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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 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. DR Genevisible; Q07889; HS. 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 //