ID SOS1_HUMAN Reviewed; 1333 AA.
AC Q07889; A8K2G3; B4DXG2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 243.
DE RecName: Full=Son of sevenless homolog 1;
DE Short=SOS-1;
GN Name=SOS1;
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), FUNCTION, AND INTERACTION WITH
RP GRB2.
RC TISSUE=Brain;
RX PubMed=8493579; DOI=10.1126/science.8493579;
RA Chardin P., Camonis J.H., Gale N.W., van Aelst L., Wigler M.H.,
RA Bar-Sagi D.;
RT "Human Sos1: a guanine nucleotide exchange factor for Ras that binds to
RT GRB2.";
RL Science 260:1338-1343(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH MUC1 AND GRB2, AND INTERACTION WITH MUC1.
RX PubMed=7664271;
RA Pandey P., Kharbanda S., Kufe D.;
RT "Association of the DF3/MUC1 breast cancer antigen with Grb2 and the
RT Sos/Ras exchange protein.";
RL Cancer Res. 55:4000-4003(1995).
RN [6]
RP INTERACTION WITH NCK1 AND NCK2.
RX PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
RA Braverman L.E., Quilliam L.A.;
RT "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing
RT adapter protein having similar binding and biological properties to Nck.";
RL J. Biol. Chem. 274:5542-5549(1999).
RN [7]
RP INTERACTION WITH LAT2.
RX PubMed=12486104; DOI=10.1084/jem.20021405;
RA Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O., Spicka J.,
RA Hilgert I., Luskova P., Draber P., Novak P., Engels N., Wienands J.,
RA Simeoni L., Oesterreicher J., Aguado E., Malissen M., Schraven B.,
RA Horejsi V.;
RT "Non-T cell activation linker (NTAL): a transmembrane adaptor protein
RT involved in immunoreceptor signaling.";
RL J. Exp. Med. 196:1617-1626(2002).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF CYS-282.
RX PubMed=17339331; DOI=10.1128/mcb.01630-06;
RA Modzelewska K., Elgort M.G., Huang J., Jongeward G., Lauritzen A.,
RA Yoon C.H., Sternberg P.W., Moghal N.;
RT "An activating mutation in sos-1 identifies its Dbl domain as a critical
RT inhibitor of the epidermal growth factor receptor pathway during
RT Caenorhabditis elegans vulval development.";
RL Mol. Cell. Biol. 27:3695-3707(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134, AND IDENTIFICATION BY
RP 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 [10]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION AT SER-1134 AND SER-1161, MUTAGENESIS OF SER-1134 AND
RP SER-1161, AND INTERACTION WITH YWHAB AND YWHAE.
RX PubMed=22827337; DOI=10.1042/bj20120938;
RA Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
RA Roux P.P., Ballif B.A.;
RT "RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
RT regulating MAPK activation.";
RL Biochem. J. 447:159-166(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082; SER-1134; SER-1178;
RP SER-1210; SER-1229 AND SER-1275, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082 AND SER-1275, AND
RP IDENTIFICATION 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., 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 [17]
RP STRUCTURE BY NMR OF 422-551.
RX PubMed=9374522; DOI=10.1074/jbc.272.48.30340;
RA Zheng J., Chen R.H., Corblan-Garcia S., Cahill S.M., Bar-Sagi D.,
RA Cowburn D.;
RT "The solution structure of the pleckstrin homology domain of human SOS1. A
RT possible structural role for the sequential association of diffuse B cell
RT lymphoma and pleckstrin homology domains.";
RL J. Biol. Chem. 272:30340-30344(1997).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 198-551.
RX PubMed=9790532; DOI=10.1016/s0092-8674(00)81756-0;
RA Soisson S.M., Nimnual A.S., Uy M., Bar-Sagi D., Kuriyan J.;
RT "Crystal structure of the Dbl and pleckstrin homology domains from the
RT human Son of sevenless protein.";
RL Cell 95:259-268(1998).
RN [19]
RP INVOLVEMENT IN GINGF1, AND TISSUE SPECIFICITY.
RX PubMed=11868160; DOI=10.1086/339689;
RA Hart T.C., Zhang Y., Gorry M.C., Hart P.S., Cooper M., Marazita M.L.,
RA Marks J.M., Cortelli J.R., Pallos D.;
RT "A mutation in the SOS1 gene causes hereditary gingival fibromatosis type
RT 1.";
RL Am. J. Hum. Genet. 70:943-954(2002).
RN [20]
RP VARIANTS NS4 LYS-266; ARG-269; TYR-309; CYS-337; ARG-434; ARG-548; GLY-552
RP AND LYS-846, AND VARIANT LEU-655.
RX PubMed=17143285; DOI=10.1038/ng1926;
RA Roberts A.E., Araki T., Swanson K.D., Montgomery K.T., Schiripo T.A.,
RA Joshi V.A., Li L., Yassin Y., Tamburino A.M., Neel B.G., Kucherlapati R.S.;
RT "Germline gain-of-function mutations in SOS1 cause Noonan syndrome.";
RL Nat. Genet. 39:70-74(2007).
RN [21]
RP VARIANTS NS4 LYS-108; ARG-269; ARG-432; LYS-433; TYR-441; ARG-548; PRO-550;
RP GLY-552; LYS-552; SER-552; HIS-702; LEU-729; PHE-733 AND LYS-846, VARIANTS
RP LEU-655; ARG-977 AND ARG-1320, AND CHARACTERIZATION OF VARIANTS NS4 GLY-552
RP AND LEU-729.
RX PubMed=17143282; DOI=10.1038/ng1939;
RA Tartaglia M., Pennacchio L.A., Zhao C., Yadav K.K., Fodale V., Sarkozy A.,
RA Pandit B., Oishi K., Martinelli S., Schackwitz W., Ustaszewska A.,
RA Martin J., Bristow J., Carta C., Lepri F., Neri C., Vasta I., Gibson K.,
RA Curry C.J., Lopez Siguero J.P., Digilio M.C., Zampino G., Dallapiccola B.,
RA Bar-Sagi D., Gelb B.D.;
RT "Gain-of-function SOS1 mutations cause a distinctive form of Noonan
RT syndrome.";
RL Nat. Genet. 39:75-79(2007).
