ID H2Q147_PANTR Unreviewed; 1066 AA.
AC H2Q147; A0A2J8QV92;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=RPS6KC1 {ECO:0000313|EMBL:JAA09895.1,
GN ECO:0000313|Ensembl:ENSPTRP00000003319.3, ECO:0000313|VGNC:VGNC:9455};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000003319.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000003319.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA09895.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA09895.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA41584.1}, Skin {ECO:0000313|EMBL:JAA31533.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA21059.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000003319.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; AACZ04071453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01001443; JAA09895.1; -; mRNA.
DR EMBL; GABF01001086; JAA21059.1; -; mRNA.
DR EMBL; GABD01001567; JAA31533.1; -; mRNA.
DR EMBL; GABE01003155; JAA41584.1; -; mRNA.
DR RefSeq; XP_001171184.1; XM_001171184.4.
DR STRING; 9598.ENSPTRP00000003319; -.
DR PaxDb; 9598-ENSPTRP00000003319; -.
DR Ensembl; ENSPTRT00000003602.4; ENSPTRP00000003319.3; ENSPTRG00000001972.6.
DR GeneID; 457727; -.
DR CTD; 26750; -.
DR VGNC; VGNC:9455; RPS6KC1.
DR eggNOG; KOG0603; Eukaryota.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00940000155656; -.
DR HOGENOM; CLU_014272_0_0_1; -.
DR OrthoDB; 5308056at2759; -.
DR TreeFam; TF323964; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001972; Expressed in temporal lobe and 21 other cell types or tissues.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02677; MIT_SNX15; 1.
DR CDD; cd07287; PX_RPK118_like; 1.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042132; PX_S6K-delta-1.
DR InterPro; IPR035053; STK_RPK118-like.
DR PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR15508:SF2; RIBOSOMAL PROTEIN S6 KINASE DELTA-1; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:JAA09895.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..132
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 794..1056
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 118712 MW; 7DBEEE3CFE303265 CRC64;
MTSYRERSAD LARFYTVTEP QRHPRGYTVY KVTARVVSRR NPEDVQEIIV WKRYSDFKKL
HKELWQIHKN LFRHSELFPP FAKGIVFGRF DETVIEERRQ CAEDLLQFSA NIPALYNSKQ
LEDFFKGGII NDSSELIGPA EAHSDSLIDT FPECSTEGFS SDSDLVSLTV DVDSLAELDD
GMASNQNSPI RTFGLNLSSD SSALGAVASD SEQSKTEEER ESRSLFPGSL KPKLGKRDYL
EKAGELIKLA LKKEEEDDYE AASDFYRKGV DLLLEGVQGE SSPTRREAVK RRTAEYLMRA
ESISSLYGKP QLDDVSQPPG SLSSRPLWNL RSPAEELKAF RVLGVIDKVL LVMDTRTEQT
FILKGLRKSS EYSRNRKTII PRCVPNMVCL HKYIISEESV FLVLQHAEGG KLWSYISKFL
NRSPEESFDI KEVKKPTLAK VHLQQPTSSP QDSSSFESRG SDGGSMLKAL PLKSSLTPSS
QDDSNQEDDG QDSSPKWPDS GSSSEEECTT SYLTLCNEYG QEKIEPGSLN EEPFMKTEGN
GVDTKAIKSF PAHLAADSDS PSTQLRAHEL KFFPNDDPEA VSSPRTSDSL SRSKNSPMEF
FRIDSKDSAS ELLGLDFGEK LYSLKSEPLK PFFTLPDGDS ASRSFNTSES KVEFKAQDTI
SRGSDDSVPV ISFKDAAFDD VSGTDEGRPD LLVNLPGELE STREAAAMGP TKFTQTNIGI
IENKLLEAPD VLCLRLSTEQ CQAHEEKGIE ELSDPSGPKS YSITEKHYAQ EDPRMLFVAA
VDHSSSGDMS LLPSSDPKFQ GLGVVESAVT ANNTEESLFR ICSPLSGANE YIASTDTLKT
EEVLLFTDQT DDLAKEEPTS LFQRDSETKG ESGLVLEGDK EIHQIFEDLD KKLALTSRFY
IPEGCIQRWA AEMVVALDAL HREGIVCRDL NPNNILLNDR GHIQLTYFSR WSEVEDSCDS
DAIERMYCAP EVGAITEETE ACDWWSLGAV LFELLTGKTL VECHPAGINT HTTLNMPECV
SEEARSLIQQ LLQFNPLERL GAGVAGVEDI KSHPFFTPVD WAELMR
//