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Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP)

 RASA1_HUMAN             Reviewed;        1047 AA.
P20936; B2R6W3; B4DTL2; Q68CU6; Q9UDI1;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
27-SEP-2017, entry version 208.
RecName: Full=Ras GTPase-activating protein 1;
Short=GAP;
Short=GTPase-activating protein;
Short=RasGAP;
AltName: Full=Ras p21 protein activator;
AltName: Full=p120GAP;
Name=RASA1; Synonyms=GAP, RASA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=3201259; DOI=10.1126/science.3201259;
Trahey M., Wong G., Halenbeck R., Rubinfeld B., Martin G.A.,
Ladner M., Long C.M., Crosier W.J., Watt K., Koths K., McCormick F.;
"Molecular cloning of two types of GAP complementary DNA from human
placenta.";
Science 242:1697-1700(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 294-303; 326-334; 392-398; 439-457; 458-466;
479-483; 777-790 AND 821-825, FUNCTION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=8360177;
Zhang Y., Zhang G., Mollat P., Carles C., Riva M., Frobert Y.,
Malassine A., Rostene W., Thang D.C., Beltchev B., Tavitian A.,
Thane M.N.;
"Purification, characterization, and cellular localization of the 100-
kDa human placental GTPase-activating protein.";
J. Biol. Chem. 268:18875-18881(1993).
[7]
PROTEIN SEQUENCE OF 1-7 (ISOFORM 2).
PubMed=2123878;
Halenbeck R., Crosier W.J., Clark R., McCormick F., Koths K.;
"Purification, characterization, and western blot analysis of human
GTPase-activating protein from native and recombinant sources.";
J. Biol. Chem. 265:21922-21928(1990).
[8]
PHOSPHORYLATION, AND FUNCTION.
PubMed=11389730; DOI=10.1046/j.1432-1327.2001.02230.x;
Giglione C., Gonfloni S., Parmeggiani A.;
"Differential actions of p60c-Src and Lck kinases on the Ras
regulators p120-GAP and GDP/GTP exchange factor CDC25Mm.";
Eur. J. Biochem. 268:3275-3283(2001).
[9]
INTERACTION WITH PDGFRB.
PubMed=1375321; DOI=10.1128/MCB.12.6.2534;
Kazlauskas A., Kashishian A., Cooper J.A., Valius M.;
"GTPase-activating protein and phosphatidylinositol 3-kinase bind to
distinct regions of the platelet-derived growth factor receptor beta
subunit.";
Mol. Cell. Biol. 12:2534-2544(1992).
[10]
INTERACTION WITH SQSTM1.
PubMed=8618896; DOI=10.1073/pnas.92.26.12338;
Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.;
"Phosphotyrosine-independent binding of a 62-kDa protein to the src
homology 2 (SH2) domain of p56lck and its regulation by
phosphorylation of Ser-59 in the lck unique N-terminal region.";
Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995).
[11]
INTERACTION WITH CAV2.
PubMed=12091389; DOI=10.1074/jbc.M204367200;
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E.,
Lisanti M.P.;
"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-
caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains
associated with lipid rafts/caveolae, but no longer forms a high
molecular mass hetero-oligomer with caveolin-1.";
J. Biol. Chem. 277:34556-34567(2002).
[12]
INTERACTION WITH CAV2.
PubMed=15504032; DOI=10.1021/bi049295+;
Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W.,
Campos-Gonzalez R., Lisanti M.P.;
"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in
the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27).";
Biochemistry 43:13694-13706(2004).
[13]
INTERACTION WITH SPSB1.
PubMed=15713673; DOI=10.1074/jbc.M413897200;
Wang D., Li Z., Messing E.M., Wu G.;
"The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with
MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum
response element pathway.";
J. Biol. Chem. 280:16393-16401(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[15]
INTERACTION WITH PDPK1.
PubMed=18024423; DOI=10.1074/jbc.M706361200;
Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S.,
Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T.,
Brazil D.P., Hemmings B.A., Park J.;
"Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by
Src involves tyrosine phosphorylation of PDK1 and Src homology 2
domain binding.";
J. Biol. Chem. 283:1480-1491(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH NCK1.
PubMed=21664272; DOI=10.1016/j.cellsig.2011.05.019;
Ger M., Zitkus Z., Valius M.;
"Adaptor protein Nck1 interacts with p120 Ras GTPase-activating
protein and regulates its activity.";
Cell. Signal. 23:1651-1658(2011).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
STRUCTURE BY NMR OF 275-350.
