SBK2_HUMAN
ID SBK2_HUMAN Reviewed; 348 AA.
AC P0C263;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine/threonine-protein kinase SBK2;
DE EC=2.7.11.1;
DE AltName: Full=SH3-binding domain kinase family member 2;
DE AltName: Full=Sugen kinase 69;
DE Short=SgK069;
GN Name=SBK2; Synonyms=SGK069;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=12471243; DOI=10.1126/science.1075762;
RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.;
RT "The protein kinase complement of the human genome.";
RL Science 298:1912-1934(2002).
RN [3]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-20; GLU-41 AND ASP-102.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. STKL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC008735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS42631.1; -.
DR RefSeq; NP_001094871.2; NM_001101401.2.
DR RefSeq; XP_006723390.1; XM_006723327.3.
DR AlphaFoldDB; P0C263; -.
DR SMR; P0C263; -.
DR IntAct; P0C263; 6.
DR STRING; 9606.ENSP00000389015; -.
DR BioMuta; SBK2; -.
DR DMDM; 254763329; -.
DR PaxDb; P0C263; -.
DR PeptideAtlas; P0C263; -.
DR PRIDE; P0C263; -.
DR Antibodypedia; 33118; 50 antibodies from 16 providers.
DR Ensembl; ENST00000344158.4; ENSP00000345044.3; ENSG00000187550.9.
DR Ensembl; ENST00000413299.6; ENSP00000389015.2; ENSG00000187550.9.
DR MANE-Select; ENST00000413299.6; ENSP00000389015.2; NM_001370096.2; NP_001357025.1.
DR UCSC; uc032ifw.2; human.
DR GeneCards; SBK2; -.
DR HGNC; HGNC:34416; SBK2.
DR HPA; ENSG00000187550; Group enriched (heart muscle, tongue).
DR neXtProt; NX_P0C263; -.
DR OpenTargets; ENSG00000187550; -.
DR VEuPathDB; HostDB:ENSG00000187550; -.
DR eggNOG; KOG1345; Eukaryota.
DR GeneTree; ENSGT00940000161663; -.
DR HOGENOM; CLU_000288_10_0_1; -.
DR InParanoid; P0C263; -.
DR OMA; HRQKGTT; -.
DR OrthoDB; 1221624at2759; -.
DR PhylomeDB; P0C263; -.
DR TreeFam; TF326736; -.
DR PathwayCommons; P0C263; -.
DR SignaLink; P0C263; -.
DR BioGRID-ORCS; 646643; 13 hits in 1101 CRISPR screens.
DR ChiTaRS; SBK2; human.
DR GenomeRNAi; 646643; -.
DR Pharos; P0C263; Tdark.
DR PRO; PR:P0C263; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0C263; protein.
DR Bgee; ENSG00000187550; Expressed in right atrium auricular region and 46 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP 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; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..348
FT /note="Serine/threonine-protein kinase SBK2"
FT /id="PRO_0000262994"
FT DOMAIN 62..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 68..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 20
FT /note="E -> K (in dbSNP:rs34316437)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041077"
FT VARIANT 41
FT /note="A -> E"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041078"
FT VARIANT 102
FT /note="G -> D (in dbSNP:rs56158623)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041079"
SQ SEQUENCE 348 AA; 38088 MW; 2A7E12C4289AC2C7 CRC64;
MPGKQSEEGP AEAGASEDSE EEGLGGLTLE ELQQGQEAAR ALEDMMTLSA QTLVRAEVDE
LYEEVRPLGQ GCYGRVLLVT HRQKGTPLAL KQLPKPRTSL RGFLYEFCVG LSLGAHSAIV
TAYGIGIESA HSYSFLTEPV LHGDLMAFIQ PKVGLPQPAV HRCAAQLASA LEYIHARGLV
YRDLKPENVL VCDPACRRFK LTDFGHTRPR GTLLRLAGPP IPYTAPELCA PPPLPEGLPI
QPALDAWALG VLLFCLLTGY FPWDRPLAEA DPFYEDFLIW QASGQPRDRP QPWFGLAAAA
DALLRGLLDP HPRRRSAVIA IREHLGRPWR QREGEAEAVG AVEEEAGQ
