ID   RPGP1_HUMAN             Reviewed;         663 AA.
AC   P47736; J3QSS6; O75062; Q5T3S9; Q5T3T4; Q7Z5S8; Q9UQ51;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Rap1 GTPase-activating protein 1;
DE            Short=Rap1GAP;
DE            Short=Rap1GAP1;
GN   Name=RAP1GAP; Synonyms=KIAA0474, RAP1GA1;
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 [MRNA] (ISOFORM 1), AND VARIANT THR-107.
RC   TISSUE=Brain;
RX   PubMed=1904317; DOI=10.1016/0092-8674(91)90555-d;
RA   Rubinfeld B., Munemitsu S., Clark R., Conroy L., Watt K., Crosier W.J.,
RA   McCormick F., Polakis P.;
RT   "Molecular cloning of a GTPase activating protein specific for the Krev-1
RT   protein p21rap1.";
RL   Cell 65:1033-1042(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
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 [MRNA] OF 1-100 (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=10476970; DOI=10.1038/23738;
RA   Mochizuki N., Ohba Y., Kiyokawa E., Kurata T., Murakami Y., Ozaki Y.,
RA   Kitakabe A., Nagashima K., Matsuda M.;
RT   "Activation of the ERK/MAPK pathway by an isoform of rap1GAP associated
RT   with G alpha(i).";
RL   Nature 400:891-894(1999).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   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   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9346962; DOI=10.1074/jbc.272.44.28081;
RA   Kurachi H., Wada Y., Tsukamoto N., Maeda M., Kubota H., Hattori M.,
RA   Iwai K., Minato N.;
RT   "Human SPA-1 product selectively expressed in lymphoid tissues is a
RT   specific GTPase-activating protein for Rap1 and Rap2.";
RL   J. Biol. Chem. 272:28081-28088(1997).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-499, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 (ISOFORM 3), AND
RP   IDENTIFICATION BY 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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-484; SER-499 AND
RP   SER-515, 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).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP   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   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 75-415, FUNCTION, SUBUNIT, AND
RP   MUTAGENESIS OF PHE-100; LEU-173; GLU-207; HIS-267; ARG-286; HIS-287;
RP   ASN-290; ASP-291 AND ARG-388.
RX   PubMed=15141215; DOI=10.1038/nature02505;
RA   Daumke O., Weyand M., Chakrabarti P.P., Vetter I.R., Wittinghofer A.;
RT   "The GTPase-activating protein Rap1GAP uses a catalytic asparagine.";
RL   Nature 429:197-201(2004).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH RAP1B, AND
RP   SUBUNIT.
RX   PubMed=18309292; DOI=10.1038/emboj.2008.30;
RA   Scrima A., Thomas C., Deaconescu D., Wittinghofer A.;
RT   "The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and
RT   arginine residues.";
RL   EMBO J. 27:1145-1153(2008).
RN   [16]
RP   VARIANTS [LARGE SCALE ANALYSIS] ARG-257 AND CYS-609.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC       protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-
CC       bound state. {ECO:0000269|PubMed:15141215}.
CC   -!- SUBUNIT: Homodimer and heterodimer with RAP1B.
CC       {ECO:0000269|PubMed:15141215, ECO:0000269|PubMed:18309292}.
CC   -!- INTERACTION:
CC       P47736; O14645: DNALI1; NbExp=3; IntAct=EBI-722307, EBI-395638;
CC       P47736; O14901: KLF11; NbExp=3; IntAct=EBI-722307, EBI-948266;
CC       P47736; P61224: RAP1B; NbExp=3; IntAct=EBI-722307, EBI-358143;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P47736-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P47736-2; Sequence=VSP_035256, VSP_035257;
CC       Name=3;
CC         IsoId=P47736-3; Sequence=VSP_040260, VSP_040261;
CC       Name=4;
CC         IsoId=P47736-4; Sequence=VSP_047025;
CC   -!- TISSUE SPECIFICITY: Significant expression seen in the brain, kidney
CC       and pancreas. Abundant in the cerebral cortex and expressed at much
CC       lower levels in the spinal cord. Not detected in the lymphoid tissues.
CC       {ECO:0000269|PubMed:9346962}.
CC   -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA) in
CC       promyelocytic HL-60 cells. {ECO:0000269|PubMed:9346962}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54490.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA32319.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42043/RAP1GAP";
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DR   EMBL; M64788; AAA60252.1; -; mRNA.
DR   EMBL; AB007943; BAA32319.3; ALT_INIT; mRNA.
DR   EMBL; AL359815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471134; EAW94980.1; -; Genomic_DNA.
DR   EMBL; CH471134; EAW94981.1; -; Genomic_DNA.
DR   EMBL; AB003930; BAA83674.1; -; mRNA.
DR   EMBL; BC054490; AAH54490.1; ALT_INIT; mRNA.
DR   CCDS; CCDS218.1; -. [P47736-1]
DR   CCDS; CCDS53276.1; -. [P47736-2]
DR   CCDS; CCDS53277.1; -. [P47736-4]
DR   PIR; A39897; A39897.