RN [22]
RP VARIANT NS4 GLU-170.
RX PubMed=19020799; DOI=10.1007/s10038-008-0343-6;
RA Ko J.M., Kim J.M., Kim G.H., Yoo H.W.;
RT "PTPN11, SOS1, KRAS, and RAF1 gene analysis, and genotype-phenotype
RT correlation in Korean patients with Noonan syndrome.";
RL J. Hum. Genet. 53:999-1006(2008).
RN [23]
RP VARIANT NS4 ARG-432.
RX PubMed=19438935; DOI=10.1111/j.1399-0004.2009.01149.x;
RA Hanna N., Parfait B., Talaat I.M., Vidaud M., Elsedfy H.H.;
RT "SOS1: a new player in the Noonan-like/multiple giant cell lesion
RT syndrome.";
RL Clin. Genet. 75:568-571(2009).
RN [24]
RP VARIANTS NS4 THR-269; ARG-477 AND HIS-702, VARIANT GLN-497, AND
RP CHARACTERIZATION OF VARIANT GLN-497.
RX PubMed=20683980; DOI=10.1002/ajmg.a.33564;
RA Longoni M., Moncini S., Cisternino M., Morella I.M., Ferraiuolo S.,
RA Russo S., Mannarino S., Brazzelli V., Coi P., Zippel R., Venturin M.,
RA Riva P.;
RT "Noonan syndrome associated with both a new Jnk-activating familial SOS1
RT and a de novo RAF1 mutations.";
RL Am. J. Med. Genet. A 152:2176-2184(2010).
RN [25]
RP VARIANT NS4 ILE-623.
RX PubMed=20673819; DOI=10.1016/j.ejmg.2010.07.011;
RA Fabretto A., Kutsche K., Harmsen M.B., Demarini S., Gasparini P.,
RA Fertz M.C., Zenker M.;
RT "Two cases of Noonan syndrome with severe respiratory and gastroenteral
RT involvement and the SOS1 mutation F623I.";
RL Eur. J. Med. Genet. 53:322-324(2010).
RN [26]
RP VARIANTS NS4 ARG-102; GLU-170; LYS-266; THR-269; ALA-378; LYS-433 AND
RP GLY-552, AND VARIANTS VAL-569 AND LEU-655.
RX PubMed=19953625; DOI=10.1002/gcc.20735;
RA Denayer E., Devriendt K., de Ravel T., Van Buggenhout G., Smeets E.,
RA Francois I., Sznajer Y., Craen M., Leventopoulos G., Mutesa L.,
RA Vandecasseye W., Massa G., Kayserili H., Sciot R., Fryns J.P., Legius E.;
RT "Tumor spectrum in children with Noonan syndrome and SOS1 or RAF1
RT mutations.";
RL Genes Chromosomes Cancer 49:242-252(2010).
RN [27]
RP VARIANTS NS4 LYS-108; ARG-112; GLU-170; THR-252; LYS-266; THR-269; ARG-269;
RP VAL-422; LYS-424; 427-LYS--ASP-430 DELINS ASN; ARG-432; 432-TRP-GLU-433
RP DEL; LYS-433; ARG-434; LYS-434; THR-437; TYR-441; ARG-477; ARG-478;
RP ARG-482; ARG-490; GLN-497; ARG-548; LYS-549; GLY-552; LYS-552; MET-552;
RP THR-552; SER-552; 554-LEU--MET-558 DELINS LYS; PHE-733; LYS-846 AND
RP ARG-894, AND VARIANTS ALA-37; LEU-478; VAL-569; LEU-655; THR-708; THR-784;
RP SER-1011; LYS-1131; ILE-1140; ALA-1257 AND ARG-1320.
RX PubMed=21387466; DOI=10.1002/humu.21492;
RA Lepri F., De Luca A., Stella L., Rossi C., Baldassarre G., Pantaleoni F.,
RA Cordeddu V., Williams B.J., Dentici M.L., Caputo V., Venanzi S.,
RA Bonaguro M., Kavamura I., Faienza M.F., Pilotta A., Stanzial F.,
RA Faravelli F., Gabrielli O., Marino B., Neri G., Silengo M.C., Ferrero G.B.,
RA Torrrente I., Selicorni A., Mazzanti L., Digilio M.C., Zampino G.,
RA Dallapiccola B., Gelb B.D., Tartaglia M.;
RT "SOS1 mutations in Noonan syndrome: molecular spectrum, structural insights
RT on pathogenic effects, and genotype-phenotype correlations.";
RL Hum. Mutat. 32:760-772(2011).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP
CC (PubMed:8493579). Probably by promoting Ras activation, regulates
CC phosphorylation of MAP kinase MAPK3 in response to EGF
CC (PubMed:17339331). Catalytic component of a trimeric complex that
CC participates in transduction of signals from Ras to Rac by promoting
CC the Rac-specific guanine nucleotide exchange factor (GEF) activity (By
CC similarity). {ECO:0000250|UniProtKB:Q62245,
CC ECO:0000269|PubMed:17339331, ECO:0000269|PubMed:8493579}.
CC -!- SUBUNIT: Interacts (via C-terminus) with GRB2 (via SH3 domain)
CC (PubMed:8493579, PubMed:7664271). Forms a complex with phosphorylated
CC MUC1 and GRB2 (via its SH3 domains) (PubMed:7664271). Interacts with
CC phosphorylated LAT2 (PubMed:12486104). Interacts with NCK1 and NCK2
CC (PubMed:10026169). Part of a complex consisting of ABI1, EPS8 and SOS1
CC (By similarity). Interacts (Ser-1134 and Ser-1161 phosphorylated form)
CC with YWHAB and YWHAE (PubMed:22827337). {ECO:0000250|UniProtKB:Q62245,
CC ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:12486104,
CC ECO:0000269|PubMed:22827337, ECO:0000269|PubMed:7664271,
CC ECO:0000269|PubMed:8493579}.
