PRR5_HUMAN
ID PRR5_HUMAN Reviewed; 388 AA.
AC P85299; B1AHF6; B1AHG5; B3KP73; O75983; O95695; Q5BIW2; Q5EAJ8; Q5EAJ9;
AC Q5XKJ6; Q96RW1; Q96RW2; Q9HA49; Q9HC46; Q9NSG0; Q9NVX8; Q9NXL1; Q9UH20;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Proline-rich protein 5;
DE AltName: Full=Protein observed with Rictor-1;
DE Short=Protor-1;
GN Name=PRR5; Synonyms=PROTOR1; ORFNames=PP610;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Colon mucosa, and Kidney;
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 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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]
RP IDENTIFICATION (ISOFORMS 1; 3 AND 4), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15718101; DOI=10.1016/j.ygeno.2004.11.002;
RA Johnstone C.N., Castellvi-Bel S., Chang L.M., Sung R.K., Bowser M.J.,
RA Pique J.M., Castells A., Rustgi A.K.;
RT "PRR5 encodes a conserved proline-rich protein predominant in kidney:
RT analysis of genomic organization, expression, and mutation status in breast
RT and colorectal carcinomas.";
RL Genomics 85:338-351(2005).
RN [7]
RP IDENTIFICATION IN THE TORC2 COMPLEX, AND INTERACTION WITH RICTOR.
RX PubMed=17461779; DOI=10.1042/bj20070540;
RA Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S., Deak M.,
RA Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R.;
RT "Identification of Protor as a novel Rictor-binding component of mTOR
RT complex-2.";
RL Biochem. J. 405:513-522(2007).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH MTOR AND
RP RICTOR, AND TISSUE SPECIFICITY.
RX PubMed=17599906; DOI=10.1074/jbc.m704343200;
RA Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I.,
RA Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.;
RT "PRR5, a novel component of mTOR complex 2, regulates platelet-derived
RT growth factor receptor beta expression and signaling.";
RL J. Biol. Chem. 282:25604-25612(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP 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).
CC -!- FUNCTION: Subunit of mTORC2, which regulates cell growth and survival
CC in response to hormonal signals. mTORC2 is activated by growth factors,
CC but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2
CC seems to function upstream of Rho GTPases to regulate the actin
CC cytoskeleton, probably by activating one or more Rho-type guanine
CC nucleotide exchange factors. mTORC2 promotes the serum-induced
CC formation of stress-fibers or F-actin. mTORC2 plays a critical role in
CC AKT1 'Ser-473' phosphorylation, which may facilitate the
CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1
CC which is a prerequisite for full activation. mTORC2 regulates the
CC phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the
CC phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in
CC regulation of PDGFRB expression and in modulation of platelet-derived
CC growth factor signaling. May act as a tumor suppressor in breast
CC cancer. {ECO:0000269|PubMed:15718101, ECO:0000269|PubMed:17599906}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2)
CC which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary
CC to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-
CC rapamycin. Binds directly to MTOR and RICTOR within the TORC2 complex.
CC {ECO:0000269|PubMed:17461779, ECO:0000269|PubMed:17599906}.
CC -!- INTERACTION:
CC P85299; Q12959: DLG1; NbExp=2; IntAct=EBI-1387467, EBI-357481;
CC P85299-2; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-12944296, EBI-11962928;
CC P85299-2; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-12944296, EBI-2806959;
CC P85299-2; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-12944296, EBI-347538;
CC P85299-2; O14964: HGS; NbExp=3; IntAct=EBI-12944296, EBI-740220;
CC P85299-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12944296, EBI-739895;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=alpha;
CC IsoId=P85299-1, Q9NSG0-5;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P85299-2, Q9NSG0-8;
CC Sequence=VSP_001646, VSP_001648;
CC Name=3; Synonyms=beta;
CC IsoId=P85299-3; Sequence=VSP_028885;
CC Name=4; Synonyms=gamma;
CC IsoId=P85299-4; Sequence=VSP_028884;
CC Name=5;
CC IsoId=P85299-5; Sequence=VSP_045883;
CC -!- TISSUE SPECIFICITY: Most abundant in kidney and liver. Also highly
CC expressed in brain, spleen, testis and placenta. Overexpressed in
CC several colorectal tumors. {ECO:0000269|PubMed:15718101,
CC ECO:0000269|PubMed:17599906}.
CC -!- SIMILARITY: Belongs to the PROTOR family. {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; AK000192; BAA90999.1; -; mRNA.
DR EMBL; AK055848; BAG51585.1; -; mRNA.
DR EMBL; AF177331; AAG17975.1; -; mRNA.
DR EMBL; Z93244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73353.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73355.1; -; Genomic_DNA.
DR EMBL; BC016921; AAH16921.1; -; mRNA.
DR EMBL; BK005635; DAA05654.1; -; mRNA.
DR EMBL; BK005636; DAA05655.1; -; mRNA.
DR EMBL; BK005637; DAA05656.1; -; mRNA.
DR EMBL; BK005638; DAA05657.1; -; mRNA.
DR EMBL; BK005639; DAA05658.1; -; mRNA.
DR CCDS; CCDS14058.1; -.
DR CCDS; CCDS14059.1; -. [P85299-3]
DR CCDS; CCDS56232.1; -. [P85299-5]
DR CCDS; CCDS74875.1; -. [P85299-4]
DR RefSeq; NP_001017528.1; NM_001017528.2. [P85299-3]
DR RefSeq; NP_001017529.1; NM_001017529.2. [P85299-4]
DR RefSeq; NP_001017530.1; NM_001017530.1. [P85299-4]
DR RefSeq; NP_001185650.1; NM_001198721.1. [P85299-5]
DR RefSeq; NP_056181.2; NM_015366.3. [P85299-3]
DR RefSeq; NP_851850.1; NM_181333.3. [P85299-1]
DR AlphaFoldDB; P85299; -.