PubMed=8137811;
Yang Y.S., Garbay C., Duschesne M., Cornille F., Jullian N.,
Fromage N., Tocque B., Roques B.P.;
"Solution structure of GAP SH3 domain by 1H NMR and spatial
arrangement of essential Ras signaling-involved sequence.";
EMBO J. 13:1270-1279(1994).
[22]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 714-1047.
PubMed=8955277; DOI=10.1038/384591a0;
Scheffzek K., Lautwein A., Kabsch W., Reza Ahmadian M.,
Wittinghofer A.;
"Crystal structure of the GTPase-activating domain of human p120GAP
and implications for the interaction with Ras.";
Nature 384:591-596(1996).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 714-1047 IN COMPLEX WITH RAS.
PubMed=9219684; DOI=10.1126/science.277.5324.333;
Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A.,
Schmitz F., Wittinghofer A.;
"The Ras-RasGAP complex: structural basis for GTPase activation and
its loss in oncogenic Ras mutants.";
Science 277:333-338(1997).
[24]
STRUCTURE BY NMR OF 282-446.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain and of the second SH2 domain of
human RAS GTPase-activating protein 1.";
Submitted (MAY-2007) to the PDB data bank.
[25]
VARIANTS LEU-398; GLU-400 AND VAL-401.
PubMed=8275088; DOI=10.1038/ng1193-242;
Friedman E., Gejman P.V., Martin G.A., McCormick F.;
"Nonsense mutations in the C-terminal SH2 region of the GTPase
activating protein (GAP) gene in human tumours.";
Nat. Genet. 5:242-247(1993).
[26]
VARIANT CMAVM TYR-540.
PubMed=14639529; DOI=10.1086/379793;
Eerola I., Boon L.M., Mulliken J.B., Burrows P.E., Dompmartin A.,
Watanabe S., Vanwijck R., Vikkula M.;
"Capillary malformation-arteriovenous malformation, a new clinical and
genetic disorder caused by RASA1 mutations.";
Am. J. Hum. Genet. 73:1240-1249(2003).
[27]
VARIANTS CMAVM CYS-528; ASP-530; GLU-626 AND VAL-763.
PubMed=24038909; DOI=10.1002/humu.22431;
Revencu N., Boon L.M., Mendola A., Cordisco M.R., Dubois J.,
Clapuyt P., Hammer F., Amor D.J., Irvine A.D., Baselga E.,
Dompmartin A., Syed S., Martin-Santiago A., Ades L., Collins F.,
Smith J., Sandaradura S., Barrio V.R., Burrows P.E., Blei F.,
Cozzolino M., Brunetti-Pierri N., Vicente A., Abramowicz M., Desir J.,
Vilain C., Chung W.K., Wilson A., Gardiner C.A., Dwight Y., Lord D.J.,
Fishman L., Cytrynbaum C., Chamlin S., Ghali F., Gilaberte Y.,
Joss S., Boente Mdel C., Leaute-Labreze C., Delrue M.A., Bayliss S.,
Martorell L., Gonzalez-Ensenat M.A., Mazereeuw-Hautier J.,
O'Donnell B., Bessis D., Pyeritz R.E., Salhi A., Tan O.T., Wargon O.,
Mulliken J.B., Vikkula M.;
"RASA1 mutations and associated phenotypes in 68 families with
capillary malformation-arteriovenous malformation.";
Hum. Mutat. 34:1632-1641(2013).
-!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
Stimulates the GTPase of normal but not oncogenic Ras p21; this
stimulation may be further increased in the presence of NCK1.
{ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:8360177}.
-!- SUBUNIT: Interacts with SQSTM1. Interacts with SPSB1; the
interaction does not promote degradation. Interacts with CAV2
(tyrosine phosphorylated form). Directly interacts with NCK1.
Interacts with PDGFRB (tyrosine phosphorylated). Interacts (via
SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1.
