KS6B2_HUMAN
ID KS6B2_HUMAN Reviewed; 482 AA.
AC Q9UBS0; B2RMZ9; B4DML8; O94809; Q9UEC1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Ribosomal protein S6 kinase beta-2;
DE Short=S6K-beta-2;
DE Short=S6K2;
DE EC=2.7.11.1;
DE AltName: Full=70 kDa ribosomal protein S6 kinase 2;
DE Short=P70S6K2;
DE Short=p70-S6K 2;
DE AltName: Full=S6 kinase-related kinase;
DE Short=SRK;
DE AltName: Full=Serine/threonine-protein kinase 14B;
DE AltName: Full=p70 ribosomal S6 kinase beta;
DE Short=S6K-beta;
DE Short=p70 S6 kinase beta;
DE Short=p70 S6K-beta;
DE Short=p70 S6KB;
DE Short=p70-beta;
GN Name=RPS6KB2; Synonyms=STK14B;
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), AND VARIANT VAL-420.
RX PubMed=9804755; DOI=10.1074/jbc.273.46.30061;
RA Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V., Waterfield M.D.,
RA Yonezawa K.;
RT "Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6
RT kinase beta containing a proline-rich region.";
RL J. Biol. Chem. 273:30061-30064(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-420.
RX PubMed=9878560; DOI=10.1006/bbrc.1998.9784;
RA Saitoh M., ten Dijke P., Miyazono K., Ichijo H.;
RT "Cloning and characterization of p70 S6Kbeta defines a novel family of p70
RT S6 kinases.";
RL Biochem. Biophys. Res. Commun. 253:470-476(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-420.
RX PubMed=10490847; DOI=10.1038/sj.onc.1202894;
RA Lee-Fruman K.K., Kuo C.J., Lippincott J., Terada N., Blenis J.;
RT "Characterization of S6K2, a novel kinase homologous to S6K1.";
RL Oncogene 18:5108-5114(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Koh H.J., Lee B.N., Choi H.S., Chung J.;
RT "Cloning and characterization of a novel S6 kinase-related kinase, SRK.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-420.
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 [9]
RP PHOSPHORYLATION BY MTOR, AND SUBCELLULAR LOCATION.
RX PubMed=12087098; DOI=10.1074/jbc.m204080200;
RA Park I.H., Bachmann R., Shirazi H., Chen J.;
RT "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin.";
RL J. Biol. Chem. 277:31423-31429(2002).
RN [10]
RP PHOSPHORYLATION AT SER-473, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION
RP SIGNAL.
RX PubMed=12529391; DOI=10.1128/mcb.23.3.852-863.2003;
RA Valovka T., Verdier F., Cramer R., Zhyvoloup A., Fenton T., Rebholz H.,
RA Wang M.L., Gzhegotsky M., Lutsyk A., Matsuka G., Filonenko V., Wang L.,
RA Proud C.G., Parker P.J., Gout I.T.;
RT "Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and
RT regulates its subcellular localization.";
RL Mol. Cell. Biol. 23:852-863(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-423, VARIANT
RP [LARGE SCALE ANALYSIS] VAL-420, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=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 VARIANTS [LARGE SCALE ANALYSIS] LEU-267; MET-368; VAL-420 AND MET-443.
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).
RN [16]
RP FUNCTION.
RX PubMed=29750193; DOI=10.1126/sciadv.aao5838;
RA Nguyen J.T., Ray C., Fox A.L., Mendonca D.B., Kim J.K., Krebsbach P.H.;
RT "Mammalian EAK-7 activates alternative mTOR signaling to regulate cell
RT proliferation and migration.";
RL Sci. Adv. 4:EAAO5838-EAAO5838(2018).
CC -!- FUNCTION: Phosphorylates specifically ribosomal protein S6
CC (PubMed:29750193). Seems to act downstream of mTOR signaling in
CC response to growth factors and nutrients to promote cell proliferation,
CC cell growth and cell cycle progression in an alternative pathway
CC regulated by MEAK7 (PubMed:29750193). {ECO:0000269|PubMed:29750193}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBS0-2; Sequence=VSP_056441, VSP_056442;
CC -!- PTM: Phosphorylated and activated by MTOR. Phosphorylation by PKC
CC within the NLS in response to mitogenic stimuli causes cytoplasmic
CC retention. {ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12529391}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB016869; BAA34402.1; ALT_INIT; mRNA.
DR EMBL; AB019245; BAA37145.1; -; mRNA.
DR EMBL; AF076931; AAD46063.1; -; mRNA.
DR EMBL; AF099739; AAD20990.1; -; mRNA.
DR EMBL; AK297527; BAG59930.1; -; mRNA.
DR EMBL; AP003419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74621.1; -; Genomic_DNA.
DR EMBL; BC000094; AAH00094.3; -; mRNA.
DR EMBL; BC136564; AAI36565.1; -; mRNA.
DR CCDS; CCDS41677.1; -. [Q9UBS0-1]
DR PIR; JE0377; JE0377.
DR RefSeq; NP_003943.2; NM_003952.2. [Q9UBS0-1]
DR AlphaFoldDB; Q9UBS0; -.
DR SMR; Q9UBS0; -.
