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P48025

- KSYK_MOUSE

UniProt

P48025 - KSYK_MOUSE

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Protein

Tyrosine-protein kinase SYK

Gene

Syk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.13 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei396 – 3961ATPPROSITE-ProRule annotation
Active sitei488 – 4881Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi371 – 3799ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. non-membrane spanning protein tyrosine kinase activity Source: MGI
  3. protein kinase binding Source: UniProtKB
  4. protein tyrosine kinase activity Source: UniProtKB
  5. receptor signaling protein tyrosine kinase activity Source: MGI

GO - Biological processi

  1. activation of JUN kinase activity Source: MGI
  2. activation of MAPK activity Source: MGI
  3. adaptive immune response Source: UniProtKB
  4. angiogenesis Source: UniProtKB-KW
  5. B cell receptor signaling pathway Source: MGI
  6. beta selection Source: MGI
  7. blood vessel morphogenesis Source: UniProtKB
  8. cell surface receptor signaling pathway Source: MGI
  9. cellular response to molecule of fungal origin Source: UniProtKB
  10. defense response to bacterium Source: UniProtKB
  11. enzyme linked receptor protein signaling pathway Source: MGI
  12. G-protein coupled receptor signaling pathway Source: MGI
  13. innate immune response Source: UniProtKB
  14. integrin-mediated signaling pathway Source: UniProtKB
  15. intracellular signal transduction Source: MGI
  16. leukocyte activation involved in immune response Source: UniProtKB
  17. leukocyte cell-cell adhesion Source: UniProtKB
  18. leukotriene biosynthetic process Source: MGI
  19. lymph vessel development Source: UniProtKB
  20. macrophage activation involved in immune response Source: UniProtKB
  21. neutrophil activation involved in immune response Source: UniProtKB
  22. neutrophil chemotaxis Source: UniProtKB
  23. peptidyl-tyrosine phosphorylation Source: UniProtKB
  24. positive regulation of alpha-beta T cell differentiation Source: MGI
  25. positive regulation of alpha-beta T cell proliferation Source: MGI
  26. positive regulation of B cell differentiation Source: MGI
  27. positive regulation of bone resorption Source: UniProtKB
  28. positive regulation of calcium-mediated signaling Source: MGI
  29. positive regulation of cell adhesion mediated by integrin Source: UniProtKB
  30. positive regulation of cytokine secretion Source: MGI
  31. positive regulation of gamma-delta T cell differentiation Source: MGI
  32. positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process Source: MGI
  33. positive regulation of interleukin-3 biosynthetic process Source: MGI
  34. positive regulation of mast cell degranulation Source: MGI
  35. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  36. protein autophosphorylation Source: MGI
  37. protein phosphorylation Source: UniProtKB
  38. regulation of arachidonic acid secretion Source: UniProtKB
  39. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  40. regulation of neutrophil degranulation Source: UniProtKB
  41. regulation of phagocytosis Source: UniProtKB
  42. regulation of platelet activation Source: UniProtKB
  43. regulation of platelet aggregation Source: UniProtKB
  44. regulation of superoxide anion generation Source: UniProtKB
  45. serotonin secretion Source: MGI
  46. serotonin secretion by platelet Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Angiogenesis, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188204. Fc epsilon receptor (FCERI) signaling.
REACT_188530. FCERI mediated MAPK activation.
REACT_196487. FCGR activation.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_220092. GPVI-mediated activation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase SYK (EC:2.7.10.2)
Alternative name(s):
Spleen tyrosine kinase
Gene namesi
Name:Syk
Synonyms:ptk72, Sykb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:99515. Syk.

Subcellular locationi

Cell membrane 1 Publication. Cytoplasmcytosol 1 Publication. Cytoplasmic vesiclephagosome 1 Publication

