GenomeNet

Database: UniProt
Entry: Q07889
LinkDB: Q07889
Original site: Q07889 
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   26-NOV-2014, entry version 165.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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
RT   to 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION IN A COMPLEX WITH MUC1 AND GRB2, AND INTERACTION WITH
RP   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-
RT   containing adapter protein having similar binding and biological
RT   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.,
RA   Spicka J., Hilgert I., Luskova P., Draber P., Novak P., Engels N.,
RA   Wienands J., Simeoni L., Oesterreicher J., Aguado E., Malissen M.,
RA   Schraven B., 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   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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
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.,
RA   Buerckstuemmer T., 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   [11]
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
RT   SOS1. A possible structural role for the sequential association of
RT   diffuse B cell lymphoma and pleckstrin homology domains.";
RL   J. Biol. Chem. 272:30340-30344(1997).
RN   [12]
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   [13]
RP   INVOLVEMENT IN GGF1, 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
RT   type 1.";
RL   Am. J. Hum. Genet. 70:943-954(2002).
RN   [14]
RP   VARIANTS NS4 LYS-266; ARG-269; TYR-309; CYS-337; ARG-434; ARG-548;
RP   GLY-552 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.,
RA   Kucherlapati R.S.;
RT   "Germline gain-of-function mutations in SOS1 cause Noonan syndrome.";
RL   Nat. Genet. 39:70-74(2007).
RN   [15]
RP   VARIANTS NS4 LYS-108; ARG-269; ARG-432; LYS-433; TYR-441; ARG-548;
RP   PRO-550; GLY-552; LYS-552; SER-552; HIS-702; LEU-729; PHE-733 AND
RP   LYS-846, VARIANTS LEU-655; ARG-977 AND ARG-1320, AND CHARACTERIZATION
RP   OF VARIANTS NS4 GLY-552 AND LEU-729.
RX   PubMed=17143282; DOI=10.1038/ng1939;
RA   Tartaglia M., Pennacchio L.A., Zhao C., Yadav K.K., Fodale V.,
RA   Sarkozy A., Pandit B., Oishi K., Martinelli S., Schackwitz W.,
RA   Ustaszewska A., Martin J., Bristow J., Carta C., Lepri F., Neri C.,
RA   Vasta I., Gibson K., Curry C.J., Lopez Siguero J.P., Digilio M.C.,
RA   Zampino G., Dallapiccola B., 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   [16]
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   [17]
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   [18]
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
RT   SOS1 and a de novo RAF1 mutations.";
RL   Am. J. Med. Genet. A 152:2176-2184(2010).
RN   [19]
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
RT   gastroenteral involvement and the SOS1 mutation F623I.";
RL   Eur. J. Med. Genet. 53:322-324(2010).
RN   [20]
RP   VARIANTS NS4 ARG-102; GLU-170; LYS-266; THR-269; LYS-433 AND GLY-552,
RP   AND VARIANTS ALA-378; 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.,
RA   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   [21]
RP   VARIANTS NS4 LYS-108; ARG-112; GLU-170; THR-252; LYS-266; THR-269;
RP   ARG-269; VAL-422; LYS-424; 427-LYS--ASP-430 DELINS ASN; ARG-432;
RP   432-TRP-GLU-433 DEL; LYS-433; ARG-434; LYS-434; THR-437; TYR-441;
RP   ARG-477; ARG-478; ARG-482; ARG-490; GLN-497; ARG-548; LYS-549;
RP   GLY-552; LYS-552; MET-552; THR-552; SER-552; 554-LEU--MET-558 DELINS
RP   LYS; PHE-733; LYS-846 AND ARG-894, AND VARIANTS ALA-37; LEU-478;
RP   VAL-569; LEU-655; THR-708; THR-784; SER-1011; LYS-1131; ILE-1140;
RP   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.,
RA   Pantaleoni F., Cordeddu V., Williams B.J., Dentici M.L., Caputo V.,
RA   Venanzi S., Bonaguro M., Kavamura I., Faienza M.F., Pilotta A.,
RA   Stanzial F., Faravelli F., Gabrielli O., Marino B., Neri G.,
RA   Silengo M.C., Ferrero G.B., Torrrente I., Selicorni A., Mazzanti L.,
RA   Digilio M.C., Zampino G., Dallapiccola B., Gelb B.D., Tartaglia M.;
RT   "SOS1 mutations in Noonan syndrome: molecular spectrum, structural
RT   insights 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. Catalytic
CC       component of a trimeric complex that participates in transduction
CC       of signals from Ras to Rac by promoting the Rac-specific guanine
CC       nucleotide exchange factor (GEF) activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of a complex consisting of ABI1, EPS8 and SOS1 (By
CC       similarity). Interacts with GRB2. Forms a complex with
CC       phosphorylated MUC1 and GRB2 (via its SH3 domains). Interacts with
CC       phosphorylated LAT2. Interacts with NCK1 and NCK2. {ECO:0000250,
CC       ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:12486104,
CC       ECO:0000269|PubMed:7664271}.
