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Proline-rich AKT1 substrate 1 (40 kDa proline-rich AKT substrate)

 AKTS1_HUMAN             Reviewed;         256 AA.
Q96B36; A8MTQ1; B2RE93; J3KPM3; Q96BI4; Q96IK7; Q96NG2; Q9BWR5;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
28-MAR-2018, entry version 131.
RecName: Full=Proline-rich AKT1 substrate 1;
AltName: Full=40 kDa proline-rich AKT substrate;
Name=AKT1S1 {ECO:0000312|EMBL:AAH16043.1};
Synonyms=PRAS40 {ECO:0000303|PubMed:12524439,
ECO:0000303|PubMed:16174443};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:BAB70937.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Coronary artery;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:AAH16043.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
PRO-47.
TISSUE=Brain {ECO:0000312|EMBL:AAH00031.2},
Eye {ECO:0000312|EMBL:AAH16043.1}, and
Skin {ECO:0000312|EMBL:AAH51844.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6] {ECO:0000305}
INTERACTION WITH 14-3-3, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT
THR-246.
PubMed=12524439; DOI=10.1074/jbc.M210837200;
Kovacina K.S., Park G.Y., Bae S.S., Guzzetta A.W., Schaefer E.,
Birnbaum M.J., Roth R.A.;
"Identification of a proline-rich Akt substrate as a 14-3-3 binding
partner.";
J. Biol. Chem. 278:10189-10194(2003).
[7] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16174443; DOI=10.1111/j.1745-7254.2005.00184.x;
Huang B., Porter G.;
"Expression of proline-rich Akt-substrate PRAS40 in cell survival
pathway and carcinogenesis.";
Acta Pharmacol. Sin. 26:1253-1258(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, AND INTERACTION WITH
RPTOR.
PubMed=17386266; DOI=10.1016/j.molcel.2007.03.003;
Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A.,
Spooner E., Carr S.A., Sabatini D.M.;
"PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein
kinase.";
Mol. Cell 25:903-915(2007).
[10]
FUNCTION, IDENTIFICATION IN THE TORC1 COMPLEX, AND MUTAGENESIS OF
THR-246.
PubMed=17277771; DOI=10.1038/ncb1547;
Vander Haar E., Lee S.-I., Bandhakavi S., Griffin T.J., Kim D.-H.;
"Insulin signalling to mTOR mediated by the Akt/PKB substrate
PRAS40.";
Nat. Cell Biol. 9:316-323(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183;
SER-202; SER-203; SER-211; SER-212 AND THR-246, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183;
SER-202; SER-212 AND THR-246, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-202; SER-203;
SER-211; SER-212 AND THR-246, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-183 AND
THR-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION AT THR-246, AND MUTAGENESIS OF THR-246.
PubMed=23415227; DOI=10.1016/j.cell.2013.01.033;
Wippich F., Bodenmiller B., Trajkovska M.G., Wanka S., Aebersold R.,
Pelkmans L.;
"Dual specificity kinase DYRK3 couples stress granule
condensation/dissolution to mTORC1 signaling.";
Cell 152:791-805(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-203 AND
SER-212, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-202 AND
SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-51, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Subunit of mTORC1, which regulates cell growth and
survival in response to nutrient and hormonal signals. mTORC1 is
activated in response to growth factors or amino acids. Growth
factor-stimulated mTORC1 activation involves a AKT1-mediated
phosphorylation of TSC1-TSC2, which leads to the activation of the
RHEB GTPase that potently activates the protein kinase activity of
mTORC1. Amino acid-signaling to mTORC1 requires its relocalization
to the lysosomes mediated by the Ragulator complex and the Rag
GTPases. Activated mTORC1 up-regulates protein synthesis by
phosphorylating key regulators of mRNA translation and ribosome
synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from
inhibiting the elongation initiation factor 4E (eiF4E). mTORC1
phosphorylates and activates S6K1 at 'Thr-389', which then
promotes protein synthesis by phosphorylating PDCD4 and targeting
it for degradation. Within mTORC1, AKT1S1 negatively regulates
mTOR activity in a manner that is dependent on its phosphorylation
state and binding to 14-3-3 proteins. Inhibits RHEB-GTP-dependent
mTORC1 activation. Substrate for AKT1 phosphorylation, but can
also be activated by AKT1-independent mechanisms. May also play a
role in nerve growth factor-mediated neuroprotection.
