GPSM1_HUMAN
ID GPSM1_HUMAN Reviewed; 675 AA.
AC Q86YR5; A9Z1X4; B1B0W3; Q86SR5; Q969T1; Q9UFS8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=G-protein-signaling modulator 1;
DE AltName: Full=Activator of G-protein signaling 3;
GN Name=GPSM1; Synonyms=AGS3;
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] (ISOFORM 4).
RC TISSUE=Brain;
RA Cismowski M.J., Kopatz S.A., Puhl H.L. III, Sharma S.V., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Fetal brain, and Rhabdomyosarcoma;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-675 (ISOFORM 1).
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION.
RX PubMed=11024022; DOI=10.1074/jbc.m006478200;
RA Natochin M., Lester B., Peterson Y.K., Bernard M.L., Lanier S.M.,
RA Artemyev N.O.;
RT "AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and
RT rhodopsin-dependent activation of transducin.";
RL J. Biol. Chem. 275:40981-40985(2000).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12642577; DOI=10.1074/jbc.m300917200;
RA Pattingre S., de Vries L., Bauvy C., Chantret I., Cluzeaud F.,
RA Ogier-Denis E., Vandewalle A., Codogno P.;
RT "The G-protein regulator AGS3 controls an early event during macroautophagy
RT in human intestinal HT-29 cells.";
RL J. Biol. Chem. 278:20995-21002(2003).
RN [8]
RP INTERACTION WITH INSC.
RX PubMed=16458856; DOI=10.1016/j.bbrc.2006.01.050;
RA Izaki T., Kamakura S., Kohjima M., Sumimoto H.;
RT "Two forms of human Inscuteable-related protein that links Par3 to the Pins
RT homologues LGN and AGS3.";
RL Biochem. Biophys. Res. Commun. 341:1001-1006(2006).
RN [9]
RP INTERACTION WITH FRMPD1, AND SUBCELLULAR LOCATION.
RX PubMed=18566450; DOI=10.1074/jbc.m803497200;
RA An N., Blumer J.B., Bernard M.L., Lanier S.M.;
RT "The PDZ and band 4.1 containing protein Frmpd1 regulates the subcellular
RT location of activator of G-protein signaling 3 and its interaction with G-
RT proteins.";
RL J. Biol. Chem. 283:24718-24728(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-492 AND SER-493, AND
RP IDENTIFICATION BY MASS 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-413, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-469; SER-471 AND
RP SER-492, AND 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).
CC -!- FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which
CC functions as a receptor-independent activator of heterotrimeric G-
CC protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form
CC thus uncoupling heterotrimeric G-proteins signaling from G protein-
CC coupled receptors. Controls spindle orientation and asymmetric cell
CC fate of cerebral cortical progenitors. May also be involved in
CC macroautophagy in intestinal cells. May play a role in drug addiction.
CC {ECO:0000269|PubMed:11024022, ECO:0000269|PubMed:12642577}.
CC -!- SUBUNIT: Interacts with GNAI1, GNAI2 and GNAI3 preferentially in their
CC GDP-bound state. May also interact with GNAO1. Interacts with
CC STK11/LKB1 and MACF1 (By similarity). Interacts with INSC/inscuteable
CC and FRMPD1. {ECO:0000250, ECO:0000269|PubMed:16458856,
CC ECO:0000269|PubMed:18566450}.
CC -!- INTERACTION:
CC Q86YR5-3; O14503: BHLHE40; NbExp=3; IntAct=EBI-10261098, EBI-711810;
CC Q86YR5-3; Q8TEB1: DCAF11; NbExp=3; IntAct=EBI-10261098, EBI-2213388;
CC Q86YR5-3; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-10261098, EBI-9679045;
CC Q86YR5-3; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-10261098, EBI-7225287;
CC Q86YR5-3; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-10261098, EBI-1384254;
CC Q86YR5-3; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-10261098, EBI-6658203;
CC Q86YR5-3; O75603: GCM2; NbExp=3; IntAct=EBI-10261098, EBI-10188645;
CC Q86YR5-3; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-10261098, EBI-7251368;
CC Q86YR5-3; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-10261098, EBI-740641;
CC Q86YR5-3; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-10261098, EBI-2556193;
CC Q86YR5-3; Q8N443: RIBC1; NbExp=3; IntAct=EBI-10261098, EBI-10265323;
CC Q86YR5-3; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-10261098, EBI-693002;
CC Q86YR5-3; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-10261098, EBI-745958;
CC Q86YR5-3; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-10261098, EBI-750487;
CC Q86YR5-3; Q14119: VEZF1; NbExp=3; IntAct=EBI-10261098, EBI-11980193;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum
CC membrane; Peripheral membrane protein; Cytoplasmic side. Golgi
CC apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell
CC membrane; Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86YR5-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q86YR5-2; Sequence=VSP_020937;
CC Name=3;
CC IsoId=Q86YR5-3; Sequence=VSP_020938, VSP_020939;
CC Name=4; Synonyms=FL;
CC IsoId=Q86YR5-4; Sequence=VSP_039028;
CC -!- TISSUE SPECIFICITY: Expressed in intestinal cells.