CC -!- INTERACTION:
CC Q07889; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-297487, EBI-350590;
CC Q07889; P46108: CRK; NbExp=5; IntAct=EBI-297487, EBI-886;
CC Q07889; P00533: EGFR; NbExp=3; IntAct=EBI-297487, EBI-297353;
CC Q07889; P62993: GRB2; NbExp=26; IntAct=EBI-297487, EBI-401755;
CC Q07889; P08631: HCK; NbExp=4; IntAct=EBI-297487, EBI-346340;
CC Q07889; P01112: HRAS; NbExp=11; IntAct=EBI-297487, EBI-350145;
CC Q07889; P16333: NCK1; NbExp=5; IntAct=EBI-297487, EBI-389883;
CC Q07889; P20929: NEB; NbExp=3; IntAct=EBI-297487, EBI-1049657;
CC Q07889; Q9UKS6: PACSIN3; NbExp=2; IntAct=EBI-297487, EBI-77926;
CC Q07889; P27986: PIK3R1; NbExp=3; IntAct=EBI-297487, EBI-79464;
CC Q07889; P19174: PLCG1; NbExp=3; IntAct=EBI-297487, EBI-79387;
CC Q07889; P29353: SHC1; NbExp=2; IntAct=EBI-297487, EBI-78835;
CC Q07889; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-297487, EBI-77848;
CC Q07889; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-297487, EBI-7353612;
CC Q07889; Q5TCZ1-2; NbExp=5; IntAct=EBI-297487, EBI-7014859;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q07889-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07889-2; Sequence=VSP_056463, VSP_056464, VSP_056465;
CC -!- TISSUE SPECIFICITY: Expressed in gingival tissues.
CC {ECO:0000269|PubMed:11868160}.
CC -!- PTM: Phosphorylation at Ser-1134 and Ser-1161 by RPS6KA3 create YWHAB
CC and YWHAE binding sites and which contribute to the negative regulation
CC of EGF-induced MAPK1/3 phosphorylation. {ECO:0000269|PubMed:22827337}.
CC -!- DISEASE: Fibromatosis, gingival, 1 (GINGF1) [MIM:135300]: A form of
CC hereditary gingival fibromatosis, a rare condition characterized by a
CC slow, progressive overgrowth of the gingiva. The excess gingival tissue
CC can cover part of or the entire crown, and can result in diastemas,
CC teeth displacement, or retention of primary or impacted teeth. GINGF1
CC is usually transmitted as an autosomal dominant trait, although
CC sporadic cases are common. {ECO:0000269|PubMed:11868160}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Noonan syndrome 4 (NS4) [MIM:610733]: A form of Noonan
CC syndrome, a disease characterized by short stature, facial dysmorphic
CC features such as hypertelorism, a downward eyeslant and low-set
CC posteriorly rotated ears, and a high incidence of congenital heart
CC defects and hypertrophic cardiomyopathy. Other features can include a
CC short neck with webbing or redundancy of skin, deafness, motor delay,
CC variable intellectual deficits, multiple skeletal defects,
CC cryptorchidism, and bleeding diathesis. Individuals with Noonan
CC syndrome are at risk of juvenile myelomonocytic leukemia, a
CC myeloproliferative disorder characterized by excessive production of
CC myelomonocytic cells. Some patients with NS4 have polyarticular
CC villonodular synovitis. {ECO:0000269|PubMed:17143282,
CC ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:19020799,
CC ECO:0000269|PubMed:19438935, ECO:0000269|PubMed:19953625,
CC ECO:0000269|PubMed:20673819, ECO:0000269|PubMed:20683980,
CC ECO:0000269|PubMed:21387466}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Son of sevenless entry;
CC URL="https://en.wikipedia.org/wiki/Son_of_Sevenless";
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CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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DR EMBL; L13857; AAA35913.1; -; mRNA.
DR EMBL; AK290228; BAF82917.1; -; mRNA.
DR EMBL; AK301960; BAG63374.1; -; mRNA.
DR EMBL; AC019171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00351.1; -; Genomic_DNA.
DR CCDS; CCDS1802.1; -. [Q07889-1]
DR PIR; A37488; A37488.
DR RefSeq; NP_005624.2; NM_005633.3. [Q07889-1]
DR PDB; 1AWE; NMR; -; A=422-551.
DR PDB; 1BKD; X-ray; 2.80 A; S=568-1044.
DR PDB; 1DBH; X-ray; 2.30 A; A=198-551.
DR PDB; 1NVU; X-ray; 2.20 A; S=566-1046.
DR PDB; 1NVV; X-ray; 2.18 A; S=566-1046.
DR PDB; 1NVW; X-ray; 2.70 A; S=566-1046.
DR PDB; 1NVX; X-ray; 3.20 A; S=566-1046.
DR PDB; 1Q9C; X-ray; 3.21 A; A/B/C/D/E/F/G/H/I=1-191.
DR PDB; 1XD2; X-ray; 2.70 A; C=566-1049.
DR PDB; 1XD4; X-ray; 3.64 A; A/B=198-1049.
DR PDB; 1XDV; X-ray; 4.10 A; A/B=198-1044.
DR PDB; 2II0; X-ray; 2.02 A; A=564-1049.
DR PDB; 3KSY; X-ray; 3.18 A; A=1-1049.
DR PDB; 4NYI; X-ray; 2.96 A; S=566-1046.
DR PDB; 4NYJ; X-ray; 2.85 A; S=566-1046.
DR PDB; 4NYM; X-ray; 3.55 A; S=566-1046.
DR PDB; 4URU; X-ray; 2.83 A; S=564-1049.