{ECO:0000269|PubMed:16174443, ECO:0000269|PubMed:17277771,
ECO:0000269|PubMed:17386266}.
-!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
(mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and
DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin.
Interacts directly with RPTOR. The phosphorylated form interacts
with 14-3-3 proteins. {ECO:0000269|PubMed:12524439,
ECO:0000269|PubMed:17277771, ECO:0000269|PubMed:17386266}.
-!- INTERACTION:
P29311:BMH1 (xeno); NbExp=3; IntAct=EBI-720593, EBI-3661;
Q04917:YWHAH; NbExp=3; IntAct=EBI-720593, EBI-306940;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Note=Found
in the cytosolic fraction of the brain. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334};
IsoId=Q96B36-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:15489334};
IsoId=Q96B36-2; Sequence=VSP_052182;
Note=No experimental confirmation available. {ECO:0000305};
Name=3;
IsoId=Q96B36-3; Sequence=VSP_047536;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels of
expression in liver and heart. Expressed at higher levels in
cancer cell lines (e.g. A-549 and HeLa) than in normal cell lines
(e.g. HEK293). {ECO:0000269|PubMed:12524439,
ECO:0000269|PubMed:16174443}.
-!- PTM: Phosphorylated by AKT1 (PubMed:12524439). Phosphorylation at
Thr-246 by DYRK3 relieves inhibitory function on mTORC1
(PubMed:23415227). {ECO:0000269|PubMed:12524439,
ECO:0000269|PubMed:23415227}.
-!- SEQUENCE CAUTION:
Sequence=AAH00031.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AK055511; BAB70937.1; -; mRNA.
EMBL; AK092610; BAG52583.1; -; mRNA.
EMBL; AK316603; BAG38190.1; -; mRNA.
EMBL; AK226004; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC118341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471177; EAW52570.1; -; Genomic_DNA.
EMBL; CH471177; EAW52568.1; -; Genomic_DNA.
EMBL; BC000031; AAH00031.2; ALT_INIT; mRNA.
EMBL; BC007416; AAH07416.1; -; mRNA.
EMBL; BC015562; AAH15562.1; -; mRNA.
EMBL; BC016043; AAH16043.1; -; mRNA.
EMBL; BC051844; AAH51844.1; -; mRNA.
CCDS; CCDS12784.1; -. [Q96B36-1]
CCDS; CCDS59410.1; -. [Q96B36-3]
RefSeq; NP_001092102.1; NM_001098632.2. [Q96B36-1]
RefSeq; NP_001092103.1; NM_001098633.3. [Q96B36-1]
RefSeq; NP_001265088.1; NM_001278159.1. [Q96B36-1]
RefSeq; NP_001265089.1; NM_001278160.1. [Q96B36-1]
RefSeq; NP_115751.3; NM_032375.5. [Q96B36-3]
UniGene; Hs.515542; -.
UniGene; Hs.610819; -.
PDB; 5WBL; X-ray; 3.35 A; T=124-139.
PDB; 5WBU; X-ray; 3.42 A; O/P/Q/R=173-256.
PDB; 5WBY; X-ray; 3.10 A; O/P=114-207.
PDBsum; 5WBL; -.
PDBsum; 5WBU; -.
PDBsum; 5WBY; -.
ProteinModelPortal; Q96B36; -.
SMR; Q96B36; -.
BioGrid; 124059; 18.
IntAct; Q96B36; 15.
MINT; Q96B36; -.
STRING; 9606.ENSP00000341698; -.
BindingDB; Q96B36; -.
ChEMBL; CHEMBL1255161; -.
iPTMnet; Q96B36; -.
PhosphoSitePlus; Q96B36; -.
DMDM; 74731194; -.
EPD; Q96B36; -.
MaxQB; Q96B36; -.