{ECO:0000269|PubMed:12091389, ECO:0000269|PubMed:1375321,
ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:15713673,
ECO:0000269|PubMed:18024423, ECO:0000269|PubMed:21664272,
ECO:0000269|PubMed:8618896, ECO:0000269|PubMed:9219684}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=2; IntAct=EBI-1026476, EBI-375446;
P10275:AR; NbExp=16; IntAct=EBI-1026476, EBI-608057;
P04632:CAPNS1; NbExp=3; IntAct=EBI-1026476, EBI-711828;
Q96QB1:DLC1; NbExp=7; IntAct=EBI-1026476, EBI-2608428;
P00533:EGFR; NbExp=7; IntAct=EBI-1026476, EBI-297353;
P04626:ERBB2; NbExp=8; IntAct=EBI-1026476, EBI-641062;
P21860:ERBB3; NbExp=6; IntAct=EBI-1026476, EBI-720706;
Q13480:GAB1; NbExp=25; IntAct=EBI-1026476, EBI-517684;
P10721:KIT; NbExp=16; IntAct=EBI-1026476, EBI-1379503;
P08581:MET; NbExp=15; IntAct=EBI-1026476, EBI-1039152;
P16333:NCK1; NbExp=6; IntAct=EBI-1026476, EBI-389883;
P09619:PDGFRB; NbExp=3; IntAct=EBI-1026476, EBI-641237;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8360177}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long;
IsoId=P20936-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P20936-2; Sequence=VSP_001625, VSP_001626;
Name=3;
IsoId=P20936-3; Sequence=VSP_057434, VSP_057435;
Note=No experimental confirmation available.;
Name=4;
IsoId=P20936-4; Sequence=VSP_057432, VSP_057433;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In placental villi, detected only in the
trophoblast layer (cytotrophoblast and syncytiotrophoblast). Not
detected in stromal, endothelial or Hofbauer cells (at protein
level). {ECO:0000269|PubMed:8360177}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Phosphorylated by SRC and LCK. The phosphorylation SRC
inhibits its ability to stimulate the Ras-GTPase activity, whereas
phosphorylation by LCK does not display any effect on stimulation
activity. {ECO:0000269|PubMed:11389730}.
-!- DISEASE: Note=Mutations in the SH2 domain of RASA seem to be
oncogenic and cause basal cell carcinomas.
-!- DISEASE: Capillary malformation-arteriovenous malformation (CMAVM)
[MIM:608354]: A disorder characterized by atypical capillary
malformations that are multiple, small, round to oval in shape and
pinkish red in color. These capillary malformations are associated
with either arteriovenous malformation, arteriovenous fistula, or
Parkes Weber syndrome. {ECO:0000269|PubMed:14639529,
ECO:0000269|PubMed:24038909}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Parkes Weber syndrome (PKWS) [MIM:608355]: Disorder
characterized by a cutaneous flush with underlying multiple micro-
arteriovenous fistulas, in association with soft tissue and
skeletal hypertrophy of the affected limb. Note=The disease is
caused by mutations affecting the gene represented in this entry.
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EMBL; M23379; AAA52517.1; -; mRNA.
EMBL; M23612; AAA35865.1; -; mRNA.
EMBL; AK300263; BAG62024.1; -; mRNA.
EMBL; AK312739; BAG35610.1; -; mRNA.
EMBL; CR749722; CAH18488.2; -; mRNA.
EMBL; AC010410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC018754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC035142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033015; AAH33015.1; -; mRNA.
CCDS; CCDS34200.1; -. [P20936-1]
CCDS; CCDS47243.1; -. [P20936-2]
PIR; A40121; A40121.
PIR; B40121; B40121.
RefSeq; NP_002881.1; NM_002890.2. [P20936-1]
RefSeq; NP_072179.1; NM_022650.2. [P20936-2]
UniGene; Hs.664080; -.
PDB; 1WER; X-ray; 1.60 A; A=714-1047.
PDB; 1WQ1; X-ray; 2.50 A; G=714-1047.
PDB; 2GQI; NMR; -; A=282-339.
PDB; 2GSB; NMR; -; A=341-446.
PDB; 2J05; X-ray; 1.50 A; A/B=281-341.
PDB; 2J06; X-ray; 1.80 A; A/B=281-341.
PDB; 2M51; NMR; -; A=281-341.
