KS6C1_HUMAN
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 03-AUG-2022, entry version 172.
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};
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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; 24.
DR IntAct; Q96S38; 12.
DR STRING; 9606.ENSP00000355927; -.
DR ChEMBL; CHEMBL1795193; -.
DR iPTMnet; Q96S38; -.
DR PhosphoSitePlus; Q96S38; -.
DR BioMuta; RPS6KC1; -.
DR DMDM; 94717650; -.
DR EPD; Q96S38; -.
DR jPOST; Q96S38; -.
DR MassIVE; Q96S38; -.
DR MaxQB; Q96S38; -.
DR PaxDb; Q96S38; -.
DR PeptideAtlas; Q96S38; -.
DR PRIDE; Q96S38; -.
DR ProteomicsDB; 3310; -.
DR ProteomicsDB; 78062; -. [Q96S38-1]
DR TopDownProteomics; Q96S38-1; -. [Q96S38-1]
DR Antibodypedia; 34615; 169 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 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; SASEATC; -.
DR OrthoDB; 255297at2759; -.
DR PhylomeDB; Q96S38; -.
DR TreeFam; TF323964; -.
DR PathwayCommons; Q96S38; -.
DR SignaLink; Q96S38; -.
DR BioGRID-ORCS; 26750; 8 hits in 1086 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 192 other tissues.
DR ExpressionAtlas; Q96S38; baseline and differential.
DR Genevisible; Q96S38; HS.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd07287; PX_RPK118_like; 1.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR Gene3D; 3.30.1520.10; -; 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 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; SSF116846; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
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
