STK4_MOUSE
ID STK4_MOUSE Reviewed; 487 AA.
AC Q9JI11;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase 4;
DE EC=2.7.11.1;
DE AltName: Full=Mammalian STE20-like protein kinase 1;
DE Short=MST-1;
DE AltName: Full=STE20-like kinase MST1;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 4 37kDa subunit;
DE Short=MST1/N;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 4 18kDa subunit;
DE Short=MST1/C;
GN Name=Stk4; Synonyms=Mst1;
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], 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-433, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and 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 [7]
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 [8]
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 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates
CC FOXO3 upon oxidative stress, which results in its nuclear translocation
CC and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2.
CC Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to
CC TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on
CC 'Ser-212' and regulates its activation and stimulates transcription of
CC PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits
CC SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53
CC dependent transcription and apoptosis upon DNA damage. Acts as an
CC inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses
CC its activity by intersecting with PKB/AKT1 signaling and antagonizing
CC formation of AR-chromatin complexes (By similarity).
CC {ECO:0000250|UniProtKB:Q13043, 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-183. Activated by
CC RASSF1 which 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 RASSF1. Interacts with FOXO3. Interacts with
CC RASSF2 (via SARAH domain). Interacts with AR, PKB/AKT1, TNNI3 and
CC SIRT1. Interacts with MARK3 and SCRIB in the presence of DLG5 (By
CC similarity). Interacts with DLG5 (via PDZ domain 3) (PubMed:28087714).
CC {ECO:0000250|UniProtKB:Q13043, ECO:0000269|PubMed:28087714}.
CC -!- INTERACTION:
CC Q9JI11; Q5EBH1: Rassf5; NbExp=3; IntAct=EBI-1181352, EBI-960530;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=The caspase-cleaved form cycles between nucleus and cytoplasm.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its:
CC kinase activity, nuclear translocation and autophosphorylation at Thr-
CC 183. It also diminishes its cleavage by caspases and its ability to
CC phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326
CC resulting in a 37 kDa form. Proteolytic cleavage results in kinase
CC activation and nuclear translocation of the truncated form (MST1/N).
CC {ECO:0000269|PubMed:11278283}.
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}.
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DR EMBL; AF271360; AAF75789.1; -; mRNA.
DR EMBL; AK028838; BAC26147.1; -; mRNA.
DR EMBL; BC054521; AAH54521.1; -; mRNA.
DR CCDS; CCDS17021.1; -.
DR RefSeq; NP_067395.1; NM_021420.3.
DR AlphaFoldDB; Q9JI11; -.
DR SMR; Q9JI11; -.
DR BioGRID; 208405; 9.
DR IntAct; Q9JI11; 10.
DR MINT; Q9JI11; -.
DR STRING; 10090.ENSMUSP00000018353; -.
DR iPTMnet; Q9JI11; -.
DR PhosphoSitePlus; Q9JI11; -.
DR EPD; Q9JI11; -.
DR jPOST; Q9JI11; -.
DR MaxQB; Q9JI11; -.
DR PaxDb; Q9JI11; -.
DR PeptideAtlas; Q9JI11; -.
DR PRIDE; Q9JI11; -.
DR ProteomicsDB; 258763; -.
DR Antibodypedia; 3325; 508 antibodies from 42 providers.
DR DNASU; 58231; -.
DR Ensembl; ENSMUST00000018353; ENSMUSP00000018353; ENSMUSG00000018209.
DR GeneID; 58231; -.
DR KEGG; mmu:58231; -.
DR UCSC; uc008ntt.1; mouse.
DR CTD; 6789; -.
DR MGI; MGI:1929004; Stk4.
DR VEuPathDB; HostDB:ENSMUSG00000018209; -.
DR eggNOG; KOG0574; Eukaryota.
DR GeneTree; ENSGT00940000159787; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9JI11; -.
DR OMA; FLKSWSV; -.
DR OrthoDB; 967913at2759; -.
DR PhylomeDB; Q9JI11; -.
DR TreeFam; TF354217; -.
DR BioGRID-ORCS; 58231; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Stk4; mouse.
DR PRO; PR:Q9JI11; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JI11; protein.
DR Bgee; ENSMUSG00000018209; Expressed in peripheral lymph node and 229 other tissues.
DR ExpressionAtlas; Q9JI11; baseline and differential.
DR Genevisible; Q9JI11; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; 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:0000902; P:cell morphogenesis; ISO: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; ISO:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; 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:0018105; P:peptidyl-serine phosphorylation; ISO: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:1903945; P:positive regulation of hepatocyte apoptotic process; IGI:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IMP:CACAO.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0060215; P:primitive hemopoiesis; IGI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP: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 Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_SARAH_domain.
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 Pfam; PF11629; Mst1_SARAH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50951; SARAH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; ATP-binding; Coiled coil; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..487
FT /note="Serine/threonine-protein kinase 4"
FT /id="PRO_0000246627"
FT CHAIN 1..326
FT /note="Serine/threonine-protein kinase 4 37kDa subunit"
FT /id="PRO_0000413741"
FT CHAIN 327..487
FT /note="Serine/threonine-protein kinase 4 18kDa subunit"
FT /id="PRO_0000413742"
FT DOMAIN 30..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 433..480
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 305..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..311
FT /evidence="ECO:0000255"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 326..327
FT /note="Cleavage; by caspase-3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 183
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 387
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13043"
FT MOD_RES 433
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
SQ SEQUENCE 487 AA; 55541 MW; A21E9519AD209C40 CRC64;
METVQLRNPP RRQLKKLDED SLTKQPEEVF DVLEKLGEGS YGSVYKAIHK ETGQIVAIKQ
VPVESDLQEI IKEISIMQQC DSPHVVKYYG SYFKNTDLWI VMEYCGAGSV SDIIRLRNKT
LTEDEIATIL QSTLKGLEYL HFMRKIHRDI KAGNILLNTE GHAKLADFGV AGQLTDTMAK
RNTVIGTPFW MAPEVIQEIG YNCVADIWSL GITAIEMAEG KPPYADIHPM RAIFMIPTNP
PPTFRKPELW SDNFMDFVKQ CLVKSPEQRA TATQLLQHPF VKSAKGVSIL RDLINEAMDV
KLKRQEAQQR EVDQDDEENS EEDEMDSGTM VRAAGDEMGT VRVASTMSGG ANTMIEHGDT
LPSQLGTMVI NTEDEEEEGT MKRRDETMQP AKPSFLEYFE QKEKENQINS FGKNVSGSLK
NSSDWKIPQD GDYEFLKSWT VEDLQKRLLA LDPMMEQEME EIRQKYRSKR QPILDAIEAK
KRRQQNF
