).
-!- 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.
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 (PubMed:26195794). {ECO:0000269|PubMed:11672534,
ECO:0000269|PubMed:11940607, ECO:0000269|PubMed:12522250,
ECO:0000269|PubMed:15845454, ECO:0000269|PubMed:15956283,
ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:17086186,
ECO:0000269|PubMed:17353363, ECO:0000269|PubMed:19124738,
ECO:0000269|PubMed:19219027, ECO:0000269|PubMed:19339971,
ECO:0000269|PubMed:19797524, ECO:0000269|PubMed:26195794,
ECO:0000269|PubMed:9171347}.
-!- 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. 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. Negatively regulated by CBL and CBLB
through ubiquitination and probable degradation. 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 (By similarity). 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. Interacts with ITGB2 and FGR; involved in
ITGB2 downstream signaling. 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.
Interacts with MSN and SELPLG; mediates the selectin-dependent
activation of SYK by SELPLG (By similarity). Interacts with BLNK
(via SH2 domain). 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. 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 with 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, leading to
a reduction of the inflammasome activity (PubMed:22496641).
Interacts (via SH2 domains) with CEACAM20 (phosphorylated form);
the interaction further enhances CEACAM20 phosphorylation
(PubMed:26195794). {ECO:0000250|UniProtKB:P43405,
ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:26195794}.
-!- INTERACTION:
P08487:PLCG1 (xeno); NbExp=4; IntAct=EBI-300116, EBI-8013886;
Q64693:Pou2af1; NbExp=2; IntAct=EBI-300116, EBI-943530;
P42227:Stat3; NbExp=5; IntAct=EBI-300116, EBI-602878;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15845454}.
Cytoplasm, cytosol {ECO:0000305|PubMed:15845454}. Cytoplasmic
vesicle, phagosome {ECO:0000269|PubMed:15845454}.
-!- 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.
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:0000269|PubMed:12771181}.
-!- DISRUPTION PHENOTYPE: Embryos display severe systemic hemorrhage
and mice are not viable dying perinatally. While T-cells
development is not affected, the development of B-cells is
impaired most probably at the pro-B to pre-B transition and mice
lack mature B-cells. {ECO:0000269|PubMed:7477352,
ECO:0000269|PubMed:7477353}.
-!- 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; U25685; AAA87462.1; -; mRNA.
EMBL; Z49877; CAA90034.1; -; mRNA.
EMBL; U36776; AAA79996.1; -; mRNA.
CCDS; CCDS26517.1; -.
PIR; I48781; I48781.
RefSeq; NP_001185906.1; NM_001198977.1.
RefSeq; NP_035648.2; NM_011518.2.
RefSeq; XP_006516958.1; XM_006516895.3.
UniGene; Mm.375031; -.
PDB; 2LCT; NMR; -; B=338-350.
PDB; 2MC1; NMR; -; B=338-350.
PDBsum; 2LCT; -.
PDBsum; 2MC1; -.
ProteinModelPortal; P48025; -.
SMR; P48025; -.
BioGrid; 203599; 13.
DIP; DIP-32621N; -.
IntAct; P48025; 14.
MINT; MINT-1209968; -.
STRING; 10090.ENSMUSP00000060828; -.
iPTMnet; P48025; -.
PhosphoSitePlus; P48025; -.
PaxDb; P48025; -.
PeptideAtlas; P48025; -.
PRIDE; P48025; -.
Ensembl; ENSMUST00000055087; ENSMUSP00000060828; ENSMUSG00000021457.
Ensembl; ENSMUST00000120135; ENSMUSP00000113852; ENSMUSG00000021457.
GeneID; 20963; -.
KEGG; mmu:20963; -.
UCSC; uc007qmz.1; mouse.
CTD; 6850; -.
MGI; MGI:99515; Syk.
eggNOG; ENOG410IH0T; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000113264; -.
HOVERGEN; HBG001540; -.
InParanoid; P48025; -.
KO; K05855; -.
OMA; KPFNRPP; -.
OrthoDB; EOG091G07KU; -.
PhylomeDB; P48025; -.
TreeFam; TF351629; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-451927; Interleukin-2 family signaling.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; Syk; mouse.
PRO; PR:P48025; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021457; -.
CleanEx; MM_SYK; -.
ExpressionAtlas; P48025; baseline and differential.
Genevisible; P48025; MM.
GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IDA:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:MGI.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; IDA:MGI.
GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IMP:MGI.
GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
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; IDA:MGI.
GO; GO:0043366; P:beta selection; IGI:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
GO; GO:0071226; P:cellular response to molecule of fungal origin; IMP:UniProtKB.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IMP:MGI.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; IDA:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:MGI.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0002366; P:leukocyte activation involved in immune response; IMP:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISS:UniProtKB.
