KS6AA_CHICK
ID KS6AA_CHICK Reviewed; 752 AA.
AC P18652;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ribosomal protein S6 kinase 2 alpha;
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase-activated protein kinase 1;
DE Short=MAPK-activated protein kinase 1;
DE Short=MAPKAP kinase 1;
DE Short=MAPKAPK-1;
DE AltName: Full=Ribosomal protein S6 kinase II alpha;
DE Short=S6KII-alpha;
DE AltName: Full=p90-RSK;
GN Name=RPS6KA; Synonyms=RSK;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2779569; DOI=10.1128/mcb.9.9.3850-3859.1989;
RA Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W.,
RA Erikson R.L.;
RT "Sequence and expression of chicken and mouse rsk: homologs of Xenopus
RT laevis ribosomal S6 kinase.";
RL Mol. Cell. Biol. 9:3850-3859(1989).
CC -!- FUNCTION: Serine/threonine kinase that may play a role in mediating the
CC growth-factor and stress induced activation of transcription.
CC {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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by multiple phosphorylations on
CC threonine and serine residues. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Small and large intestine, spleen, stomach, and
CC bursa, and to a lesser extent lung and kidney.
CC -!- PTM: Autophosphorylated on Ser-398, as part of the activation process.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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DR EMBL; M28488; AAA21877.1; -; mRNA.
DR PIR; A32571; A32571.
DR RefSeq; NP_001103241.1; NM_001109771.2.
DR AlphaFoldDB; P18652; -.
DR SMR; P18652; -.
DR BioGRID; 675357; 1.
DR ELM; P18652; -.
DR STRING; 9031.ENSGALP00000000497; -.
DR iPTMnet; P18652; -.
DR PaxDb; P18652; -.
DR Ensembl; ENSGALT00000073238; ENSGALP00000051132; ENSGALG00000037136.
DR GeneID; 386579; -.
DR KEGG; gga:386579; -.
DR CTD; 6195; -.
DR VEuPathDB; HostDB:geneid_386579; -.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000159314; -.
DR HOGENOM; CLU_000288_58_3_1; -.
DR InParanoid; P18652; -.
DR OMA; ILEHSWV; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; P18652; -.
DR BRENDA; 2.7.11.1; 1306.
DR PRO; PR:P18652; -.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000037136; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; P18652; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; 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:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05582; STKc_RSK_N; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR InterPro; IPR041906; RSK_N.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..752
FT /note="Ribosomal protein S6 kinase 2 alpha"
FT /id="PRO_0000086210"
FT DOMAIN 80..339
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 340..409
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 435..692
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 552
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 86..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 441..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 398
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 752 AA; 84440 MW; CA4D74CCC934E236 CRC64;
MPLAQLAEPW PNMELVQLDT ENGQAAPEEG GNPPCKAKSD ITWVEKDLVD STDKGEGVVK
EINITHHVKE GSEKADPSQF ELLKVLGQGS FGKVFLVRKI TPPDSNHLYA MKVLKKATLK
VRDRVRTKIE RDILADVNHP FVVKLHYAFQ TEGKLYLILD FLRGGDLFTR LSKEVMFTEE
DVKFYLAELA LGLDHLHSLG IIYRDLKPEN ILLDEEGHIK LTDFGLSKEA IDHEKKAYSF
CGTVEYMAPE VVNRQGHSHS ADWWSYGVLM FEMLTGSLPF QGKDRKETMT LILKAKLGMP
QFLSAEAQSL LRALFKRNPA NRLGSGPDGA EEIKRHPFYS TIDWNKLYRR EIKPPFKPAV
GQPDDTFYFD TEFTSRTPKD SPGIPPSAGA HQLFRGFSFV ATGLMEDSKV KPAQPPLHSV
VQQLHGKNIQ FSDGYVVKEA IGVGSYSVCK RCIHKTTNME YAVKVIDKSK RDPSEEIEIL
LRYGQHPNII TLKDVYDDGK YVYLVTELMR GGELLDKILR QKFFSEREAS SVLHTICKTV
EYLHSQGVVH RDLKPSNILY VDESGNPESI RICDFGFAKQ LRAENGLLMT PCYTANFVAP
EVLKRQGYDE GCDIWSLGVL LYTMLAGCTP FANGPSDTPE EILTRIGGGK FSVNGGNWDT
ISDVAKDLVS KMLHVDPHQR LTAKQVLQHP WITQKDSLPQ SQLNYQDVQL VKGAMAATYS
ALNSSKPSPQ LKPIESSILA QRRVKKLPST TL