GO - Cellular componenti

  1. B cell receptor complex Source: MGI
  2. cytosol Source: Reactome
  3. early phagosome Source: UniProtKB
  4. protein complex Source: MGI
  5. T cell receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411R → A: Loss of interaction with FCER1G and TYROBP; when associated with A-194. 1 Publication
Mutagenesisi194 – 1941R → A: Loss of interaction with FCER1G and TYROBP; when associated with A-41. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 629629Tyrosine-protein kinase SYKPRO_0000088166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphotyrosineBy similarity
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei46 – 461PhosphotyrosineBy similarity
Modified residuei130 – 1301PhosphotyrosineBy similarity
Modified residuei201 – 2011PhosphoserineBy similarity
Modified residuei255 – 2551PhosphothreonineBy similarity
Modified residuei289 – 2891PhosphoserineBy similarity
Modified residuei290 – 2901PhosphotyrosineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei311 – 3111PhosphothreonineBy similarity
Modified residuei313 – 3131Phosphoserine1 Publication
Modified residuei317 – 3171Phosphotyrosine; by LYN2 Publications
Modified residuei339 – 3391PhosphothreonineBy similarity
Modified residuei342 – 3421Phosphotyrosine3 Publications
Modified residuei344 – 3441PhosphoserineBy similarity
Modified residuei346 – 3461Phosphotyrosine2 Publications
Modified residuei358 – 3581PhosphotyrosineBy similarity
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei378 – 3781PhosphothreonineBy similarity
Modified residuei478 – 4781PhosphotyrosineBy similarity
Modified residuei501 – 5011PhosphotyrosineBy similarity
Modified residuei519 – 5191Phosphotyrosine; by autocatalysis2 Publications
Modified residuei520 – 5201Phosphotyrosine2 Publications
Modified residuei524 – 5241PhosphothreonineBy similarity
Modified residuei540 – 5401Phosphotyrosine1 Publication
Modified residuei573 – 5731PhosphoserineBy similarity
Modified residuei576 – 5761PhosphothreonineBy similarity
Modified residuei623 – 6231Phosphotyrosine1 Publication
Modified residuei624 – 6241Phosphotyrosine1 Publication
Modified residuei625 – 6251PhosphotyrosineBy similarity

Post-translational modificationi

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).By similarity
Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP48025.
PaxDbiP48025.
PRIDEiP48025.

PTM databases

PhosphoSiteiP48025.

Expressioni

Gene expression databases

BgeeiP48025.
CleanExiMM_SYK.
ExpressionAtlasiP48025. baseline and differential.
GenevestigatoriP48025.

Interactioni

Subunit structurei

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 with FCRL3 (By similarity). 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PLCG1P084874EBI-300116,EBI-8013886From a different organism.
Pou2af1Q646932EBI-300116,EBI-943530

Protein-protein interaction databases

BioGridi203599. 11 interactions.
DIPiDIP-32621N.
IntActiP48025. 9 interactions.
MINTiMINT-1209968.

Structurei

Secondary structure

1
629
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi346 – 3483Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LCTNMR-B338-350[»]
2MC1NMR-B338-350[»]
ProteinModelPortaliP48025.
SMRiP48025. Positions 7-629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 10693SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini167 – 25892SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini365 – 625261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 16660Interdomain AAdd
BLAST
Regioni259 – 364106Interdomain BAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000113264.
HOVERGENiHBG001540.
InParanoidiP48025.
KOiK05855.
OMAiKGYYQMK.
OrthoDBiEOG7MWGWD.
PhylomeDBiP48025.
TreeFamiTF351629.

Family and domain databases

Gene3Di1.10.930.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PIRSFiPIRSF000604. TyrPK_SYK. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48025-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGSAVDSAN HLTYFFGNIT REEAEDYLVQ GGMTDGLYLL RQSRNYLGGF
60 70 80 90 100
ALSVAHNRKA HHYTIERELN GTYAISGGRA HASPADLCHY HSQEPDGLIC
110 120 130 140 150
LLKKPFNRPP GVQPKTGPFE DLKENLIREY VKQTWNLQGQ ALEQAIISQK
160 170 180 190 200
PQLEKLIATT AHEKMPWFHG NISRDESEQT VLIGSKTNGK FLIRARDNSG
210 220 230 240 250
SYALCLLHEG KVLHYRIDRD KTGKLSIPEG KKFDTLWQLV EHYSYKPDGL
260 270 280 290 300
LRVLTVPCQK IGAQMGHPGS PNAHPVTWSP GGIISRIKSY SFPKPGHKKP
310 320 330 340 350
APPQGSRPES TVSFNPYEPT GGPWGPDRGL QREALPMDTE VYESPYADPE
360 370 380 390 400
EIRPKEVYLD RSLLTLEDNE LGSGNFGTVK KGYYQMKKVV KTVAVKILKN
410 420 430 440 450
EANDPALKDE LLAEANVMQQ LDNPYIVRMI GICEAESWML VMEMAELGPL
460 470 480 490 500
NKYLQQNRHI KDKNIIELVH QVSMGMKYLE ESNFVHRDLA ARNVLLVTQH
510 520 530 540 550
YAKISDFGLS KALRADENYY KAQTHGKWPV KWYAPECINY YKFSSKSDVW
560 570 580 590 600
SFGVLMWEAF SYGQKPYRGM KGSEVTAMLE KGERMGCPAG CPREMYDLMN
610 620
LCWTYDVENR PGFTAVELRL RNYYYDVVN
Length:629
Mass (Da):71,376
Last modified:October 1, 1996 - v2
Checksum:i2F98D21601F8224E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261Missing in CAA90034. (PubMed:7639745)Curated
Sequence conflicti446 – 4472EL → DV in CAA90034. (PubMed:7639745)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25685 mRNA. Translation: AAA87462.1.
Z49877 mRNA. Translation: CAA90034.1.
U36776 mRNA. Translation: AAA79996.1.
CCDSiCCDS26517.1.
PIRiI48781.
RefSeqiNP_001185906.1. NM_001198977.1.
NP_035648.2. NM_011518.2.
XP_006516958.1. XM_006516895.1.
UniGeneiMm.375031.

