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Son of sevenless homolog 1 (SOS-1)

 SOS1_HUMAN              Reviewed;        1333 AA.
Q07889; A8K2G3; B4DXG2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 198.
RecName: Full=Son of sevenless homolog 1;
Short=SOS-1;
Name=SOS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
GRB2.
TISSUE=Brain;
PubMed=8493579; DOI=10.1126/science.8493579;
Chardin P., Camonis J.H., Gale N.W., van Aelst L., Wigler M.H.,
Bar-Sagi D.;
"Human Sos1: a guanine nucleotide exchange factor for Ras that binds
to GRB2.";
Science 260:1338-1343(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION IN A COMPLEX WITH MUC1 AND GRB2, AND INTERACTION WITH
MUC1.
PubMed=7664271;
Pandey P., Kharbanda S., Kufe D.;
"Association of the DF3/MUC1 breast cancer antigen with Grb2 and the
Sos/Ras exchange protein.";
Cancer Res. 55:4000-4003(1995).
[6]
INTERACTION WITH NCK1 AND NCK2.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[7]
INTERACTION WITH LAT2.
PubMed=12486104; DOI=10.1084/jem.20021405;
Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O.,
Spicka J., Hilgert I., Luskova P., Draber P., Novak P., Engels N.,
Wienands J., Simeoni L., Oesterreicher J., Aguado E., Malissen M.,
Schraven B., Horejsi V.;
"Non-T cell activation linker (NTAL): a transmembrane adaptor protein
involved in immunoreceptor signaling.";
J. Exp. Med. 196:1617-1626(2002).
[8]
FUNCTION, AND MUTAGENESIS OF CYS-282.
PubMed=17339331; DOI=10.1128/MCB.01630-06;
Modzelewska K., Elgort M.G., Huang J., Jongeward G., Lauritzen A.,
Yoon C.H., Sternberg P.W., Moghal N.;
"An activating mutation in sos-1 identifies its Dbl domain as a
critical inhibitor of the epidermal growth factor receptor pathway
during Caenorhabditis elegans vulval development.";
Mol. Cell. Biol. 27:3695-3707(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION AT SER-1134 AND 1161, MUTAGENESIS OF SER-1134 AND
SER-1161, AND INTERACTION WITH YWHAB AND YWHAE.
PubMed=22827337; DOI=10.1042/BJ20120938;
Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
Roux P.P., Ballif B.A.;
"RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
regulating MAPK activation.";
Biochem. J. 447:159-166(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082; SER-1134;
SER-1178; SER-1210; SER-1229 AND SER-1275, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082 AND SER-1275, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
STRUCTURE BY NMR OF 422-551.
PubMed=9374522; DOI=10.1074/jbc.272.48.30340;
Zheng J., Chen R.H., Corblan-Garcia S., Cahill S.M., Bar-Sagi D.,
Cowburn D.;
"The solution structure of the pleckstrin homology domain of human
SOS1. A possible structural role for the sequential association of
diffuse B cell lymphoma and pleckstrin homology domains.";
J. Biol. Chem. 272:30340-30344(1997).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 198-551.
PubMed=9790532; DOI=10.1016/S0092-8674(00)81756-0;
Soisson S.M., Nimnual A.S., Uy M., Bar-Sagi D., Kuriyan J.;
"Crystal structure of the Dbl and pleckstrin homology domains from the
human Son of sevenless protein.";
Cell 95:259-268(1998).
[19]
INVOLVEMENT IN GINGF1, AND TISSUE SPECIFICITY.
PubMed=11868160; DOI=10.1086/339689;
Hart T.C., Zhang Y., Gorry M.C., Hart P.S., Cooper M., Marazita M.L.,
Marks J.M., Cortelli J.R., Pallos D.;
"A mutation in the SOS1 gene causes hereditary gingival fibromatosis
type 1.";
Am. J. Hum. Genet. 70:943-954(2002).
[20]
VARIANTS NS4 LYS-266; ARG-269; TYR-309; CYS-337; ARG-434; ARG-548;
GLY-552 AND LYS-846, AND VARIANT LEU-655.
PubMed=17143285; DOI=10.1038/ng1926;
Roberts A.E., Araki T., Swanson K.D., Montgomery K.T., Schiripo T.A.,
Joshi V.A., Li L., Yassin Y., Tamburino A.M., Neel B.G.,
Kucherlapati R.S.;
"Germline gain-of-function mutations in SOS1 cause Noonan syndrome.";
Nat. Genet. 39:70-74(2007).
