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Database: UniProt
Entry: H2Q147_PANTR
LinkDB: H2Q147_PANTR
Original site: H2Q147_PANTR 
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};
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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
//
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