ID STK3_MOUSE Reviewed; 497 AA. AC Q9JI10; Q60877; Q80UG4; Q8CI58; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=Serine/threonine-protein kinase 3; DE EC=2.7.11.1; DE AltName: Full=Mammalian STE20-like protein kinase 2; DE Short=MST-2; DE AltName: Full=STE20-like kinase MST2; DE Contains: DE RecName: Full=Serine/threonine-protein kinase 3 36kDa subunit; DE Short=MST2/N; DE Contains: DE RecName: Full=Serine/threonine-protein kinase 3 20kDa subunit; DE Short=MST2/C; GN Name=Stk3; Synonyms=Mess1, Mst2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEOLYTIC PROCESSING. RC STRAIN=BALB/cJ; RX PubMed=11278283; DOI=10.1074/jbc.m005109200; RA Lee K.-K., Ohyama T., Yajima N., Tsubuki S., Yonehara S.; RT "MST, a physiological caspase substrate, highly sensitizes apoptosis both RT upstream and downstream of caspase activation."; RL J. Biol. Chem. 276:19276-19285(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Han J.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Olfactory epithelium; RA de las Heras R., Mackay-Sim A., Bushell G.R.; RT "Molecular cloning and characterization of mouse MST2 kinase from olfactory RT receptor neurons."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-316 AND SER-391, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012; RA Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K., RA Larsen B.G., Rossant J., Wrana J.L.; RT "The Crumbs complex couples cell density sensing to Hippo-dependent control RT of the TGF-beta-SMAD pathway."; RL Dev. Cell 19:831-844(2010). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=20080689; DOI=10.1073/pnas.0911427107; RA Lu L., Li Y., Kim S.M., Bossuyt W., Liu P., Qiu Q., Wang Y., Halder G., RA Finegold M.J., Lee J.S., Johnson R.L.; RT "Hippo signaling is a potent in vivo growth and tumor suppressor pathway in RT the mammalian liver."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1437-1442(2010). RN [11] RP INTERACTION WITH DLG5. RX PubMed=28087714; DOI=10.1101/gad.284539.116; RA Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S., RA Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.; RT "DLG5 connects cell polarity and Hippo signaling protein networks by RT linking PAR-1 with MST1/2."; RL Genes Dev. 30:2696-2709(2016). CC -!- FUNCTION: Stress-activated, pro-apoptotic kinase which, following CC caspase-cleavage, enters the nucleus and induces chromatin condensation CC followed by internucleosomal DNA fragmentation. Key component of the CC Hippo signaling pathway which plays a pivotal role in organ size CC control and tumor suppression by restricting proliferation and CC promoting apoptosis. The core of this pathway is composed of a kinase CC cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory CC protein SAV1, phosphorylates and activates LATS1/2 in complex with its CC regulatory protein MOB1, which in turn phosphorylates and inactivates CC YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 CC inhibits its translocation into the nucleus to regulate cellular genes CC important for cell proliferation, cell death, and cell migration. CC STK3/MST2 and STK4/MST1 are required to repress proliferation of mature CC hepatocytes, to prevent activation of facultative adult liver stem CC cells (oval cells), and to inhibit tumor formation. Phosphorylates CC NKX2-1. Phosphorylates NEK2 and plays a role in centrosome disjunction CC by regulating the localization of NEK2 to centrosomes, and its ability CC to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates CC the transcriptional activity of ESR1 through the modulation of its CC phosphorylation. Positively regulates RAF1 activation via suppression CC of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates CC MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts CC cooperatively with MOBKL1B to activate STK38 (By similarity). CC {ECO:0000250|UniProtKB:Q13188, ECO:0000269|PubMed:20080689}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited by the C-terminal non-catalytic region. CC Activated by caspase-cleavage. Full activation also requires CC homodimerization and autophosphorylation of Thr-180, which are CC inhibited by the proto-oncogene product RAF1. Activated by RASSF1 which CC acts by preventing its dephosphorylation (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer; mediated via