[21]
VARIANTS NS4 LYS-108; ARG-269; ARG-432; LYS-433; TYR-441; ARG-548;
PRO-550; GLY-552; LYS-552; SER-552; HIS-702; LEU-729; PHE-733 AND
LYS-846, VARIANTS LEU-655; ARG-977 AND ARG-1320, AND CHARACTERIZATION
OF VARIANTS NS4 GLY-552 AND LEU-729.
PubMed=17143282; DOI=10.1038/ng1939;
Tartaglia M., Pennacchio L.A., Zhao C., Yadav K.K., Fodale V.,
Sarkozy A., Pandit B., Oishi K., Martinelli S., Schackwitz W.,
Ustaszewska A., Martin J., Bristow J., Carta C., Lepri F., Neri C.,
Vasta I., Gibson K., Curry C.J., Lopez Siguero J.P., Digilio M.C.,
Zampino G., Dallapiccola B., Bar-Sagi D., Gelb B.D.;
"Gain-of-function SOS1 mutations cause a distinctive form of Noonan
syndrome.";
Nat. Genet. 39:75-79(2007).
[22]
VARIANT NS4 GLU-170.
PubMed=19020799; DOI=10.1007/s10038-008-0343-6;
Ko J.M., Kim J.M., Kim G.H., Yoo H.W.;
"PTPN11, SOS1, KRAS, and RAF1 gene analysis, and genotype-phenotype
correlation in Korean patients with Noonan syndrome.";
J. Hum. Genet. 53:999-1006(2008).
[23]
VARIANT NS4 ARG-432.
PubMed=19438935; DOI=10.1111/j.1399-0004.2009.01149.x;
Hanna N., Parfait B., Talaat I.M., Vidaud M., Elsedfy H.H.;
"SOS1: a new player in the Noonan-like/multiple giant cell lesion
syndrome.";
Clin. Genet. 75:568-571(2009).
[24]
VARIANTS NS4 THR-269; ARG-477 AND HIS-702, VARIANT GLN-497, AND
CHARACTERIZATION OF VARIANT GLN-497.
PubMed=20683980; DOI=10.1002/ajmg.a.33564;
Longoni M., Moncini S., Cisternino M., Morella I.M., Ferraiuolo S.,
Russo S., Mannarino S., Brazzelli V., Coi P., Zippel R., Venturin M.,
Riva P.;
"Noonan syndrome associated with both a new Jnk-activating familial
SOS1 and a de novo RAF1 mutations.";
Am. J. Med. Genet. A 152:2176-2184(2010).
[25]
VARIANT NS4 ILE-623.
PubMed=20673819; DOI=10.1016/j.ejmg.2010.07.011;
Fabretto A., Kutsche K., Harmsen M.B., Demarini S., Gasparini P.,
Fertz M.C., Zenker M.;
"Two cases of Noonan syndrome with severe respiratory and
gastroenteral involvement and the SOS1 mutation F623I.";
Eur. J. Med. Genet. 53:322-324(2010).
[26]
VARIANTS NS4 ARG-102; GLU-170; LYS-266; THR-269; LYS-433 AND GLY-552,
AND VARIANTS ALA-378; VAL-569 AND LEU-655.
PubMed=19953625; DOI=10.1002/gcc.20735;
Denayer E., Devriendt K., de Ravel T., Van Buggenhout G., Smeets E.,
Francois I., Sznajer Y., Craen M., Leventopoulos G., Mutesa L.,
Vandecasseye W., Massa G., Kayserili H., Sciot R., Fryns J.P.,
Legius E.;
"Tumor spectrum in children with Noonan syndrome and SOS1 or RAF1
mutations.";
Genes Chromosomes Cancer 49:242-252(2010).
[27]
VARIANTS NS4 LYS-108; ARG-112; GLU-170; THR-252; LYS-266; THR-269;
ARG-269; VAL-422; LYS-424; 427-LYS--ASP-430 DELINS ASN; ARG-432;
432-TRP-GLU-433 DEL; LYS-433; ARG-434; LYS-434; THR-437; TYR-441;
ARG-477; ARG-478; ARG-482; ARG-490; GLN-497; ARG-548; LYS-549;
GLY-552; LYS-552; MET-552; THR-552; SER-552; 554-LEU--MET-558 DELINS
LYS; PHE-733; LYS-846 AND ARG-894, AND VARIANTS ALA-37; LEU-478;
VAL-569; LEU-655; THR-708; THR-784; SER-1011; LYS-1131; ILE-1140;
ALA-1257 AND ARG-1320.