PDB; 4FSS; X-ray; 2.25 A; A/B/C=281-341.
PDBsum; 1WER; -.
PDBsum; 1WQ1; -.
PDBsum; 2GQI; -.
PDBsum; 2GSB; -.
PDBsum; 2J05; -.
PDBsum; 2J06; -.
PDBsum; 2M51; -.
PDBsum; 4FSS; -.
ProteinModelPortal; P20936; -.
SMR; P20936; -.
BioGrid; 111856; 54.
CORUM; P20936; -.
DIP; DIP-144N; -.
IntAct; P20936; 54.
MINT; MINT-195165; -.
STRING; 9606.ENSP00000274376; -.
iPTMnet; P20936; -.
PhosphoSitePlus; P20936; -.
BioMuta; RASA1; -.
DMDM; 121743; -.
EPD; P20936; -.
MaxQB; P20936; -.
PaxDb; P20936; -.
PeptideAtlas; P20936; -.
PRIDE; P20936; -.
Ensembl; ENST00000274376; ENSP00000274376; ENSG00000145715. [P20936-1]
Ensembl; ENST00000456692; ENSP00000411221; ENSG00000145715. [P20936-2]
Ensembl; ENST00000512763; ENSP00000422008; ENSG00000145715. [P20936-4]
Ensembl; ENST00000515800; ENSP00000423395; ENSG00000145715. [P20936-3]
GeneID; 5921; -.
KEGG; hsa:5921; -.
UCSC; uc003kiw.4; human. [P20936-1]
UCSC; uc011ctv.3; human.
UCSC; uc063fdq.1; human.
CTD; 5921; -.
DisGeNET; 5921; -.
EuPathDB; HostDB:ENSG00000145715.14; -.
GeneCards; RASA1; -.
GeneReviews; RASA1; -.
HGNC; HGNC:9871; RASA1.
HPA; CAB007789; -.
HPA; HPA036393; -.
HPA; HPA064556; -.
MalaCards; RASA1; -.
MIM; 139150; gene.
MIM; 608354; phenotype.
MIM; 608355; phenotype.
neXtProt; NX_P20936; -.
OpenTargets; ENSG00000145715; -.
Orphanet; 137667; Capillary malformation - arteriovenous malformation.
Orphanet; 90307; Parkes Weber syndrome.
PharmGKB; PA34232; -.
eggNOG; KOG3508; Eukaryota.
eggNOG; ENOG410XPU1; LUCA.
GeneTree; ENSGT00760000119092; -.
HOGENOM; HOG000007794; -.
HOVERGEN; HBG057470; -.
InParanoid; P20936; -.
KO; K04352; -.
OMA; GDMFIVH; -.
OrthoDB; EOG091G022Q; -.
PhylomeDB; P20936; -.
TreeFam; TF105301; -.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLink; P20936; -.
SIGNOR; P20936; -.
ChiTaRS; RASA1; human.
EvolutionaryTrace; P20936; -.
GeneWiki; RAS_p21_protein_activator_1; -.
GenomeRNAi; 5921; -.
PMAP-CutDB; P20936; -.
PRO; PR:P20936; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145715; -.
CleanEx; HS_RASA1; -.
ExpressionAtlas; P20936; baseline and differential.
Genevisible; P20936; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
GO; GO:0001726; C:ruffle; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; EXP:Reactome.
GO; GO:0003924; F:GTPase activity; TAS:Reactome.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0019870; F:potassium channel inhibitor activity; NAS:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:UniProtKB.
GO; GO:0009790; P:embryo development; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:GO_Central.
GO; GO:0030833; P:regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; NAS:UniProtKB.
GO; GO:0051252; P:regulation of RNA metabolic process; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
CDD; cd10354; SH2_Cterm_RasGAP; 1.
CDD; cd10353; SH2_Nterm_RasGAP; 1.
CDD; cd11788; SH3_RasGAP; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.30.505.10; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR028554; p120-RasGAP.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR035842; RasGAP_C_SH2.
InterPro; IPR023152; RasGAP_CS.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR035841; RasGAP_N_SH2.
InterPro; IPR035652; RasGAP_SH3.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10194:SF116; PTHR10194:SF116; 1.
Pfam; PF00168; C2; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00616; RasGAP; 1.