DR PDB; 4URV; X-ray; 2.58 A; S=564-1049.
DR PDB; 4URW; X-ray; 2.76 A; S=564-1049.
DR PDB; 4URX; X-ray; 2.49 A; S=564-1049.
DR PDB; 4URY; X-ray; 2.47 A; S=564-1049.
DR PDB; 4URZ; X-ray; 2.24 A; S=564-1049.
DR PDB; 4US0; X-ray; 2.17 A; S=564-1049.
DR PDB; 4US1; X-ray; 2.65 A; S=564-1049.
DR PDB; 4US2; X-ray; 2.48 A; S=564-1049.
DR PDB; 5OVD; X-ray; 1.90 A; A=560-1049.
DR PDB; 5OVE; X-ray; 1.85 A; A=560-1049.
DR PDB; 5OVF; X-ray; 2.01 A; A=560-1049.
DR PDB; 5OVG; X-ray; 2.30 A; A=560-1049.
DR PDB; 5OVH; X-ray; 2.30 A; A=560-1049.
DR PDB; 5OVI; X-ray; 2.20 A; A=560-1049.
DR PDB; 5WFO; X-ray; 1.99 A; N=566-1046.
DR PDB; 5WFP; X-ray; 2.08 A; N=566-1046.
DR PDB; 5WFQ; X-ray; 2.26 A; N=566-1046.
DR PDB; 5WFR; X-ray; 2.46 A; N=566-1046.
DR PDB; 6BVI; X-ray; 1.75 A; B=566-1046.
DR PDB; 6BVJ; X-ray; 1.75 A; B=566-1046.
DR PDB; 6BVK; X-ray; 1.80 A; B=566-1046.
DR PDB; 6BVL; X-ray; 1.75 A; B=566-1046.
DR PDB; 6BVM; X-ray; 1.80 A; B=566-1046.
DR PDB; 6CUO; X-ray; 1.73 A; B=566-1046.
DR PDB; 6CUP; X-ray; 1.83 A; B=566-1046.
DR PDB; 6CUR; X-ray; 1.73 A; B=566-1046.
DR PDB; 6D55; X-ray; 1.68 A; B=566-1046.
DR PDB; 6D56; X-ray; 1.68 A; B=566-1046.
DR PDB; 6D59; X-ray; 1.70 A; B=566-1046.
DR PDB; 6D5E; X-ray; 1.75 A; B=566-1046.
DR PDB; 6D5G; X-ray; 1.92 A; B=566-1046.
DR PDB; 6D5H; X-ray; 1.80 A; B=566-1046.
DR PDB; 6D5J; X-ray; 1.75 A; B=566-1046.
DR PDB; 6D5L; X-ray; 1.70 A; B=566-1046.
DR PDB; 6D5M; X-ray; 2.08 A; S=566-1046.
DR PDB; 6D5V; X-ray; 2.04 A; S=566-1046.
DR PDB; 6D5W; X-ray; 2.48 A; S=566-1046.
DR PDB; 6EPL; X-ray; 2.55 A; S=563-1049.
DR PDB; 6EPM; X-ray; 2.50 A; S=563-1049.
DR PDB; 6EPN; X-ray; 2.50 A; S=563-1049.
DR PDB; 6EPO; X-ray; 2.40 A; S=563-1049.
DR PDB; 6EPP; X-ray; 2.40 A; S=563-1049.
DR PDB; 6F08; X-ray; 1.90 A; D/K/N/Q=1155-1167.
DR PDB; 6SCM; X-ray; 1.87 A; A=564-1049.
DR PDB; 6SFR; X-ray; 1.92 A; A/B=564-1049.
DR PDB; 6V94; X-ray; 1.80 A; B=566-1046.
DR PDB; 6V9F; X-ray; 1.85 A; B=566-1046.
DR PDB; 6V9J; X-ray; 1.76 A; B=566-1046.
DR PDB; 6V9L; X-ray; 1.70 A; B=566-1046.
DR PDB; 6V9M; X-ray; 1.65 A; B=566-1046.
DR PDB; 6V9N; X-ray; 1.65 A; B=566-1046.
DR PDB; 6V9O; X-ray; 1.80 A; B=566-1046.
DR PDB; 6Y44; X-ray; 1.71 A; P=1155-1167.
DR PDB; 7AVI; X-ray; 1.93 A; A/B=564-1049.
DR PDB; 7AVL; X-ray; 1.72 A; A/B=564-1049.
DR PDB; 7AVS; X-ray; 2.28 A; A/B=564-1049.
DR PDB; 7AVT; X-ray; 1.88 A; A/B=564-1049.
DR PDB; 7AVU; X-ray; 2.10 A; A/B=564-1049.
DR PDB; 7AVV; X-ray; 2.12 A; A=564-1049.
DR PDB; 7KFZ; EM; 3.47 A; B=564-1049.
DR PDB; 7UKR; X-ray; 2.50 A; A/B=564-1049.
DR PDB; 7UKS; X-ray; 2.29 A; A=564-1049.
DR PDB; 8BE2; X-ray; 1.90 A; S=564-1049.
DR PDB; 8BE4; X-ray; 1.90 A; S=564-1049.
DR PDB; 8BE5; X-ray; 3.13 A; AAZA=564-1049.
DR PDB; 8BE6; X-ray; 2.90 A; S=564-1049.
DR PDB; 8BE7; X-ray; 3.00 A; S=564-1049.
DR PDB; 8BE8; X-ray; 2.40 A; S=564-1049.
DR PDB; 8BE9; X-ray; 2.51 A; S=564-1049.
DR PDB; 8BEA; X-ray; 2.47 A; S=564-1049.
DR PDBsum; 1AWE; -.
DR PDBsum; 1BKD; -.
DR PDBsum; 1DBH; -.
DR PDBsum; 1NVU; -.
DR PDBsum; 1NVV; -.
DR PDBsum; 1NVW; -.