the coiled-coil region. Interacts with CC NORE1, which inhibits autoactivation. Interacts with and stabilizes CC SAV1. Interacts with RAF1, which prevents dimerization and CC phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) CC with NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts CC with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. CC Interacts with RASSF2 (via SARAH domain). Interacts with LATS1; this CC interaction is inhibited in the presence of DLG5. Interacts with MARK3 CC in the presence of DLG5 (By similarity). Interacts with DLG5 (via PDZ CC domain 3) (PubMed:28087714). Interacts with RASSF5; this interaction CC inhibits STK3 autoactivation through heterodimerization (By CC similarity). {ECO:0000250|UniProtKB:Q13188, CC ECO:0000269|PubMed:28087714}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21145499}. Nucleus CC {ECO:0000269|PubMed:21145499}. Note=The caspase-cleaved form cycles CC between nucleus and cytoplasm (By similarity). Phosphorylation at Thr- CC 117 leads to inhibition of nuclear translocation (By similarity). CC {ECO:0000250|UniProtKB:Q13188}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9JI10-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JI10-2; Sequence=VSP_020047; CC -!- PTM: Autophosphorylated on two residues Thr-174 and Thr-180, leading to CC activation. Phosphorylation at Thr-117 and Thr-390 by PKB/AKT1, leads CC to inhibition of its: cleavage, kinase activity, autophosphorylation at CC Thr-180, binding to RASSF1 and nuclear translocation, and increase in CC its binding to RAF1. Phosphorylated at Ser-15 by PLK1, leading to CC activation. {ECO:0000250|UniProtKB:Q13188}. CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic CC cleavage results in kinase activation and nuclear translocation of the CC truncated form (MST1/N). {ECO:0000269|PubMed:11278283}. CC -!- PTM: Ubiquitinated by TRIM69; leading to its redistribution to the CC perinuclear cytoskeleton. {ECO:0000250|UniProtKB:Q13188}. CC -!- DISRUPTION PHENOTYPE: Mice show progressive hepatomegaly with a 2-fold CC increase in liver mass relative to total body mass at 1 month of age CC and a 3-fold increase by 3 months of age. CC {ECO:0000269|PubMed:20080689}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA75300.1; Type=Frameshift; 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; AF271361; AAF75790.1; -; mRNA. DR EMBL; U28726; AAA75300.1; ALT_FRAME; mRNA. DR EMBL; AY058922; AAL29682.1; -; mRNA. DR EMBL; BC037440; AAH37440.1; -; mRNA. DR EMBL; BC049123; AAH49123.2; -; mRNA. DR CCDS; CCDS37059.1; -. [Q9JI10-1] DR RefSeq; NP_062609.2; NM_019635.2. [Q9JI10-1] DR AlphaFoldDB; Q9JI10; -. DR SMR; Q9JI10; -. DR BioGRID; 207869; 3. DR DIP; DIP-61760N; -. DR IntAct; Q9JI10; 4. DR MINT; Q9JI10; -. DR STRING; 10090.ENSMUSP00000018476; -. DR BindingDB; Q9JI10; -. DR ChEMBL; CHEMBL4310; -. DR DrugCentral; Q9JI10; -. DR GlyGen; Q9JI10; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9JI10; -. DR PhosphoSitePlus; Q9JI10; -. DR SwissPalm; Q9JI10; -. DR EPD; Q9JI10; -. DR jPOST; Q9JI10; -. DR MaxQB; Q9JI10; -. DR PaxDb; 10090-ENSMUSP00000018476; -. DR PeptideAtlas; Q9JI10; -. DR ProteomicsDB; 254590; -. [Q9JI10-1] DR ProteomicsDB; 254591; -. [Q9JI10-2] DR Pumba; Q9JI10; -. DR Antibodypedia; 26075; 569 antibodies from 42 providers. DR DNASU; 56274; -. DR Ensembl; ENSMUST00000018476.14; ENSMUSP00000018476.8; ENSMUSG00000022329.16. [Q9JI10-1] DR Ensembl; ENSMUST00000067033.8; ENSMUSP00000064225.8; ENSMUSG00000022329.16. [Q9JI10-2] DR GeneID; 56274; -. DR KEGG; mmu:56274; -. DR UCSC; uc007vlz.1; mouse. [Q9JI10-1] DR UCSC; uc011zrz.1; mouse. [Q9JI10-2] DR AGR; MGI:1928487; -. DR CTD; 6788; -. DR MGI; MGI:1928487; Stk3. DR VEuPathDB; HostDB:ENSMUSG00000022329; -. DR eggNOG; KOG0574; Eukaryota. DR GeneTree; ENSGT00940000154984; -. DR HOGENOM; CLU_000288_63_23_1; -. DR InParanoid; Q9JI10; -. DR OMA; QRMANLD; -. DR OrthoDB; 152877at2759; -. DR PhylomeDB; Q9JI10; -. DR TreeFam; TF354217; -. DR Reactome; R-MMU-2028269; Signaling by Hippo. DR BioGRID-ORCS; 56274; 3 hits in 82 CRISPR screens. DR ChiTaRS; Stk3; mouse. DR PRO; PR:Q9JI10; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q9JI10; Protein. DR Bgee; ENSMUSG00000022329; Expressed in embryonic post-anal tail and 253 other cell types or tissues. DR