PubMed=21387466; DOI=10.1002/humu.21492;
Lepri F., De Luca A., Stella L., Rossi C., Baldassarre G.,
Pantaleoni F., Cordeddu V., Williams B.J., Dentici M.L., Caputo V.,
Venanzi S., Bonaguro M., Kavamura I., Faienza M.F., Pilotta A.,
Stanzial F., Faravelli F., Gabrielli O., Marino B., Neri G.,
Silengo M.C., Ferrero G.B., Torrrente I., Selicorni A., Mazzanti L.,
Digilio M.C., Zampino G., Dallapiccola B., Gelb B.D., Tartaglia M.;
"SOS1 mutations in Noonan syndrome: molecular spectrum, structural
insights on pathogenic effects, and genotype-phenotype correlations.";
Hum. Mutat. 32:760-772(2011).
-!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP
(PubMed:8493579). Probably by promoting Ras activation, regulates
phosphorylation of MAP kinase MAPK3 in response to EGF
(PubMed:17339331). Catalytic component of a trimeric complex that
participates in transduction of signals from Ras to Rac by
promoting the Rac-specific guanine nucleotide exchange factor
(GEF) activity (By similarity). {ECO:0000250|UniProtKB:Q62245,
ECO:0000269|PubMed:17339331, ECO:0000269|PubMed:8493579}.
-!- SUBUNIT: Interacts (via C-terminus) with GRB2 (via SH3 domain)
(PubMed:8493579, PubMed:7664271). Forms a complex with
phosphorylated MUC1 and GRB2 (via its SH3 domains)
(PubMed:7664271). Interacts with phosphorylated LAT2
(PubMed:12486104). Interacts with NCK1 and NCK2 (PubMed:10026169).
Part of a complex consisting of ABI1, EPS8 and SOS1 (By
similarity). Interacts (Ser-1134 and Ser-1161 phosphorylated form)
with YWHAB and YWHAE (PubMed:22827337).
{ECO:0000250|UniProtKB:Q62245, ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:12486104, ECO:0000269|PubMed:22827337,
ECO:0000269|PubMed:7664271, ECO:0000269|PubMed:8493579}.
-!- INTERACTION:
Q5TCZ1-2:-; NbExp=5; IntAct=EBI-297487, EBI-7014859;
P46108:CRK; NbExp=3; IntAct=EBI-297487, EBI-886;
P46109:CRKL; NbExp=2; IntAct=EBI-297487, EBI-910;
P62993:GRB2; NbExp=22; IntAct=EBI-297487, EBI-401755;
P08631:HCK; NbExp=4; IntAct=EBI-297487, EBI-346340;
P01112:HRAS; NbExp=11; IntAct=EBI-297487, EBI-350145;
P16333:NCK1; NbExp=5; IntAct=EBI-297487, EBI-389883;
P20929:NEB; NbExp=3; IntAct=EBI-297487, EBI-1049657;
Q9UKS6:PACSIN3; NbExp=2; IntAct=EBI-297487, EBI-77926;
P27986:PIK3R1; NbExp=3; IntAct=EBI-297487, EBI-79464;
P19174:PLCG1; NbExp=3; IntAct=EBI-297487, EBI-79387;
P29353:SHC1; NbExp=2; IntAct=EBI-297487, EBI-78835;
Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-297487, EBI-77848;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q07889-1; Sequence=Displayed;
Name=2;
IsoId=Q07889-2; Sequence=VSP_056463, VSP_056464, VSP_056465;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in gingival tissues.
{ECO:0000269|PubMed:11868160}.
-!- PTM: Phosphorylation at Ser-1134 and Ser-1161 by RPS6KA3 create
YWHAB and YWHAE binding sites and which contribute to the negative
regulation of EGF-induced MAPK1/3 phosphorylation.
{ECO:0000269|PubMed:22827337}.
-!- DISEASE: Fibromatosis, gingival, 1 (GINGF1) [MIM:135300]: A form
of hereditary gingival fibromatosis, a rare condition
characterized by a slow, progressive overgrowth of the gingiva.