DR PDBsum; 1NVX; -.
DR PDBsum; 1Q9C; -.
DR PDBsum; 1XD2; -.
DR PDBsum; 1XD4; -.
DR PDBsum; 1XDV; -.
DR PDBsum; 2II0; -.
DR PDBsum; 3KSY; -.
DR PDBsum; 4NYI; -.
DR PDBsum; 4NYJ; -.
DR PDBsum; 4NYM; -.
DR PDBsum; 4URU; -.
DR PDBsum; 4URV; -.
DR PDBsum; 4URW; -.
DR PDBsum; 4URX; -.
DR PDBsum; 4URY; -.
DR PDBsum; 4URZ; -.
DR PDBsum; 4US0; -.
DR PDBsum; 4US1; -.
DR PDBsum; 4US2; -.
DR PDBsum; 5OVD; -.
DR PDBsum; 5OVE; -.
DR PDBsum; 5OVF; -.
DR PDBsum; 5OVG; -.
DR PDBsum; 5OVH; -.
DR PDBsum; 5OVI; -.
DR PDBsum; 5WFO; -.
DR PDBsum; 5WFP; -.
DR PDBsum; 5WFQ; -.
DR PDBsum; 5WFR; -.
DR PDBsum; 6BVI; -.
DR PDBsum; 6BVJ; -.
DR PDBsum; 6BVK; -.
DR PDBsum; 6BVL; -.
DR PDBsum; 6BVM; -.
DR PDBsum; 6CUO; -.
DR PDBsum; 6CUP; -.
DR PDBsum; 6CUR; -.
DR PDBsum; 6D55; -.
DR PDBsum; 6D56; -.
DR PDBsum; 6D59; -.
DR PDBsum; 6D5E; -.
DR PDBsum; 6D5G; -.
DR PDBsum; 6D5H; -.
DR PDBsum; 6D5J; -.
DR PDBsum; 6D5L; -.
DR PDBsum; 6D5M; -.
DR PDBsum; 6D5V; -.
DR PDBsum; 6D5W; -.
DR PDBsum; 6EPL; -.
DR PDBsum; 6EPM; -.
DR PDBsum; 6EPN; -.
DR PDBsum; 6EPO; -.
DR PDBsum; 6EPP; -.
DR PDBsum; 6F08; -.
DR PDBsum; 6SCM; -.
DR PDBsum; 6SFR; -.
DR PDBsum; 6V94; -.
DR PDBsum; 6V9F; -.
DR PDBsum; 6V9J; -.
DR PDBsum; 6V9L; -.
DR PDBsum; 6V9M; -.
DR PDBsum; 6V9N; -.
DR PDBsum; 6V9O; -.
DR PDBsum; 6Y44; -.
DR PDBsum; 7AVI; -.
DR PDBsum; 7AVL; -.
DR PDBsum; 7AVS; -.
DR PDBsum; 7AVT; -.
DR PDBsum; 7AVU; -.
DR PDBsum; 7AVV; -.
DR PDBsum; 7KFZ; -.
DR PDBsum; 7UKR; -.
DR PDBsum; 7UKS; -.
DR PDBsum; 8BE2; -.
DR PDBsum; 8BE4; -.
DR PDBsum; 8BE5; -.
DR PDBsum; 8BE6; -.
DR PDBsum; 8BE7; -.
DR PDBsum; 8BE8; -.
DR PDBsum; 8BE9; -.
DR PDBsum; 8BEA; -.
DR AlphaFoldDB; Q07889; -.
DR EMDB; EMD-22857; -.
DR SMR; Q07889; -.
DR BioGRID; 112537; 81.
DR ComplexPortal; CPX-395; GTPase HRAS - Son of sevenless homolog 1 complex.
DR CORUM; Q07889; -.
DR DIP; DIP-31802N; -.
DR IntAct; Q07889; 42.
DR MINT; Q07889; -.
DR STRING; 9606.ENSP00000384675; -.
DR BindingDB; Q07889; -.
DR ChEMBL; CHEMBL2079846; -.
DR GuidetoPHARMACOLOGY; 3096; -.
DR GlyGen; Q07889; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q07889; -.
DR PhosphoSitePlus; Q07889; -.
DR BioMuta; SOS1; -.
DR DMDM; 6094322; -.
DR CPTAC; CPTAC-1554; -.
DR CPTAC; CPTAC-1555; -.
DR EPD; Q07889; -.
DR jPOST; Q07889; -.
DR MassIVE; Q07889; -.
DR MaxQB; Q07889; -.
DR PaxDb; 9606-ENSP00000387784; -.
DR PeptideAtlas; Q07889; -.
DR ProteomicsDB; 5432; -.
DR ProteomicsDB; 58554; -. [Q07889-1]
DR Pumba; Q07889; -.
DR Antibodypedia; 2769; 267 antibodies from 36 providers.
DR DNASU; 6654; -.
DR Ensembl; ENST00000402219.8; ENSP00000384675.2; ENSG00000115904.15. [Q07889-1]
DR GeneID; 6654; -.
DR KEGG; hsa:6654; -.
DR MANE-Select; ENST00000402219.8; ENSP00000384675.2; NM_005633.4; NP_005624.2.
DR UCSC; uc002rrk.5; human. [Q07889-1]
DR AGR; HGNC:11187; -.
DR CTD; 6654; -.
DR DisGeNET; 6654; -.
DR GeneCards; SOS1; -.
DR GeneReviews; SOS1; -.
DR HGNC; HGNC:11187; SOS1.
DR HPA; ENSG00000115904; Low tissue specificity.
DR MalaCards; SOS1; -.
DR MIM; 135300; phenotype.
DR MIM; 182530; gene.
DR MIM; 610733; phenotype.
DR neXtProt; NX_Q07889; -.
DR OpenTargets; ENSG00000115904; -.
DR Orphanet; 2024; Hereditary gingival fibromatosis.
DR Orphanet; 648; Noonan syndrome.
