Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

F1N9Y5 (KSYK_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase SYK

EC=2.7.10.2
Gene names
Name:SYK
ORF Names:RCJMB04_19o18
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3

Catalytic activity

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

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. Downstream signaling adapters and intermediates may mediate positive and/or negative feedback regulation By similarity.

Subcellular location

Cell membrane Probable. Cytoplasmcytosol Probable.

Domain

The SH2 domains mediate the interaction of SYK with the phosphorylated ITAM domains of transmembrane proteins By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.

Contains 1 protein kinase domain.

Contains 2 SH2 domains.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from mutant phenotype Ref.3. Source: UniProtKB

activation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

adaptive immune response

Inferred from mutant phenotype Ref.3. Source: UniProtKB

beta selection

Inferred from electronic annotation. Source: Ensembl

blood vessel morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to molecule of fungal origin

Inferred from sequence or structural similarity. Source: UniProtKB

defense response to bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme linked receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from sequence or structural similarity. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

leukocyte activation involved in immune response

Inferred from sequence or structural similarity. Source: UniProtKB

leukocyte cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

leukotriene biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lymph vessel development

Inferred from sequence or structural similarity. Source: UniProtKB

macrophage activation involved in immune response

Inferred from sequence or structural similarity. Source: UniProtKB

neutrophil activation involved in immune response

Inferred from sequence or structural similarity. Source: UniProtKB

neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of B cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of alpha-beta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of alpha-beta T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone resorption

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of gamma-delta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-3 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell degranulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from mutant phenotype Ref.3. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of arachidonic acid secretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neutrophil degranulation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of platelet activation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of superoxide anion generation

Inferred from sequence or structural similarity. Source: UniProtKB

serotonin secretion by platelet

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentB cell receptor complex

Inferred from electronic annotation. Source: Ensembl

T cell receptor complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

early phagosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from mutant phenotype Ref.3. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 613613Tyrosine-protein kinase SYK
PRO_0000415332

Regions

Domain14 – 10693SH2 1
Domain167 – 25892SH2 2
Domain349 – 613265Protein kinase
Nucleotide binding355 – 3639ATP By similarity
Region107 – 16660Interdomain A
Region259 – 34890Interdomain B

Sites

Active site4721Proton acceptor By similarity
Binding site3801ATP By similarity

Experimental info

Sequence conflict1881N → D in CAG32202. Ref.1
Sequence conflict3981E → G in CAG32202. Ref.1

Sequences

Sequence LengthMass (Da)Tools
F1N9Y5 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: 32783B7D0C8EBC82

FASTA61369,901
        10         20         30         40         50         60 
MASNMANPAN HLPYFFGNIT REEAEEYLMQ GGMSDGLYLL RQSRNYLGGF ALSLAYGRKV 

        70         80         90        100        110        120 
HHYTIERELS GTYAIAGGKS HASPAELINY HSEEADGLIC LLRKSFNRPP GVEPKTGPFE 

       130        140        150        160        170        180 
DLKENLIREY VKQTWNLQGH ALEQAIISQK PQLEKLIATT AHEKMPWFHG RISREESEHR 

       190        200        210        220        230        240 
ILIGSRNNGK FLIRERDSNG SYALCLLNDG KVLHYRIDRD KTGKLSIPDG KRFDTLWQLV 

       250        260        270        280        290        300 
EHYSYKPDGL LRVLSIPCPR HGSESDNVVF DTRPLPGTPS KLQTPIGAPS DDQTPFNPYV 

       310        320        330        340        350        360 
LQRARGLIGA EKGDQREALP MDTEVYESPY ADPDEIKPKN VTLDRKLLTL EEGELGSGNF 

       370        380        390        400        410        420 
GTVKKGFYKM KKGAKPVAVK ILKNESNDPA IKDELLREAN VMQQLDNPYI VRMIGICEAE 

       430        440        450        460        470        480 
AWMLVMEMAE LGPLNKFLQK NRHVTEKNIT ELVHQVSMGM KYLEENNFVH RDLAARNVLL 

       490        500        510        520        530        540 
VTQHYAKISD FGLSKALSAD ENYYKAQSHG KWPVKWYAPE CMNFYKFSSK SDVWSFGVLM 

       550        560        570        580        590        600 
WEAFSYGQKP YKGMKGGEVA QMIERGERME CPEACPVEVY DLMKLCWTYN VDDRPGFVAV 

       610 
ELRLRNYYYD ISH 

« Hide

References

« Hide 'large scale' references
[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.
[2]"Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A. expand/collapse author list , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Red jungle fowl.
[3]"BLNK: a central linker protein in B cell activation."
Fu C., Turck C.W., Kurosaki T., Chan A.C.
Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN B-CELL RECEPTOR SIGNALING PATHWAY, FUNCTION IN PHOSPHORYLATION OF BLNK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ720543 mRNA. Translation: CAG32202.1.
AADN02069860 Genomic DNA. No translation available.
AADN02069861 Genomic DNA. No translation available.
AADN02069862 Genomic DNA. No translation available.
AADN02069863 Genomic DNA. No translation available.
AADN02069864 Genomic DNA. No translation available.
AADN02069865 Genomic DNA. No translation available.
AADN02069866 Genomic DNA. No translation available.
AADN02069867 Genomic DNA. No translation available.
AADN02069868 Genomic DNA. No translation available.
AADN02069869 Genomic DNA. No translation available.
RefSeqNP_001026601.1. NM_001031430.1.
UniGeneGga.22529.

3D structure databases

ProteinModelPortalF1N9Y5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000032170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000032807; ENSGALP00000032170; ENSGALG00000015216.
GeneID427272.
KEGGgga:427272.

Organism-specific databases

CTD6850.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115195.
HOGENOMHOG000113264.
HOVERGENHBG001540.
InParanoidQ5ZJ91.
KOK05855.
OMAKGYYQMK.
OrthoDBEOG7MWGWD.

Family and domain databases

Gene3D1.10.930.10. 1 hit.
3.30.505.10. 2 hits.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PIRSFPIRSF000604. TyrPK_SYK. 1 hit.
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20828556.
PROF1N9Y5.

Entry information

Entry nameKSYK_CHICK
AccessionPrimary (citable) accession number: F1N9Y5
Secondary accession number(s): Q5ZJ91
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: April 16, 2014
This is version 26 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families