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Ribosomal protein S6 kinase beta-1 (S6K-beta-1) (S6K1) (EC 2.7.11.1) (70 kDa ribosomal protein S6 kinase 1) (P70S6K1) (p70-S6K 1) (Ribosomal protein S6 kinase I) (p70 ribosomal S6 kinase alpha) (p70 S6 kinase alpha) (p70 S6K-alpha) (p70 S6KA)

 KS6B1_RABIT             Reviewed;         525 AA.
P67998; P21425;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
22-NOV-2017, entry version 103.
RecName: Full=Ribosomal protein S6 kinase beta-1;
Short=S6K-beta-1;
Short=S6K1;
EC=2.7.11.1;
AltName: Full=70 kDa ribosomal protein S6 kinase 1;
Short=P70S6K1;
Short=p70-S6K 1;
AltName: Full=Ribosomal protein S6 kinase I;
AltName: Full=p70 ribosomal S6 kinase alpha;
Short=p70 S6 kinase alpha;
Short=p70 S6K-alpha;
Short=p70 S6KA;
Name=RPS6KB1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1699810; DOI=10.1016/0014-5793(90)81096-7;
Harmann B., Kilimann M.W.;
"cDNA encoding a 59 kDa homolog of ribosomal protein S6 kinase from
rabbit liver.";
FEBS Lett. 273:248-252(1990).
-!- FUNCTION: Serine/threonine-protein kinase that acts downstream of
mTOR signaling in response to growth factors and nutrients to
promote cell proliferation, cell growth and cell cycle
progression. Regulates protein synthesis through phosphorylation
of EIF4B, RPS6 and EEF2K, and contributes to cell survival by
repressing the pro-apoptotic function of BAD. Under conditions of
nutrient depletion, the inactive form associates with the EIF3
translation initiation complex. Upon mitogenic stimulation,
phosphorylation by the mammalian target of rapamycin complex 1
(mTORC1) leads to dissociation from the EIF3 complex and
activation. The active form then phosphorylates and activates
several substrates in the preinitiation complex, including the
EIF2B complex and the cap-binding complex component EIF4B. Also
controls translation initiation by phosphorylating a negative
regulator of EIF4A, PDCD4, targeting it for ubiquitination and
subsequent proteolysis. Promotes initiation of the pioneer round
of protein synthesis by phosphorylating POLDIP3/SKAR. In response
to IGF1, activates translation elongation by phosphorylating EEF2
kinase (EEF2K), which leads to its inhibition and thus activation
of EEF2. Also plays a role in feedback regulation of mTORC2 by
mTORC1 by phosphorylating RICTOR, resulting in the inhibition of
mTORC2 and AKT1 signaling. Mediates cell survival by
phosphorylating the pro-apoptotic protein BAD and suppressing its
pro-apoptotic function. Phosphorylates mitochondrial RMP leading
to dissociation of a RMP:PPP1CC complex. The free mitochondrial
PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is
proposed to be a negative feedback mechanism for the RPS6KB1 anti-
apoptotic function. Mediates TNF-alpha-induced insulin resistance
by phosphorylating IRS1 at multiple serine residues, resulting in
accelerated degradation of IRS1. In cells lacking functional TSC1-
2 complex, constitutively phosphorylates and inhibits GSK3B. May
be involved in cytoskeletal rearrangement through binding to
neurabin. Phosphorylates and activates the pyrimidine biosynthesis
enzyme CAD, downstream of MTOR (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activation requires multiple phosphorylation
events on serine/threonine residues. Activation appears to be
first mediated by phosphorylation of multiple sites in the
autoinhibitory domain, which facilitates phosphorylation at Thr-
412, disrupting the autoinhibitory mechanism and allowing
phosphorylation of Thr-252 by PDPK1. The active conformation of
the kinase is believed to be stabilized by a mechanism involving
three conserved phosphorylation sites located in the kinase domain
activation loop (Thr-252) and in the AGC-kinase C-terminal domain
(Ser-394 in the middle of the tail/linker region and Thr-412
within a hydrophobic motif at its end). Activated by mTORC1;
isoform Alpha I and isoform Alpha II are sensitive to rapamycin,
which inhibits activating phosphorylation at Thr-412. Activated by
PDPK1 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PPP1R9A/neurabin-1. Interacts with RPTOR.
Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts
with TRAF4. Interacts with POLDIP3. Interacts (via N-terminus)
with IER5. {ECO:0000250|UniProtKB:P23443,
ECO:0000250|UniProtKB:P67999}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction,
synapse, synaptosome {ECO:0000250}. Mitochondrion outer membrane
{ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Colocalizes with
URI1 at mitochondrion. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Alpha I;
IsoId=P67998-1; Sequence=Displayed;
Name=Alpha II;
IsoId=P67998-2; Sequence=VSP_018841;
-!- DOMAIN: The autoinhibitory domain is believed to block
phosphorylation within the AGC-kinase C-terminal domain and the
activation loop. {ECO:0000250}.
-!- DOMAIN: The TOS (TOR signaling) motif is essential for activation
by mTORC1. {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-412 is regulated by mTORC1. The
phosphorylation at this site is maintained by an agonist-dependent
autophosphorylation mechanism. Activated by phosphorylation at
Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in
mitochondrion (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X54415; CAA38279.1; -; mRNA.
PIR; S12906; S12906.
RefSeq; NP_001095160.1; NM_001101690.1. [P67998-1]
UniGene; Ocu.3260; -.
ProteinModelPortal; P67998; -.
SMR; P67998; -.
STRING; 9986.ENSOCUP00000003969; -.
PRIDE; P67998; -.
GeneID; 100009260; -.
KEGG; ocu:100009260; -.
CTD; 6198; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P67998; -.
KO; K04688; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016238; Ribosomal_S6_kinase.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000605; Ribsml_S6_kin_1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
Acetylation; Alternative initiation; Apoptosis; ATP-binding;
Cell junction; Complete proteome; Cytoplasm; Kinase; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Synapse; Synaptosome; Transferase.
CHAIN 1 525 Ribosomal protein S6 kinase beta-1.
/FTId=PRO_0000024346.
DOMAIN 91 352 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 353 423 AGC-kinase C-terminal.
NP_BIND 97 105 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 424 525 Autoinhibitory domain.
MOTIF 28 32 TOS motif.
ACT_SITE 218 218 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 123 123 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 252 252 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 412 412 Phosphothreonine; by MTOR, NEK6 and NEK7.
{ECO:0000250|UniProtKB:P67999}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P67999}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 444 444 Phosphothreonine.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000250|UniProtKB:P23443}.
MOD_RES 516 516 N6-acetyllysine.
{ECO:0000250|UniProtKB:P67999}.
VAR_SEQ 1 23 Missing (in isoform Alpha II).
{ECO:0000305}.
/FTId=VSP_018841.
SEQUENCE 525 AA; 59109 MW; 013BA13CCDB908D7 CRC64;
MRRRRRRDGF YPAPDFRDRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL NESMDHGGVG
PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG GYGKVFQVRK VTGANTGKIF
AMKVLKKAMI VRNAKDTAHT KAERNILEEV KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL
FMQLEREGIF MEDTACFYLA EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC
KESIHDGTVT HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP FFRHINWEEL
LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL SESANQVFLG FTYVAPSVLE
SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK FSPGDFWGRG ASASTANPQT PVEYPMETSG
IEQMDVTTSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL


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