DR PharmGKB; PA36024; -.
DR VEuPathDB; HostDB:ENSG00000115904; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000155423; -.
DR InParanoid; Q07889; -.
DR OMA; FREPFIS; -.
DR OrthoDB; 68574at2759; -.
DR PhylomeDB; Q07889; -.
DR TreeFam; TF317296; -.
DR PathwayCommons; Q07889; -.
DR Reactome; R-HSA-112412; SOS-mediated signalling.
DR Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR Reactome; R-HSA-1433559; Regulation of KIT signaling.
DR Reactome; R-HSA-167044; Signalling to RAS.
DR Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-HSA-210993; Tie2 Signaling.
DR Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-HSA-2424491; DAP12 signaling.
DR Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-428540; Activation of RAC1.
DR Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
DR Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
DR Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-5655332; Signaling by FGFR3 in disease.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-74749; Signal attenuation.
DR Reactome; R-HSA-74751; Insulin receptor signalling cascade.
DR Reactome; R-HSA-8851805; MET activates RAS signaling.
DR Reactome; R-HSA-8853659; RET signaling.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9026519; Activated NTRK2 signals through RAS.
DR Reactome; R-HSA-9027284; Erythropoietin activates RAS.
DR Reactome; R-HSA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR Reactome; R-HSA-9034864; Activated NTRK3 signals through RAS.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR Reactome; R-HSA-9607240; FLT3 Signaling.
DR Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants.
DR Reactome; R-HSA-9673767; Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants.
DR Reactome; R-HSA-9673770; Signaling by PDGFRA extracellular domain mutants.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9680350; Signaling by CSF1 (M-CSF) in myeloid cells.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR Reactome; R-HSA-9703648; Signaling by FLT3 ITD and TKD mutants.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q07889; -.
DR SIGNOR; Q07889; -.
DR BioGRID-ORCS; 6654; 117 hits in 1167 CRISPR screens.
DR ChiTaRS; SOS1; human.
DR EvolutionaryTrace; Q07889; -.
DR GeneWiki; SOS1; -.
DR GenomeRNAi; 6654; -.
DR Pharos; Q07889; Tchem.
DR PRO; PR:Q07889; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q07889; Protein.
DR Bgee; ENSG00000115904; Expressed in colonic epithelium and 212 other cell types or tissues.
DR ExpressionAtlas; Q07889; baseline and differential.
DR Genevisible; Q07889; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1905360; C:GTPase complex; IPI:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR GO; GO:0140693; F:molecular condensate scaffold activity; IDA:DisProt.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR GO; GO:1904693; P:midbrain morphogenesis; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0003344; P:pericardium morphogenesis; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:ComplexPortal.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:ComplexPortal.
DR GO; GO:2000973; P:regulation of pro-B cell differentiation; IEA:Ensembl.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
DR CDD; cd01261; PH_SOS; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd00160; RhoGEF; 1.
DR DisProt; DP01534; -.
DR Gene3D; 6.10.250.3060; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF168; SON OF SEVENLESS HOMOLOG 1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..1333
FT /note="Son of sevenless homolog 1"
FT /id="PRO_0000068894"
FT DOMAIN 200..390
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 444..548
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 597..741
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 780..1019
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 1019..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62245"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1134
FT /note="Phosphoserine; by RPS6KA3"
FT /evidence="ECO:0000269|PubMed:22827337,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1161
FT /note="Phosphoserine; by RPS6KA3"
FT /evidence="ECO:0000269|PubMed:22827337"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056463"
FT VAR_SEQ 359..371
FT /note="QLEEKSEDQEDKE -> FPFGDLSRLRDSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056464"
FT VAR_SEQ 372..1333
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056465"
FT VARIANT 37
FT /note="T -> A (in a patient with Noonan syndrome;
FT dbSNP:rs150565592)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066031"
FT VARIANT 102
FT /note="P -> R (in NS4; dbSNP:rs1553362937)"
FT /evidence="ECO:0000269|PubMed:19953625"
FT /id="VAR_066032"
FT VARIANT 108
FT /note="E -> K (in NS4; dbSNP:rs397517164)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030423"
FT VARIANT 112
FT /note="P -> R (in NS4; dbSNP:rs397517166)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066033"
FT VARIANT 170
FT /note="K -> E (in NS4; dbSNP:rs397517172)"
FT /evidence="ECO:0000269|PubMed:19020799,
FT ECO:0000269|PubMed:19953625, ECO:0000269|PubMed:21387466"
FT /id="VAR_066034"
FT VARIANT 252
FT /note="I -> T (in NS4; dbSNP:rs142094234)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066035"
FT VARIANT 266
FT /note="T -> K (in NS4; dbSNP:rs137852812)"
FT /evidence="ECO:0000269|PubMed:17143285,
FT ECO:0000269|PubMed:19953625, ECO:0000269|PubMed:21387466"
FT /id="VAR_030424"
FT VARIANT 269
FT /note="M -> R (in NS4; dbSNP:rs137852813)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:21387466"
FT /id="VAR_030425"
FT VARIANT 269
FT /note="M -> T (in NS4; dbSNP:rs137852813)"
FT /evidence="ECO:0000269|PubMed:19953625,
FT ECO:0000269|PubMed:20683980, ECO:0000269|PubMed:21387466"
FT /id="VAR_064504"
FT VARIANT 309
FT /note="D -> Y (in NS4; dbSNP:rs397517180)"
FT /evidence="ECO:0000269|PubMed:17143285"
FT /id="VAR_030426"
FT VARIANT 337
FT /note="Y -> C (in NS4; dbSNP:rs724160007)"
FT /evidence="ECO:0000269|PubMed:17143285"
FT /id="VAR_030427"
FT VARIANT 378