CC {ECO:0000269|PubMed:12642577}.
CC -!- DOMAIN: The GoLoco domains mediate interaction with G(i/o) alpha (By
CC similarity). The GoLoco domains are essential for the GDI activity
CC toward G(i/o) alpha. {ECO:0000250}.
CC -!- PTM: Phosphorylation regulates interaction with G(i/o) alpha.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GPSM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09979.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH17353.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB55951.1; 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; AY173053; AAO17260.1; -; mRNA.
DR EMBL; BX649589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88216.1; -; Genomic_DNA.
DR EMBL; BC009979; AAH09979.1; ALT_INIT; mRNA.
DR EMBL; BC017353; AAH17353.1; ALT_INIT; mRNA.
DR EMBL; BC048343; AAH48343.1; -; mRNA.
DR EMBL; AL117478; CAB55951.1; ALT_FRAME; mRNA.
DR CCDS; CCDS48055.1; -. [Q86YR5-1]
DR CCDS; CCDS48056.1; -. [Q86YR5-2]
DR CCDS; CCDS6996.2; -. [Q86YR5-3]
DR PIR; T17261; T17261.
DR RefSeq; NP_001139110.2; NM_001145638.2.
DR RefSeq; NP_001139111.1; NM_001145639.1. [Q86YR5-2]
DR RefSeq; NP_001186932.1; NM_001200003.1. [Q86YR5-2]
DR RefSeq; NP_056412.5; NM_015597.5.
DR RefSeq; XP_016870088.1; XM_017014599.1. [Q86YR5-2]
DR AlphaFoldDB; Q86YR5; -.
DR SMR; Q86YR5; -.
DR BioGRID; 117539; 61.
DR IntAct; Q86YR5; 35.
DR MINT; Q86YR5; -.
DR STRING; 9606.ENSP00000392828; -.
DR iPTMnet; Q86YR5; -.
DR MetOSite; Q86YR5; -.
DR PhosphoSitePlus; Q86YR5; -.
DR BioMuta; GPSM1; -.
DR DMDM; 294862435; -.
DR EPD; Q86YR5; -.
DR jPOST; Q86YR5; -.
DR MassIVE; Q86YR5; -.
DR MaxQB; Q86YR5; -.
DR PaxDb; Q86YR5; -.
DR PeptideAtlas; Q86YR5; -.
DR PRIDE; Q86YR5; -.
DR ProteomicsDB; 70452; -. [Q86YR5-1]
DR ProteomicsDB; 70453; -. [Q86YR5-2]
DR ProteomicsDB; 70454; -. [Q86YR5-3]
DR ProteomicsDB; 70455; -. [Q86YR5-4]
DR Antibodypedia; 32122; 212 antibodies from 27 providers.
DR DNASU; 26086; -.
DR Ensembl; ENST00000291775.3; ENSP00000291775.3; ENSG00000160360.13. [Q86YR5-2]
DR Ensembl; ENST00000392944.5; ENSP00000376673.1; ENSG00000160360.13. [Q86YR5-2]
DR Ensembl; ENST00000429455.5; ENSP00000390705.1; ENSG00000160360.13. [Q86YR5-2]
DR GeneID; 26086; -.
DR KEGG; hsa:26086; -.
DR UCSC; uc004che.3; human. [Q86YR5-1]
DR CTD; 26086; -.
DR DisGeNET; 26086; -.
DR GeneCards; GPSM1; -.
DR HGNC; HGNC:17858; GPSM1.
DR HPA; ENSG00000160360; Low tissue specificity.
DR MIM; 609491; gene.
DR neXtProt; NX_Q86YR5; -.
DR OpenTargets; ENSG00000160360; -.
DR PharmGKB; PA134986171; -.