The excess gingival tissue can cover part of or the entire crown,
and can result in diastemas, teeth displacement, or retention of
primary or impacted teeth. GINGF1 is usually transmitted as an
autosomal dominant trait, although sporadic cases are common.
{ECO:0000269|PubMed:11868160}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Noonan syndrome 4 (NS4) [MIM:610733]: A form of Noonan
syndrome, a disease characterized by short stature, facial
dysmorphic features such as hypertelorism, a downward eyeslant and
low-set posteriorly rotated ears, and a high incidence of
congenital heart defects and hypertrophic cardiomyopathy. Other
features can include a short neck with webbing or redundancy of
skin, deafness, motor delay, variable intellectual deficits,
multiple skeletal defects, cryptorchidism, and bleeding diathesis.
Individuals with Noonan syndrome are at risk of juvenile
myelomonocytic leukemia, a myeloproliferative disorder
characterized by excessive production of myelomonocytic cells.
Some patients with NS4 have polyarticular villonodular synovitis.
{ECO:0000269|PubMed:17143282, ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:19020799, ECO:0000269|PubMed:19438935,
ECO:0000269|PubMed:19953625, ECO:0000269|PubMed:20673819,
ECO:0000269|PubMed:20683980, ECO:0000269|PubMed:21387466}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=Wikipedia; Note=Son of sevenless entry;
URL="https://en.wikipedia.org/wiki/Son_of_Sevenless";
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EMBL; L13857; AAA35913.1; -; mRNA.
EMBL; AK290228; BAF82917.1; -; mRNA.
EMBL; AK301960; BAG63374.1; -; mRNA.
EMBL; AC019171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00351.1; -; Genomic_DNA.
CCDS; CCDS1802.1; -. [Q07889-1]
PIR; A37488; A37488.
RefSeq; NP_005624.2; NM_005633.3. [Q07889-1]
UniGene; Hs.709893; -.
UniGene; Hs.732497; -.
PDB; 1AWE; NMR; -; A=422-551.
PDB; 1BKD; X-ray; 2.80 A; S=568-1044.
PDB; 1DBH; X-ray; 2.30 A; A=198-551.
PDB; 1NVU; X-ray; 2.20 A; S=566-1046.
PDB; 1NVV; X-ray; 2.18 A; S=566-1046.
PDB; 1NVW; X-ray; 2.70 A; S=566-1046.
PDB; 1NVX; X-ray; 3.20 A; S=566-1046.
PDB; 1Q9C; X-ray; 3.21 A; A/B/C/D/E/F/G/H/I=1-191.
PDB; 1XD2; X-ray; 2.70 A; C=566-1049.
PDB; 1XD4; X-ray; 3.64 A; A/B=198-1049.
PDB; 1XDV; X-ray; 4.10 A; A/B=198-1044.
PDB; 2II0; X-ray; 2.02 A; A=564-1049.
PDB; 3KSY; X-ray; 3.18 A; A=1-1049.
PDB; 4NYI; X-ray; 2.96 A; S=566-1046.
PDB; 4NYJ; X-ray; 2.85 A; S=566-1046.
PDB; 4NYM; X-ray; 3.55 A; S=566-1046.
PDB; 4URU; X-ray; 2.83 A; S=564-1049.
PDB; 4URV; X-ray; 2.58 A; S=564-1049.
PDB; 4URW; X-ray; 2.76 A; S=564-1049.
PDB; 4URX; X-ray; 2.49 A; S=564-1049.
PDB; 4URY; X-ray; 2.47 A; S=564-1049.
PDB; 4URZ; X-ray; 2.24 A; S=564-1049.
PDB; 4US0; X-ray; 2.17 A; S=564-1049.
PDB; 4US1; X-ray; 2.65 A; S=564-1049.
PDB; 4US2; X-ray; 2.48 A; S=564-1049.
PDBsum; 1AWE; -.
PDBsum; 1BKD; -.
PDBsum; 1DBH; -.
PDBsum; 1NVU; -.
PDBsum; 1NVV; -.
PDBsum; 1NVW; -.
PDBsum; 1NVX; -.
PDBsum; 1Q9C; -.
PDBsum; 1XD2; -.
PDBsum; 1XD4; -.
PDBsum; 1XDV; -.
PDBsum; 2II0; -.
PDBsum; 3KSY; -.
PDBsum; 4NYI; -.
PDBsum; 4NYJ; -.
PDBsum; 4NYM; -.
PDBsum; 4URU; -.
PDBsum; 4URV; -.
