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Database: UniProt
Entry: P43405
LinkDB: P43405
Original site: P43405 
ID   KSYK_HUMAN              Reviewed;         635 AA.
AC   P43405;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-SEP-2014, entry version 171.
DE   RecName: Full=Tyrosine-protein kinase SYK;
DE            EC=2.7.10.2;
DE   AltName: Full=Spleen tyrosine kinase;
DE   AltName: Full=p72-Syk;
GN   Name=SYK;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7513161; DOI=10.1006/bbrc.1994.1409;
RA   Yagi S., Suzuki K., Hasegawa A., Okumura K., Ra C.;
RT   "Cloning of the cDNA for the deleted syk kinase homologous to ZAP-70
RT   from human basophilic leukemia cell line (KU812).";
RL   Biochem. Biophys. Res. Commun. 200:28-34(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND
RP   AUTOPHOSPHORYLATION.
RX   PubMed=8163536;
RA   Law C.-L., Sidorenko S.P., Chandran K.A., Draves K.E., Chan A.C.,
RA   Weiss A., Edelhoff S., Disteche C.M., Clark E.A.;
RT   "Molecular cloning of human Syk. A B cell protein-tyrosine kinase
RT   associated with the surface immunoglobulin M-B cell receptor
RT   complex.";
RL   J. Biol. Chem. 269:12310-12319(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
RC   TISSUE=Eye, and Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-635.
RC   TISSUE=Tonsil;
RX   PubMed=8168854; DOI=10.1007/BF00189234;
RA   Mueller B., Cooper L., Terhorst C.;
RT   "Molecular cloning of the human homologue to the pig protein-tyrosine
RT   kinase syk.";
RL   Immunogenetics 39:359-362(1994).
RN   [6]
RP   INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
RX   PubMed=7895172; DOI=10.1016/S1074-7613(95)80040-9;
RA   Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R.,
RA   Bolen J.B., Kieff E.;
RT   "Integral membrane protein 2 of Epstein-Barr virus regulates
RT   reactivation from latency through dominant negative effects on
RT   protein-tyrosine kinases.";
RL   Immunity 2:155-166(1995).
RN   [7]
RP   INTERACTION WITH VAV1.
RX   PubMed=8986718; DOI=10.1016/S1074-7613(00)80273-3;
RA   Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.;
RT   "Functional and physical interactions of Syk family kinases with the
RT   Vav proto-oncogene product.";
RL   Immunity 5:591-604(1996).
RN   [8]
RP   FUNCTION IN PHOSPHORYLATION OF PLCG1, AND INTERACTION WITH PLCG1.
RX   PubMed=8657103;
RA   Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.;
RT   "Phospholipase C-gamma1 interacts with conserved phosphotyrosyl
RT   residues in the linker region of Syk and is a substrate for Syk.";
RL   Mol. Cell. Biol. 16:1305-1315(1996).
RN   [9]
RP   FUNCTION IN PHOSPHORYLATION OF CBL, AND INTERACTION WITH CBL.
RX   PubMed=9535867; DOI=10.1074/jbc.273.15.8867;
RA   Deckert M., Elly C., Altman A., Liu Y.C.;
RT   "Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn
RT   and Syk tyrosine kinases.";
RL   J. Biol. Chem. 273:8867-8874(1998).
RN   [10]
RP   ENZYME REGULATION, AND INTERACTION WITH CBL.
RX   PubMed=9857068; DOI=10.1074/jbc.273.52.35273;
RA   Lupher M.L. Jr., Rao N., Lill N.L., Andoniou C.E., Miyake S.,
RA   Clark E.A., Druker B., Band H.;
RT   "Cbl-mediated negative regulation of the Syk tyrosine kinase. A
RT   critical role for Cbl phosphotyrosine-binding domain binding to Syk
RT   phosphotyrosine 323.";
RL   J. Biol. Chem. 273:35273-35281(1998).
RN   [11]
RP   PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN6, AND ENZYME REGULATION.
RX   PubMed=10458769;
RX   DOI=10.1002/(SICI)1521-4141(199908)29:08<2539::AID-IMMU2539>3.0.CO;2-M;
RA   Brockdorff J., Williams S., Couture C., Mustelin T.;
RT   "Dephosphorylation of ZAP-70 and inhibition of T cell activation by
RT   activated SHP1.";
RL   Eur. J. Immunol. 29:2539-2550(1999).
RN   [12]
RP   INTERACTION WITH SLA.
RX   PubMed=10449770; DOI=10.1073/pnas.96.17.9775;
RA   Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.;
RT   "SLAP, a dimeric adapter protein, plays a functional role in T cell
RT   receptor signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999).
RN   [13]
RP   INTERACTION WITH FCRL3.
