SHKB_DICDI
ID SHKB_DICDI Reviewed; 653 AA.
AC Q54IP4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Dual specificity protein kinase shkB;
DE EC=2.7.11.1;
DE AltName: Full=SH2 domain-containing protein 2;
DE AltName: Full=SH2 domain-containing protein B;
GN Name=shkB; ORFNames=DDB_G0288617;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15073273; DOI=10.1074/mcp.m300131-mcp200;
RA Gao Q., Hua J., Kimura R., Headd J.J., Fu X.-Y., Chin Y.E.;
RT "Identification of the linker-SH2 domain of STAT as the origin of the SH2
RT domain using two-dimensional structural alignment.";
RL Mol. Cell. Proteomics 3:704-714(2004).
CC -!- FUNCTION: Required for proper chemotaxis and phagocytosis; proper
CC spatiotemporal control of F-actin levels in chemotaxing cells. Negative
CC regulator of the PI3K (phosphatidylinositol 3 kinase) pathway.
CC Predominantly phosphorylates serines and threonines and tyrosines at a
CC lower level (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. SH2 domain-containing protein kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000119; EAL63133.1; -; Genomic_DNA.
DR RefSeq; XP_636635.1; XM_631543.1.
DR AlphaFoldDB; Q54IP4; -.
DR SMR; Q54IP4; -.
DR BioGRID; 1251719; 1.
DR STRING; 44689.DDB0229941; -.
DR PaxDb; Q54IP4; -.
DR PRIDE; Q54IP4; -.
DR EnsemblProtists; EAL63133; EAL63133; DDB_G0288617.
DR GeneID; 8626716; -.
DR KEGG; ddi:DDB_G0288617; -.
DR dictyBase; DDB_G0288617; shkB.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_024030_0_0_1; -.
DR InParanoid; Q54IP4; -.
DR OMA; VFEENTM; -.
DR PhylomeDB; Q54IP4; -.
DR Reactome; R-DDI-3295583; TRP channels.
DR Reactome; R-DDI-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death.
DR PRO; PR:Q54IP4; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..653
FT /note="Dual specificity protein kinase shkB"
FT /id="PRO_0000327809"
FT DOMAIN 174..432
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 534..625
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 112..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 180..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 653 AA; 73807 MW; 5968FDC60AAA3AAE CRC64;
MNDKISKLES SILQLTEEVK QLESKQASKE LEIRTLVDNA INSQNPAQER ELINKLFTES
LIDLKLKAEK IQTLERYRQE IITNLLVEQK QPNDTSIISA WEQLKISSFR INPNNNNNNS
NNTNSSDSNQ NYSSVILNGS LTEDSTSTIS PDSTKNRDEE EIIRWEIDRN EISYNREAKL
GSGAFGSVYK GIVRGKEVAI KKLTQTVFEE NTMNEFKKEV SLMAKLRNPH LLLFMGACTA
PEDLSIVTEL MPKGSVHSLL RAKEDTSDFI TFKRAILIAR DTVLGMTWLH ASNILHLDLK
PANLLVDQNW VVKVADFGLS KYMKPDSKDK LLGQAGSPLY MAPEMLVNQP YDGKVDVFSF
SILLWELLTK QEPYNKLYSS YPQLVEGVVN KKNRPIIPDY FPTRLKDLLA RCWDHYPSRR
PSFAEISKQR ILETILIDGL ILDSSARQFW SQYYMGKEEV PWNSFIVNFS LYCGFESNLS
ADDIKIKFLK LLLVPVDSDM VTIDNFGKIL TWVGPLTNGR EFFDKVYSIC SIKGFMAATS
SKNASQYLAG KKTGTYILRF SSDPGSYAIS YLNKNKEIIH ARVIYKQGSG YIHHGGQTHY
ATLDDLIKNT FKSLGIKEPF EGGPFHALTV AASSSKPFNI AGAYIPVAPS KKI