PDBsum; 4URW; -.
PDBsum; 4URX; -.
PDBsum; 4URY; -.
PDBsum; 4URZ; -.
PDBsum; 4US0; -.
PDBsum; 4US1; -.
PDBsum; 4US2; -.
ProteinModelPortal; Q07889; -.
SMR; Q07889; -.
BioGrid; 112537; 48.
CORUM; Q07889; -.
DIP; DIP-31802N; -.
IntAct; Q07889; 33.
MINT; MINT-106583; -.
STRING; 9606.ENSP00000384675; -.
BindingDB; Q07889; -.
ChEMBL; CHEMBL2079846; -.
iPTMnet; Q07889; -.
PhosphoSitePlus; Q07889; -.
BioMuta; SOS1; -.
DMDM; 6094322; -.
EPD; Q07889; -.
MaxQB; Q07889; -.
PaxDb; Q07889; -.
PeptideAtlas; Q07889; -.
PRIDE; Q07889; -.
DNASU; 6654; -.
Ensembl; ENST00000402219; ENSP00000384675; ENSG00000115904. [Q07889-1]
Ensembl; ENST00000426016; ENSP00000387784; ENSG00000115904. [Q07889-1]
GeneID; 6654; -.
KEGG; hsa:6654; -.
UCSC; uc002rrk.5; human. [Q07889-1]
CTD; 6654; -.
DisGeNET; 6654; -.
EuPathDB; HostDB:ENSG00000115904.12; -.
GeneCards; SOS1; -.
GeneReviews; SOS1; -.
HGNC; HGNC:11187; SOS1.
HPA; CAB005396; -.
HPA; HPA012613; -.
MalaCards; SOS1; -.
MIM; 135300; phenotype.
MIM; 182530; gene.
MIM; 610733; phenotype.
neXtProt; NX_Q07889; -.
OpenTargets; ENSG00000115904; -.
Orphanet; 2024; Hereditary gingival fibromatosis.
Orphanet; 648; Noonan syndrome.
PharmGKB; PA36024; -.
eggNOG; KOG3417; Eukaryota.
eggNOG; ENOG410XR96; LUCA.
GeneTree; ENSGT00900000140793; -.
HOGENOM; HOG000013040; -.
HOVERGEN; HBG017831; -.
InParanoid; Q07889; -.
KO; K03099; -.
OMA; MENGDQP; -.
OrthoDB; EOG091G04UL; -.
PhylomeDB; Q07889; -.
TreeFam; TF317296; -.
Reactome; R-HSA-112412; SOS-mediated signalling.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-167044; Signalling to RAS.
Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-428540; Activation of RAC1.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-8851805; MET activates RAS signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; Q07889; -.
SIGNOR; Q07889; -.
ChiTaRS; SOS1; human.
EvolutionaryTrace; Q07889; -.
GeneWiki; SOS1; -.
GenomeRNAi; 6654; -.
PRO; PR:Q07889; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115904; -.
CleanEx; HS_SOS1; -.
ExpressionAtlas; Q07889; baseline and differential.
Genevisible; Q07889; HS.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; EXP:Reactome.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0003209; P:cardiac atrium morphogenesis; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
GO; GO:0061384; P:heart trabecula morphogenesis; IEA:Ensembl.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:1904693; P:midbrain morphogenesis; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0003344; P:pericardium morphogenesis; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:2000973; P:regulation of pro-B cell differentiation; IEA:Ensembl.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0033081; P:regulation of T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.10.840.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
Pfam; PF00125; Histone; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00233; PH; 1.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF47113; SSF47113; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF48366; SSF48366; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00720; RASGEF; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Guanine-nucleotide releasing factor; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 1333 Son of sevenless homolog 1.
/FTId=PRO_0000068894.
DOMAIN 200 390 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 444 548 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 597 741 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 780 1019 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
COMPBIAS 1258 1261 Poly-Pro.
MOD_RES 1078 1078 Phosphoserine.
{ECO:0000250|UniProtKB:Q62245}.
MOD_RES 1082 1082 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1134 1134 Phosphoserine; by RPS6KA3.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22827337}.
MOD_RES 1161 1161 Phosphoserine; by RPS6KA3.
{ECO:0000269|PubMed:22827337}.
MOD_RES 1178 1178 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1210 1210 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1229 1229 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1275 1275 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 57 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056463.