DR   PIR; B39897; B39897.
DR   RefSeq; NP_001139129.1; NM_001145657.1. [P47736-2]
DR   RefSeq; NP_001139130.1; NM_001145658.1. [P47736-4]
DR   RefSeq; NP_002876.2; NM_002885.2. [P47736-1]
DR   RefSeq; XP_005246012.2; XM_005245955.3.
DR   RefSeq; XP_016857459.1; XM_017001970.1.
DR   RefSeq; XP_016857462.1; XM_017001973.1.
DR   RefSeq; XP_016857473.1; XM_017001984.1.
DR   RefSeq; XP_016857475.1; XM_017001986.1.
DR   RefSeq; XP_016857476.1; XM_017001987.1.
DR   RefSeq; XP_016857477.1; XM_017001988.1.
DR   PDB; 1SRQ; X-ray; 2.90 A; A/B/C/D=75-415.
DR   PDB; 3BRW; X-ray; 3.40 A; A/B/C=75-415.
DR   PDBsum; 1SRQ; -.
DR   PDBsum; 3BRW; -.
DR   AlphaFoldDB; P47736; -.
DR   SMR; P47736; -.
DR   BioGRID; 111844; 40.
DR   IntAct; P47736; 24.
DR   MINT; P47736; -.
DR   STRING; 9606.ENSP00000363895; -.
DR   iPTMnet; P47736; -.
DR   PhosphoSitePlus; P47736; -.
DR   BioMuta; RAP1GAP; -.
DR   DMDM; 215273877; -.
DR   EPD; P47736; -.
DR   jPOST; P47736; -.
DR   MassIVE; P47736; -.
DR   MaxQB; P47736; -.
DR   PaxDb; 9606-ENSP00000434033; -.
DR   PeptideAtlas; P47736; -.
DR   ProteomicsDB; 55789; -. [P47736-1]
DR   ProteomicsDB; 55790; -. [P47736-2]
DR   ProteomicsDB; 55791; -. [P47736-3]
DR   Pumba; P47736; -.
DR   Antibodypedia; 1096; 298 antibodies from 30 providers.
DR   DNASU; 5909; -.
DR   Ensembl; ENST00000374765.9; ENSP00000363897.4; ENSG00000076864.21. [P47736-1]
DR   Ensembl; ENST00000495204.5; ENSP00000434033.2; ENSG00000076864.21. [P47736-4]
DR   Ensembl; ENST00000542643.6; ENSP00000441661.1; ENSG00000076864.21. [P47736-2]
DR   GeneID; 5909; -.
DR   KEGG; hsa:5909; -.
DR   MANE-Select; ENST00000374765.9; ENSP00000363897.4; NM_002885.4; NP_002876.2.
DR   UCSC; uc001bew.4; human. [P47736-1]
DR   AGR; HGNC:9858; -.
DR   CTD; 5909; -.
DR   DisGeNET; 5909; -.
DR   GeneCards; RAP1GAP; -.
DR   HGNC; HGNC:9858; RAP1GAP.
DR   HPA; ENSG00000076864; Tissue enhanced (brain, kidney, thyroid gland).
DR   MIM; 600278; gene.
DR   neXtProt; NX_P47736; -.
DR   OpenTargets; ENSG00000076864; -.
DR   PharmGKB; PA34220; -.
DR   VEuPathDB; HostDB:ENSG00000076864; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   GeneTree; ENSGT00940000156138; -.
DR   InParanoid; P47736; -.
DR   OMA; XESVSSS; -.
DR   OrthoDB; 25782at2759; -.
DR   PhylomeDB; P47736; -.
DR   TreeFam; TF318626; -.
DR   PathwayCommons; P47736; -.
DR   Reactome; R-HSA-392517; Rap1 signalling.
DR   Reactome; R-HSA-8853659; RET signaling.
DR   SignaLink; P47736; -.
DR   SIGNOR; P47736; -.
DR   BioGRID-ORCS; 5909; 10 hits in 1167 CRISPR screens.
DR   EvolutionaryTrace; P47736; -.
DR   GeneWiki; RAP1GAP; -.
DR   GenomeRNAi; 5909; -.
DR   Pharos; P47736; Tbio.
DR   PRO; PR:P47736; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P47736; Protein.
DR   Bgee; ENSG00000076864; Expressed in renal medulla and 158 other cell types or tissues.
DR   ExpressionAtlas; P47736; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; TAS:Reactome.
DR   GO; GO:1990792; P:cellular response to glial cell derived neurotrophic factor; IEA:Ensembl.
DR   GO; GO:1903697; P:negative regulation of microvillus assembly; IMP:UniProtKB.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:1904442; P:negative regulation of thyroid gland epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 6.10.140.210; -; 1.
DR   Gene3D; 3.40.50.11210; Rap/Ran-GAP; 1.
DR   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR035974; Rap/Ran-GAP_sf.
DR   InterPro; IPR000331; Rap/Ran_GAP_dom.