CC   -!- INTERACTION:
CC       Q5TCZ1-2:-; NbExp=5; IntAct=EBI-297487, EBI-7014859;
CC       P46108:CRK; NbExp=3; IntAct=EBI-297487, EBI-886;
CC       P46109:CRKL; NbExp=2; IntAct=EBI-297487, EBI-910;
CC       P62993:GRB2; NbExp=22; IntAct=EBI-297487, EBI-401755;
CC       P08631:HCK; NbExp=4; IntAct=EBI-297487, EBI-346340;
CC       P01112:HRAS; NbExp=8; IntAct=EBI-297487, EBI-350145;
CC       P16333:NCK1; NbExp=5; IntAct=EBI-297487, EBI-389883;
CC       P20929:NEB; NbExp=3; IntAct=EBI-297487, EBI-1049657;
CC       Q9UKS6:PACSIN3; NbExp=2; IntAct=EBI-297487, EBI-77926;
CC       P27986:PIK3R1; NbExp=3; IntAct=EBI-297487, EBI-79464;
CC       P19174:PLCG1; NbExp=3; IntAct=EBI-297487, EBI-79387;
CC       P29353:SHC1; NbExp=2; IntAct=EBI-297487, EBI-78835;
CC       Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-297487, EBI-77848;
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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in gingival tissues.
CC       {ECO:0000269|PubMed:11868160}.
CC   -!- DISEASE: Gingival fibromatosis 1 (GGF1) [MIM:135300]: Gingival
CC       fibromatosis is a rare overgrowth condition characterized by a
CC       benign, slowly progressive, nonhemorrhagic, fibrous enlargement of
CC       maxillary and mandibular keratinized gingiva. GGF1 is usually
CC       transmitted as an autosomal dominant trait, although sporadic
CC       cases are common. {ECO:0000269|PubMed:11868160}. Note=The disease
CC       is caused by mutations 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
CC       dysmorphic features such as hypertelorism, a downward eyeslant and
CC       low-set posteriorly rotated ears, and a high incidence of
CC       congenital heart defects and hypertrophic cardiomyopathy. Other
CC       features can include a short neck with webbing or redundancy of
CC       skin, deafness, motor delay, variable intellectual deficits,
CC       multiple skeletal defects, cryptorchidism, and bleeding diathesis.
CC       Individuals with Noonan syndrome are at risk of juvenile
CC       myelomonocytic leukemia, a myeloproliferative disorder
CC       characterized by excessive production of myelomonocytic cells.
CC       Some patients with NS4 have polyarticular villonodular synovitis.
CC       {ECO:0000269|PubMed:17143282, ECO:0000269|PubMed:17143285,
CC       ECO:0000269|PubMed:19020799, ECO:0000269|PubMed:19438935,
CC       ECO:0000269|PubMed:19953625, ECO:0000269|PubMed:20673819,
CC       ECO:0000269|PubMed:20683980, ECO:0000269|PubMed:21387466}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00062}.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00135}.
CC   -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00145}.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00168}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Son of sevenless entry;
CC       URL="http://en.wikipedia.org/wiki/Son_of_Sevenless";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs 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   UniGene; Hs.709893; -.
DR   UniGene; Hs.732497; -.
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   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   ProteinModelPortal; Q07889; -.
DR   SMR; Q07889; 6-183, 198-1046.
DR   BioGrid; 112537; 47.
DR   DIP; DIP-31802N; -.
DR   IntAct; Q07889; 31.
DR   MINT; MINT-106583; -.
DR   STRING; 9606.ENSP00000384675; -.
DR   BindingDB; Q07889; -.
DR   ChEMBL; CHEMBL2079846; -.
