KS6AB_XENLA
ID KS6AB_XENLA Reviewed; 629 AA.
AC P10666;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ribosomal protein S6 kinase 2 beta;
DE EC=2.7.11.1;
DE AltName: Full=Ribosomal protein S6 kinase II beta;
DE Short=S6KII-beta;
DE AltName: Full=p90-RSK;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3368449; DOI=10.1073/pnas.85.10.3377;
RA Jones S.W., Erikson E., Blenis J., Maller J.L., Erikson R.L.;
RT "A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that
RT are each similar to distinct protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3377-3381(1988).
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 -!- PTM: Autophosphorylated on Ser-380, 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; M20188; AAA49959.1; -; mRNA.
DR PIR; A30001; A30001.
DR AlphaFoldDB; P10666; -.
DR SMR; P10666; -.
DR PRIDE; P10666; -.
DR BRENDA; 2.7.11.1; 6725.
DR Proteomes; UP000186698; Genome assembly.
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; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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..629
FT /note="Ribosomal protein S6 kinase 2 beta"
FT /id="PRO_0000086212"
FT DOMAIN 62..321
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 322..391
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 416..629
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 533
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 68..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 422..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 380
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 629 AA; 71287 MW; BC6144415F1DECE0 CRC64;
MPLAQLVDLW PEVELVHEDT ENGHGGPEDR GRHTSKDEVV VKEIPITHHV KEGAEKADQS
HFVLLKVLGQ GSFGKVFLVR KITPPDANQL YAMKVLKKAT LKVRDRVRTK MERDILADVH
HPFVVRLHYA FQTEGKLYLI LDFLRGGDLF TRLSKEVMFT EEDVKFYLAE LALGLDHLHS
LGIIYRDLKP ENILLDEEGH IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS
HGADWWSYGV LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSNEAQ SLLRALFKRN
ATNRLGSGVE GAEELKRHPF FSTIDWNKLY RRELSPPFKP SVTQPDDTYY FDTEFTSRTP
KDSPGIPPSA GAHQLFRGFS FVAPVLVEED AKKTSSPPVL SVPKTHSKNV LFTDVYTVRE
TIGVGSYSVC KRCVHKGTNM EYAVKVIDKS KRDPSEEIEI LRRYGQHPNI ITLKDVYEEC
NSIYLVTELM RGGELLDRIL RQKFFSEREA CSVLFTVCKT VEYLHSQGVV HRDLKPSNIL
YVDESGDPES IRICDFGFSK QLRAENGLLM TPCYTANFVA PEVLKRQGYD EGCDIWSLGI
LLYTMLAGYT PFANGPGDTP EEILARIGS