RX   PubMed=11162587; DOI=10.1006/bbrc.2000.4213;
RA   Xu M.-J., Zhao R., Zhao Z.J.;
RT   "Molecular cloning and characterization of SPAP1, an inhibitory
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 280:768-775(2001).
RN   [14]
RP   FUNCTION IN B-CELL RECEPTOR SIGNALING PATHWAY, AND FUNCTION IN
RP   PHOSPHORYLATION OF BLNK.
RX   PubMed=12456653; DOI=10.1093/emboj/cdf658;
RA   Chiu C.W., Dalton M., Ishiai M., Kurosaki T., Chan A.C.;
RT   "BLNK: molecular scaffolding through 'cis'-mediated organization of
RT   signaling proteins.";
RL   EMBO J. 21:6461-6472(2002).
RN   [15]
RP   FUNCTION IN CELL ADHESION, AND INTERACTION WITH SELPLG AND MSN.
RX   PubMed=12387735; DOI=10.1016/S1074-7613(02)00420-X;
RA   Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A.,
RA   Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J.,
RA   Sanchez-Madrid F.;
RT   "ITAM-based interaction of ERM proteins with Syk mediates signaling by
RT   the leukocyte adhesion receptor PSGL-1.";
RL   Immunity 17:401-412(2002).
RN   [16]
RP   INTERACTION WITH ITGB3.
RX   PubMed=11940607; DOI=10.1083/jcb.200112113;
RA   Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L.,
RA   Brugge J.S., Lowell C.A., Shattil S.J.;
RT   "Coordinate interactions of Csk, Src, and Syk kinases with
RT   [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton.";
RL   J. Cell Biol. 157:265-275(2002).
RN   [17]
RP   FUNCTION IN PHOSPHORYLATION OF LCP2.
RX   PubMed=15388330; DOI=10.1016/j.febslet.2004.07.090;
RA   Shim E.K., Moon C.S., Lee G.Y., Ha Y.J., Chae S.K., Lee J.R.;
RT   "Association of the Src homology 2 domain-containing leukocyte
RT   phosphoprotein of 76 kD (SLP-76) with the p85 subunit of
RT   phosphoinositide 3-kinase.";
RL   FEBS Lett. 575:35-40(2004).
RN   [18]
RP   INTERACTION WITH BLNK, ENZYME REGULATION, MUTAGENESIS OF TYR-630, AND
RP   PHOSPHORYLATION AT TYR-630.
RX   PubMed=18369315; DOI=10.1038/emboj.2008.62;
RA   Kulathu Y., Hobeika E., Turchinovich G., Reth M.;
RT   "The kinase Syk as an adaptor controlling sustained calcium signalling
RT   and B-cell development.";
RL   EMBO J. 27:1333-1344(2008).
RN   [19]
RP   ENZYME REGULATION.
RX   PubMed=18818202; DOI=10.1074/jbc.M806340200;
RA   Tsang E., Giannetti A.M., Shaw D., Dinh M., Tse J.K., Gandhi S.,
RA   Ho H., Wang S., Papp E., Bradshaw J.M.;
RT   "Molecular mechanism of the Syk activation switch.";
RL   J. Biol. Chem. 283:32650-32659(2008).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-323, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [23]
RP   INTERACTION WITH CLEC1B.
RX   PubMed=20154219; DOI=10.1182/blood-2009-08-237834;
RA   Hughes C.E., Pollitt A.Y., Mori J., Eble J.A., Tomlinson M.G.,
RA   Hartwig J.H., O'Callaghan C.A., Fuetterer K., Watson S.P.;
RT   "CLEC-2 activates Syk through dimerization.";
RL   Blood 115:2947-2955(2010).
RN   [24]
RP   INTERACTION WITH USP25, AND FUNCTION.
RX   PubMed=19909739; DOI=10.1016/j.yexcr.2009.10.023;
RA   Cholay M., Reverdy C., Benarous R., Colland F., Daviet L.;
RT   "Functional interaction between the ubiquitin-specific protease 25 and
RT   the SYK tyrosine kinase.";
RL   Exp. Cell Res. 316:667-675(2010).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [26]
RP   PHOSPHORYLATION AT TYR-28; SER-44; TYR-47; TYR-131; SER-202; THR-256;
RP   SER-295; TYR-296; SER-297; SER-316; THR-317; SER-319; TYR-323;
RP   THR-345; TYR-348; SER-350; TYR-352; TYR-364; SER-379; THR-384;
RP   TYR-484; TYR-507; TYR-525; TYR-526; THR-530; SER-579; THR-582;
RP   TYR-629; TYR-630 AND TYR-631, INTERACTION WITH YWHAG, AND MUTAGENESIS
RP   OF SER-297.