DR   PhosphoSite; Q07889; -.
DR   DMDM; 6094322; -.
DR   MaxQB; Q07889; -.
DR   PaxDb; Q07889; -.
DR   PRIDE; Q07889; -.
DR   DNASU; 6654; -.
DR   Ensembl; ENST00000402219; ENSP00000384675; ENSG00000115904. [Q07889-1]
DR   Ensembl; ENST00000426016; ENSP00000387784; ENSG00000115904. [Q07889-1]
DR   GeneID; 6654; -.
DR   KEGG; hsa:6654; -.
DR   UCSC; uc002rrk.4; human. [Q07889-1]
DR   CTD; 6654; -.
DR   GeneCards; GC02M039208; -.
DR   GeneReviews; SOS1; -.
DR   HGNC; HGNC:11187; SOS1.
DR   HPA; CAB005396; -.
DR   HPA; HPA012613; -.
DR   MIM; 135300; phenotype.
DR   MIM; 182530; gene.
DR   MIM; 610733; phenotype.
DR   neXtProt; NX_Q07889; -.
DR   Orphanet; 2024; Hereditary gingival fibromatosis.
DR   Orphanet; 648; Noonan syndrome.
DR   PharmGKB; PA36024; -.
DR   eggNOG; NOG265981; -.
DR   GeneTree; ENSGT00770000120448; -.
DR   HOGENOM; HOG000013040; -.
DR   HOVERGEN; HBG017831; -.
DR   InParanoid; Q07889; -.
DR   KO; K03099; -.
DR   OMA; SVFDSDH; -.
DR   OrthoDB; EOG7XSTD0; -.
DR   PhylomeDB; Q07889; -.
DR   TreeFam; TF317296; -.
DR   Reactome; REACT_11051; Rho GTPase cycle.
DR   Reactome; REACT_111040; Signaling by SCF-KIT.
DR   Reactome; REACT_111225; Regulation of KIT signaling.
DR   Reactome; REACT_115852; Signaling by constitutively active EGFR.
DR   Reactome; REACT_115854; GRB2 events in ERBB2 signaling.
DR   Reactome; REACT_115993; SHC1 events in ERBB2 signaling.
DR   Reactome; REACT_116005; SHC1 events in ERBB4 signaling.
DR   Reactome; REACT_118700; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   Reactome; REACT_12033; Signalling to RAS.
DR   Reactome; REACT_121096; EGFR Transactivation by Gastrin.
DR   Reactome; REACT_121398; Signaling by FGFR mutants.
DR   Reactome; REACT_12579; SHC1 events in EGFR signaling.
DR   Reactome; REACT_12606; GRB2 events in EGFR signaling.
DR   Reactome; REACT_12621; Tie2 Signaling.
DR   Reactome; REACT_13638; NRAGE signals death through JNK.
DR   Reactome; REACT_147814; DAP12 signaling.
DR   Reactome; REACT_163701; FCERI mediated MAPK activation.
DR   Reactome; REACT_163769; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; REACT_163834; FCERI mediated Ca+2 mobilization.
DR   Reactome; REACT_17025; Downstream signal transduction.
DR   Reactome; REACT_18334; NCAM signaling for neurite out-growth.
DR   Reactome; REACT_18407; G alpha (12/13) signalling events.
DR   Reactome; REACT_19226; Activation of Rac.
DR   Reactome; REACT_21247; FRS2-mediated cascade.
DR   Reactome; REACT_21374; SHC-mediated cascade.
DR   Reactome; REACT_23891; Interleukin receptor SHC signaling.
DR   Reactome; REACT_508; Signal attenuation.
DR   Reactome; REACT_524; SOS-mediated signalling.
DR   Reactome; REACT_661; SHC-mediated signalling.
DR   SignaLink; Q07889; -.
DR   ChiTaRS; SOS1; human.
DR   EvolutionaryTrace; Q07889; -.
DR   GeneWiki; SOS1; -.
DR   GenomeRNAi; 6654; -.
DR   NextBio; 25939; -.
DR   PRO; PR:Q07889; -.
DR   Bgee; Q07889; -.
DR   CleanEx; HS_SOS1; -.
DR   ExpressionAtlas; Q07889; baseline and differential.
DR   Genevestigator; Q07889; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR   GO; GO:0005100; F:Rho GTPase activator activity; TAS:ProtInc.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:ProtInc.
