KS6A1_CAEEL
ID KS6A1_CAEEL Reviewed; 784 AA.
AC Q21734; Q58A96; Q7YSN4; Q93972; Q93973;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Putative ribosomal protein S6 kinase alpha-1;
DE EC=2.7.11.1;
GN Name=rskn-1; ORFNames=T01H8.1;
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].
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).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22820175; DOI=10.1016/j.bbamcr.2012.07.006;
RA Cha D.S., Datla U.S., Hollis S.E., Kimble J., Lee M.H.;
RT "The Ras-ERK MAPK regulatory network controls dedifferentiation in
RT Caenorhabditis elegans germline.";
RL Biochim. Biophys. Acta 1823:1847-1855(2012).
CC -!- FUNCTION: Serine/threonine kinase that may play a role in mediating the
CC growth-factor and stress induced activation of transcription (By
CC similarity). Suppresses germline tumor formation by preventing the
CC dedifferentiation of secondary spermatocytes probably downstream of
CC mpk-1 (PubMed:22820175). {ECO:0000250|UniProtKB:Q15418,
CC ECO:0000269|PubMed:22820175}.
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=4;
CC Name=a;
CC IsoId=Q21734-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q21734-2; Sequence=VSP_004796, VSP_004797;
CC Name=c;
CC IsoId=Q21734-3; Sequence=VSP_009636;
CC Name=d;
CC IsoId=Q21734-4; Sequence=VSP_020793, VSP_020794, VSP_020795;
CC -!- PTM: Autophosphorylated on Ser-422, as part of the activation process.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in lip-1 and puf-8 double
CC mutant causes a decrease in number of germline tumors and restores
CC normal microtubule organization in spermatocytes.
CC {ECO:0000269|PubMed:22820175}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z80219; CAB02301.2; -; Genomic_DNA.
DR EMBL; Z80219; CAB02302.2; -; Genomic_DNA.
DR EMBL; Z75546; CAB02302.2; JOINED; Genomic_DNA.
DR EMBL; Z80219; CAE17938.1; -; Genomic_DNA.
DR EMBL; Z75546; CAE17938.1; JOINED; Genomic_DNA.
DR EMBL; Z80219; CAI70409.1; -; Genomic_DNA.
DR EMBL; Z75546; CAI70409.1; JOINED; Genomic_DNA.
DR PIR; T23927; T23927.
DR PIR; T24340; T24340.
DR RefSeq; NP_001021602.1; NM_001026431.2. [Q21734-3]
DR RefSeq; NP_001021603.1; NM_001026432.3. [Q21734-4]
DR RefSeq; NP_492319.2; NM_059918.2. [Q21734-1]
DR RefSeq; NP_492320.2; NM_059919.3.
DR AlphaFoldDB; Q21734; -.
DR SMR; Q21734; -.
DR BioGRID; 38080; 2.
DR IntAct; Q21734; 1.
DR STRING; 6239.T01H8.1e; -.
DR EPD; Q21734; -.
DR PaxDb; Q21734; -.
DR PeptideAtlas; Q21734; -.
DR PRIDE; Q21734; -.
DR EnsemblMetazoa; T01H8.1a.1; T01H8.1a.1; WBGene00011352. [Q21734-1]
DR EnsemblMetazoa; T01H8.1b.1; T01H8.1b.1; WBGene00011352. [Q21734-2]
DR EnsemblMetazoa; T01H8.1c.1; T01H8.1c.1; WBGene00011352. [Q21734-3]
DR EnsemblMetazoa; T01H8.1d.1; T01H8.1d.1; WBGene00011352. [Q21734-4]
DR GeneID; 172647; -.
DR UCSC; T01H8.1d.2; c. elegans. [Q21734-1]
DR CTD; 172647; -.
DR WormBase; T01H8.1a; CE34493; WBGene00011352; rskn-1. [Q21734-1]
DR WormBase; T01H8.1b; CE34494; WBGene00011352; rskn-1. [Q21734-2]
DR WormBase; T01H8.1c; CE34495; WBGene00011352; rskn-1. [Q21734-3]
DR WormBase; T01H8.1d; CE38217; WBGene00011352; rskn-1. [Q21734-4]
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000169049; -.
DR InParanoid; Q21734; -.
DR SignaLink; Q21734; -.
DR PRO; PR:Q21734; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011352; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q21734; 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 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; 1.
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..784
FT /note="Putative ribosomal protein S6 kinase alpha-1"
FT /id="PRO_0000086213"
FT DOMAIN 104..363
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 364..433
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 454..712
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 572
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 110..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 460..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 422
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_004796"
FT VAR_SEQ 2..39
FT /note="GLQRGMPLAQLGEPFGITPSSIENVSPGIDQCKDHRMD -> TFDFELPFRN
FT FLESRKINT (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_020793"
FT VAR_SEQ 40..78
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_009636"
FT VAR_SEQ 58..77
FT /note="HSSIHIIQPPPNNGFRLMNW -> MLILAEVEEFAENEIEQGEE (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_004797"
FT VAR_SEQ 689..753
FT /note="VRKMLDVDPNRRVTAKQALQHKWIGQKEALPDRPIQSEQVGELDMQNVKVAL
FT EQTYKAIASAPSV -> QNKHCNISGSDKRKHFRIGQFNQNKLESLICKMSRLHLSRHI
FT KQSHRLQVFNFVQLDRLHLRNDE (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_020794"
FT VAR_SEQ 754..784
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_020795"
SQ SEQUENCE 784 AA; 88120 MW; DD43EA5104128FB0 CRC64;
MGLQRGMPLA QLGEPFGITP SSIENVSPGI DQCKDHRMDV SMRSDPTDCS SDTTNTFHSS
IHIIQPPPNN GFRLMNWKTD SSSETEIDIG DVRKCGEKAD PRQFELLKVL GQGSFGKVFL
VRKVRGRDSG HVYAMKVLKK ATLKVRDRQR TKLERNILAH ISHPFIVKLH YAFQTEGKLY
LILDFLRGGD LFTRLSKEVM FTEDDVKFYL AELTLALEHL HSLGIVYRDL KPENILLDAD
GHIKVTDFGL SKEAIDSEKK TYSFCGTVEY MAPEVINRRG HSMAADFWSL GVLMFEMLTG
HLPFQGRDRN DTMTQILKAK LSMPHFLTQE AQSLLRALFK RNSQNRLGAG PDGVEEIKRH
AFFAKIDFVK LLNKEIDPPF KPALSTVDST SYFDPEFTKR TPKDSPALPA SANGHEIFRG
FSFVSNAVME ERKLIAKSVR SVPTAKTNPF TDDYEILEKI GNGAHSVVHK CQMKATRRKY
AVKIVKKAVF DATEEVDILL RHSHHQFVVK LFDVYEDETA IYMIEELCEG GELLDKLVNK
KSLGSEKEVA AIMANLLNAV QYLHSQQVAH RDLTAANILF ALKDGDPSSL RIVDFGFAKQ
SRAENGMLMT PCYTAQFVAP EVLRKQGYDR SCDVWSLGVL LHTMLTGCTP FAMGPNDTPD
QILQRVGDGK ISMTHPVWDT ISDEAKDLVR KMLDVDPNRR VTAKQALQHK WIGQKEALPD
RPIQSEQVGE LDMQNVKVAL EQTYKAIASA PSVQLRPVGS SALAKRRMKE ILYANYTKNV
SANA