PaxDb; Q96B36; -.
PeptideAtlas; Q96B36; -.
PRIDE; Q96B36; -.
Ensembl; ENST00000344175; ENSP00000341698; ENSG00000204673. [Q96B36-1]
Ensembl; ENST00000391831; ENSP00000375707; ENSG00000204673. [Q96B36-1]
Ensembl; ENST00000391832; ENSP00000375708; ENSG00000204673. [Q96B36-1]
Ensembl; ENST00000391833; ENSP00000375709; ENSG00000204673. [Q96B36-1]
Ensembl; ENST00000391834; ENSP00000375710; ENSG00000204673. [Q96B36-1]
Ensembl; ENST00000391835; ENSP00000375711; ENSG00000204673. [Q96B36-3]
GeneID; 84335; -.
KEGG; hsa:84335; -.
UCSC; uc002pql.6; human. [Q96B36-1]
CTD; 84335; -.
DisGeNET; 84335; -.
EuPathDB; HostDB:ENSG00000204673.10; -.
GeneCards; AKT1S1; -.
HGNC; HGNC:28426; AKT1S1.
HPA; CAB021903; -.
HPA; HPA043590; -.
HPA; HPA064427; -.
MIM; 610221; gene.
neXtProt; NX_Q96B36; -.
OpenTargets; ENSG00000204673; -.
PharmGKB; PA134943587; -.
eggNOG; ENOG410IXEE; Eukaryota.
eggNOG; ENOG41121RI; LUCA.
GeneTree; ENSGT00390000017397; -.
HOVERGEN; HBG059465; -.
InParanoid; Q96B36; -.
KO; K16184; -.
OMA; RDCEPFF; -.
OrthoDB; EOG091G0IBG; -.
PhylomeDB; Q96B36; -.
Reactome; R-HSA-165159; mTOR signalling.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
SABIO-RK; Q96B36; -.
SignaLink; Q96B36; -.
SIGNOR; Q96B36; -.
ChiTaRS; AKT1S1; human.
GeneWiki; AKT1S1; -.
GenomeRNAi; 84335; -.
PRO; PR:Q96B36; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000204673; -.
CleanEx; HS_AKT1S1; -.
ExpressionAtlas; Q96B36; baseline and differential.
Genevisible; Q96B36; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0045792; P:negative regulation of cell size; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; IDA:UniProtKB.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:InterPro.
GO; GO:0043491; P:protein kinase B signaling; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0038202; P:TORC1 signaling; IBA:GO_Central.
InterPro; IPR026682; AKT1S1.
PANTHER; PTHR21844; PTHR21844; 2.
Pfam; PF15798; PRAS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Methylation; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 256 Proline-rich AKT1 substrate 1.
/FTId=PRO_0000253446.
COMPBIAS 35 43 Poly-Pro. {ECO:0000255}.
COMPBIAS 77 96 Pro-rich. {ECO:0000255}.
MOD_RES 51 51 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D1F4}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 246 246 Phosphothreonine; by PKB/AKT1 and DYRK3.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:12524439,
ECO:0000269|PubMed:23415227}.
VAR_SEQ 1 130 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052182.
VAR_SEQ 1 1 M -> MSFEGGDGAGPAMLATGTARM (in isoform
3). {ECO:0000303|Ref.2}.
/FTId=VSP_047536.
VARIANT 47 47 A -> P (in dbSNP:rs17850191).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_028239.
MUTAGEN 246 246 T->A: Suppresses S6K1 phosphorylation by
mTORC1. {ECO:0000269|PubMed:17277771,
ECO:0000269|PubMed:23415227}.
CONFLICT 108 108 D -> G (in Ref. 1; BAB70937).
{ECO:0000305}.
CONFLICT 196 196 K -> M (in Ref. 1; BAB70937).
{ECO:0000305}.
CONFLICT 233 233 T -> A (in Ref. 1; BAB70937).
{ECO:0000305}.
STRAND 190 192 {ECO:0000244|PDB:5WBY}.
HELIX 213 231 {ECO:0000244|PDB:5WBU}.
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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