RC   TISSUE=B-cell;
RX   PubMed=21469132; DOI=10.1002/eji.201041326;
RA   Bohnenberger H., Oellerich T., Engelke M., Hsiao H.H., Urlaub H.,
RA   Wienands J.;
RT   "Complex phosphorylation dynamics control the composition of the Syk
RT   interactome in B cells.";
RL   Eur. J. Immunol. 41:1550-1562(2011).
RN   [27]
RP   INTERACTION WITH GCSAM.
RX   PubMed=23299888; DOI=10.1038/ncomms2334;
RA   Romero-Camarero I., Jiang X., Natkunam Y., Lu X., Vicente-Duenas C.,
RA   Gonzalez-Herrero I., Flores T., Garcia J.L., McNamara G., Kunder C.,
RA   Zhao S., Segura V., Fontan L., Martinez-Climent J.A.,
RA   Garcia-Criado F.J., Theis J.D., Dogan A., Campos-Sanchez E.,
RA   Green M.R., Alizadeh A.A., Cobaleda C., Sanchez-Garcia I.,
RA   Lossos I.S.;
RT   "Germinal centre protein HGAL promotes lymphoid hyperplasia and
RT   amyloidosis via BCR-mediated Syk activation.";
RL   Nat. Commun. 4:1338-1338(2013).
RN   [28]
RP   STRUCTURE BY NMR OF 163-265.
RX   PubMed=8590001; DOI=10.1016/S0969-2126(01)00242-8;
RA   Narula S.S., Yuan R.W., Adams S.E., Green O.M., Green J.,
RA   Philips T.B., Zydowsky L.D., Botfield M.C., Hatada M., Laird E.R.,
RA   Zoller M.J., Karas J.L., Dalgarno D.C.;
RT   "Solution structure of the C-terminal SH2 domain of the human tyrosine
RT   kinase Syk complexed with a phosphotyrosine pentapeptide.";
RL   Structure 3:1061-1073(1995).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF SH2 DOMAINS IN COMPLEX WITH
RP   CD3E PHOSPHORYLATED ITAM DOMAIN.
RX   PubMed=9698567; DOI=10.1006/jmbi.1998.1964;
RA   Fuetterer K., Wong J., Grucza R.A., Chan A.C., Waksman G.;
RT   "Structural basis for Syk tyrosine kinase ubiquity in signal
RT   transduction pathways revealed by the crystal structure of its
RT   regulatory SH2 domains bound to a dually phosphorylated ITAM
RT   peptide.";
RL   J. Mol. Biol. 281:523-537(1998).
CC   -!- FUNCTION: Non-receptor tyrosine kinase which mediates signal
CC       transduction downstream of a variety of transmembrane receptors
CC       including classical immunoreceptors like the B-cell receptor
CC       (BCR). Regulates several biological processes including innate and
CC       adaptive immunity, cell adhesion, osteoclast maturation, platelet
CC       activation and vascular development. Assembles into signaling
CC       complexes with activated receptors at the plasma membrane via
CC       interaction between its SH2 domains and the receptor tyrosine-
CC       phosphorylated ITAM domains. The association with the receptor can
CC       also be indirect and mediated by adapter proteins containing ITAM
CC       or partial hemITAM domains. The phosphorylation of the ITAM
CC       domains is generally mediated by SRC subfamily kinases upon
CC       engagement of the receptor. More rarely signal transduction via
CC       SYK could be ITAM-independent. Direct downstream effectors
CC       phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and
CC       BLNK. Initially identified as essential in B-cell receptor (BCR)
CC       signaling, it is necessary for the maturation of B-cells most
CC       probably at the pro-B to pre-B transition. Activated upon BCR
CC       engagement, it phosphorylates and activates BLNK an adapter
CC       linking the activated BCR to downstream signaling adapters and
CC       effectors. It also phosphorylates and activates PLCG1 and the PKC
CC       signaling pathway. It also phosphorylates BTK and regulates its
CC       activity in B-cell antigen receptor (BCR)-coupled signaling.
CC       Beside its function downstream of BCR plays also a role in T-cell
CC       receptor signaling. Plays also a crucial role in the innate immune
CC       response to fungal, bacterial and viral pathogens. It is for
CC       instance activated by the membrane lectin CLEC7A. Upon stimulation
CC       by fungal proteins, CLEC7A together with SYK activates immune
CC       cells inducing the production of ROS. Also activates the
CC       inflammasome and NF-kappa-B-mediated transcription of chemokines
CC       and cytokines in presence of pathogens. Regulates neutrophil
CC       degranulation and phagocytosis through activation of the MAPK
CC       signaling cascade. Also mediates the activation of dendritic cells
CC       by cell necrosis stimuli. Also involved in mast cells activation.