Pfam; PF00017; SH2; 2.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00323; RasGAP; 1.
SMART; SM00252; SH2; 2.
SMART; SM00326; SH3; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50004; C2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PROSITE; PS50001; SH2; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation;
GTPase activation; Phosphoprotein; Reference proteome; Repeat;
SH2 domain; SH3 domain; Tumor suppressor.
CHAIN 1 1047 Ras GTPase-activating protein 1.
/FTId=PRO_0000056636.
DOMAIN 181 272 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 279 341 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 351 441 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 474 577 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 581 676 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 748 942 Ras-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00167}.
COMPBIAS 17 22 Poly-Gly.
COMPBIAS 135 141 Poly-Pro.
COMPBIAS 163 168 Poly-Glu.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 615 615 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 177 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:3201259}.
/FTId=VSP_001625.
VAR_SEQ 1 13 MMAAEAGSEEGGP -> MRTGYSSVPSKLR (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057432.
VAR_SEQ 14 180 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057433.
VAR_SEQ 178 180 TNQ -> MKG (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:3201259}.
/FTId=VSP_001626.
VAR_SEQ 538 539 PN -> CS (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_057434.
VAR_SEQ 540 1047 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_057435.
VARIANT 398 398 R -> L (in basal cell carcinomas;
dbSNP:rs137853214).
{ECO:0000269|PubMed:8275088}.
/FTId=VAR_002650.
VARIANT 400 400 K -> E (in basal cell carcinomas;
dbSNP:rs137853215).
{ECO:0000269|PubMed:8275088}.
/FTId=VAR_002651.
VARIANT 401 401 I -> V (in basal cell carcinomas;
dbSNP:rs137853216).
{ECO:0000269|PubMed:8275088}.
/FTId=VAR_002652.
VARIANT 528 528 Y -> C (in CMAVM; dbSNP:rs145752649).
{ECO:0000269|PubMed:24038909}.
/FTId=VAR_072088.
VARIANT 530 530 V -> D (in CMAVM).
{ECO:0000269|PubMed:24038909}.
/FTId=VAR_072089.
VARIANT 540 540 C -> Y (in CMAVM; dbSNP:rs137853217).
{ECO:0000269|PubMed:14639529}.
/FTId=VAR_017744.
VARIANT 626 626 A -> E (in CMAVM).
{ECO:0000269|PubMed:24038909}.
/FTId=VAR_072090.
VARIANT 763 763 E -> V (in CMAVM; unknown pathological
significance; dbSNP:rs373098580).
{ECO:0000269|PubMed:24038909}.
/FTId=VAR_072091.
CONFLICT 789 789 R -> A (in Ref. 6; AA sequence).
{ECO:0000305}.
STRAND 283 288 {ECO:0000244|PDB:2J05}.
STRAND 296 298 {ECO:0000244|PDB:2J05}.
STRAND 306 312 {ECO:0000244|PDB:2J05}.
STRAND 316 322 {ECO:0000244|PDB:2J05}.
TURN 323 325 {ECO:0000244|PDB:2J05}.
STRAND 328 332 {ECO:0000244|PDB:2J05}.
HELIX 333 335 {ECO:0000244|PDB:2J05}.
STRAND 336 338 {ECO:0000244|PDB:2J05}.
HELIX 346 348 {ECO:0000244|PDB:2GSB}.
STRAND 350 352 {ECO:0000244|PDB:2GSB}.
HELIX 358 366 {ECO:0000244|PDB:2GSB}.
STRAND 371 378 {ECO:0000244|PDB:2GSB}.
STRAND 380 382 {ECO:0000244|PDB:2GSB}.
STRAND 386 391 {ECO:0000244|PDB:2GSB}.
STRAND 401 404 {ECO:0000244|PDB:2GSB}.
TURN 405 407 {ECO:0000244|PDB:2GSB}.
STRAND 408 413 {ECO:0000244|PDB:2GSB}.
HELIX 419 426 {ECO:0000244|PDB:2GSB}.
HELIX 720 723 {ECO:0000244|PDB:1WER}.
HELIX 724 730 {ECO:0000244|PDB:1WER}.
HELIX 736 744 {ECO:0000244|PDB:1WER}.