Genome annotation databases

EnsembliENSMUST00000055087; ENSMUSP00000060828; ENSMUSG00000021457.
ENSMUST00000120135; ENSMUSP00000113852; ENSMUSG00000021457.
GeneIDi20963.
KEGGimmu:20963.
UCSCiuc007qmz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25685 mRNA. Translation: AAA87462.1 .
Z49877 mRNA. Translation: CAA90034.1 .
U36776 mRNA. Translation: AAA79996.1 .
CCDSi CCDS26517.1.
PIRi I48781.
RefSeqi NP_001185906.1. NM_001198977.1.
NP_035648.2. NM_011518.2.
XP_006516958.1. XM_006516895.1.
UniGenei Mm.375031.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LCT NMR - B 338-350 [» ]
2MC1 NMR - B 338-350 [» ]
ProteinModelPortali P48025.
SMRi P48025. Positions 7-629.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203599. 11 interactions.
DIPi DIP-32621N.
IntActi P48025. 9 interactions.
MINTi MINT-1209968.

PTM databases

PhosphoSitei P48025.

Proteomic databases

MaxQBi P48025.
PaxDbi P48025.
PRIDEi P48025.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055087 ; ENSMUSP00000060828 ; ENSMUSG00000021457 .
ENSMUST00000120135 ; ENSMUSP00000113852 ; ENSMUSG00000021457 .
GeneIDi 20963.
KEGGi mmu:20963.
UCSCi uc007qmz.1. mouse.

Organism-specific databases

CTDi 6850.
MGIi MGI:99515. Syk.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000113264.
HOVERGENi HBG001540.
InParanoidi P48025.
KOi K05855.
OMAi KGYYQMK.
OrthoDBi EOG7MWGWD.
PhylomeDBi P48025.
TreeFami TF351629.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188204. Fc epsilon receptor (FCERI) signaling.
REACT_188530. FCERI mediated MAPK activation.
REACT_196487. FCGR activation.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_220092. GPVI-mediated activation cascade.

Miscellaneous databases

ChiTaRSi SYK. mouse.
NextBioi 299918.
PROi P48025.
SOURCEi Search...

Gene expression databases

Bgeei P48025.
CleanExi MM_SYK.
ExpressionAtlasi P48025. baseline and differential.
Genevestigatori P48025.