DR   PANTHER; PTHR15711; RAP GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR15711:SF3; RAP1 GTPASE-ACTIVATING PROTEIN 1; 1.
DR   Pfam; PF02188; GoLoco; 1.
DR   Pfam; PF21022; Rap-GAP_dimer; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SMART; SM00390; GoLoco; 1.
DR   SUPFAM; SSF111347; Rap/Ran-GAP; 1.
DR   PROSITE; PS50877; GOLOCO; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
DR   Genevisible; P47736; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Golgi apparatus; GTPase activation;
KW   Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..663
FT                   /note="Rap1 GTPase-activating protein 1"
FT                   /id="PRO_0000056743"
FT   DOMAIN          1..17
FT                   /note="GoLoco"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT   DOMAIN          181..397
FT                   /note="Rap-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         499
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         515
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2ALS5"
FT   MOD_RES         542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2ALS5"
FT   VAR_SEQ         1
FT                   /note="M -> MAQLRPAVPPGRPRRGSLPAGASWQNTDLFEM (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:10476970"
FT                   /id="VSP_040260"
FT   VAR_SEQ         1
FT                   /note="M -> MSGRKRSFTFGAYGGVDKSFTSRRSVWRSDGQNQHFPQALDLSRVNL
FT                   VPSYTPSLYPKNTDLFEM (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047025"
FT   VAR_SEQ         280
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10476970"
FT                   /id="VSP_040261"
FT   VAR_SEQ         476
FT                   /note="I -> ISLLIPGKSASRFGRRGSAIGIGTVEE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9455484"
FT                   /id="VSP_035256"
FT   VAR_SEQ         626..633
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9455484"
FT                   /id="VSP_035257"
FT   VARIANT         107
FT                   /note="A -> T (in dbSNP:rs2275363)"
FT                   /evidence="ECO:0000269|PubMed:1904317"
FT                   /id="VAR_047792"
FT   VARIANT         257
FT                   /note="C -> R (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035547"
FT   VARIANT         609
FT                   /note="Y -> C (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs147394161)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035548"
FT   MUTAGEN         100
FT                   /note="F->E: Impaired dimerization; when associated with
FT                   E-173."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         173
FT                   /note="L->E: Impaired dimerization; when associated with
FT                   E-100."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         207
FT                   /note="E->A: Reduces GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         267
FT                   /note="H->A: Abolishes GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         286
FT                   /note="R->A: Reduces GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         287
FT                   /note="H->A: Abolishes GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         290
FT                   /note="N->A,K: Abolishes GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         291
FT                   /note="D->A: Abolishes GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   MUTAGEN         388
FT                   /note="R->A,P: Reduces GTPase activation."
FT                   /evidence="ECO:0000269|PubMed:15141215"
FT   CONFLICT        304
FT                   /note="F -> L (in Ref. 6; AAH54490)"
FT                   /evidence="ECO:0000305"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           89..93
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          110..121
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          124..132
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           153..160
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           177..186
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          192..200
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           207..211
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           218..227
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           282..288
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          292..300
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           306..308
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          316..323
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:3BRW"
FT   STRAND          331..338
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   STRAND          354..358
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           359..376
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   HELIX           380..409
FT                   /evidence="ECO:0007829|PDB:1SRQ"
FT   MOD_RES         P47736-3:17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
SQ   SEQUENCE   663 AA;  73361 MW;  89B307CC67F975DD CRC64;
     MIEKMQGSRM DEQRCSFPPP LKTEEDYIPY PSVHEVLGRE GPFPLILLPQ FGGYWIEGTN
     HEITSIPETE PLQSPTTKVK LECNPTARIY RKHFLGKEHF NYYSLDAALG HLVFSLKYDV
     IGDQEHLRLL LRTKCRTYHD VIPISCLTEF PNVVQMAKLV CEDVNVDRFY PVLYPKASRL
     IVTFDEHVIS NNFKFGVIYQ KLGQTSEEEL FSTNEESPAF VEFLEFLGQK VKLQDFKGFR
     GGLDVTHGQT GTESVYCNFR NKEIMFHVST KLPYTEGDAQ QLQRKRHIGN DIVAVVFQDE
     NTPFVPDMIA SNFLHAYVVV QAEGGGPDGP LYKVSVTARD DVPFFGPPLP DPAVFRKGPE
     FQEFLLTKLI NAEYACYKAE KFAKLEERTR AALLETLYEE LHIHSQSMMG LGGDEDKMEN
     GSGGGGFFES FKRVIRSRSQ SMDAMGLSNK KPNTVSTSHS GSFAPNNPDL AKAAGISLIV
     PGKSPTRKKS GPFGSRRSSA IGIENIQEVQ EKRESPPAGQ KTPDSGHVSQ EPKSENSSTQ
     SSPEMPTTKN RAETAAQRAE ALKDFSRSSS SASSFASVVE ETEGVDGEDT GLESVSSSGT
     PHKRDSFIYS TWLEDSVSTT SGGSSPGPSR SPHPDAGKLG DPACPEIKIQ LEASEQHMPQ
     LGC
//