VAR_SEQ 359 371 QLEEKSEDQEDKE -> FPFGDLSRLRDSV (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056464.
VAR_SEQ 372 1333 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056465.
VARIANT 37 37 T -> A (in a patient with Noonan
syndrome; dbSNP:rs150565592).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066031.
VARIANT 102 102 P -> R (in NS4).
{ECO:0000269|PubMed:19953625}.
/FTId=VAR_066032.
VARIANT 108 108 E -> K (in NS4; dbSNP:rs397517164).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030423.
VARIANT 112 112 P -> R (in NS4; dbSNP:rs397517166).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066033.
VARIANT 170 170 K -> E (in NS4; dbSNP:rs397517172).
{ECO:0000269|PubMed:19020799,
ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_066034.
VARIANT 252 252 I -> T (in NS4; dbSNP:rs142094234).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066035.
VARIANT 266 266 T -> K (in NS4; dbSNP:rs137852812).
{ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030424.
VARIANT 269 269 M -> R (in NS4; dbSNP:rs137852813).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030425.
VARIANT 269 269 M -> T (in NS4; dbSNP:rs137852813).
{ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:20683980,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_064504.
VARIANT 309 309 D -> Y (in NS4; dbSNP:rs397517180).
{ECO:0000269|PubMed:17143285}.
/FTId=VAR_030426.
VARIANT 337 337 Y -> C (in NS4; dbSNP:rs724160007).
{ECO:0000269|PubMed:17143285}.
/FTId=VAR_030427.
VARIANT 378 378 T -> A (in a patient with Noonan
syndrome; dbSNP:rs397517146).
{ECO:0000269|PubMed:19953625}.
/FTId=VAR_066036.
VARIANT 422 422 M -> V (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066037.
VARIANT 424 424 E -> K (in NS4; dbSNP:rs730881041).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066038.
VARIANT 427 430 KNID -> N (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066039.
VARIANT 432 433 Missing (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066040.
VARIANT 432 432 W -> R (in NS4; dbSNP:rs267607080).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:19438935,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030428.
VARIANT 433 433 E -> K (in NS4; dbSNP:rs397517147).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030429.
VARIANT 434 434 G -> K (in NS4; requires 2 nucleotide
substitutions; dbSNP:rs730881048).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066041.
VARIANT 434 434 G -> R (in NS4; dbSNP:rs397517148).
{ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030430.
VARIANT 437 437 I -> T (in NS4; dbSNP:rs397517150).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066042.
VARIANT 441 441 C -> Y (in NS4; dbSNP:rs727504295).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030431.
VARIANT 477 477 Q -> R (in NS4; dbSNP:rs730881044).
{ECO:0000269|PubMed:20683980,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_064505.
VARIANT 478 478 P -> L (found in patients with Noonan
syndrome). {ECO:0000269|PubMed:21387466}.
/FTId=VAR_066043.
VARIANT 478 478 P -> R (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066044.
VARIANT 482 482 G -> R (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066045.
VARIANT 490 490 L -> R (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066046.
VARIANT 497 497 R -> Q (in NS4; one patient with Noonan
syndrome also carries a likely pathogenic
mutation Ser-261 in RAF1; the mutant
protein cannot induce ERK1
phosphorylation; dbSNP:rs371314838).
{ECO:0000269|PubMed:20683980,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_064506.
VARIANT 548 548 S -> R (in NS4; dbSNP:rs397517149).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030432.
VARIANT 549 549 T -> K (in NS4; dbSNP:rs730881046).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066047.
VARIANT 550 550 L -> P (in NS4; dbSNP:rs397517153).
{ECO:0000269|PubMed:17143282}.
/FTId=VAR_030433.
VARIANT 552 552 R -> G (in NS4; increases the basal level
of active RAS; prolonges RAS activation
after EGF stimulation and enhances ERK
activation; dbSNP:rs137852814).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030434.
VARIANT 552 552 R -> K (in NS4; dbSNP:rs397517154).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030435.
VARIANT 552 552 R -> M (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066048.
VARIANT 552 552 R -> S (in NS4; dbSNP:rs267607079).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030436.
VARIANT 552 552 R -> T (in NS4; dbSNP:rs397517154).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066049.
VARIANT 554 558 LDVTM -> K (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066050.
VARIANT 569 569 L -> V (in dbSNP:rs200786705).
{ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_066051.
VARIANT 623 623 F -> I (in NS4).
{ECO:0000269|PubMed:20673819}.
