KS6AA_XENLA
ID KS6AA_XENLA Reviewed; 733 AA.
AC P10665; Q6DE78;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 139.
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;
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], AND PARTIAL PROTEIN SEQUENCE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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; M20187; AAA49958.1; -; mRNA.
DR EMBL; BC077262; AAH77262.1; -; mRNA.
DR PIR; B30001; B30001.
DR RefSeq; NP_001085310.1; NM_001091841.1.
DR AlphaFoldDB; P10665; -.
DR SMR; P10665; -.
DR BioGRID; 101893; 1.
DR IntAct; P10665; 1.
DR MINT; P10665; -.
DR PRIDE; P10665; -.
DR DNASU; 443729; -.
DR GeneID; 443729; -.
DR KEGG; xla:443729; -.
DR CTD; 443729; -.
DR Xenbase; XB-GENE-6487851; rps6ka6.S.
DR OrthoDB; 1132245at2759; -.
DR BRENDA; 2.7.11.1; 6725.
DR PRO; PR:P10665; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 443729; Expressed in zone of skin and 19 other tissues.
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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..733
FT /note="Ribosomal protein S6 kinase 2 alpha"
FT /id="PRO_0000086211"
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..673
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 733 AA; 82639 MW; 2BA4B137EE7DBDDC CRC64;
MPLAQLVNLW PEVAVVHEDP ENGHGSPEEG GRHTSKDEVV VKEFPITHHV KEGSEKADQS
DFVLLKVLGQ GSFGKVFLVR KITPPDANQL YAMKVLKKAT LKVRDRVRTK MERDILADVH
HPFVVRLHYA FQTEGKLYLI LDFLRGGDLF TRLSKEVMFT EEDVKFYLAE LALGLDHLHS
LGIIYRDLKP ENILLDEEGH IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS
HSADWWSYGV LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSNEAQ SLLRALFKRN
PTNRLGSAME GAEEIKRQPF FSTIDWNKLF RREMSPPFKP AVTQADDTYY FDTEFTSRTP
KDSPGIPPSA GAHQLFRGFS FVAPALVEED AKKTSSPPVL SVPKTHSKNI LFMDVYTVRE
TIGVGSYSVC KRCVHKGTNM EYAVKVIDKT KRDPSEEIEI LRRYGQHPNI IALKDVYKEG
NSIYVVTELM RGGELLDRIL RQKFFSEREA SSVLFTVCKT VENLHSQGVV HRDLKPSNIL
YVDESGDPES IRICDFGFAK QLRADNGLLM TPCYTANFVA PEVLKRQGYD EGCDIWSLGI
LLYTMLAGYT PFANGLGDTP EEILARIGSG KFTLRGGNWN TVSAAAKDLV SRMLHVDPHK
RLTAKQVLQH EWITKRDALP QSQLNRQDVH LVKGAMAATY SALNSSKPTP LLQPIKSSIL
AQRRVKKLPS TTL
