ID KS6C1_HUMAN Reviewed; 1066 AA. AC Q96S38; B1APS8; B3KVM4; D3DTA4; Q8TDD3; Q9NSF4; Q9UL66; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 181. DE RecName: Full=Ribosomal protein S6 kinase delta-1; DE Short=S6K-delta-1; DE EC=2.7.11.1; DE AltName: Full=52 kDa ribosomal protein S6 kinase; DE AltName: Full=Ribosomal S6 kinase-like protein with two PSK domains 118 kDa protein; DE AltName: Full=SPHK1-binding protein; GN Name=RPS6KC1; Synonyms=RPK118; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION RP WITH SPHK1 AND PHOSPHATIDYLINOSITOL 3-PHOSPHATE, SUBCELLULAR LOCATION, AND RP FUNCTION. RX PubMed=12077123; DOI=10.1074/jbc.m201442200; RA Hayashi S., Okada T., Igarashi N., Fujita T., Jahangeer S., Nakamura S.; RT "Identification and characterization of RPK118, a novel sphingosine kinase- RT 1-binding protein."; RL J. Biol. Chem. 277:33319-33324(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Guo J.H., Yu L.; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 598-1066 (ISOFORM 1). RX PubMed=10552933; DOI=10.1006/geno.1999.5963; RA Zhang H., Yu L., Mao N., Fu Q., Tu Q., Gao J., Zhao S.; RT "Cloning, characterization, and chromosome mapping of RPS6KC1, a novel RT putative member of the ribosome protein S6 kinase family, to chromosome RT 12q12-q13.1."; RL Genomics 61:314-318(1999). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 683-1066 (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRDX3. RX PubMed=15750338; RA Liu L., Yang C., Yuan J., Chen X., Xu J., Wei Y., Yang J., Lin G., Yu L.; RT "RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 RT through pseudo-kinase domains."; RL Mol. Cells 19:39-45(2005). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-427, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-423; SER-427; RP SER-455; SER-528; SER-583; SER-605; SER-661; SER-664; SER-667 AND SER-872, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP VARIANTS [LARGE SCALE ANALYSIS] THR-42; LYS-96; LEU-319; LEU-424; PRO-546; RP ILE-554; SER-575; ALA-663; PHE-853; TYR-1003 AND LYS-1022. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: May be involved in transmitting sphingosine-1 phosphate CC (SPP)-mediated signaling into the cell (PubMed:12077123). Plays a role CC in the recruitment of PRDX3 to early endosomes (PubMed:15750338). CC {ECO:0000269|PubMed:12077123, ECO:0000269|PubMed:15750338}. 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 -!- SUBUNIT: Interacts with SPHK1 and phosphatidylinositol 3-phosphate CC (PubMed:12077123). Interacts (via PX domain) with PRDX3 CC (PubMed:15750338). {ECO:0000269|PubMed:12077123, CC ECO:0000269|PubMed:15750338}. CC -!- INTERACTION: CC Q96S38; P11473-2: VDR; NbExp=3; IntAct=EBI-347731, EBI-12874016; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12077123, CC ECO:0000269|PubMed:15750338}. Membrane {ECO:0000269|PubMed:12077123}. CC Early endosome {ECO:0000269|PubMed:15750338}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96S38-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96S38-2; Sequence=VSP_046333; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, skeletal muscle, brain, CC heart, placenta, kidney and liver and weakly expressed in thymus, small CC intestine, lung and colon. {ECO:0000269|PubMed:12077123}. CC -!- DOMAIN: The PX domain is essential for its localization to the early CC endosomes. {ECO:0000269|PubMed:15750338}. CC -!- DOMAIN: The first protein kinase domain appears to be a pseudokinase CC domain as it does not contain the classical characteristics, such as CC the ATP-binding motif, ATP-binding site and active site. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. S6 kinase subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC -!- CAUTION: Instead of Lys-820, Arg-820 is found at the binding site. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB92850.1; Type=Erroneous initiation; Evidence={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; AB070706; BAB63956.1; -; mRNA. DR EMBL; AF477978; AAL84818.1; -; mRNA. DR EMBL; AK122921; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK122989; BAG53836.1; -; mRNA. DR EMBL; AL645860; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL512449; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL583826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471100; EAW93362.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93363.1; -; Genomic_DNA. DR EMBL; BC104769; AAI04770.1; -; mRNA. DR EMBL; AF037447; AAF13027.1; -; mRNA. DR EMBL; AL356893; CAB92850.1; ALT_INIT; mRNA. DR CCDS; CCDS1513.1; -. [Q96S38-1] DR CCDS; CCDS44317.1; -. [Q96S38-2] DR RefSeq; NP_001129610.1; NM_001136138.2. [Q96S38-2] DR RefSeq; NP_036556.2; NM_012424.4. [Q96S38-1] DR AlphaFoldDB; Q96S38; -. DR SMR; Q96S38; -. DR BioGRID; 117810; 28. DR IntAct; Q96S38; 12. DR STRING; 9606.ENSP00000355927; -. DR ChEMBL; CHEMBL1795193; -. DR iPTMnet; Q96S38; -. DR PhosphoSitePlus; Q96S38; -. DR BioMuta; RPS6KC1; -. DR DMDM; 94717650; -. DR CPTAC; non-CPTAC-5679; -. DR EPD; Q96S38; -. DR jPOST; Q96S38; -. DR MassIVE; Q96S38; -. DR MaxQB; Q96S38; -. DR PaxDb; 9606-ENSP00000355927; -. DR PeptideAtlas; Q96S38; -. DR ProteomicsDB; 3310; -. DR ProteomicsDB; 78062; -. [Q96S38-1] DR