GenomeNet

Database: UniProt
Entry: Q96B36
LinkDB: Q96B36
Original site: Q96B36 
ID   AKTS1_HUMAN             Reviewed;         256 AA.
AC   Q96B36; A8MTQ1; B2RE93; J3KPM3; Q96BI4; Q96IK7; Q96NG2; Q9BWR5;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 147.
DE   RecName: Full=Proline-rich AKT1 substrate 1;
DE   AltName: Full=40 kDa proline-rich AKT substrate;
GN   Name=AKT1S1 {ECO:0000312|EMBL:AAH16043.1};
GN   Synonyms=PRAS40 {ECO:0000303|PubMed:12524439, ECO:0000303|PubMed:16174443};
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] {ECO:0000305, ECO:0000312|EMBL:BAB70937.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Prostate, and Synovium;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Coronary artery;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
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   [5] {ECO:0000305, ECO:0000312|EMBL:AAH16043.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   PRO-47.
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH00031.2},
RC   Eye {ECO:0000312|EMBL:AAH16043.1}, and Skin {ECO:0000312|EMBL:AAH51844.1};
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   [6] {ECO:0000305}
RP   INTERACTION WITH 14-3-3, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT
RP   THR-246.
RX   PubMed=12524439; DOI=10.1074/jbc.m210837200;
RA   Kovacina K.S., Park G.Y., Bae S.S., Guzzetta A.W., Schaefer E.,
RA   Birnbaum M.J., Roth R.A.;
RT   "Identification of a proline-rich Akt substrate as a 14-3-3 binding
RT   partner.";
RL   J. Biol. Chem. 278:10189-10194(2003).
RN   [7] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16174443; DOI=10.1111/j.1745-7254.2005.00184.x;
RA   Huang B., Porter G.;
RT   "Expression of proline-rich Akt-substrate PRAS40 in cell survival pathway
RT   and carcinogenesis.";
RL   Acta Pharmacol. Sin. 26:1253-1258(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, 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   [9]
RP   FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, AND INTERACTION WITH RPTOR.
RX   PubMed=17386266; DOI=10.1016/j.molcel.2007.03.003;
RA   Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A.,
RA   Spooner E., Carr S.A., Sabatini D.M.;
RT   "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase.";
RL   Mol. Cell 25:903-915(2007).
RN   [10]
RP   FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, AND MUTAGENESIS OF THR-246.
RX   PubMed=17277771; DOI=10.1038/ncb1547;
RA   Vander Haar E., Lee S.-I., Bandhakavi S., Griffin T.J., Kim D.-H.;
RT   "Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40.";
RL   Nat. Cell Biol. 9:316-323(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183; SER-202;
RP   SER-203; SER-211; SER-212 AND THR-246, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183; SER-202;
RP   SER-212 AND THR-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-202; SER-203;
RP   SER-211; SER-212 AND THR-246, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183 AND
RP   THR-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [17]
RP   PHOSPHORYLATION AT THR-246, AND MUTAGENESIS OF THR-246.
RX   PubMed=23415227; DOI=10.1016/j.cell.2013.01.033;
RA   Wippich F., Bodenmiller B., Trajkovska M.G., Wanka S., Aebersold R.,
RA   Pelkmans L.;
RT   "Dual specificity kinase DYRK3 couples stress granule
RT   condensation/dissolution to mTORC1 signaling.";
RL   Cell 152:791-805(2013).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-203 AND SER-212, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-202 AND
RP   SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-51, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [21]
RP   PHOSPHORYLATION AT THR-246.
RX   PubMed=29634919; DOI=10.1016/j.jmb.2018.04.001;
RA   Kim K., Cha J.S., Cho Y.S., Kim H., Chang N., Kim H.J., Cho H.S.;
RT   "Crystal structure of human dual-specificity tyrosine-regulated kinase 3
RT   reveals new structural features and insights into its auto-
RT   phosphorylation.";
RL   J. Mol. Biol. 430:1521-1530(2018).
CC   -!- FUNCTION: Subunit of mTORC1, which regulates cell growth and survival
CC       in response to nutrient and hormonal signals. mTORC1 is activated in
CC       response to growth factors or amino acids. Growth factor-stimulated
CC       mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-
CC       TSC2, which leads to the activation of the RHEB GTPase that potently
CC       activates the protein kinase activity of mTORC1. Amino acid-signaling
CC       to mTORC1 requires its relocalization to the lysosomes mediated by the
CC       Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates
CC       protein synthesis by phosphorylating key regulators of mRNA translation
CC       and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it
CC       from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1
CC       phosphorylates and activates S6K1 at 'Thr-389', which then promotes
CC       protein synthesis by phosphorylating PDCD4 and targeting it for
CC       degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity
CC       in a manner that is dependent on its phosphorylation state and binding
CC       to 14-3-3 proteins. Inhibits RHEB-GTP-dependent mTORC1 activation.
