KS6A2_CAEEL
ID KS6A2_CAEEL Reviewed; 772 AA.
AC Q18846; Q1ZXU3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Putative ribosomal protein S6 kinase alpha-2;
DE EC=2.7.11.1;
DE AltName: Full=Ribosomal protein S6 kinase alpha-5 homolog;
GN Name=rskn-2; ORFNames=C54G4.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Serine/threonine kinase that may play a role in mediating the
CC mitogen- and stress-induced effects on transcription. May repress
CC transcription via phosphorylation of 'Ser-1' of histone H2A. May
CC phosphorylate histone H3 (By similarity). {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q18846-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q18846-2; Sequence=VSP_020796;
CC -!- DOMAIN: Enzyme activity requires the presence of both kinase domains.
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; Z75533; CAA99814.2; -; Genomic_DNA.
DR EMBL; Z75533; CAJ85755.1; -; Genomic_DNA.
DR PIR; T20232; T20232.
DR RefSeq; NP_001040645.1; NM_001047180.2. [Q18846-1]
DR RefSeq; NP_001040646.1; NM_001047181.1. [Q18846-2]
DR AlphaFoldDB; Q18846; -.
DR SMR; Q18846; -.
DR BioGRID; 38016; 16.
DR DIP; DIP-25877N; -.
DR IntAct; Q18846; 1.
DR STRING; 6239.C54G4.1a; -.
DR iPTMnet; Q18846; -.
DR EPD; Q18846; -.
DR PaxDb; Q18846; -.
DR PeptideAtlas; Q18846; -.
DR EnsemblMetazoa; C54G4.1a.1; C54G4.1a.1; WBGene00008311. [Q18846-1]
DR EnsemblMetazoa; C54G4.1b.1; C54G4.1b.1; WBGene00008311. [Q18846-2]
DR GeneID; 172581; -.
DR UCSC; C54G4.1a; c. elegans. [Q18846-1]
DR CTD; 172581; -.
DR WormBase; C54G4.1a; CE32338; WBGene00008311; rskn-2. [Q18846-1]
DR WormBase; C54G4.1b; CE40030; WBGene00008311; rskn-2. [Q18846-2]
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000167362; -.
DR HOGENOM; CLU_000288_58_0_1; -.
DR InParanoid; Q18846; -.
DR OMA; IMQRICR; -.
DR PhylomeDB; Q18846; -.
DR Reactome; R-CEL-198753; ERK/MAPK targets.
DR Reactome; R-CEL-199920; CREB phosphorylation.
DR Reactome; R-CEL-375165; NCAM signaling for neurite out-growth.
DR SignaLink; Q18846; -.
DR PRO; PR:Q18846; -.
DR Proteomes; UP000001940; Chromosome I.
DR ExpressionAtlas; Q18846; 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:0016572; P:histone phosphorylation; 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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; 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 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..772
FT /note="Putative ribosomal protein S6 kinase alpha-2"
FT /id="PRO_0000239002"
FT DOMAIN 17..284
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 285..353
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 382..653
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 706..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 500
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 388..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 180
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 342
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 347
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 712
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..583
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020796"
SQ SEQUENCE 772 AA; 87069 MW; C9E7AC269354ACFB CRC64;
MEDILMPEGE KVSMENFALL RVLGKGAYGK VFLVRKVGGK DHNTIYAMKV LRKTRVLTKQ
KTLEHTMAER QVLERLRGTP FLVNLFYAFQ TDTKLHIVME YVRGGELFTH LCSRGHFDLE
AARFVIAELV VAIDSLHQRK VIYRDLKLEN ILLDEEGHVK LTDFGLSKLF LPGELDRANS
YCGTIEYMSP EVINRPEGGY SDVVDWWSLG VISFELLTGC SPFTVDGAQN SSKDIAKRIM
TKKVPFPKTM DVDARDFIGQ LLEKKLEKRL GYNGVDEIKN HKFMSSIDWD AAVKRTLKPV
IVPRIGHDLD TQFFSAEFTS QPPLYSPAES PLNANTLFRG YSYVSPSVIF ANDNVIGEEL
MAEDVNALLA SSSFFAKYKL DKSDAGLLGK GAFSVVRRCE RVVDGAQFAV KIVSQKFASQ
AQREARILEM VQGHPNIVQL HDVHSDPLHF YLVMEILTGN ELLERIRKLE RFTESEAADI
MRQLVSAVKY LHDKRIVHRD LKPENILFES IDSSARLRLV DFGFARLLPN SMEQQLKSVQ
VLRKMTPCFT LQYAAPEVLD VGDSQPEYNE QCDLWSLGVV LFTMLSGQVP FHARSRQESA
TEIMQRICRA EFSFTGDAWT NVSADAKNLI TGLLTVDPKK RLSMQELTAH MWLKSSASMD
TPLQTPSILP SSADETFNET LRAFLHANRD GFHLLDVAAA PLMKRRGIKR QSGDKDASGN
SKNSRVTQFE CLPEEQEAEM TSSTSRPSNL GMMNYREPNS GTIRETRGSD SS