FT /note="T -> A (in NS4; dbSNP:rs397517146)"
FT /evidence="ECO:0000269|PubMed:19953625"
FT /id="VAR_066036"
FT VARIANT 422
FT /note="M -> V (in NS4)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066037"
FT VARIANT 424
FT /note="E -> K (in NS4; dbSNP:rs730881041)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066038"
FT VARIANT 427..430
FT /note="KNID -> N (in NS4)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066039"
FT VARIANT 432..433
FT /note="Missing (in NS4)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066040"
FT VARIANT 432
FT /note="W -> R (in NS4; dbSNP:rs267607080)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:19438935, ECO:0000269|PubMed:21387466"
FT /id="VAR_030428"
FT VARIANT 433
FT /note="E -> K (in NS4; dbSNP:rs397517147)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:19953625, ECO:0000269|PubMed:21387466"
FT /id="VAR_030429"
FT VARIANT 434
FT /note="G -> K (in NS4; requires 2 nucleotide substitutions;
FT dbSNP:rs730881048)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066041"
FT VARIANT 434
FT /note="G -> R (in NS4; dbSNP:rs397517148)"
FT /evidence="ECO:0000269|PubMed:17143285,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030430"
FT VARIANT 437
FT /note="I -> T (in NS4; dbSNP:rs397517150)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066042"
FT VARIANT 441
FT /note="C -> Y (in NS4; dbSNP:rs727504295)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030431"
FT VARIANT 477
FT /note="Q -> R (in NS4; dbSNP:rs730881044)"
FT /evidence="ECO:0000269|PubMed:20683980,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_064505"
FT VARIANT 478
FT /note="P -> L (found in patients with Noonan syndrome;
FT dbSNP:rs1553356111)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066043"
FT VARIANT 478
FT /note="P -> R (in NS4; dbSNP:rs1553356111)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066044"
FT VARIANT 482
FT /note="G -> R (in NS4; dbSNP:rs1431574387)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066045"
FT VARIANT 490
FT /note="L -> R (in NS4)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066046"
FT VARIANT 497
FT /note="R -> Q (in NS4; one patient with Noonan syndrome
FT also carries a likely causative mutation in RAF1; the
FT mutant protein cannot induce ERK1 phosphorylation;
FT dbSNP:rs371314838)"
FT /evidence="ECO:0000269|PubMed:20683980,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_064506"
FT VARIANT 548
FT /note="S -> R (in NS4; dbSNP:rs397517149)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:21387466"
FT /id="VAR_030432"
FT VARIANT 549
FT /note="T -> K (in NS4; dbSNP:rs730881046)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066047"
FT VARIANT 550
FT /note="L -> P (in NS4; dbSNP:rs397517153)"
FT /evidence="ECO:0000269|PubMed:17143282"
FT /id="VAR_030433"
FT VARIANT 552
FT /note="R -> G (in NS4; increases the basal level of active
FT RAS; prolonges RAS activation after EGF stimulation and
FT enhances ERK activation; dbSNP:rs137852814)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:19953625,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030434"
FT VARIANT 552
FT /note="R -> K (in NS4; dbSNP:rs397517154)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030435"
FT VARIANT 552
FT /note="R -> M (in NS4; dbSNP:rs397517154)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066048"
FT VARIANT 552
FT /note="R -> S (in NS4; dbSNP:rs267607079)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030436"
FT VARIANT 552
FT /note="R -> T (in NS4; dbSNP:rs397517154)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066049"
FT VARIANT 554..558
FT /note="LDVTM -> K (in NS4)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066050"
FT VARIANT 569
FT /note="L -> V (in dbSNP:rs200786705)"
FT /evidence="ECO:0000269|PubMed:19953625,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_066051"
FT VARIANT 623
FT /note="F -> I (in NS4; dbSNP:rs727505093)"
FT /evidence="ECO:0000269|PubMed:20673819"
FT /id="VAR_066052"
FT VARIANT 655
FT /note="P -> L (in dbSNP:rs56219475)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:19953625,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030437"
FT VARIANT 702
FT /note="Y -> H (in NS4; dbSNP:rs727505381)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:20683980"
FT /id="VAR_030438"
FT VARIANT 708
FT /note="A -> T (in dbSNP:rs140811086)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066053"
FT VARIANT 729
FT /note="W -> L (in NS4; promotes constitutive RAS activation
FT and enhances ERK activation)"
FT /evidence="ECO:0000269|PubMed:17143282"
FT /id="VAR_030439"
FT VARIANT 733
FT /note="I -> F (in NS4; dbSNP:rs574088829)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030440"
FT VARIANT 784
FT /note="I -> T (in a patient with Noonan syndrome;
FT dbSNP:rs1335137808)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066054"
FT VARIANT 846
FT /note="E -> K (in NS4; dbSNP:rs397517159)"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:17143285, ECO:0000269|PubMed:21387466"
FT /id="VAR_030441"
FT VARIANT 894
FT /note="P -> R (in NS4; dbSNP:rs1367714753)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066055"
FT VARIANT 977
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:17143282"
FT /id="VAR_030442"
FT VARIANT 1011
FT /note="N -> S (in dbSNP:rs8192671)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066056"
FT VARIANT 1131
FT /note="R -> K (in a patient with Noonan syndrome;
FT dbSNP:rs768113420)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066057"
FT VARIANT 1140
FT /note="L -> I (in a patient with Noonan syndrome;
FT dbSNP:rs375550588)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066058"
FT VARIANT 1257
FT /note="T -> A (in a patient with Noonan syndrome;
FT dbSNP:rs553805862)"
FT /evidence="ECO:0000269|PubMed:21387466"
FT /id="VAR_066059"
FT VARIANT 1320
FT /note="H -> R"
FT /evidence="ECO:0000269|PubMed:17143282,
FT ECO:0000269|PubMed:21387466"
FT /id="VAR_030443"
FT MUTAGEN 282
FT /note="C->R: Increases MAPK3 phosphorylation in response to
FT EGF stimulation."
