(data stored in SCRATCH zone)

SWISSPROT: 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   10-MAY-2017, entry version 152.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Crosier W.J., McCormick F., Polakis P.;
RT   "Molecular cloning of a GTPase activating protein specific for the
RT   Krev-1 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
RT   from 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   associated 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
RT   project: 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.,
RA   Walther T.C., 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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
RP   AND SER-515, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 75-415, FUNCTION, SUBUNIT,
RP   AND MUTAGENESIS OF PHE-100; LEU-173; GLU-207; HIS-267; ARG-286;
RP   HIS-287; 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,
RP   AND 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
RT   and 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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   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
CC       GDP-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       P61224:RAP1B; NbExp=3; IntAct=EBI-722307, EBI-358143;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral
CC       membrane 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         Note=Contains a phosphoserine at position 17.
CC         {ECO:0000244|PubMed:19690332};
CC       Name=4;
CC         IsoId=P47736-4; Sequence=VSP_047025;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Significant expression seen in the brain,
CC       kidney and pancreas. Abundant in the cerebral cortex and expressed
CC       at much lower levels in the spinal cord. Not detected in the
CC       lymphoid tissues. {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=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAA32319.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RAP1GAPID42043ch1p36.html";
DR   EMBL; M64788; AAA60252.1; -; mRNA.
DR   EMBL; AB007943; BAA32319.3; ALT_INIT; mRNA.
DR   EMBL; AL359815; CAI16250.1; -; Genomic_DNA.
DR   EMBL; AL359815; CAI16255.1; -; 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. [P47736-1]
DR   RefSeq; XP_016857476.1; XM_017001987.1. [P47736-1]
DR   RefSeq; XP_016857477.1; XM_017001988.1. [P47736-1]
DR   UniGene; Hs.148178; -.
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   ProteinModelPortal; P47736; -.
DR   SMR; P47736; -.
DR   BioGrid; 111844; 17.
DR   IntAct; P47736; 10.
DR   MINT; MINT-3308298; -.
DR   STRING; 9606.ENSP00000290101; -.
DR   iPTMnet; P47736; -.
DR   PhosphoSitePlus; P47736; -.
DR   BioMuta; RAP1GAP; -.
DR   DMDM; 215273877; -.
DR   MaxQB; P47736; -.
DR   PaxDb; P47736; -.
DR   PeptideAtlas; P47736; -.
DR   PRIDE; P47736; -.
DR   DNASU; 5909; -.
DR   Ensembl; ENST00000374765; ENSP00000363897; ENSG00000076864. [P47736-1]
DR   Ensembl; ENST00000495204; ENSP00000434033; ENSG00000076864. [P47736-4]
DR   Ensembl; ENST00000542643; ENSP00000441661; ENSG00000076864. [P47736-2]
DR   GeneID; 5909; -.
DR   KEGG; hsa:5909; -.
DR   UCSC; uc001bew.4; human. [P47736-1]
DR   CTD; 5909; -.
DR   DisGeNET; 5909; -.
DR   GeneCards; RAP1GAP; -.
DR   HGNC; HGNC:9858; RAP1GAP.
DR   HPA; HPA001922; -.
DR   MIM; 600278; gene.
DR   neXtProt; NX_P47736; -.
DR   OpenTargets; ENSG00000076864; -.
DR   PharmGKB; PA34220; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   eggNOG; ENOG410XTIX; LUCA.
DR   GeneTree; ENSGT00760000119182; -.
DR   HOGENOM; HOG000231640; -.
DR   HOVERGEN; HBG016371; -.
DR   InParanoid; P47736; -.
DR   KO; K17700; -.
DR   PhylomeDB; P47736; -.
DR   TreeFam; TF318626; -.
DR   Reactome; R-HSA-392517; Rap1 signalling.
DR   Reactome; R-HSA-8853659; RET signaling.
DR   SignaLink; P47736; -.
DR   SIGNOR; P47736; -.
DR   ChiTaRS; RAP1GAP; human.
DR   EvolutionaryTrace; P47736; -.
