Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tyrosine-protein kinase SYK

Gene

Syk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. Involved in interleukin-3/IL3-mediated signaling pathway in basophils (PubMed:19098920). 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).15 Publications

Catalytic activityi

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

Activity 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)DescriptionActionsGraphical viewLength
Binding sitei396ATPPROSITE-ProRule annotation1
Active sitei488Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi371 – 379ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Angiogenesis, Immunity, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 3474
ReactomeiR-MMU-114604 GPVI-mediated activation cascade
R-MMU-2029481 FCGR activation
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-2029485 Role of phospholipids in phagocytosis
R-MMU-2424491 DAP12 signaling
R-MMU-2454202 Fc epsilon receptor (FCERI) signaling
R-MMU-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-2871809 FCERI mediated Ca+2 mobilization
R-MMU-354192 Integrin alphaIIb beta3 signaling
R-MMU-9020558 Interleukin-2 signaling
R-MMU-912631 Regulation of signaling by CBL
R-MMU-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:99515 Syk

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi41R → A: Loss of interaction with FCER1G and TYROBP; when associated with A-194. 1 Publication1
Mutagenesisi194R → A: Loss of interaction with FCER1G and TYROBP; when associated with A-41. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000881661 – 629Tyrosine-protein kinase SYKAdd BLAST629

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphotyrosineBy similarity1
Modified residuei43PhosphoserineBy similarity1
Modified residuei46PhosphotyrosineBy similarity1
Modified residuei130PhosphotyrosineBy similarity1
Modified residuei201PhosphoserineBy similarity1
Modified residuei255PhosphothreonineBy similarity1
Modified residuei270PhosphoserineCombined sources1
Modified residuei289PhosphoserineBy similarity1
Modified residuei290PhosphotyrosineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei310PhosphoserineCombined sources1
Modified residuei311PhosphothreonineBy similarity1
Modified residuei313PhosphoserineCombined sources1
Modified residuei317Phosphotyrosine; by LYNCombined sources1 Publication1
Modified residuei339PhosphothreonineBy similarity1
Modified residuei342PhosphotyrosineCombined sources2 Publications1
Modified residuei344PhosphoserineBy similarity1
Modified residuei346PhosphotyrosineCombined sources1 Publication1
Modified residuei358PhosphotyrosineBy similarity1
Modified residuei373PhosphoserineBy similarity1
Modified residuei378PhosphothreonineBy similarity1
Modified residuei478PhosphotyrosineBy similarity1
Modified residuei501PhosphotyrosineBy similarity1
Modified residuei519Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei520PhosphotyrosineCombined sources1 Publication1
Modified residuei524PhosphothreonineBy similarity1
Modified residuei540PhosphotyrosineCombined sources1
Modified residuei573PhosphoserineBy similarity1
Modified residuei576PhosphothreonineBy similarity1
Modified residuei623PhosphotyrosineCombined sources1
Modified residuei624PhosphotyrosineCombined sources1
Modified residuei625PhosphotyrosineBy similarity1

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

PaxDbiP48025
PeptideAtlasiP48025
PRIDEiP48025

PTM databases

iPTMnetiP48025
PhosphoSitePlusiP48025

Expressioni

Gene expression databases

BgeeiENSMUSG00000021457 Expressed in 202 organ(s), highest expression level in bone marrow
CleanExiMM_SYK
ExpressionAtlasiP48025 baseline and differential
GenevisibleiP48025 MM

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 (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 (PubMed:19098920). 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).By similarity3 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203599, 13 interactors
DIPiDIP-32621N
IntActiP48025, 14 interactors
MINTiP48025
STRINGi10090.ENSMUSP00000060828

Structurei

Secondary structure

1629
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP48025
SMRiP48025
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 106SH2 1PROSITE-ProRule annotationAdd BLAST93
Domaini167 – 258SH2 2PROSITE-ProRule annotationAdd BLAST92
Domaini365 – 625Protein kinasePROSITE-ProRule annotationAdd BLAST261

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni107 – 166Interdomain AAdd BLAST60
Regioni259 – 364Interdomain BAdd BLAST106

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

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiENOG410IH0T Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118799
HOGENOMiHOG000113264
HOVERGENiHBG001540
InParanoidiP48025
KOiK05855
OrthoDBiEOG091G07KU
PhylomeDBiP48025
TreeFamiTF351629

Family and domain databases

CDDicd09938 SH2_N-SH2_Zap70_Syk_like, 1 hit
Gene3Di1.10.930.10, 1 hit
3.30.505.10, 2 hits
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR023420 Kinase_SYK/ZAP-70_inter-SH2_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR035838 SYK/ZAP-70_N_SH2
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR012234 Tyr_kinase_non-rcpt_SYK/ZAP70
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 2 hits
PIRSFiPIRSF000604 TyrPK_SYK, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 2 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF55550 SSF55550, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 2 hits

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PWE9E9PWE9_MOUSE
Tyrosine-protein kinase
Syk
583Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti326Missing in CAA90034 (PubMed:7639745).Curated1
Sequence conflicti446 – 447EL → DV in CAA90034 (PubMed:7639745).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006516895.3
UniGeneiMm.375031

Genome annotation databases

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

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006516895.3
UniGeneiMm.375031

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LCTNMR-B338-350[»]
2MC1NMR-B338-350[»]
ProteinModelPortaliP48025
SMRiP48025
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203599, 13 interactors
DIPiDIP-32621N
IntActiP48025, 14 interactors
MINTiP48025
STRINGi10090.ENSMUSP00000060828

PTM databases

iPTMnetiP48025
PhosphoSitePlusiP48025

Proteomic databases

PaxDbiP48025
PeptideAtlasiP48025
PRIDEiP48025

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6850
MGIiMGI:99515 Syk

Phylogenomic databases

eggNOGiENOG410IH0T Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118799
HOGENOMiHOG000113264
HOVERGENiHBG001540
InParanoidiP48025
KOiK05855
OrthoDBiEOG091G07KU
PhylomeDBiP48025
TreeFamiTF351629

Enzyme and pathway databases

BRENDAi2.7.10.2 3474
ReactomeiR-MMU-114604 GPVI-mediated activation cascade
R-MMU-2029481 FCGR activation
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-2029485 Role of phospholipids in phagocytosis
R-MMU-2424491 DAP12 signaling
R-MMU-2454202 Fc epsilon receptor (FCERI) signaling
R-MMU-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-2871809 FCERI mediated Ca+2 mobilization
R-MMU-354192 Integrin alphaIIb beta3 signaling
R-MMU-9020558 Interleukin-2 signaling
R-MMU-912631 Regulation of signaling by CBL
R-MMU-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

Miscellaneous databases

ChiTaRSiSyk mouse
PROiPR:P48025
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021457 Expressed in 202 organ(s), highest expression level in bone marrow
CleanExiMM_SYK
ExpressionAtlasiP48025 baseline and differential
GenevisibleiP48025 MM

Family and domain databases

CDDicd09938 SH2_N-SH2_Zap70_Syk_like, 1 hit
Gene3Di1.10.930.10, 1 hit
3.30.505.10, 2 hits
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR023420 Kinase_SYK/ZAP-70_inter-SH2_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR035838 SYK/ZAP-70_N_SH2
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR012234 Tyr_kinase_non-rcpt_SYK/ZAP70
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 2 hits
PIRSFiPIRSF000604 TyrPK_SYK, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 2 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF55550 SSF55550, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiKSYK_MOUSE
AccessioniPrimary (citable) accession number: P48025
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: November 7, 2018
This is version 192 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again