CC       Substrate for AKT1 phosphorylation, but can also be activated by AKT1-
CC       independent mechanisms. May also play a role in nerve growth factor-
CC       mediated neuroprotection. {ECO:0000269|PubMed:16174443,
CC       ECO:0000269|PubMed:17277771, ECO:0000269|PubMed:17386266}.
CC   -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC       which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1
CC       binds to and is inhibited by FKBP12-rapamycin. Interacts directly with
CC       RPTOR. The phosphorylated form interacts with 14-3-3 proteins.
CC       {ECO:0000269|PubMed:12524439, ECO:0000269|PubMed:17277771,
CC       ECO:0000269|PubMed:17386266}.
CC   -!- INTERACTION:
CC       P29311:BMH1 (xeno); NbExp=3; IntAct=EBI-720593, EBI-3661;
CC       Q04917:YWHAH; NbExp=4; IntAct=EBI-720593, EBI-306940;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Note=Found in
CC       the cytosolic fraction of the brain. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334};
CC         IsoId=Q96B36-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334};
CC         IsoId=Q96B36-2; Sequence=VSP_052182;
CC       Name=3;
CC         IsoId=Q96B36-3; Sequence=VSP_047536;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels of expression
CC       in liver and heart. Expressed at higher levels in cancer cell lines
CC       (e.g. A-549 and HeLa) than in normal cell lines (e.g. HEK293).
CC       {ECO:0000269|PubMed:12524439, ECO:0000269|PubMed:16174443}.
CC   -!- PTM: Phosphorylated by AKT1 (PubMed:12524439). Phosphorylation at Thr-
CC       246 by DYRK3 relieves inhibitory function on mTORC1 (PubMed:23415227).
CC       {ECO:0000269|PubMed:12524439, ECO:0000269|PubMed:23415227}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH00031.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AK055511; BAB70937.1; -; mRNA.
DR   EMBL; AK092610; BAG52583.1; -; mRNA.
DR   EMBL; AK316603; BAG38190.1; -; mRNA.
DR   EMBL; AK226004; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC118341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52570.1; -; Genomic_DNA.
DR   EMBL; CH471177; EAW52568.1; -; Genomic_DNA.
DR   EMBL; BC000031; AAH00031.2; ALT_INIT; mRNA.
DR   EMBL; BC007416; AAH07416.1; -; mRNA.
DR   EMBL; BC015562; AAH15562.1; -; mRNA.
DR   EMBL; BC016043; AAH16043.1; -; mRNA.
DR   EMBL; BC051844; AAH51844.1; -; mRNA.
DR   CCDS; CCDS12784.1; -. [Q96B36-1]
DR   CCDS; CCDS59410.1; -. [Q96B36-3]
DR   RefSeq; NP_001092102.1; NM_001098632.2. [Q96B36-1]
DR   RefSeq; NP_001092103.1; NM_001098633.3. [Q96B36-1]
DR   RefSeq; NP_001265088.1; NM_001278159.1. [Q96B36-1]
DR   RefSeq; NP_001265089.1; NM_001278160.1. [Q96B36-1]
DR   RefSeq; NP_115751.3; NM_032375.5. [Q96B36-3]
DR   PDB; 5WBL; X-ray; 3.35 A; T=124-139.
DR   PDB; 5WBU; X-ray; 3.42 A; O/P/Q/R=173-256.
DR   PDB; 5WBY; X-ray; 3.10 A; O/P=114-207.
DR   PDBsum; 5WBL; -.
DR   PDBsum; 5WBU; -.
DR   PDBsum; 5WBY; -.
DR   SMR; Q96B36; -.
DR   BioGrid; 124059; 24.
DR   IntAct; Q96B36; 15.
DR   MINT; Q96B36; -.
DR   STRING; 9606.ENSP00000375711; -.
DR   BindingDB; Q96B36; -.
DR   ChEMBL; CHEMBL1255161; -.
DR   iPTMnet; Q96B36; -.
DR   PhosphoSitePlus; Q96B36; -.
DR   BioMuta; AKT1S1; -.
DR   DMDM; 74731194; -.
DR   CPTAC; CPTAC-1038; -.
DR   CPTAC; CPTAC-785; -.
DR   CPTAC; CPTAC-787; -.
DR   EPD; Q96B36; -.
DR   jPOST; Q96B36; -.
DR   MassIVE; Q96B36; -.
DR   MaxQB; Q96B36; -.
DR   PaxDb; Q96B36; -.
DR   PeptideAtlas; Q96B36; -.
DR   PRIDE; Q96B36; -.
