SIK1B_HUMAN
ID SIK1B_HUMAN Reviewed; 783 AA.
AC A0A0B4J2F2;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Putative serine/threonine-protein kinase SIK1B {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P57059, ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Salt-inducible kinase 1B {ECO:0000305};
GN Name=SIK1B {ECO:0000305};
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=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable serine/threonine-protein kinase.
CC {ECO:0000250|UniProtKB:P57059}.
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 Evidence={ECO:0000250|UniProtKB:P57059};
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; Evidence={ECO:0000250|UniProtKB:P57059};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- INTERACTION:
CC A0A0B4J2F2; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-22345187, EBI-747500;
CC A0A0B4J2F2; Q68G74: LHX8; NbExp=3; IntAct=EBI-22345187, EBI-8474075;
CC A0A0B4J2F2; Q14696: MESD; NbExp=3; IntAct=EBI-22345187, EBI-6165891;
CC A0A0B4J2F2; P78337: PITX1; NbExp=3; IntAct=EBI-22345187, EBI-748265;
CC A0A0B4J2F2; Q9NRG1: PRTFDC1; NbExp=3; IntAct=EBI-22345187, EBI-739759;
CC A0A0B4J2F2; P62072: TIMM10; NbExp=3; IntAct=EBI-22345187, EBI-1200391;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. AMPK subfamily. {ECO:0000305}.
CC -!- CAUTION: Product of a dubious gene prediction. The corresponding gene
CC is on a region of chromosome 21 that is known to be an artifactual
CC duplication of another chromosome 21 region in the GRCh38 assembly.
CC This entry may represent an artifactual copy of AC P57059.
CC {ECO:0000305}.
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DR EMBL; CU639417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09495.1; -; Genomic_DNA.
DR CCDS; CCDS82645.1; -.
DR RefSeq; NP_001307572.1; NM_001320643.2.
DR AlphaFoldDB; A0A0B4J2F2; -.
DR SMR; A0A0B4J2F2; -.
DR IntAct; A0A0B4J2F2; 6.
DR STRING; 9606.ENSP00000482829; -.
DR iPTMnet; A0A0B4J2F2; -.
DR PhosphoSitePlus; A0A0B4J2F2; -.
DR BioMuta; ENSG00000275993; -.
DR jPOST; A0A0B4J2F2; -.
DR MassIVE; A0A0B4J2F2; -.
DR PeptideAtlas; A0A0B4J2F2; -.
DR Antibodypedia; 76132; 39 antibodies from 3 providers.
DR DNASU; 102724428; -.
DR GeneID; 102724428; -.
DR KEGG; hsa:102724428; -.
DR DisGeNET; 102724428; -.
DR GeneCards; SIK1B; -.
DR HPA; ENSG00000275993; Tissue enhanced (skin).
DR MalaCards; SIK1B; -.
DR neXtProt; NX_A0A0B4J2F2; -.
DR OpenTargets; ENSG00000275993; -.
DR VEuPathDB; HostDB:ENSG00000275993; -.
DR eggNOG; KOG0586; Eukaryota.
DR GeneTree; ENSGT00940000154989; -.
DR HOGENOM; CLU_000288_87_2_1; -.
DR OMA; YNHIHIV; -.
DR OrthoDB; 1127668at2759; -.
DR PathwayCommons; A0A0B4J2F2; -.
DR BioGRID-ORCS; 102724428; 0 hits in 4 CRISPR screens.
DR ChiTaRS; SIK1B; human.
DR GenomeRNAi; 102724428; -.
DR Pharos; A0A0B4J2F2; Tdark.
DR PRO; PR:A0A0B4J2F2; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; A0A0B4J2F2; protein.
DR Bgee; ENSG00000275993; Expressed in skin of abdomen and 94 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd14071; STKc_SIK; 1.
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 InterPro; IPR017090; Ser/Thr_kinase_SIK1/2.
DR InterPro; IPR034672; SIK.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037014; Ser/Thr_PK_SNF1-like; 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.
DR PROSITE; PS50030; UBA; 1.
PE 5: Uncertain;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..783
FT /note="Putative serine/threonine-protein kinase SIK1B"
FT /id="PRO_0000444512"
FT DOMAIN 27..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 303..343
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 353..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 783 AA; 84930 MW; 0A1B6D67DD2EC90E CRC64;
MVIMSEFSAD PAGQGQGQQK PLRVGFYDIE RTLGKGNFAV VKLARHRVTK TQVAIKIIDK
TRLDSSNLEK IYREVQLMKL LNHPHIIKLY QVMETKDMLY IVTEFAKNGE MFDYLTSNGH
LSENEARKKF WQILSAVEYC HDHHIVHRDL KTENLLLDGN MDIKLADFGF GNFYKSGEPL
STWCGSPPYA APEVFEGKEY EGPQLDIWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR
FRIPFFMSQD CESLIRRMLV VDPARRITIA QIRQHRWMRA EPCLPGPACP AFSAHSYTSN
LGDYDEQALG IMQTLGVDRQ RTVESLQNSS YNHFAAIYYL LLERLKEYRN AQCARPGPAR
QPRPRSSDLS GLEVPQEGLS TDPFRPALLC PQPQTLVQSV LQAEMDCELQ SSLQWPLFFP
VDASCSGVFR PRPVSPSSLL DTAISEEARQ GPGLEEEQDT QESLPSSTGR RHTLAEVSTR
LSPLTAPCIV VSPSTTASPA EGTSSDSCLT FSASKSPAGL SGTPATQGLL GACSPVRLAS
PFLGSQSATP VLQAQGGLGG AVLLPVSFQE GRRASDTSLT QGLKAFRQQL RKTTRTKGFL
GLNKIKGLAR QVCQVPASRA SRGGLSPFHA PAQSPGLHGG AAGSREGWSL LEEVLEQQRL
LQLQHHPAAA PGCSQAPQPA PAPFVIAPCD GPGAAPLPST LLTSGLPLLP PPLLQTGASP
VASAAQLLDT HLHIGTGPTA LPAVPPPRLA RLAPGCEPLG LLQGDCEMED LMPCSLGTFV
LVQ