DR SMR; P85299; -.
DR BioGRID; 120755; 38.
DR ComplexPortal; CPX-4402; mTORC2 complex.
DR IntAct; P85299; 25.
DR MINT; P85299; -.
DR STRING; 9606.ENSP00000384848; -.
DR GlyGen; P85299; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P85299; -.
DR PhosphoSitePlus; P85299; -.
DR BioMuta; PRR5; -.
DR DMDM; 160016058; -.
DR EPD; P85299; -.
DR jPOST; P85299; -.
DR MassIVE; P85299; -.
DR MaxQB; P85299; -.
DR PaxDb; P85299; -.
DR PeptideAtlas; P85299; -.
DR PRIDE; P85299; -.
DR ProteomicsDB; 2938; -.
DR ProteomicsDB; 57768; -.
DR ProteomicsDB; 57769; -. [P85299-2]
DR ProteomicsDB; 57770; -. [P85299-3]
DR ProteomicsDB; 57771; -. [P85299-4]
DR Antibodypedia; 46008; 192 antibodies from 30 providers.
DR DNASU; 55615; -.
DR Ensembl; ENST00000006251.11; ENSP00000006251.7; ENSG00000186654.21. [P85299-3]
DR Ensembl; ENST00000336985.11; ENSP00000337464.6; ENSG00000186654.21. [P85299-1]
DR Ensembl; ENST00000403581.5; ENSP00000384848.1; ENSG00000186654.21. [P85299-5]
DR Ensembl; ENST00000611394.4; ENSP00000480357.1; ENSG00000186654.21. [P85299-3]
DR Ensembl; ENST00000617066.4; ENSP00000479623.1; ENSG00000186654.21. [P85299-4]
DR Ensembl; ENST00000624862.3; ENSP00000485597.1; ENSG00000186654.21. [P85299-4]
DR GeneID; 55615; -.
DR KEGG; hsa:55615; -.
DR MANE-Select; ENST00000336985.11; ENSP00000337464.6; NM_181333.4; NP_851850.1.
DR UCSC; uc003bew.2; human.
DR CTD; 55615; -.
DR DisGeNET; 55615; -.
DR GeneCards; PRR5; -.
DR HGNC; HGNC:31682; PRR5.
DR HPA; ENSG00000186654; Low tissue specificity.
DR MIM; 609406; gene.
DR neXtProt; NX_P85299; -.
DR OpenTargets; ENSG00000186654; -.
DR PharmGKB; PA144596392; -.
DR VEuPathDB; HostDB:ENSG00000186654; -.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00530000063981; -.
DR HOGENOM; CLU_046146_0_0_1; -.
DR InParanoid; P85299; -.
DR OMA; HSVCEMS; -.
DR OrthoDB; 1260193at2759; -.
DR PhylomeDB; P85299; -.
DR TreeFam; TF314826; -.
DR PathwayCommons; P85299; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR SignaLink; P85299; -.
DR SIGNOR; P85299; -.
DR BioGRID-ORCS; 55615; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; PRR5; human.
DR GenomeRNAi; 55615; -.
DR Pharos; P85299; Tbio.
DR PRO; PR:P85299; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P85299; protein.
DR Bgee; ENSG00000186654; Expressed in spleen and 157 other tissues.
DR ExpressionAtlas; P85299; baseline and differential.
DR Genevisible; P85299; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031669; P:cellular response to nutrient levels; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IC:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IDA:ComplexPortal.
DR GO; GO:0030307; P:positive regulation of cell growth; IC:ComplexPortal.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR InterPro; IPR013745; Bit61/PRR5.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR PANTHER; PTHR32428; PTHR32428; 1.
DR Pfam; PF08539; HbrB; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Phosphoprotein; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..388
FT /note="Proline-rich protein 5"
FT /id="PRO_0000308162"
FT REGION 10..95
FT /note="Interaction with RICTOR"
FT REGION 12..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..218
FT /note="Interaction with RICTOR"
FT REGION 254..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q812A5"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_001646"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_028884"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_028885"
FT VAR_SEQ 1..5
FT /note="MRTLR -> MVCLELSQREAWGSGSPEKMPAQPEGLY (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045883"
FT VAR_SEQ 102..107
FT /note="KIRFYE -> MAPMPT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_001648"
FT VARIANT 243
FT /note="V -> M (in dbSNP:rs36082900)"
FT /id="VAR_062230"
FT CONFLICT 280
FT /note="R -> W (in Ref. 1; BAA90999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42753 MW; FA6B90495623EF3F CRC64;
MRTLRRLKFM SSPSLSDLGK REPAAAADER GTQQRRACAN ATWNSIHNGV IAVFQRKGLP
DQELFSLNEG VRQLLKTELG SFFTEYLQNQ LLTKGMVILR DKIRFYEGQK LLDSLAETWD
FFFSDVLPML QAIFYPVQGK EPSVRQLALL HFRNAITLSV KLEDALARAH ARVPPAIVQM
LLVLQGVHES RGVTEDYLRL ETLVQKVVSP YLGTYGLHSS EGPFTHSCIL EKRLLRRSRS
GDVLAKNPVV RSKSYNTPLL NPVQEHEAEG AAAGGTSIRR HSVSEMTSCP EPQGFSDPPG
QGPTGTFRSS PAPHSGPCPS RLYPTTQPPE QGLDPTRSSL PRSSPENLVD QILESVDSDS
EGIFIDFGRG RGSGMSDLEG SGGRQSVV