CC       Also functions downstream of receptors mediating cell adhesion.
CC       Relays for instance, integrin-mediated neutrophils and macrophages
CC       activation and P-selectin receptor/SELPG-mediated recruitment of
CC       leukocytes to inflammatory loci. Plays also a role in non-immune
CC       processes. It is for instance involved in vascular development
CC       where it may regulate blood and lymphatic vascular separation. It
CC       is also required for osteoclast development and function.
CC       Functions in the activation of platelets by collagen, mediating
CC       PLCG2 phosphorylation and activation. May be coupled to the
CC       collagen receptor by the ITAM domain-containing FCER1G. Also
CC       activated by the membrane lectin CLEC1B that is required for
CC       activation of platelets by PDPN/podoplanin. Involved in platelet
CC       adhesion being activated by ITGB3 engaged by fibrinogen.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- ENZYME REGULATION: Autoinhibited. Intramolecular binding of the
CC       interdomains A and B (also called linker region) to parts of the
CC       catalytic domain keep the catalytic center in an inactive
CC       conformation. The phosphorylation of the interdomains or the
CC       binding of the SH2 domains with dually phosphorylated ITAM domains
CC       on transmembrane proteins disrupt those intramolecular
CC       interactions allowing the kinase domain to adopt an active
CC       conformation. The phosphorylation of SYK and of the ITAM domains
CC       which is responsible for SYK activation is essentially mediated by
CC       SRC subfamily kinases, like LYN, upon transmembrane receptors
CC       engagement. May also be negatively regulated by PTPN6 through
CC       dephosphorylation. Downstream signaling adapters and intermediates
CC       like BLNK or RHOH may mediate positive and/or negative feedback
CC       regulation. Negatively regulated by CBL and CBLB through
CC       ubiquitination and probable degradation. Phosphorylates SH3BP2
CC       which in turn may regulate SYK through LYN (By similarity).
CC   -!- SUBUNIT: Interacts with LYN; phosphorylates SYK (By similarity).
CC       Interacts with RHOH (phosphorylated); regulates mast cells
CC       activation (By similarity). Interacts with NFAM1 (phosphorylated);
CC       probably involved in BCR signaling (By similarity). Interacts with
CC       VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR activation.
CC       Interacts with GAB2 (phosphorylated); probably involved in IgE Fc
CC       receptor signaling (By similarity). Interacts (via its SH2
CC       domains) with CD79A (via its phosphorylated ITAM domain); the
CC       interaction stimulates SYK autophosphorylation and activation (By
CC       similarity). Interacts with FCRL3. Interacts (via SH2 domains)
CC       with FCER1G (via ITAM domain); activates SYK and mediates
CC       neutrophils and macrophages integrin-mediated activation (By
CC       similarity). Interacts with ITGB2 and FGR; involved in ITGB2
CC       downstream signaling (By similarity). Interacts with ITGB3; upon
CC       activation by ITGB3 promotes platelet adhesion. Interacts (via SH2
CC       domains) with TYROBP (via ITAM domain); involved in neutrophils
CC       and macrophages integrin-mediated activation (By similarity).
CC       Interacts with MSN and SELPLG; mediates the selectin-dependent
CC       activation of SYK by SELPLG. Interacts with BLNK (via SH2 domain).
CC       Interacts (via the second SH2 domain) with USP25 (via C-terminus);
CC       phosphorylates USP25 and regulates USP25 intracellular levels.
CC       Interacts (via SH2 domains) with CLEC1B (dimer). Interacts with
CC       CLEC7A; participates in leukocyte activation in presence of fungal
CC       pathogens. Interacts (phosphorylated) with SLA; may regulate SYK
CC       through CBL recruitment. Interacts with YWHAG; attenuates BCR-
CC       induced membrane translocation and activation of SYK. Interacts
CC       with Epstein-Barr virus LMP2A. Interacts (via SH2 domains) with
CC       GCSAM; the interaction increases after B-cell receptor
CC       stimulation, resulting in enhanced SYK autophosphorylation and
CC       activity.