DR   GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032320; P:positive regulation of Ras GTPase activity; EXP:GOC.
DR   GO; GO:0032321; P:positive regulation of Rho GTPase activity; TAS:GOC.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   Gene3D; 1.10.20.10; -; 1.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   Pfam; PF00125; Histone; 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; SSF47113; SSF47113; 1.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Disease mutation; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Polymorphism; Reference proteome.
FT   CHAIN         1   1333       Son of sevenless homolog 1.
FT                                /FTId=PRO_0000068894.
FT   DOMAIN      200    390       DH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00062}.
FT   DOMAIN      444    548       PH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00145}.
FT   DOMAIN      597    741       N-terminal Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00135}.
FT   DOMAIN      780   1019       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   COMPBIAS   1258   1261       Poly-Pro.
FT   MOD_RES    1043   1043       Phosphoserine.
FT   MOD_RES    1078   1078       Phosphoserine. {ECO:0000250}.
FT   MOD_RES    1082   1082       Phosphoserine. {ECO:0000250}.
FT   VAR_SEQ       1     57       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056463.
FT   VAR_SEQ     359    371       QLEEKSEDQEDKE -> FPFGDLSRLRDSV (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056464.
FT   VAR_SEQ     372   1333       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056465.
FT   VARIANT      37     37       T -> A (in a patient with Noonan
FT                                syndrome; dbSNP:rs150565592).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066031.
FT   VARIANT     102    102       P -> R (in NS4).
FT                                {ECO:0000269|PubMed:19953625}.
FT                                /FTId=VAR_066032.
FT   VARIANT     108    108       E -> K (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030423.
FT   VARIANT     112    112       P -> R (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066033.
FT   VARIANT     170    170       K -> E (in NS4).
FT                                {ECO:0000269|PubMed:19020799,
FT                                ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066034.
FT   VARIANT     252    252       I -> T (in NS4; dbSNP:rs142094234).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066035.
FT   VARIANT     266    266       T -> K (in NS4; dbSNP:rs137852812).
FT                                {ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030424.
FT   VARIANT     269    269       M -> R (in NS4; dbSNP:rs137852813).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030425.
FT   VARIANT     269    269       M -> T (in NS4).
FT                                {ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:20683980,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_064504.
FT   VARIANT     309    309       D -> Y (in NS4).
FT                                {ECO:0000269|PubMed:17143285}.
FT                                /FTId=VAR_030426.
FT   VARIANT     337    337       Y -> C (in NS4).
FT                                {ECO:0000269|PubMed:17143285}.
FT                                /FTId=VAR_030427.
FT   VARIANT     378    378       T -> A (in a patient with Noonan
FT                                syndrome). {ECO:0000269|PubMed:19953625}.
FT                                /FTId=VAR_066036.
FT   VARIANT     422    422       M -> V (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066037.
FT   VARIANT     424    424       E -> K (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066038.
FT   VARIANT     427    430       KNID -> N (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066039.
FT   VARIANT     432    433       Missing (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066040.
FT   VARIANT     432    432       W -> R (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:19438935,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030428.
FT   VARIANT     433    433       E -> K (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030429.
FT   VARIANT     434    434       G -> K (in NS4; requires 2 nucleotide
FT                                substitutions).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066041.
FT   VARIANT     434    434       G -> R (in NS4).
FT                                {ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030430.
FT   VARIANT     437    437       I -> T (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066042.
FT   VARIANT     441    441       C -> Y (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030431.
FT   VARIANT     477    477       Q -> R (in NS4).
FT                                {ECO:0000269|PubMed:20683980,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_064505.
FT   VARIANT     478    478       P -> L (found in patients with Noonan
FT                                syndrome). {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066043.
FT   VARIANT     478    478       P -> R (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066044.
FT   VARIANT     482    482       G -> R (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066045.
FT   VARIANT     490    490       L -> R (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066046.
FT   VARIANT     497    497       R -> Q (in NS4; one patient with Noonan
FT                                syndrome also carries a likely pathogenic
FT                                mutation Ser-261 in RAF1; the mutant
FT                                protein cannot induce ERK1
FT                                phosphorylation).
FT                                {ECO:0000269|PubMed:20683980,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_064506.
FT   VARIANT     548    548       S -> R (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030432.
FT   VARIANT     549    549       T -> K (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066047.
FT   VARIANT     550    550       L -> P (in NS4).