/FTId=VAR_066052.
VARIANT 655 655 P -> L (in dbSNP:rs56219475).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:19953625,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030437.
VARIANT 702 702 Y -> H (in NS4; dbSNP:rs727505381).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:20683980}.
/FTId=VAR_030438.
VARIANT 708 708 A -> T (in dbSNP:rs140811086).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066053.
VARIANT 729 729 W -> L (in NS4; promotes constitutive RAS
activation and enhances ERK activation).
{ECO:0000269|PubMed:17143282}.
/FTId=VAR_030439.
VARIANT 733 733 I -> F (in NS4; dbSNP:rs574088829).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030440.
VARIANT 784 784 I -> T (in a patient with Noonan
syndrome). {ECO:0000269|PubMed:21387466}.
/FTId=VAR_066054.
VARIANT 846 846 E -> K (in NS4; dbSNP:rs397517159).
{ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:17143285,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030441.
VARIANT 894 894 P -> R (in NS4).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066055.
VARIANT 977 977 Q -> R. {ECO:0000269|PubMed:17143282}.
/FTId=VAR_030442.
VARIANT 1011 1011 N -> S (in dbSNP:rs8192671).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066056.
VARIANT 1131 1131 R -> K (in a patient with Noonan
syndrome; dbSNP:rs768113420).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066057.
VARIANT 1140 1140 L -> I (in a patient with Noonan
syndrome; dbSNP:rs375550588).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066058.
VARIANT 1257 1257 T -> A (in a patient with Noonan
syndrome; dbSNP:rs553805862).
{ECO:0000269|PubMed:21387466}.
/FTId=VAR_066059.
VARIANT 1320 1320 H -> R. {ECO:0000269|PubMed:17143282,
ECO:0000269|PubMed:21387466}.
/FTId=VAR_030443.
MUTAGEN 282 282 C->R: Increases MAPK3 phosphorylation in
response to EGF stimulation.
{ECO:0000269|PubMed:17339331}.
MUTAGEN 1134 1134 S->A: Loss of phosphorylation, disruption
of interaction with YWHAB and YWHAE, and
modest increase in the magnitude and
duration of EGF-induced MAPK1/3
phosphorylation; when associated with A-
1161. {ECO:0000269|PubMed:22827337}.
MUTAGEN 1161 1161 S->A: Loss of phosphorylation, disruption
of interaction with YWHAB and YWHAE, and
modest increase in the magnitude and
duration of EGF-induced MAPK1/3
phosphorylation; when associated with A-
1134. {ECO:0000269|PubMed:22827337}.
TURN 13 15 {ECO:0000244|PDB:1Q9C}.
STRAND 19 23 {ECO:0000244|PDB:3KSY}.
HELIX 24 34 {ECO:0000244|PDB:3KSY}.
STRAND 36 39 {ECO:0000244|PDB:1Q9C}.
HELIX 42 61 {ECO:0000244|PDB:3KSY}.
HELIX 67 77 {ECO:0000244|PDB:3KSY}.
HELIX 82 94 {ECO:0000244|PDB:3KSY}.
STRAND 100 102 {ECO:0000244|PDB:3KSY}.
HELIX 107 118 {ECO:0000244|PDB:3KSY}.
HELIX 124 151 {ECO:0000244|PDB:3KSY}.
HELIX 159 168 {ECO:0000244|PDB:3KSY}.
HELIX 172 175 {ECO:0000244|PDB:3KSY}.
HELIX 201 224 {ECO:0000244|PDB:1DBH}.
TURN 225 227 {ECO:0000244|PDB:1DBH}.
HELIX 228 232 {ECO:0000244|PDB:1DBH}.
TURN 234 236 {ECO:0000244|PDB:1DBH}.
HELIX 239 246 {ECO:0000244|PDB:1DBH}.
HELIX 249 268 {ECO:0000244|PDB:1DBH}.
STRAND 274 276 {ECO:0000244|PDB:1DBH}.
HELIX 280 288 {ECO:0000244|PDB:1DBH}.
TURN 289 292 {ECO:0000244|PDB:1DBH}.
HELIX 293 302 {ECO:0000244|PDB:1DBH}.
HELIX 307 316 {ECO:0000244|PDB:1DBH}.
HELIX 320 327 {ECO:0000244|PDB:1DBH}.
HELIX 331 337 {ECO:0000244|PDB:1DBH}.
