KS6A6_DANRE
ID KS6A6_DANRE Reviewed; 740 AA.
AC Q6PFQ0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ribosomal protein S6 kinase alpha-6;
DE Short=S6K-alpha-6;
DE EC=2.7.11.1;
DE AltName: Full=S6K-alpha 6-like;
GN Name=rps6ka6; Synonyms=rps6kal;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) 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 the transcription factor
CC CREB. {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 -!- SUBUNIT: Forms a complex with either ERK1 or ERK2 in quiescent cells.
CC Transiently dissociates following mitogenic stimulation (By
CC similarity). {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; BC057467; AAH57467.1; -; mRNA.
DR RefSeq; NP_956367.1; NM_200073.1.
DR AlphaFoldDB; Q6PFQ0; -.
DR SMR; Q6PFQ0; -.
DR PaxDb; Q6PFQ0; -.
DR GeneID; 337670; -.
DR KEGG; dre:337670; -.
DR CTD; 337670; -.
DR ZFIN; ZDB-GENE-030131-9616; rps6kal.
DR InParanoid; Q6PFQ0; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; Q6PFQ0; -.
DR PRO; PR:Q6PFQ0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..740
FT /note="Ribosomal protein S6 kinase alpha-6"
FT /id="PRO_0000278163"
FT DOMAIN 67..326
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 327..396
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 420..677
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 537
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 426..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 740 AA; 83397 MW; 1EED47AD9C722C49 CRC64;
MISFGPAQES SLKMEVQSVS SEVNGHQIMD EPMEEESYTH CDEGAYKEIP ITHHVKEGCE
KADPSQFELL KVLGQGSFGK VFLVRKLMGP DAGQLYAMKV LKKASLKVRD RVRTKMERDI
LVEVNHPFIV KLHYAFQTEG KLYLILDFLR GGDVFTRLSK EVMFTEEDVK FYLAELALAL
DHLHNLGIVY RDLKPENILL DEAGHIKLTD FGLSKESVDQ DKKAYSFCGT VEYMAPEVVN
RRGHTQSADW WSLGVLMFEM LTGTLPFQGK DRNETMNMIL KAKLGMPQFL SLEAQGLLRM
LFKRNPSNRL GAGPDGVEEI KRHTFFSTID WNKLYRRELQ PPFKPASGKP DDTFCFDPEF
TAKTPKDSPG IPPSANAHQL FKGFSFVAPV SLEESKSAPL VNILPIVQVH GSSAQFSDVY
ELKEDIGVGS YSICKRCIHR VTAMEFAVKI IDKSKRDPSE EIEILMRYGQ HPNIITLKDV
YDEGRFVYLV TELMKGGELL DKILRQKFFS EREASAVLYT ITKTVDYLHC QGVVHRDLKP
SNILYMDDSG NPDSIRICDF GFAKQLRGDN GLLLTPCYTA NFVAPEVLMR QGYDAACDIW
SLGVLLYTML AGYTPFANGP NDTPEEILLR IGSGKFSLSG GNWDSVSDSS KDLLSHMLHV
DPHHRYTAEQ VLKHSWIACR DQNPHFQLTR HEAPHLVKGA MAATYSALNH KTCKPVLEPV
AASSLAQRRN MKKLTSTDMS