CC   -!- INTERACTION:
CC       P22681:CBL; NbExp=2; IntAct=EBI-78302, EBI-518228;
CC       P20273:CD22; NbExp=4; IntAct=EBI-78302, EBI-78277;
CC       P11049:CD37; NbExp=3; IntAct=EBI-78302, EBI-6139068;
CC       P07766:CD3E; NbExp=6; IntAct=EBI-78302, EBI-1211297;
CC       P00533:EGFR; NbExp=6; IntAct=EBI-78302, EBI-297353;
CC       P04626:ERBB2; NbExp=7; IntAct=EBI-78302, EBI-641062;
CC       P21860:ERBB3; NbExp=6; IntAct=EBI-78302, EBI-720706;
CC       P30273:FCER1G; NbExp=2; IntAct=EBI-78302, EBI-515289;
CC       Q13480:GAB1; NbExp=4; IntAct=EBI-78302, EBI-517684;
CC       P06239:LCK; NbExp=7; IntAct=EBI-78302, EBI-1348;
CC       P08581:MET; NbExp=3; IntAct=EBI-78302, EBI-1039152;
CC       P19174:PLCG1; NbExp=4; IntAct=EBI-78302, EBI-79387;
CC       Q8TF42:UBASH3B; NbExp=2; IntAct=EBI-78302, EBI-1380492;
CC   -!- SUBCELLULAR LOCATION: Cell membrane (Probable). Cytoplasm, cytosol
CC       (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P43405-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P43405-2; Sequence=VSP_005010;
CC   -!- TISSUE SPECIFICITY: Widely expressed in hematopoietic cells (at
CC       protein level). Within the B-cells compartment it is for instance
CC       expressed for pro-B-cells to plasma cells.
CC   -!- DOMAIN: The SH2 domains mediate the interaction of SYK with the
CC       phosphorylated ITAM domains of transmembrane proteins. Some
CC       proteins like CLEC1B have a partial ITAM domain (also called
CC       hemITAM) containing a single YxxL motif. The interaction with SYK
CC       requires CLEC1B homodimerization.
CC   -!- PTM: Ubiquitinated by CBLB after BCR activation; which promotes
CC       proteasomal degradation (By similarity).
CC   -!- PTM: Autophosphorylated. Phosphorylated on tyrosine residues by
CC       LYN following receptors engagement. Phosphorylation on Tyr-323
CC       creates a binding site for CBL, an adapter protein that serves as
CC       a negative regulator of BCR-stimulated calcium ion signaling.
CC       Phosphorylation at Tyr-348 creates a binding site for VAV1.
CC       Phosphorylation on Tyr-348 and Tyr-352 enhances the
CC       phosphorylation and activation of phospholipase C-gamma and the
CC       early phase of calcium ion mobilization via a phosphoinositide 3-
CC       kinase-independent pathway (By similarity). Phosphorylation on
CC       Ser-297 is very common, it peaks 5 minutes after BCR stimulation,
CC       and creates a binding site for YWHAG. Phosphorylation at Tyr-630
CC       creates a binding site for BLNK. Dephosphorylated by PTPN6.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SYK/ZAP-70 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH2 domains.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SYKID394.html";
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DR   EMBL; Z29630; CAA82737.1; -; mRNA.
DR   EMBL; L28824; AAA36526.1; -; mRNA.
DR   EMBL; AL354862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001645; AAH01645.1; -; mRNA.
DR   EMBL; BC011399; AAH11399.1; -; mRNA.
DR   EMBL; BC002962; AAH02962.1; -; mRNA.
DR   EMBL; X73568; CAA51970.1; -; mRNA.
DR   CCDS; CCDS47992.1; -. [P43405-2]
DR   CCDS; CCDS6688.1; -. [P43405-1]
DR   PIR; A53596; A53596.
DR   RefSeq; NP_001128524.1; NM_001135052.3. [P43405-2]
DR   RefSeq; NP_001167638.1; NM_001174167.2. [P43405-1]
DR   RefSeq; NP_001167639.1; NM_001174168.2. [P43405-2]
DR   RefSeq; NP_003168.2; NM_003177.6. [P43405-1]
DR   RefSeq; XP_005252204.1; XM_005252147.2. [P43405-1]
DR   UniGene; Hs.371720; -.
DR   PDB; 1A81; X-ray; 3.00 A; A/C/E/G/I/K=9-262.
DR   PDB; 1CSY; NMR; -; A=163-265.
DR   PDB; 1CSZ; NMR; -; A=163-265.
DR   PDB; 1XBA; X-ray; 2.00 A; A=356-635.
DR   PDB; 1XBB; X-ray; 1.57 A; A=356-635.
DR   PDB; 1XBC; X-ray; 2.00 A; A=356-635.
DR   PDB; 3BUW; X-ray; 1.45 A; A/C=317-329.
DR   PDB; 3EMG; X-ray; 2.60 A; A=349-635.
DR   PDB; 3FQE; X-ray; 2.50 A; A=356-635.
DR   PDB; 3FQH; X-ray; 2.26 A; A/B=356-635.
DR   PDB; 3FQS; X-ray; 2.10 A; A=356-635.
DR   PDB; 3SRV; X-ray; 1.95 A; A/B=360-635.
DR   PDB; 3TUB; X-ray; 2.23 A; A=343-635.
DR   PDB; 3TUC; X-ray; 2.10 A; A=343-635.
