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SBK3_HUMAN
ID   SBK3_HUMAN              Reviewed;         359 AA.
AC   P0C264;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Uncharacterized serine/threonine-protein kinase SBK3;
DE            EC=2.7.11.1;
DE   AltName: Full=SH3-binding domain kinase family member 3;
DE   AltName: Full=Sugen kinase 110;
GN   Name=SBK3; Synonyms=SGK110;
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).
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   -!- INTERACTION:
CC       P0C264; Q13155: AIMP2; NbExp=3; IntAct=EBI-17181801, EBI-745226;
CC       P0C264; O95561: C1orf105; NbExp=3; IntAct=EBI-17181801, EBI-10191951;
CC       P0C264; Q49AN0: CRY2; NbExp=3; IntAct=EBI-17181801, EBI-2212355;
CC       P0C264; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-17181801, EBI-399105;
CC       P0C264; Q13868: EXOSC2; NbExp=3; IntAct=EBI-17181801, EBI-301735;
CC       P0C264; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-17181801, EBI-923440;
CC       P0C264; Q8NHZ7: MBD3L2; NbExp=3; IntAct=EBI-17181801, EBI-11989378;
CC       P0C264; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-17181801, EBI-17490746;
CC       P0C264; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-17181801, EBI-10276663;
CC       P0C264; P84022: SMAD3; NbExp=3; IntAct=EBI-17181801, EBI-347161;
CC       P0C264; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-17181801, EBI-12938570;
CC       P0C264; P13805-3: TNNT1; NbExp=3; IntAct=EBI-17181801, EBI-12151635;
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; CCDS74457.1; -.
DR   RefSeq; NP_001186753.1; NM_001199824.2.
DR   AlphaFoldDB; P0C264; -.
DR   SMR; P0C264; -.
DR   BioGRID; 934928; 13.
DR   IntAct; P0C264; 12.
DR   STRING; 9606.ENSP00000483467; -.
DR   BindingDB; P0C264; -.
DR   ChEMBL; CHEMBL5116; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; P0C264; -.
DR   iPTMnet; P0C264; -.
DR   PhosphoSitePlus; P0C264; -.
DR   BioMuta; SBK3; -.
DR   DMDM; 161783904; -.
DR   jPOST; P0C264; -.
DR   MassIVE; P0C264; -.
DR   PaxDb; P0C264; -.
DR   PeptideAtlas; P0C264; -.
DR   PRIDE; P0C264; -.
DR   Antibodypedia; 70937; 19 antibodies from 7 providers.
DR   DNASU; 100130827; -.
DR   Ensembl; ENST00000612221.1; ENSP00000483467.1; ENSG00000231274.5.
DR   GeneID; 100130827; -.
DR   KEGG; hsa:100130827; -.
DR   MANE-Select; ENST00000612221.1; ENSP00000483467.1; NM_001199824.2; NP_001186753.1.
DR   UCSC; uc032ifx.1; human.
DR   CTD; 100130827; -.
DR   GeneCards; SBK3; -.
DR   HGNC; HGNC:44121; SBK3.
DR   HPA; ENSG00000231274; Tissue enhanced (heart muscle, tongue).
DR   neXtProt; NX_P0C264; -.
DR   OpenTargets; ENSG00000231274; -.
DR   VEuPathDB; HostDB:ENSG00000231274; -.
DR   eggNOG; KOG1345; Eukaryota.
DR   GeneTree; ENSGT00940000154852; -.
DR   HOGENOM; CLU_000288_10_0_1; -.
DR   InParanoid; P0C264; -.
DR   OMA; RPPPPWD; -.
DR   OrthoDB; 1221624at2759; -.
DR   PhylomeDB; P0C264; -.
DR   PathwayCommons; P0C264; -.
DR   SignaLink; P0C264; -.
DR   BioGRID-ORCS; 100130827; 8 hits in 267 CRISPR screens.
DR   GenomeRNAi; 100130827; -.
DR   Pharos; P0C264; Tchem.
DR   PRO; PR:P0C264; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P0C264; protein.
DR   Bgee; ENSG00000231274; Expressed in right atrium auricular region and 66 other tissues.
DR   ExpressionAtlas; P0C264; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..359
FT                   /note="Uncharacterized serine/threonine-protein kinase
FT                   SBK3"
FT                   /id="PRO_0000262995"
FT   DOMAIN          43..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          314..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         49..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   359 AA;  38488 MW;  3E6AFF74412256C9 CRC64;
     MERRASETPE DGDPEEDTAT ALQRLVELTT SRVTPVRSLR DQYHLIRKLG SGSYGRVLLA
     QPHQGGPAVA LKLLRRDLVL RSTFLREFCV GRCVSAHPGL LQTLAGPLQT PRYFAFAQEY
     APCGDLSGML QERGLPELLV KRVVAQLAGA LDFLHSRGLV HADVKPDNVL VFDPVCSRVA
     LGDLGLTRPE GSPTPAPPVP LPTAPPELCL LLPPDTLPLR PAVDSWGLGV LLFCAATACF
     PWDVALAPNP EFEAFAGWVT TKPQPPQPPP PWDQFAPPAL ALLQGLLDLD PETRSPPLAV
     LDFLGDDWGL QGNREGPGVL GSAVSYEDRE EGGSSLEEWT DEGDDSKSGG RTGTDGGAP
 
 
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