Family and domain databases

Gene3Di 1.10.930.10. 1 hit.
3.30.505.10. 2 hits.
InterProi IPR011009. Kinase-like_dom.
IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view ]
PIRSFi PIRSF000604. TyrPK_SYK. 1 hit.
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk."
    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.
    Nature 378:298-302(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
  2. "Molecular characterization of the murine syk protein tyrosine kinase cDNA, transcripts and protein."
    Flueck M., Zuercher G., Andres A., Ziemiecki A.
    Biochem. Biophys. Res. Commun. 213:273-281(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.
  3. Richards J.D., Gold M.R., Hourihane S.L., Defranco A.L., Matsuuchi L.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling."
    Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T., Yamamoto T., Yamamura H.
    J. Exp. Med. 179:1725-1729(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY LYN.
  5. "Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation."
    Rowley R.B., Burkhardt A.L., Chao H.-G., Matsueda G.R., Bolen J.B.
    J. Biol. Chem. 270:11590-11594(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD79A.
  6. "Syk tyrosine kinase required for mouse viability and B-cell development."
    Cheng A.M., Rowley B., Pao W., Hayday A., Bolen J.B., Pawson T.
    Nature 378:303-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "The Fc receptor gamma-chain and the tyrosine kinase Syk are essential for activation of mouse platelets by collagen."
    Poole A., Gibbins J.M., Turner M., van Vugt M.J., van de Winkel J.G., Saito T., Tybulewicz V.L., Watson S.P.
    EMBO J. 16:2333-2341(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF PLATELETS BY COLLAGEN, FUNCTION IN PLCG2 PHOSPHORYLATION.
  8. "Inhibition of beta 2 integrin receptor and Syk kinase signaling in monocytes by the Src family kinase Fgr."
    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.
    Immunity 15:507-519(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTEGRIN SIGNALING, PHOSPHORYLATION AT TYR-342; TYR-519 AND TYR-520, INTERACTION WITH ITGB2 AND FGR.
  9. "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."
    Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.
    J. Biol. Chem. 277:31703-31714(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-317; TYR-342 AND TYR-346.
  10. "Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton."
    Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L., Brugge J.S., Lowell C.A., Shattil S.J.
    J. Cell Biol. 157:265-275(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTEGRIN-MEDIATED PLATELET ADHESION.
  11. "Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through ubiquitination of the tyrosine kinase Syk."
    Sohn H.W., Gu H., Pierce S.K.
    J. Exp. Med. 197:1511-1524(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY CBLB, ENZYME REGULATION.
  12. Cited for: FUNCTION IN VASCULAR DEVELOPMENT.
  13. "NFAM1, an immunoreceptor tyrosine-based activation motif-bearing molecule that regulates B cell development and signaling."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 101:8126-8131(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFAM1.
  14. "Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production."
    Underhill D.M., Rossnagle E., Lowell C.A., Simmons R.M.
    Blood 106:2543-2550(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ROS PRODUCTION, FUNCTION IN RESPONSE TO FUNGAL PATHOGEN.
  15. "Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins."
    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.
    Immunity 22:507-517(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RESPONSE TO FUNGAL PATHOGEN, INTERACTION WITH CLEC7A, SUBCELLULAR LOCATION.
  16. Cited for: FUNCTION IN ACTIVATION OF PLATELETS BY CLEC1B.
  17. "Scaffolding adapter Grb2-associated binder 2 requires Syk to transmit signals from FcepsilonRI."
    Yu M., Lowell C.A., Neel B.G., Gu H.
    J. Immunol. 176:2421-2429(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAB2.
  18. "Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs."
    Mocsai A., Abram C.L., Jakus Z., Hu Y., Lanier L.L., Lowell C.A.
    Nat. Immunol. 7:1326-1333(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTEGRIN-MEDIATED NEUTROPHIL ACTIVATION, INTERACTION WITH FCER1G AND TYROBP, MUTAGENESIS OF ARG-41 AND ARG-194.
  19. "Syk, c-Src, the alphavbeta3 integrin, and ITAM immunoreceptors, in concert, regulate osteoclastic bone resorption."
    Zou W., Kitaura H., Reeve J., Long F., Tybulewicz V.L., Shattil S.J., Ginsberg M.H., Ross F.P., Teitelbaum S.L.
    J. Cell Biol. 176:877-888(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOCLASTIC BONE RESORPTION.
  20. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  21. "The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development."
    Kulathu Y., Hobeika E., Turchinovich G., Reth M.
    EMBO J. 27:1333-1344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLNK.
  22. "Neutrophil-specific deletion of Syk kinase results in reduced host defense to bacterial infection."
    Van Ziffle J.A., Lowell C.A.
    Blood 114:4871-4882(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RESPONSE TO BACTERIA.
  23. "RhoH plays critical roles in Fc epsilon RI-dependent signal transduction in mast cells."
    Oda H., Fujimoto M., Patrick M.S., Chida D., Sato Y., Azuma Y., Aoki H., Abe T., Suzuki H., Shirai M.
    J. Immunol. 182:957-962(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAST CELL ACTIVATION, INTERACTION WITH RHOH, ENZYME REGULATION.
  24. Cited for: FUNCTION IN RESPONSE TO FUNGAL PATHOGEN, FUNCTION IN INFLAMMASOME ACTIVATION, FUNCTION IN REGULATION OF TRANSCRIPTION.
  25. "Identification of a dendritic cell receptor that couples sensing of necrosis to immunity."
    Sancho D., Joffre O.P., Keller A.M., Rogers N.C., Martinez D., Hernanz-Falcon P., Rosewell I., Reis e Sousa C.
    Nature 458:899-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IMMUNE SYSTEM STIMULATION BY CELL NECROSIS.

Entry informationi

Entry nameiKSYK_MOUSE
AccessioniPrimary (citable) accession number: P48025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3