DR   PDB; 3TUD; X-ray; 2.33 A; A=343-635.
DR   PDB; 3VF8; X-ray; 2.08 A; A=343-635.
DR   PDB; 3VF9; X-ray; 2.30 A; A=343-635.
DR   PDB; 4DFL; X-ray; 1.98 A; A=363-635.
DR   PDB; 4DFN; X-ray; 2.48 A; A=363-635.
DR   PDB; 4F4P; X-ray; 2.37 A; A=365-635.
DR   PDB; 4FL1; X-ray; 1.79 A; A=356-635.
DR   PDB; 4FL2; X-ray; 2.19 A; A=1-635.
DR   PDB; 4FL3; X-ray; 1.90 A; A=1-635.
DR   PDB; 4FYN; X-ray; 2.32 A; A=356-635.
DR   PDB; 4FYO; X-ray; 1.40 A; A=356-635.
DR   PDB; 4FZ6; X-ray; 1.85 A; A=356-635.
DR   PDB; 4FZ7; X-ray; 1.75 A; A=356-635.
DR   PDB; 4GFG; X-ray; 2.35 A; A=356-635.
DR   PDB; 4I0R; X-ray; 2.10 A; A=356-635.
DR   PDB; 4I0S; X-ray; 1.98 A; A=356-635.
DR   PDB; 4I0T; X-ray; 1.70 A; A=356-635.
DR   PDB; 4PUZ; X-ray; 2.08 A; A/B=356-635.
DR   PDB; 4PV0; X-ray; 2.00 A; A=363-635.
DR   PDB; 4PX6; X-ray; 1.60 A; A=356-635.
DR   PDBsum; 1A81; -.
DR   PDBsum; 1CSY; -.
DR   PDBsum; 1CSZ; -.
DR   PDBsum; 1XBA; -.
DR   PDBsum; 1XBB; -.
DR   PDBsum; 1XBC; -.
DR   PDBsum; 3BUW; -.
DR   PDBsum; 3EMG; -.
DR   PDBsum; 3FQE; -.
DR   PDBsum; 3FQH; -.
DR   PDBsum; 3FQS; -.
DR   PDBsum; 3SRV; -.
DR   PDBsum; 3TUB; -.
DR   PDBsum; 3TUC; -.
DR   PDBsum; 3TUD; -.
DR   PDBsum; 3VF8; -.
DR   PDBsum; 3VF9; -.
DR   PDBsum; 4DFL; -.
DR   PDBsum; 4DFN; -.
DR   PDBsum; 4F4P; -.
DR   PDBsum; 4FL1; -.
DR   PDBsum; 4FL2; -.
DR   PDBsum; 4FL3; -.
DR   PDBsum; 4FYN; -.
DR   PDBsum; 4FYO; -.
DR   PDBsum; 4FZ6; -.
DR   PDBsum; 4FZ7; -.
DR   PDBsum; 4GFG; -.
DR   PDBsum; 4I0R; -.
DR   PDBsum; 4I0S; -.
DR   PDBsum; 4I0T; -.
DR   PDBsum; 4PUZ; -.
DR   PDBsum; 4PV0; -.
DR   PDBsum; 4PX6; -.
DR   ProteinModelPortal; P43405; -.
DR   SMR; P43405; 9-265, 330-635.
DR   BioGrid; 112717; 95.
DR   DIP; DIP-253N; -.
DR   IntAct; P43405; 34.
DR   MINT; MINT-148486; -.
DR   STRING; 9606.ENSP00000364898; -.
DR   BindingDB; P43405; -.
DR   ChEMBL; CHEMBL2599; -.
DR   GuidetoPHARMACOLOGY; 2230; -.
DR   PhosphoSite; P43405; -.
DR   DMDM; 1174527; -.
DR   MaxQB; P43405; -.
DR   PaxDb; P43405; -.
DR   PeptideAtlas; P43405; -.
DR   PRIDE; P43405; -.
DR   DNASU; 6850; -.
DR   Ensembl; ENST00000375746; ENSP00000364898; ENSG00000165025. [P43405-1]
DR   Ensembl; ENST00000375747; ENSP00000364899; ENSG00000165025. [P43405-2]
DR   Ensembl; ENST00000375751; ENSP00000364904; ENSG00000165025. [P43405-2]
DR   Ensembl; ENST00000375754; ENSP00000364907; ENSG00000165025. [P43405-1]
DR   GeneID; 6850; -.
DR   KEGG; hsa:6850; -.
DR   UCSC; uc004aqz.3; human. [P43405-1]
DR   UCSC; uc004ara.3; human. [P43405-2]
DR   CTD; 6850; -.
DR   GeneCards; GC09P093564; -.