STRAND 746 748 {ECO:0000244|PDB:1WQ1}.
HELIX 749 762 {ECO:0000244|PDB:1WER}.
HELIX 766 780 {ECO:0000244|PDB:1WER}.
HELIX 784 786 {ECO:0000244|PDB:1WER}.
TURN 787 789 {ECO:0000244|PDB:1WQ1}.
HELIX 793 805 {ECO:0000244|PDB:1WER}.
HELIX 807 823 {ECO:0000244|PDB:1WER}.
HELIX 832 834 {ECO:0000244|PDB:1WER}.
HELIX 841 860 {ECO:0000244|PDB:1WER}.
HELIX 861 865 {ECO:0000244|PDB:1WER}.
HELIX 868 884 {ECO:0000244|PDB:1WER}.
HELIX 891 900 {ECO:0000244|PDB:1WER}.
TURN 901 904 {ECO:0000244|PDB:1WER}.
HELIX 905 910 {ECO:0000244|PDB:1WER}.
TURN 912 916 {ECO:0000244|PDB:1WER}.
HELIX 924 941 {ECO:0000244|PDB:1WER}.
STRAND 946 949 {ECO:0000244|PDB:1WQ1}.
HELIX 951 956 {ECO:0000244|PDB:1WER}.
HELIX 957 974 {ECO:0000244|PDB:1WER}.
HELIX 992 1004 {ECO:0000244|PDB:1WER}.
HELIX 1006 1013 {ECO:0000244|PDB:1WER}.
HELIX 1020 1038 {ECO:0000244|PDB:1WER}.
SEQUENCE 1047 AA; 116403 MW; C35B6567F5BC5370 CRC64;
MMAAEAGSEE GGPVTAGAGG GGAAAGSSAY PAVCRVKIPA ALPVAAAPYP GLVETGVAGT
LGGGAALGSE FLGAGSVAGA LGGAGLTGGG TAAGVAGAAA GVAGAAVAGP SGDMALTKLP
TSLLAETLGP GGGFPPLPPP PYLPPLGAGL GTVDEGDSLD GPEYEEEEVA IPLTAPPTNQ
WYHGKLDRTI AEERLRQAGK SGSYLIRESD RRPGSFVLSF LSQMNVVNHF RIIAMCGDYY
IGGRRFSSLS DLIGYYSHVS CLLKGEKLLY PVAPPEPVED RRRVRAILPY TKVPDTDEIS
FLKGDMFIVH NELEDGWMWV TNLRTDEQGL IVEDLVEEVG REEDPHEGKI WFHGKISKQE
AYNLLMTVGQ VCSFLVRPSD NTPGDYSLYF RTNENIQRFK ICPTPNNQFM MGGRYYNSIG
DIIDHYRKEQ IVEGYYLKEP VPMQDQEQVL NDTVDGKEIY NTIRRKTKDA FYKNIVKKGY
LLKKGKGKRW KNLYFILEGS DAQLIYFESE KRATKPKGLI DLSVCSVYVV HDSLFGRPNC
FQIVVQHFSE EHYIFYFAGE TPEQAEDWMK GLQAFCNLRK SSPGTSNKRL RQVSSLVLHI
EEAHKLPVKH FTNPYCNIYL NSVQVAKTHA REGQNPVWSE EFVFDDLPPD INRFEITLSN
KTKKSKDPDI LFMRCQLSRL QKGHATDEWF LLSSHIPLKG IEPGSLRVRA RYSMEKIMPE
EEYSEFKELI LQKELHVVYA LSHVCGQDRT LLASILLRIF LHEKLESLLL CTLNDREISM
EDEATTLFRA TTLASTLMEQ YMKATATQFV HHALKDSILK IMESKQSCEL SPSKLEKNED
VNTNLTHLLN ILSELVEKIF MASEILPPTL RYIYGCLQKS VQHKWPTNTT MRTRVVSGFV
FLRLICPAIL NPRMFNIISD SPSPIAARTL ILVAKSVQNL ANLVEFGAKE PYMEGVNPFI
KSNKHRMIMF LDELGNVPEL PDTTEHSRTD LSRDLAALHE ICVAHSDELR TLSNERGAQQ
HVLKKLLAIT ELLQQKQNQY TKTNDVR


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