ExpressionAtlas; Q9JI10; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IGI:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI. DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IGI:MGI. DR GO; GO:0008283; P:cell population proliferation; IGI:MGI. DR GO; GO:0007417; P:central nervous system development; IGI:MGI. DR GO; GO:0003157; P:endocardium development; IGI:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI. DR GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI. DR GO; GO:0035329; P:hippo signaling; IMP:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB. DR GO; GO:0007254; P:JNK cascade; IGI:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IGI:MGI. DR GO; GO:0046621; P:negative regulation of organ growth; IGI:MGI. DR GO; GO:0001841; P:neural tube formation; IGI:MGI. DR GO; GO:0035265; P:organ growth; IGI:MGI. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI. DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IGI:MGI. DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:MGI. DR GO; GO:0060215; P:primitive hemopoiesis; IGI:MGI. DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI. DR GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISO:MGI. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0060800; P:regulation of cell differentiation involved in embryonic placenta development; IGI:MGI. DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central. DR CDD; cd21888; SARAH_MST2; 1. DR CDD; cd06612; STKc_MST1_2; 1. DR Gene3D; 1.10.287.4270; -; 1. DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR024205; Mst1_2_SARAH_domain. DR InterPro; IPR049568; Mst2_SARAH. DR InterPro; IPR036674; p53_tetramer_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR011524; SARAH_dom. DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1. DR PANTHER; PTHR48015:SF23; SERINE_THREONINE-PROTEIN KINASE 3; 1. DR Pfam; PF11629; Mst1_SARAH; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50951; SARAH; 1. DR Genevisible; Q9JI10; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Coiled coil; KW Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase; Ubl conjugation. FT CHAIN 1..497 FT /note="Serine/threonine-protein kinase 3" FT /id="PRO_0000086690" FT CHAIN 1..322 FT /note="Serine/threonine-protein kinase 3 36kDa subunit" FT /id="PRO_0000413715" FT CHAIN 323..497 FT /note="Serine/threonine-protein kinase 3 20kDa subunit" FT /id="PRO_0000413716" FT DOMAIN 27..278 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 443..490 FT /note="SARAH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 301..343 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 368..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 287..328 FT /evidence="ECO:0000255" FT COILED 366..387 FT /evidence="ECO:0000255" FT COILED 448..479 FT /evidence="ECO:0000255" FT COMPBIAS 327..343 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..382 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 33..41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT SITE 322..323 FT /note="Cleavage; by caspase-3" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q13188" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 117 FT /note="Phosphothreonine; by PKB/AKT1" FT /evidence="ECO:0000250|UniProtKB:Q13188" FT MOD_RES 180 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:O54748" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 336 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q13188" FT MOD_RES 390 FT /note="Phosphothreonine; by PKB/AKT1" FT /evidence="ECO:0000250|UniProtKB:Q13188" FT MOD_RES 391 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13188" FT VAR_SEQ 9..78 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020047" SQ SEQUENCE 497 AA; 56855 MW; 9CDD365437581665 CRC64; MEQPPASKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG QVVAIKQVPV ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME YCGAGSVSDI IRLRNKTLTE DEIATILKST LKGLEYLHFM RKIHRDIKAG NILLNTEGHA KLADFGVAGQ LTDTMAKRNT VIGTPFWMAP EVIQEIGYNC VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT FRKPELWSDD FTDFVKKCLV KSPEQRATAT QLLQHPFIKN AKPVSILRDL IAEAMEIKAK RHEEQQRELE EEEENSDEDE LDSHTMVKTS SESVGTMRAT STMSEGAQTM IEHNSTMLES DLGTMVINSE EEEEEEEEEE EDGTMKRNAT SPQVQRPSFM DYFDKQDFKN KSHENCDQSM REPGPMSNSV FPDNWRVPQD GDFDFLKNLS LEELQMRLKA LDPMMEREIE ELHQRYSAKR QPILDAMDAK KRRQQNF //