DR   HGNC; HGNC:11491; SYK.
DR   HPA; CAB007773; -.
DR   HPA; HPA001384; -.
DR   MIM; 600085; gene.
DR   neXtProt; NX_P43405; -.
DR   PharmGKB; PA36273; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000113264; -.
DR   HOVERGEN; HBG001540; -.
DR   InParanoid; P43405; -.
DR   KO; K05855; -.
DR   OMA; KGYYQMK; -.
DR   OrthoDB; EOG7MWGWD; -.
DR   PhylomeDB; P43405; -.
DR   TreeFam; TF351629; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   Reactome; REACT_118700; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   Reactome; REACT_147814; DAP12 signaling.
DR   Reactome; REACT_15523; Integrin alphaIIb beta3 signaling.
DR   Reactome; REACT_160086; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; REACT_160158; Role of phospholipids in phagocytosis.
DR   Reactome; REACT_160274; FCGR activation.
DR   Reactome; REACT_163701; FCERI mediated MAPK activation.
DR   Reactome; REACT_163769; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; REACT_163834; FCERI mediated Ca+2 mobilization.
DR   Reactome; REACT_163936; Fc epsilon receptor (FCERI) signaling.
DR   Reactome; REACT_1695; GPVI-mediated activation cascade.
DR   Reactome; REACT_23787; Regulation of signaling by CBL.
DR   Reactome; REACT_27283; Interleukin-2 signaling.
DR   SignaLink; P43405; -.
DR   EvolutionaryTrace; P43405; -.
DR   GeneWiki; Syk; -.
DR   GenomeRNAi; 6850; -.
DR   NextBio; 26739; -.
DR   PRO; PR:P43405; -.
DR   Bgee; P43405; -.
DR   CleanEx; HS_SYK; -.
DR   Genevestigator; P43405; -.
DR   GO; GO:0019815; C:B cell receptor complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IC:UniProtKB.
DR   GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0042101; C:T cell receptor complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; NAS:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
DR   GO; GO:0004716; F:receptor signaling protein tyrosine kinase activity; IEA:Ensembl.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IEA:Ensembl.
DR   GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043366; P:beta selection; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR   GO; GO:0071226; P:cellular response to molecule of fungal origin; ISS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; IEA:Ensembl.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0002366; P:leukocyte activation involved in immune response; ISS:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001945; P:lymph vessel development; ISS:UniProtKB.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; ISS:UniProtKB.
DR   GO; GO:0002283; P:neutrophil activation involved in immune response; ISS:UniProtKB.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR   GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
DR   GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0045425; P:positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045401; P:positive regulation of interleukin-3 biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0090237; P:regulation of arachidonic acid secretion; ISS:UniProtKB.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0043313; P:regulation of neutrophil degranulation; ISS:UniProtKB.
DR   GO; GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
DR   GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
DR   GO; GO:0032928; P:regulation of superoxide anion generation; ISS:UniProtKB.
DR   GO; GO:0002554; P:serotonin secretion by platelet; ISS:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.930.10; -; 1.
DR   Gene3D; 3.30.505.10; -; 2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 2.
DR   PIRSF; PIRSF000604; TyrPK_SYK; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF55550; SSF55550; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Alternative splicing; Angiogenesis;
KW   ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
KW   Host-virus interaction; Immunity; Innate immunity; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; SH2 domain; Transferase; Tyrosine-protein kinase;
KW   Ubl conjugation.
FT   CHAIN         1    635       Tyrosine-protein kinase SYK.
FT                                /FTId=PRO_0000088165.
FT   DOMAIN       15    107       SH2 1.
FT   DOMAIN      168    259       SH2 2.
FT   DOMAIN      371    631       Protein kinase.
FT   NP_BIND     377    385       ATP (By similarity).
FT   REGION      108    167       Interdomain A.
FT   REGION      260    370       Interdomain B.
FT   ACT_SITE    494    494       Proton acceptor (By similarity).
FT   BINDING     402    402       ATP (By similarity).
FT   MOD_RES      28     28       Phosphotyrosine.
FT   MOD_RES      44     44       Phosphoserine.
FT   MOD_RES      47     47       Phosphotyrosine.
FT   MOD_RES     131    131       Phosphotyrosine.
FT   MOD_RES     202    202       Phosphoserine.
FT   MOD_RES     256    256       Phosphothreonine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     296    296       Phosphotyrosine.
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     316    316       Phosphoserine.
FT   MOD_RES     317    317       Phosphothreonine.
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     323    323       Phosphotyrosine; by LYN.
FT   MOD_RES     345    345       Phosphothreonine.
FT   MOD_RES     348    348       Phosphotyrosine.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     352    352       Phosphotyrosine.