GO; GO:0019370; P:leukotriene biosynthetic process; IMP:MGI.
GO; GO:0001945; P:lymph vessel development; IMP:UniProtKB.
GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
GO; GO:0002283; P:neutrophil activation involved in immune response; IMP:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IGI:MGI.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IGI:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
GO; GO:0045780; P:positive regulation of bone resorption; IMP:UniProtKB.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:MGI.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; IGI:MGI.
GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IMP:MGI.
GO; GO:0045425; P:positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process; IMP:MGI.
GO; GO:0045401; P:positive regulation of interleukin-3 biosynthetic process; IMP:MGI.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:MGI.
GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IMP:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0002092; P:positive regulation of receptor internalization; IMP:CACAO.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:CACAO.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0090237; P:regulation of arachidonic acid secretion; IMP:UniProtKB.
GO; GO:0051090; P:regulation of DNA binding transcription factor activity; ISO:MGI.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0043313; P:regulation of neutrophil degranulation; IMP:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
GO; GO:0010543; P:regulation of platelet activation; IMP:UniProtKB.
GO; GO:0090330; P:regulation of platelet aggregation; IMP:UniProtKB.
GO; GO:0032928; P:regulation of superoxide anion generation; IMP:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
GO; GO:0001820; P:serotonin secretion; IMP:MGI.
GO; GO:0002554; P:serotonin secretion by platelet; IMP:UniProtKB.
GO; GO:0042991; P:transcription factor import into nucleus; ISO:MGI.
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;
3D-structure; Adaptive immunity; Angiogenesis; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
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_0000088166.
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.
REGION 259 364 Interdomain B.
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:0000244|PubMed:21183079}.
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:0000244|PubMed:17947660}.
MOD_RES 311 311 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 313 313 Phosphoserine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 317 317 Phosphotyrosine; by LYN.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:12077122}.
MOD_RES 339 339 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 342 342 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:11672534,
ECO:0000269|PubMed:12077122}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 346 346 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
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:0000244|PubMed:17947660,
ECO:0000269|PubMed:11672534}.
MOD_RES 520 520 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:11672534}.
MOD_RES 524 524 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 540 540 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 576 576 Phosphothreonine.
{ECO:0000250|UniProtKB:P43405}.
MOD_RES 623 623 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 624 624 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 625 625 Phosphotyrosine.
{ECO:0000250|UniProtKB:P43405}.
MUTAGEN 41 41 R->A: Loss of interaction with FCER1G and
TYROBP; when associated with A-194.
{ECO:0000269|PubMed:17086186}.
MUTAGEN 194 194 R->A: Loss of interaction with FCER1G and
TYROBP; when associated with A-41.
{ECO:0000269|PubMed:17086186}.
CONFLICT 326 326 Missing (in Ref. 2; CAA90034).
{ECO:0000305}.
CONFLICT 446 447 EL -> DV (in Ref. 2; CAA90034).
{ECO:0000305}.
STRAND 346 348 {ECO:0000244|PDB:2LCT}.
SEQUENCE 629 AA; 71376 MW; 2F98D21601F8224E CRC64;
MAGSAVDSAN HLTYFFGNIT REEAEDYLVQ GGMTDGLYLL RQSRNYLGGF ALSVAHNRKA
HHYTIERELN GTYAISGGRA HASPADLCHY HSQEPDGLIC LLKKPFNRPP GVQPKTGPFE
DLKENLIREY VKQTWNLQGQ ALEQAIISQK PQLEKLIATT AHEKMPWFHG NISRDESEQT
VLIGSKTNGK FLIRARDNSG SYALCLLHEG KVLHYRIDRD KTGKLSIPEG KKFDTLWQLV
EHYSYKPDGL LRVLTVPCQK IGAQMGHPGS PNAHPVTWSP GGIISRIKSY SFPKPGHKKP
APPQGSRPES TVSFNPYEPT GGPWGPDRGL QREALPMDTE VYESPYADPE EIRPKEVYLD
RSLLTLEDNE LGSGNFGTVK KGYYQMKKVV KTVAVKILKN EANDPALKDE LLAEANVMQQ
LDNPYIVRMI GICEAESWML VMEMAELGPL NKYLQQNRHI KDKNIIELVH QVSMGMKYLE
ESNFVHRDLA ARNVLLVTQH YAKISDFGLS KALRADENYY KAQTHGKWPV KWYAPECINY
YKFSSKSDVW SFGVLMWEAF SYGQKPYRGM KGSEVTAMLE KGERMGCPAG CPREMYDLMN
LCWTYDVENR PGFTAVELRL RNYYYDVVN


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