RPGP1_HUMAN
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 03-AUG-2022, entry version 182.
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="http://atlasgeneticsoncology.org/Genes/RAP1GAPID42043ch1p36.html";
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; 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. [P47736-2]
DR RefSeq; XP_016857459.1; XM_017001970.1. [P47736-2]
DR RefSeq; XP_016857462.1; XM_017001973.1. [P47736-1]
DR RefSeq; XP_016857473.1; XM_017001984.1. [P47736-2]
DR RefSeq; XP_016857475.1; XM_017001986.1.
DR RefSeq; XP_016857476.1; XM_017001987.1. [P47736-1]
DR RefSeq; XP_016857477.1; XM_017001988.1. [P47736-1]
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; 30.
DR IntAct; P47736; 14.
DR MINT; P47736; -.
DR STRING; 9606.ENSP00000434033; -.
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; P47736; -.
DR PeptideAtlas; P47736; -.
DR PRIDE; P47736; -.
DR ProteomicsDB; 55789; -. [P47736-1]
DR ProteomicsDB; 55790; -. [P47736-2]
DR ProteomicsDB; 55791; -. [P47736-3]
DR Antibodypedia; 1096; 248 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 CTD; 5909; -.
DR DisGeNET; 5909; -.
DR GeneCards; RAP1GAP; -.
DR HGNC; HGNC:9858; RAP1GAP.
DR HPA; ENSG00000076864; Tissue enhanced (thyroid).
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; ESISCVT; -.
DR OrthoDB; 845465at2759; -.
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; 8 hits in 1078 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 157 other tissues.
DR ExpressionAtlas; P47736; baseline and differential.
DR Genevisible; P47736; HS.
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:0090630; P:activation of GTPase activity; IBA:GO_Central.
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:1904425; P:negative regulation of GTP binding; 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; 3.40.50.11210; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR Pfam; PF02188; GoLoco; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SMART; SM00390; GoLoco; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50085; RAPGAP; 1.
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 E-
FT 173."
FT /evidence="ECO:0000269|PubMed:15141215"
FT MUTAGEN 173
FT /note="L->E: Impaired dimerization; when associated with E-
FT 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