FT   MOD_RES     364    364       Phosphotyrosine.
FT   MOD_RES     379    379       Phosphoserine.
FT   MOD_RES     384    384       Phosphothreonine.
FT   MOD_RES     484    484       Phosphotyrosine.
FT   MOD_RES     507    507       Phosphotyrosine.
FT   MOD_RES     525    525       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     526    526       Phosphotyrosine.
FT   MOD_RES     530    530       Phosphothreonine.
FT   MOD_RES     546    546       Phosphotyrosine (By similarity).
FT   MOD_RES     579    579       Phosphoserine.
FT   MOD_RES     582    582       Phosphothreonine.
FT   MOD_RES     629    629       Phosphotyrosine.
FT   MOD_RES     630    630       Phosphotyrosine.
FT   MOD_RES     631    631       Phosphotyrosine.
FT   VAR_SEQ     283    305       Missing (in isoform Short).
FT                                /FTId=VSP_005010.
FT   VARIANT      45     45       R -> H (in dbSNP:rs16906862).
FT                                /FTId=VAR_033838.
FT   MUTAGEN     297    297       S->A: Abolishes YWHAG binding.
FT   MUTAGEN     630    630       Y->F: Loss of interaction with BLNK.
FT   CONFLICT    119    119       P -> A (in Ref. 5; CAA51970).
FT   CONFLICT    250    250       G -> P (in Ref. 5; CAA51970).
FT   HELIX        22     31
FT   STRAND       38     43
FT   STRAND       47     49
FT   STRAND       51     57
FT   STRAND       60     68
FT   STRAND       74     76
FT   STRAND       82     84
FT   HELIX        85     92
FT   STRAND       99    101
FT   HELIX       119    136
FT   HELIX       140    158
FT   HELIX       163    165
FT   STRAND      169    172
FT   HELIX       175    183
FT   STRAND      184    186
FT   STRAND      187    189
FT   STRAND      192    201
FT   STRAND      203    209
FT   STRAND      212    220
FT   STRAND      221    224
FT   STRAND      226    228
FT   STRAND      229    231
FT   STRAND      234    236
FT   HELIX       237    244
FT   STRAND      251    253
FT   HELIX       342    344
FT   HELIX       346    348
FT   HELIX       351    353
FT   STRAND      361    364
FT   HELIX       367    369
FT   STRAND      370    372
FT   STRAND      376    379
FT   STRAND      381    391
FT   STRAND      393    403
FT   HELIX       406    409
FT   HELIX       412    425
FT   STRAND      435    449
FT   HELIX       456    462
FT   HELIX       468    487
FT   HELIX       497    499
FT   STRAND      500    504
FT   STRAND      507    510
FT   HELIX       515    518
FT   STRAND      524    527
FT   HELIX       536    538
FT   HELIX       541    546
FT   STRAND      548    550
FT   HELIX       551    566
FT   TURN        567    569
FT   TURN        572    575
FT   HELIX       578    586
FT   STRAND      589    591
FT   HELIX       599    608
FT   TURN        613    615
FT   HELIX       619    635
SQ   SEQUENCE   635 AA;  72066 MW;  EAA6BDE65881FC68 CRC64;
     MASSGMADSA NHLPFFFGNI TREEAEDYLV QGGMSDGLYL LRQSRNYLGG FALSVAHGRK
     AHHYTIEREL NGTYAIAGGR THASPADLCH YHSQESDGLV CLLKKPFNRP QGVQPKTGPF
     EDLKENLIRE YVKQTWNLQG QALEQAIISQ KPQLEKLIAT TAHEKMPWFH GKISREESEQ
     IVLIGSKTNG KFLIRARDNN GSYALCLLHE GKVLHYRIDK DKTGKLSIPE GKKFDTLWQL
     VEHYSYKADG LLRVLTVPCQ KIGTQGNVNF GGRPQLPGSH PATWSAGGII SRIKSYSFPK
     PGHRKSSPAQ GNRQESTVSF NPYEPELAPW AADKGPQREA LPMDTEVYES PYADPEEIRP
     KEVYLDRKLL TLEDKELGSG NFGTVKKGYY QMKKVVKTVA VKILKNEAND PALKDELLAE
     ANVMQQLDNP YIVRMIGICE AESWMLVMEM AELGPLNKYL QQNRHVKDKN IIELVHQVSM
     GMKYLEESNF VHRDLAARNV LLVTQHYAKI SDFGLSKALR ADENYYKAQT HGKWPVKWYA
     PECINYYKFS SKSDVWSFGV LMWEAFSYGQ KPYRGMKGSE VTAMLEKGER MGCPAGCPRE
     MYDLMNLCWT YDVENRPGFA AVELRLRNYY YDVVN
//
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