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 27-MAR-2024, entry version 217. 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}; 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; 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; 256. DR ELM; Q9UBS0; -. DR IntAct; Q9UBS0; 22. 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 CPTAC; CPTAC-2967; -. DR CPTAC; CPTAC-2968; -. DR EPD; Q9UBS0; -. DR jPOST; Q9UBS0; -. DR MassIVE; Q9UBS0; -. DR MaxQB; Q9UBS0; -. DR PaxDb; 9606-ENSP00000308413; -. DR PeptideAtlas; Q9UBS0; -. DR ProteomicsDB; 4623; -. DR ProteomicsDB; 84044; -. [Q9UBS0-1] DR Pumba; Q9UBS0; -. DR Antibodypedia; 1546; 937 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 AGR; HGNC:10437; -. 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; DGHICIT; -. DR OrthoDB; 5489497at2759; -. 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 1191 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 142 other cell types or tissues. DR ExpressionAtlas; Q9UBS0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; 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; IDA:UniProt. DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; IEA:Ensembl. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:UniProt. 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 CDD; cd05584; STKc_p70S6K; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR PANTHER; PTHR24351:SF171; RIBOSOMAL PROTEIN S6 KINASE BETA-2; 1. 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; Protein kinase-like (PK-like); 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. DR Genevisible; Q9UBS0; HS. 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 //