KS6A5_CHICK
ID KS6A5_CHICK Reviewed; 789 AA.
AC Q5F3L1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribosomal protein S6 kinase alpha-5;
DE Short=S6K-alpha-5;
DE EC=2.7.11.1;
GN Name=RPS6KA5; ORFNames=RCJMB04_14g1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Serine/threonine-protein kinase that is required for the
CC mitogen or stress-induced phosphorylation of the transcription factors
CC CREB1 and ATF1 and that contributes to gene activation by histone
CC phosphorylation. Phosphorylates CREB1 and ATF1 in response to mitogenic
CC or stress stimuli such as UV-C irradiation, epidermal growth factor
CC (EGF) and anisomycin. Directly represses transcription via
CC phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of
CC histone H3 in response to mitogenics, stress stimuli and EGF, which
CC results in the transcriptional activation of several immediate early
CC genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also
CC phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-
CC induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14)
CC (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 phosphorylation at Ser-350, Thr-571
CC and Thr-690 by MAP kinases, and by further autophosphorylation of Ser-
CC 202, Ser-366 and Ser-371 by the activated C-terminal kinase domain. The
CC active N-terminal kinase domain finally phosphorylates downstream
CC substrates, as well as Ser-740, Ser-742 and Ser-748 in its own C-
CC terminal region (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in heart, brain
CC and placenta. Less abundant in lung, kidney and liver.
CC -!- DOMAIN: Enzyme activity requires the presence of both kinase domains.
CC {ECO:0000250}.
CC -!- PTM: Ser-366 and Thr-571 phosphorylation is required for kinase
CC activity. Ser-366 and Ser-202 are autophosphorylated by the C-terminal
CC kinase domain, and their phosphorylation is essential for the catalytic
CC activity of the N-terminal kinase domain. Phosphorylated at Ser-350,
CC Thr-571 and Thr-690 by MAP kinases. Autophosphorylated at Ser-740, Ser-
CC 742 and Ser-748 by the N-terminal kinase domain.
CC -!- MISCELLANEOUS: Enzyme activity requires the presence of both kinase
CC domains. {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; AJ851639; CAH65273.1; -; mRNA.
DR RefSeq; NP_001012605.1; NM_001012587.2.
DR AlphaFoldDB; Q5F3L1; -.
DR SMR; Q5F3L1; -.
DR STRING; 9031.ENSGALP00000017378; -.
DR PaxDb; Q5F3L1; -.
DR Ensembl; ENSGALT00000071253; ENSGALP00000047730; ENSGALG00000030580.
DR GeneID; 423408; -.
DR KEGG; gga:423408; -.
DR CTD; 9252; -.
DR VEuPathDB; HostDB:geneid_423408; -.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000156886; -.
DR InParanoid; Q5F3L1; -.
DR OMA; IMQRICR; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; Q5F3L1; -.
DR TreeFam; TF313438; -.
DR PRO; PR:Q5F3L1; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000030580; Expressed in spleen and 13 other tissues.
DR ExpressionAtlas; Q5F3L1; 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:0044024; F:histone kinase activity (H2A-S1 specific); IEA:Ensembl.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IEA:Ensembl.
DR GO; GO:0044022; F:histone kinase activity (H3-S28 specific); IEA:Ensembl.
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:0004713; F:protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..789
FT /note="Ribosomal protein S6 kinase alpha-5"
FT /id="PRO_0000232734"
FT DOMAIN 39..308
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 309..377
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 416..677
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 731..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 534
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 71
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 202
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 366
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 371
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 740
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 742
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 748
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 789 AA; 89040 MW; 2FA3FC00B6098B1C CRC64;
MEGPSGSAQG SEWPLLTVTH ELRNANLTGH AEKVGIENFE LLKVLGTGAY GKVFLVRKVS
GHDAGKLYAM KVLKKATIVQ KAKTTEHTRT ERQVLEHIRQ SPFLVTLHYA FQTDTKLHLI
LDYINGGELF THLSQRERFS ENEVQIYIGE IVLALEHLHK LGIIYRDIKL ENILLDSDGH
VVLTDFGLSK EFLTDENERA YSFCGTIEYM APDIVRGGDT GHDKAVDWWS VGVLMYELLT
GASPFTVDGE KNSQAEISRR ILKSEPPYPQ EMSALSKDII QRLLMKDPKK RLGCGPTDAD
EIKQHPFFQN INWDDLAAKK VPAPFKPVIR DELDVSNFAE EFTEMDPTYS PAATPQTSEK
IFQGYSFVAP SILFKRNAAT VDPVQFYVGD ERPGTTTIAR SAMMKDSPFF QHYELDLKEK
PLGEGSFSIC RKCLHKKTSQ EYAVKIISKR MEANTQREIT ALKLCEGHPN VVKLHEVYHD
QLHTFLVMEL LKGGELLERI QKKQHFSETE ASHIMRRLVS AVSHMHDVGV VHRDLKPENL
LFTDETDNSE IKIIDFGFAR LKPPDNQPLK TPCFTLHYAA PELFNHNGYD ESCDLWSLGV
ILYTMLSGQV PFQSQDKSLT CTSALEIMKK IKKGEFSFEG EAWKNVSEEA KELIQGLLTV
DPNKRIKMSS LRYNEWLQDG SQLSSNPLMT PDNLGSSGAA VHTYVKATFH AFNKYKREGF
CLQNVDKAPL AKRRKMKKTS TSTETRSSSS ESSHSSSSHS HGKTTPTKTL QPTNPTDSNN
PETIFQFSD