FT /evidence="ECO:0000269|PubMed:17339331"
FT MUTAGEN 1134
FT /note="S->A: Loss of phosphorylation, disruption of
FT interaction with YWHAB and YWHAE, and modest increase in
FT the magnitude and duration of EGF-induced MAPK1/3
FT phosphorylation; when associated with A-1161."
FT /evidence="ECO:0000269|PubMed:22827337"
FT MUTAGEN 1161
FT /note="S->A: Loss of phosphorylation, disruption of
FT interaction with YWHAB and YWHAE, and modest increase in
FT the magnitude and duration of EGF-induced MAPK1/3
FT phosphorylation; when associated with A-1134."
FT /evidence="ECO:0000269|PubMed:22827337"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1Q9C"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3KSY"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1Q9C"
FT HELIX 42..61
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:3KSY"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 124..151
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 201..224
FT /evidence="ECO:0007829|PDB:1DBH"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1DBH"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 249..268
FT /evidence="ECO:0007829|PDB:1DBH"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:1DBH"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 345..363
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 381..392
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 394..402
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 420..426
FT /evidence="ECO:0007829|PDB:1DBH"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:1DBH"
FT STRAND 444..452
FT /evidence="ECO:0007829|PDB:1DBH"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:1AWE"
FT STRAND 459..473
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:1AWE"
FT STRAND 487..496
FT /evidence="ECO:0007829|PDB:1DBH"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:1DBH"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:1DBH"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:1DBH"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:1AWE"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 531..545
FT /evidence="ECO:0007829|PDB:1DBH"
FT TURN 546..549
FT /evidence="ECO:0007829|PDB:1DBH"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:7AVL"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:6V9M"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:8BEA"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:4US0"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 606..613
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:5OVE"
FT HELIX 621..630
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 637..648
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 657..664
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:3KSY"
FT HELIX 672..680
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 682..699
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 702..706
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 708..719
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 724..726
FT /evidence="ECO:0007829|PDB:6V9N"
FT HELIX 727..742
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 771..773
FT /evidence="ECO:0007829|PDB:6V9M"
FT TURN 776..778
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 781..797
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 805..810
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:5OVH"
FT HELIX 814..817
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 819..840
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 845..864
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 868..878
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 881..884
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 887..891
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 895..906
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 909..919
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 931..942
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 946..950
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 953..957
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 958..974
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 985..992
FT /evidence="ECO:0007829|PDB:6V9M"
FT TURN 996..999
FT /evidence="ECO:0007829|PDB:6V9M"
FT HELIX 1002..1016
FT /evidence="ECO:0007829|PDB:6V9M"
FT STRAND 1020..1022
FT /evidence="ECO:0007829|PDB:7UKS"
SQ SEQUENCE 1333 AA; 152464 MW; C6B99CCA11A8DE45 CRC64;
MQAQQLPYEF FSEENAPKWR GLLVPALKKV QGQVHPTLES NDDALQYVEE LILQLLNMLC
QAQPRSASDV EERVQKSFPH PIDKWAIADA QSAIEKRKRR NPLSLPVEKI HPLLKEVLGY
KIDHQVSVYI VAVLEYISAD ILKLVGNYVR NIRHYEITKQ DIKVAMCADK VLMDMFHQDV
EDINILSLTD EEPSTSGEQT YYDLVKAFMA EIRQYIRELN LIIKVFREPF VSNSKLFSAN
DVENIFSRIV DIHELSVKLL GHIEDTVEMT DEGSPHPLVG SCFEDLAEEL AFDPYESYAR
DILRPGFHDR FLSQLSKPGA ALYLQSIGEG FKEAVQYVLP RLLLAPVYHC LHYFELLKQL
EEKSEDQEDK ECLKQAITAL LNVQSGMEKI CSKSLAKRRL SESACRFYSQ QMKGKQLAIK
KMNEIQKNID GWEGKDIGQC CNEFIMEGTL TRVGAKHERH IFLFDGLMIC CKSNHGQPRL
PGASNAEYRL KEKFFMRKVQ INDKDDTNEY KHAFEIILKD ENSVIFSAKS AEEKNNWMAA
LISLQYRSTL ERMLDVTMLQ EEKEEQMRLP SADVYRFAEP DSEENIIFEE NMQPKAGIPI
IKAGTVIKLI ERLTYHMYAD PNFVRTFLTT YRSFCKPQEL LSLIIERFEI PEPEPTEADR
IAIENGDQPL SAELKRFRKE YIQPVQLRVL NVCRHWVEHH FYDFERDAYL LQRMEEFIGT
VRGKAMKKWV ESITKIIQRK KIARDNGPGH NITFQSSPPT VEWHISRPGH IETFDLLTLH
PIEIARQLTL LESDLYRAVQ PSELVGSVWT KEDKEINSPN LLKMIRHTTN LTLWFEKCIV
ETENLEERVA VVSRIIEILQ VFQELNNFNG VLEVVSAMNS SPVYRLDHTF EQIPSRQKKI
LEEAHELSED HYKKYLAKLR SINPPCVPFF GIYLTNILKT EEGNPEVLKR HGKELINFSK
RRKVAEITGE IQQYQNQPYC LRVESDIKRF FENLNPMGNS MEKEFTDYLF NKSLEIEPRN
PKPLPRFPKK YSYPLKSPGV RPSNPRPGTM RHPTPLQQEP RKISYSRIPE SETESTASAP
NSPRTPLTPP PASGASSTTD VCSVFDSDHS SPFHSSNDTV FIQVTLPHGP RSASVSSISL
TKGTDEVPVP PPVPPRRRPE SAPAESSPSK IMSKHLDSPP AIPPRQPTSK AYSPRYSISD
RTSISDPPES PPLLPPREPV RTPDVFSSSP LHLQPPPLGK KSDHGNAFFP NSPSPFTPPP
PQTPSPHGTR RHLPSPPLTQ EVDLHSIAGP PVPPRQSTSQ HIPKLPPKTY KREHTHPSMH
RDGPPLLENA HSS
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