HELIX 339 342 {ECO:0000244|PDB:1DBH}.
HELIX 345 363 {ECO:0000244|PDB:1DBH}.
HELIX 367 379 {ECO:0000244|PDB:1DBH}.
HELIX 381 392 {ECO:0000244|PDB:1DBH}.
HELIX 394 402 {ECO:0000244|PDB:1DBH}.
HELIX 420 426 {ECO:0000244|PDB:1DBH}.
STRAND 429 431 {ECO:0000244|PDB:1DBH}.
HELIX 437 439 {ECO:0000244|PDB:1DBH}.
STRAND 444 452 {ECO:0000244|PDB:1DBH}.
TURN 453 456 {ECO:0000244|PDB:1AWE}.
STRAND 459 473 {ECO:0000244|PDB:1DBH}.
HELIX 480 482 {ECO:0000244|PDB:1AWE}.
STRAND 487 496 {ECO:0000244|PDB:1DBH}.
STRAND 500 503 {ECO:0000244|PDB:1DBH}.
STRAND 507 509 {ECO:0000244|PDB:1DBH}.
STRAND 512 516 {ECO:0000244|PDB:1DBH}.
TURN 519 521 {ECO:0000244|PDB:1AWE}.
STRAND 524 527 {ECO:0000244|PDB:1DBH}.
HELIX 531 545 {ECO:0000244|PDB:1DBH}.
TURN 546 549 {ECO:0000244|PDB:1DBH}.
TURN 572 574 {ECO:0000244|PDB:2II0}.
HELIX 576 578 {ECO:0000244|PDB:2II0}.
TURN 583 585 {ECO:0000244|PDB:2II0}.
STRAND 586 588 {ECO:0000244|PDB:2II0}.
STRAND 590 592 {ECO:0000244|PDB:3KSY}.
TURN 594 596 {ECO:0000244|PDB:4US0}.
STRAND 601 604 {ECO:0000244|PDB:2II0}.
HELIX 606 613 {ECO:0000244|PDB:2II0}.
STRAND 616 618 {ECO:0000244|PDB:2II0}.
HELIX 621 630 {ECO:0000244|PDB:2II0}.
HELIX 631 633 {ECO:0000244|PDB:2II0}.
HELIX 637 648 {ECO:0000244|PDB:2II0}.
HELIX 657 664 {ECO:0000244|PDB:2II0}.
STRAND 665 667 {ECO:0000244|PDB:3KSY}.
HELIX 672 680 {ECO:0000244|PDB:2II0}.
HELIX 682 699 {ECO:0000244|PDB:2II0}.
HELIX 702 706 {ECO:0000244|PDB:2II0}.
HELIX 708 718 {ECO:0000244|PDB:2II0}.
TURN 724 726 {ECO:0000244|PDB:2II0}.
HELIX 727 742 {ECO:0000244|PDB:2II0}.
STRAND 764 766 {ECO:0000244|PDB:4US0}.
HELIX 771 773 {ECO:0000244|PDB:2II0}.
TURN 776 778 {ECO:0000244|PDB:2II0}.
HELIX 781 798 {ECO:0000244|PDB:2II0}.
HELIX 801 803 {ECO:0000244|PDB:2II0}.
HELIX 805 810 {ECO:0000244|PDB:2II0}.
HELIX 814 817 {ECO:0000244|PDB:2II0}.
HELIX 819 840 {ECO:0000244|PDB:2II0}.
HELIX 845 864 {ECO:0000244|PDB:2II0}.
HELIX 868 878 {ECO:0000244|PDB:2II0}.
HELIX 881 884 {ECO:0000244|PDB:2II0}.
HELIX 887 892 {ECO:0000244|PDB:2II0}.
HELIX 895 920 {ECO:0000244|PDB:2II0}.
HELIX 931 942 {ECO:0000244|PDB:2II0}.
STRAND 946 950 {ECO:0000244|PDB:2II0}.
STRAND 953 957 {ECO:0000244|PDB:2II0}.
HELIX 958 971 {ECO:0000244|PDB:2II0}.
HELIX 972 974 {ECO:0000244|PDB:2II0}.
HELIX 985 992 {ECO:0000244|PDB:2II0}.
TURN 996 999 {ECO:0000244|PDB:2II0}.
HELIX 1002 1016 {ECO:0000244|PDB:2II0}.
STRAND 1020 1022 {ECO:0000244|PDB:3KSY}.
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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