Pumba; Q96S38; -. DR TopDownProteomics; Q96S38-1; -. [Q96S38-1] DR Antibodypedia; 34615; 191 antibodies from 27 providers. DR DNASU; 26750; -. DR Ensembl; ENST00000366959.4; ENSP00000355926.3; ENSG00000136643.12. [Q96S38-2] DR Ensembl; ENST00000366960.8; ENSP00000355927.3; ENSG00000136643.12. [Q96S38-1] DR GeneID; 26750; -. DR KEGG; hsa:26750; -. DR MANE-Select; ENST00000366960.8; ENSP00000355927.3; NM_012424.6; NP_036556.2. DR UCSC; uc001hkd.5; human. [Q96S38-1] DR AGR; HGNC:10439; -. DR CTD; 26750; -. DR DisGeNET; 26750; -. DR GeneCards; RPS6KC1; -. DR HGNC; HGNC:10439; RPS6KC1. DR HPA; ENSG00000136643; Low tissue specificity. DR MIM; 617517; gene. DR neXtProt; NX_Q96S38; -. DR OpenTargets; ENSG00000136643; -. DR PharmGKB; PA34854; -. DR VEuPathDB; HostDB:ENSG00000136643; -. DR eggNOG; KOG0603; Eukaryota. DR eggNOG; KOG2101; Eukaryota. DR GeneTree; ENSGT00940000155656; -. DR HOGENOM; CLU_014272_0_0_1; -. DR InParanoid; Q96S38; -. DR OMA; PECQNND; -. DR OrthoDB; 5308056at2759; -. DR PhylomeDB; Q96S38; -. DR TreeFam; TF323964; -. DR PathwayCommons; Q96S38; -. DR SignaLink; Q96S38; -. DR SIGNOR; Q96S38; -. DR BioGRID-ORCS; 26750; 8 hits in 1164 CRISPR screens. DR ChiTaRS; RPS6KC1; human. DR GeneWiki; RPS6KC1; -. DR GenomeRNAi; 26750; -. DR Pharos; Q96S38; Tdark. DR PRO; PR:Q96S38; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96S38; Protein. DR Bgee; ENSG00000136643; Expressed in sperm and 193 other cell types or tissues. DR ExpressionAtlas; Q96S38; baseline and differential. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:HPA. DR GO; GO:0005764; C:lysosome; IDA:HPA. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. 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. DR Genevisible; Q96S38; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Endosome; Kinase; KW Lipid-binding; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..1066 FT /note="Ribosomal protein S6 kinase delta-1" FT /id="PRO_0000233127" FT DOMAIN 8..132 FT /note="PX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147" FT DOMAIN 277..305 FT /note="MIT" FT DOMAIN 344..445 FT /note="Protein kinase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 794..1056 FT /note="Protein kinase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" 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" FT ACT_SITE 929 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 801..809 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 820 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 449 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BLK9" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 494 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BLK9" FT MOD_RES 528 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 583 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 605 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BLK9" FT MOD_RES 640 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BLK9" FT MOD_RES 661 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 664 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 667 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 794 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BLK9" FT MOD_RES 872 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 36..47 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046333" FT VARIANT 42 FT /note="P -> T (in dbSNP:rs56087470)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040647" FT VARIANT 96 FT /note="E -> K (in dbSNP:rs56032860)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040648" FT VARIANT 319 FT /note="P -> L (in dbSNP:rs56369827)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040649" FT VARIANT 424 FT /note="P -> L (in dbSNP:rs56183862)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040650" FT VARIANT 546 FT /note="A -> P (in dbSNP:rs35281247)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040651" FT VARIANT 554 FT /note="L -> I (in a lung neuroendocrine carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040652" FT VARIANT 561 FT /note="P -> R (in dbSNP:rs17020314)" FT /id="VAR_051635" FT VARIANT 575 FT /note="N -> S (in dbSNP:rs56060894)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040653" FT VARIANT 663 FT /note="G -> A (in an ovarian mucinous carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040654" FT VARIANT 853 FT /note="L -> F (in dbSNP:rs34080597)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040655" FT VARIANT 1003 FT /note="C -> Y (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040656" FT VARIANT 1022 FT /note="E -> K (in a breast infiltrating ductal carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040657" FT CONFLICT 35 FT /note="R -> G (in Ref. 1; BAB63956)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="A -> V (in Ref. 1; BAB63956)" FT /evidence="ECO:0000305" FT CONFLICT 1065 FT /note="Missing (in Ref. 7)" FT /evidence="ECO:0000305" SQ SEQUENCE 1066 AA; 118682 MW; 670EE5965F3B8274 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 KKLALASRFY IPEGCIQRWA AEMVVALDAL HREGIVCRDL NPNNILLNDR GHIQLTYFSR WSEVEDSCDS DAIERMYCAP EVGAITEETE ACDWWSLGAV LFELLTGKTL VECHPAGINT HTTLNMPECV SEEARSLIQQ LLQFNPLERL GAGVAGVEDI KSHPFFTPVD WAELMR //