DR   ProteomicsDB; 76040; -. [Q96B36-1]
DR   ProteomicsDB; 76041; -. [Q96B36-2]
DR   Ensembl; ENST00000344175; ENSP00000341698; ENSG00000204673. [Q96B36-1]
DR   Ensembl; ENST00000391831; ENSP00000375707; ENSG00000204673. [Q96B36-1]
DR   Ensembl; ENST00000391832; ENSP00000375708; ENSG00000204673. [Q96B36-1]
DR   Ensembl; ENST00000391833; ENSP00000375709; ENSG00000204673. [Q96B36-1]
DR   Ensembl; ENST00000391834; ENSP00000375710; ENSG00000204673. [Q96B36-1]
DR   Ensembl; ENST00000391835; ENSP00000375711; ENSG00000204673. [Q96B36-3]
DR   GeneID; 84335; -.
DR   KEGG; hsa:84335; -.
DR   UCSC; uc002pql.6; human. [Q96B36-1]
DR   CTD; 84335; -.
DR   DisGeNET; 84335; -.
DR   EuPathDB; HostDB:ENSG00000204673.10; -.
DR   GeneCards; AKT1S1; -.
DR   HGNC; HGNC:28426; AKT1S1.
DR   HPA; CAB021903; -.
DR   HPA; HPA043590; -.
DR   HPA; HPA064427; -.
DR   MIM; 610221; gene.
DR   neXtProt; NX_Q96B36; -.
DR   OpenTargets; ENSG00000204673; -.
DR   PharmGKB; PA134943587; -.
DR   eggNOG; ENOG410IXEE; Eukaryota.
DR   eggNOG; ENOG41121RI; LUCA.
DR   GeneTree; ENSGT00390000017397; -.
DR   InParanoid; Q96B36; -.
DR   KO; K16184; -.
DR   OMA; AYCQKSG; -.
DR   OrthoDB; 927670at2759; -.
DR   PhylomeDB; Q96B36; -.
DR   Reactome; R-HSA-165159; mTOR signalling.
DR   Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR   Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
DR   Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR   Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR   SABIO-RK; Q96B36; -.
DR   SignaLink; Q96B36; -.
DR   SIGNOR; Q96B36; -.
DR   ChiTaRS; AKT1S1; human.
DR   GeneWiki; AKT1S1; -.
DR   GenomeRNAi; 84335; -.
DR   Pharos; Q96B36; Tchem.
DR   PRO; PR:Q96B36; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96B36; protein.
DR   Bgee; ENSG00000204673; Expressed in 169 organ(s), highest expression level in gastrocnemius.
DR   ExpressionAtlas; Q96B36; baseline and differential.
DR   Genevisible; Q96B36; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR   GO; GO:0045792; P:negative regulation of cell size; IDA:UniProtKB.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IDA:UniProtKB.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR   InterPro; IPR026682; AKT1S1.
DR   PANTHER; PTHR21844; PTHR21844; 1.
DR   Pfam; PF15798; PRAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein;
KW   Polymorphism; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Proline-rich AKT1 substrate 1"
FT                   /id="PRO_0000253446"
FT   COMPBIAS        35..43
FT                   /note="Poly-Pro"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        77..96
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         51
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D1F4"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         246
FT                   /note="Phosphothreonine; by PKB/AKT1 and DYRK3"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000269|PubMed:12524439,
FT                   ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919"
FT   VAR_SEQ         1..130
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052182"
FT   VAR_SEQ         1
FT                   /note="M -> MSFEGGDGAGPAMLATGTARM (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_047536"
FT   VARIANT         47
FT                   /note="A -> P (in dbSNP:rs17850191)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028239"
FT   MUTAGEN         246
FT                   /note="T->A: Suppresses S6K1 phosphorylation by mTORC1."
FT                   /evidence="ECO:0000269|PubMed:17277771,
FT                   ECO:0000269|PubMed:23415227"
FT   CONFLICT        108
FT                   /note="D -> G (in Ref. 1; BAB70937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="K -> M (in Ref. 1; BAB70937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        233
FT                   /note="T -> A (in Ref. 1; BAB70937)"
FT                   /evidence="ECO:0000305"
FT   STRAND          190..192
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           213..231
FT                   /evidence="ECO:0000244|PDB:5WBU"
SQ   SEQUENCE   256 AA;  27383 MW;  F6CB195CBB54326C CRC64;
     MASGRPEELW EAVVGAAERF RARTGTELVL LTAAPPPPPR PGPCAYAAHG RGALAEAARR
     CLHDIALAHR AATAARPPAP PPAPQPPSPT PSPPRPTLAR EDNEEDEDEP TETETSGEQL
     GISDNGGLFV MDEDATLQDL PPFCESDPES TDDGSLSEET PAGPPTCSVP PASALPTQQY
     AKSLPVSVPV WGFKEKRTEA RSSDEENGPP SSPDLDRIAA SMRALVLREA EDTQVFGDLP
     RPRLNTSDFQ KLKRKY
//
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