ID KS6A1_HUMAN STANDARD; PRT; 735 AA. AC Q15418; Q5SVM5; Q5SVM8; Q5SVM9; Q96C05; Q9BQK2; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 04-APR-2006, entry version 55. DE Ribosomal protein S6 kinase alpha 1 (EC 2.7.11.1) (S6K-alpha 1) (90 DE kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (Ribosomal S6 kinase 1) DE (RSK-1) (pp90RSK1) (MAP kinase-activated protein kinase 1a) DE (MAPKAPK1A). GN Name=RPS6KA1; Synonyms=RSK1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-335. RX MEDLINE=94189676; PubMed=8141249; RA Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.; RT "Human rsk isoforms: cloning and characterization of tissue-specific RT expression."; RL Am. J. Physiol. 266:C351-C359(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Human chromosome 1 international sequencing consortium; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP SUBCELLULAR LOCATION. RX MEDLINE=98353467; PubMed=9687510; DOI=10.1093/emboj/17.15.4426; RA Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.; RT "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly RT activated by MAPK and SAPK2/p38, and may mediate activation of CREB."; RL EMBO J. 17:4426-4441(1998). RN [5] RP FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION OF SER-221; THR-359; RP SER-363; SER-380; THR-573 AND SER-732. RX PubMed=9430688; DOI=10.1074/jbc.273.3.1496; RA Dalby K.N., Morrice N., Caudwell F.B., Avruch J., Cohen P.; RT "Identification of regulatory phosphorylation sites in mitogen- RT activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk RT that are inducible by MAPK."; RL J. Biol. Chem. 273:1496-1505(1998). RN [6] RP INTERACTION WITH MAPK1 OR MAPK3. RX PubMed=12832467; DOI=10.1128/MCB.23.14.4796-4804.2003; RA Roux P.P., Richards S.A., Blenis J.; RT "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates RT extracellular signal-regulated kinase docking and RSK activity."; RL Mol. Cell. Biol. 23:4796-4804(2003). CC -!- FUNCTION: Serine/threonine kinase that may play a role in CC mediating the growth-factor and stress induced activation of the CC transcription factor CREB. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: Magnesium. CC -!- ENZYME REGULATION: Activated by multiple phosphorylations on CC threonine and serine residues. CC -!- SUBUNIT: Forms a complex with either ERK1 or ERK2 in quiescent CC cells. Transiently dissociates following mitogenic stimulation. CC -!- PTM: Autophosphorylated on Ser-380, as part of the activation CC process. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. S6 CC kinase subfamily. 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; L07597; AAC82497.1; -; mRNA. DR EMBL; AL109743; CAC36348.1; -; Genomic_DNA. DR EMBL; AL627313; CAI14647.1; -; Genomic_DNA. DR EMBL; AL627313; CAI14648.1; -; Genomic_DNA. DR EMBL; AL627313; CAI14649.1; -; Genomic_DNA. DR EMBL; BC014966; AAH14966.1; -; mRNA. DR PIR; I51901; I51901. DR UniGene; Hs.149957; -. DR HSSP; P31751; 1GZK. DR Ensembl; ENSG00000117676; Homo sapiens. DR H-InvDB; HIX0022890; -. DR HGNC; HGNC:10430; RPS6KA1. DR MIM; 601684; gene. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 2. DR Pfam; PF00433; Pkinase_C; 1. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2. KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Phosphorylation; Polymorphism; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 735 Ribosomal protein S6 kinase alpha 1. FT /FTId=PRO_0000086198. FT DOMAIN 62 321 Protein kinase 1. FT DOMAIN 418 675 Protein kinase 2. FT NP_BIND 68 76 ATP (By similarity). FT NP_BIND 424 432 ATP (By similarity). FT ACT_SITE 187 187 Proton acceptor (By similarity). FT ACT_SITE 535 535 Proton acceptor (By similarity). FT BINDING 94 94 ATP (By similarity). FT BINDING 447 447 ATP (By similarity). FT MOD_RES 221 221 Phosphoserine. FT MOD_RES 348 348 Phosphothreonine. FT MOD_RES 363 363 Phosphoserine. FT MOD_RES 380 380 Phosphoserine (by autocatalysis). FT MOD_RES 573 573 Phosphothreonine. FT MOD_RES 732 732 Phosphoserine. FT VARIANT 335 335 K -> T (in dbSNP:3816540). FT /FTId=VAR_021864. SQ SEQUENCE 735 AA; 82723 MW; 765731A4442A53DF CRC64; MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV KAGSEKADPS HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT LKVRDRVRTK MERDILADVN HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF TRLSKEVMFT EEDVKFYLAE LALGLDHLHS LGIIYRDLKP ENILLDEEGH IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS HSADWWSYGV LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREIKPPFKP AVAQPDDTFY FDTEFTSRTP KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL HSVVQQLHGK NLVFSDGYVV KETIGVGSYS ECKRCVHKAT NMEYAVKVID KSKRDPSEEI EILLRYGQHP NIITLKDVYD DGKHVYLVTE LMRGGELLDK ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN ILYVDESGNP ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD LVSKMLHVDP HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA TYSALNSSKP TPQLKPIESS ILAQRRVRKL PSTTL //