DR BioGRID; 112113; 231.
DR ELM; Q9UBS0; -.
DR IntAct; Q9UBS0; 21.
DR MINT; Q9UBS0; -.
DR STRING; 9606.ENSP00000308413; -.
DR BindingDB; Q9UBS0; -.
DR ChEMBL; CHEMBL3111; -.
DR iPTMnet; Q9UBS0; -.
DR PhosphoSitePlus; Q9UBS0; -.
DR BioMuta; RPS6KB2; -.
DR DMDM; 296434560; -.
DR EPD; Q9UBS0; -.
DR jPOST; Q9UBS0; -.
DR MassIVE; Q9UBS0; -.
DR MaxQB; Q9UBS0; -.
DR PaxDb; Q9UBS0; -.
DR PeptideAtlas; Q9UBS0; -.
DR PRIDE; Q9UBS0; -.
DR ProteomicsDB; 4623; -.
DR ProteomicsDB; 84044; -. [Q9UBS0-1]
DR Antibodypedia; 1546; 805 antibodies from 39 providers.
DR DNASU; 6199; -.
DR Ensembl; ENST00000312629.10; ENSP00000308413.5; ENSG00000175634.15. [Q9UBS0-1]
DR Ensembl; ENST00000528964.5; ENSP00000432847.1; ENSG00000175634.15. [Q9UBS0-2]
DR GeneID; 6199; -.
DR KEGG; hsa:6199; -.
DR MANE-Select; ENST00000312629.10; ENSP00000308413.5; NM_003952.3; NP_003943.2.
DR UCSC; uc001old.4; human. [Q9UBS0-1]
DR CTD; 6199; -.
DR DisGeNET; 6199; -.
DR GeneCards; RPS6KB2; -.
DR HGNC; HGNC:10437; RPS6KB2.
DR HPA; ENSG00000175634; Low tissue specificity.
DR MIM; 608939; gene.
DR neXtProt; NX_Q9UBS0; -.
DR OpenTargets; ENSG00000175634; -.
DR PharmGKB; PA34852; -.
DR VEuPathDB; HostDB:ENSG00000175634; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000155062; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q9UBS0; -.
DR OMA; CVIYDMM; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; Q9UBS0; -.
DR TreeFam; TF313438; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q9UBS0; -.
DR Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR SignaLink; Q9UBS0; -.
DR SIGNOR; Q9UBS0; -.
DR BioGRID-ORCS; 6199; 14 hits in 1107 CRISPR screens.
DR ChiTaRS; RPS6KB2; human.
DR GeneWiki; RPS6KB2; -.
DR GenomeRNAi; 6199; -.
DR Pharos; Q9UBS0; Tchem.
DR PRO; PR:Q9UBS0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UBS0; protein.
DR Bgee; ENSG00000175634; Expressed in lower esophagus mucosa and 140 other tissues.
DR ExpressionAtlas; Q9UBS0; baseline and differential.
DR Genevisible; Q9UBS0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; IMP:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016238; Ribosomal_S6_kinase.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000605; Ribsml_S6_kin_1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..482
FT /note="Ribosomal protein S6 kinase beta-2"
FT /id="PRO_0000086214"
FT DOMAIN 67..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 329..399
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 471..477
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12529391"
FT COMPBIAS 435..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 473
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:12529391"
FT VAR_SEQ 153..154
FT /note="GG -> VD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056441"
FT VAR_SEQ 155..482
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056442"
FT VARIANT 267
FT /note="P -> L (in dbSNP:rs55987642)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040643"
FT VARIANT 368
FT /note="V -> M (in dbSNP:rs55642995)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040644"
FT VARIANT 420
FT /note="A -> V (in dbSNP:rs13859)"
FT /evidence="ECO:0000269|PubMed:10490847,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:9804755, ECO:0000269|PubMed:9878560,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_040645"
FT VARIANT 443
FT /note="T -> M (in an ovarian mucinous carcinoma sample;
FT somatic mutation; dbSNP:rs374535834)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040646"
FT CONFLICT 90
FT /note="Missing (in Ref. 2; BAA37145)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> C (in Ref. 2; BAA37145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 53455 MW; 5D33660D24A2C7BE CRC64;
MAAVFDLDLE TEEGSEGEGE PELSPADACP LAELRAAGLE PVGHYEEVEL TETSVNVGPE
RIGPHCFELL RVLGKGGYGK VFQVRKVQGT NLGKIYAMKV LRKAKIVRNA KDTAHTRAER
NILESVKHPF IVELAYAFQT GGKLYLILEC LSGGELFTHL EREGIFLEDT ACFYLAEITL
ALGHLHSQGI IYRDLKPENI MLSSQGHIKL TDFGLCKESI HEGAVTHTFC GTIEYMAPEI
LVRSGHNRAV DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIRGKLALPP YLTPDARDLV
KKFLKRNPSQ RIGGGPGDAA DVQRHPFFRH MNWDDLLAWR VDPPFRPCLQ SEEDVSQFDT
RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE GFSFQPKLRS PRRLNSSPRA
PVSPLKFSPF EGFRPSPSLP EPTELPLPPL LPPPPPSTTA PLPIRPPSGT KKSKRGRGRP
GR