DR   GeneWiki; RAP1GAP; -.
DR   GenomeRNAi; 5909; -.
DR   PRO; PR:P47736; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000076864; -.
DR   CleanEx; HS_RAP1GAP; -.
DR   ExpressionAtlas; P47736; baseline and differential.
DR   Genevisible; P47736; HS.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
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:0017016; F:Ras GTPase binding; IPI:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:1903697; P:negative regulation of microvillus assembly; IMP:UniProtKB.
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   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR000331; Rap_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;
DR   PRODOM; P47736.
DR   SWISS-2DPAGE; P47736.
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Golgi apparatus; GTPase activation; Membrane; Phosphoprotein;
KW   Polymorphism; Reference proteome.
FT   CHAIN         1    663       Rap1 GTPase-activating protein 1.
FT                                /FTId=PRO_0000056743.
FT   DOMAIN        1     17       GoLoco. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00097}.
FT   DOMAIN      181    397       Rap-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00165}.
FT   MOD_RES     441    441       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     484    484       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     499    499       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     515    515       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     541    541       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2ALS5}.
FT   MOD_RES     542    542       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2ALS5}.
FT   VAR_SEQ       1      1       M -> MAQLRPAVPPGRPRRGSLPAGASWQNTDLFEM (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:10476970}.
FT                                /FTId=VSP_040260.
FT   VAR_SEQ       1      1       M -> MSGRKRSFTFGAYGGVDKSFTSRRSVWRSDGQNQHF
FT                                PQALDLSRVNLVPSYTPSLYPKNTDLFEM (in isoform
FT                                4). {ECO:0000305}.
FT                                /FTId=VSP_047025.
FT   VAR_SEQ     280    280       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10476970}.
FT                                /FTId=VSP_040261.
FT   VAR_SEQ     476    476       I -> ISLLIPGKSASRFGRRGSAIGIGTVEE (in
FT                                isoform 2). {ECO:0000303|PubMed:9455484}.
FT                                /FTId=VSP_035256.
FT   VAR_SEQ     626    633       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9455484}.
FT                                /FTId=VSP_035257.
FT   VARIANT     107    107       A -> T (in dbSNP:rs2275363).
FT                                {ECO:0000269|PubMed:1904317}.
FT                                /FTId=VAR_047792.
FT   VARIANT     257    257       C -> R (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035547.
FT   VARIANT     609    609       Y -> C (in a breast cancer sample;
FT                                somatic mutation; dbSNP:rs147394161).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035548.
FT   MUTAGEN     100    100       F->E: Impaired dimerization; when
FT                                associated with E-173.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     173    173       L->E: Impaired dimerization; when
FT                                associated with E-100.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     207    207       E->A: Reduces GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     267    267       H->A: Abolishes GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     286    286       R->A: Reduces GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     287    287       H->A: Abolishes GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     290    290       N->A,K: Abolishes GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     291    291       D->A: Abolishes GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   MUTAGEN     388    388       R->A,P: Reduces GTPase activation.
FT                                {ECO:0000269|PubMed:15141215}.
FT   CONFLICT    304    304       F -> L (in Ref. 6; AAH54490).
FT                                {ECO:0000305}.
FT   HELIX        85     88       {ECO:0000244|PDB:1SRQ}.
FT   HELIX        89     93       {ECO:0000244|PDB:1SRQ}.
FT   TURN         94     96       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      100    106       {ECO:0000244|PDB:1SRQ}.
FT   TURN        107    109       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      110    121       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      124    132       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      137    143       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       153    160       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       177    186       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      192    200       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       207    211       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       218    227       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      228    233       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      245    247       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      252    258       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      263    268       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       269    271       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       282    288       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      292    300       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       306    308       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      316    323       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      327    329       {ECO:0000244|PDB:3BRW}.
FT   STRAND      331    338       {ECO:0000244|PDB:1SRQ}.
FT   STRAND      354    358       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       359    376       {ECO:0000244|PDB:1SRQ}.
FT   HELIX       380    409       {ECO:0000244|PDB:1SRQ}.
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
//

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