DR VEuPathDB; HostDB:ENSG00000160360; -.
DR eggNOG; KOG1130; Eukaryota.
DR GeneTree; ENSGT00940000154667; -.
DR HOGENOM; CLU_102588_0_0_1; -.
DR InParanoid; Q86YR5; -.
DR PhylomeDB; Q86YR5; -.
DR TreeFam; TF328344; -.
DR PathwayCommons; Q86YR5; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q86YR5; -.
DR BioGRID-ORCS; 26086; 19 hits in 1080 CRISPR screens.
DR ChiTaRS; GPSM1; human.
DR GeneWiki; GPSM1; -.
DR GenomeRNAi; 26086; -.
DR Pharos; Q86YR5; Tbio.
DR PRO; PR:Q86YR5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q86YR5; protein.
DR Bgee; ENSG00000160360; Expressed in tibia and 164 other tissues.
DR ExpressionAtlas; Q86YR5; baseline and differential.
DR Genevisible; Q86YR5; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF02188; GoLoco; 4.
DR SMART; SM00390; GoLoco; 4.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50877; GOLOCO; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW Differentiation; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Methylation; Neurogenesis; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..675
FT /note="G-protein-signaling modulator 1"
FT /id="PRO_0000252402"
FT REPEAT 28..61
FT /note="TPR 1"
FT REPEAT 66..99
FT /note="TPR 2"
FT REPEAT 106..139
FT /note="TPR 3"
FT REPEAT 146..181
FT /note="TPR 4"
FT REPEAT 183..202
FT /note="TPR 5"
FT REPEAT 209..242
FT /note="TPR 6"
FT REPEAT 249..282
FT /note="TPR 7"
FT REPEAT 289..322
FT /note="TPR 8"
FT REPEAT 329..362
FT /note="TPR 9"
FT DOMAIN 495..517
FT /note="GoLoco 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 548..570
FT /note="GoLoco 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 596..618
FT /note="GoLoco 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 630..652
FT /note="GoLoco 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 1..509
FT /note="Mediates association with membranes"
FT /evidence="ECO:0000250"
FT REGION 364..487
FT /note="Interaction with STK11/LKB1"
FT /evidence="ECO:0000250"
FT REGION 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 421
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6IR34"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R080"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R080"
FT VAR_SEQ 1..509
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020937"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039028"
FT VAR_SEQ 404..457
FT /note="ARPKRTQRLSAETWDLLRLPLEREQNGDSHHSGDWRGPSRDSLPLPVRSRKY
FT QE -> EFQGCGGVLLPTGTDRIRSCGGVGSRPGQHGGGGSRQKMAPTSQFFLASGTAQ
FT A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020938"
FT VAR_SEQ 458..675
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020939"
SQ SEQUENCE 675 AA; 74510 MW; 27EB86667EEC1951 CRC64;
MAGPAPPVAD ELPGPAARRL YSRMEASCLE LALEGERLCK AGDFKTGVAF FEAAVQVGTE
DLKTLSAIYS QLGNAYFYLK EHGRALEYHK HDLLLARTIG DRMGEAKASG NLGNTLKVLG
RFDEAAVCCQ RHLSIAQEQG DKVGEARALY NIGNVYHAKG KQLSWNAANA TQDPGHLPPD
VRETLCKASE FYERNLSLVK ELGDRAAQGR AYGNLGNTHY LLGNFTEATT FHKERLAIAK
EFGDKAAERR AYSNLGNAHV FLGRFDVAAE YYKKTLQLSR QLRDQAVEAQ ACYSLGNTYT
LLQDYERAAE YHLRHLLIAQ ELADRVGEGR ACWSLGNAYV SMGRPAQALT FAKKHLQISQ
EIGDRHGELT ARMNVAQLQL VLGRLTSPAA SEKPDLAGYE AQGARPKRTQ RLSAETWDLL
RLPLEREQNG DSHHSGDWRG PSRDSLPLPV RSRKYQEGPD AERRPREGSH SPLDSADVRV
HVPRTSIPRA PSSDEECFFD LLTKFQSSRM DDQRCPLDDG QAGAAEATAA PTLEDRIAQP
SMTASPQTEE FFDLIASSQS RRLDDQRASV GSLPGLRITH SNAGHLRGHG EPQEPGDDFF
NMLIKYQSSR IDDQRCPPPD VLPRGPTMPD EDFFSLIQRV QAKRMDEQRV DLAGGPEQGA
GGPPEPQQQC QPGAS