FT                                {ECO:0000269|PubMed:17143282}.
FT                                /FTId=VAR_030433.
FT   VARIANT     552    552       R -> G (in NS4; increases the basal level
FT                                of active RAS; prolonges RAS activation
FT                                after EGF stimulation and enhances ERK
FT                                activation; dbSNP:rs137852814).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030434.
FT   VARIANT     552    552       R -> K (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030435.
FT   VARIANT     552    552       R -> M (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066048.
FT   VARIANT     552    552       R -> S (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030436.
FT   VARIANT     552    552       R -> T (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066049.
FT   VARIANT     554    558       LDVTM -> K (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066050.
FT   VARIANT     569    569       L -> V. {ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066051.
FT   VARIANT     623    623       F -> I (in NS4).
FT                                {ECO:0000269|PubMed:20673819}.
FT                                /FTId=VAR_066052.
FT   VARIANT     655    655       P -> L (in dbSNP:rs56219475).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:19953625,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030437.
FT   VARIANT     702    702       Y -> H (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:20683980}.
FT                                /FTId=VAR_030438.
FT   VARIANT     708    708       A -> T (in dbSNP:rs140811086).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066053.
FT   VARIANT     729    729       W -> L (in NS4; promotes constitutive RAS
FT                                activation and enhances ERK activation).
FT                                {ECO:0000269|PubMed:17143282}.
FT                                /FTId=VAR_030439.
FT   VARIANT     733    733       I -> F (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030440.
FT   VARIANT     784    784       I -> T (in a patient with Noonan
FT                                syndrome). {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066054.
FT   VARIANT     846    846       E -> K (in NS4).
FT                                {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:17143285,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030441.
FT   VARIANT     894    894       P -> R (in NS4).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066055.
FT   VARIANT     977    977       Q -> R. {ECO:0000269|PubMed:17143282}.
FT                                /FTId=VAR_030442.
FT   VARIANT    1011   1011       N -> S (in dbSNP:rs8192671).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066056.
FT   VARIANT    1131   1131       R -> K (in a patient with Noonan
FT                                syndrome; dbSNP:rs141676532).
FT                                {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066057.
FT   VARIANT    1140   1140       L -> I (in a patient with Noonan
FT                                syndrome). {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066058.
FT   VARIANT    1257   1257       T -> A (in a patient with Noonan
FT                                syndrome). {ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_066059.
FT   VARIANT    1320   1320       H -> R. {ECO:0000269|PubMed:17143282,
FT                                ECO:0000269|PubMed:21387466}.
FT                                /FTId=VAR_030443.
FT   TURN         13     15       {ECO:0000244|PDB:1Q9C}.
FT   STRAND       19     23       {ECO:0000244|PDB:3KSY}.
FT   HELIX        24     34       {ECO:0000244|PDB:3KSY}.
FT   STRAND       36     39       {ECO:0000244|PDB:1Q9C}.
FT   HELIX        42     61       {ECO:0000244|PDB:3KSY}.
FT   HELIX        67     77       {ECO:0000244|PDB:3KSY}.
FT   HELIX        82     94       {ECO:0000244|PDB:3KSY}.
FT   STRAND      100    102       {ECO:0000244|PDB:3KSY}.
FT   HELIX       107    118       {ECO:0000244|PDB:3KSY}.
FT   HELIX       124    151       {ECO:0000244|PDB:3KSY}.
FT   HELIX       159    168       {ECO:0000244|PDB:3KSY}.
FT   HELIX       172    175       {ECO:0000244|PDB:3KSY}.
FT   HELIX       201    224       {ECO:0000244|PDB:1DBH}.
FT   TURN        225    227       {ECO:0000244|PDB:1DBH}.
FT   HELIX       228    232       {ECO:0000244|PDB:1DBH}.
FT   TURN        234    236       {ECO:0000244|PDB:1DBH}.
FT   HELIX       239    246       {ECO:0000244|PDB:1DBH}.
FT   HELIX       249    268       {ECO:0000244|PDB:1DBH}.
FT   STRAND      274    276       {ECO:0000244|PDB:1DBH}.
FT   HELIX       280    288       {ECO:0000244|PDB:1DBH}.
FT   TURN        289    292       {ECO:0000244|PDB:1DBH}.
FT   HELIX       293    302       {ECO:0000244|PDB:1DBH}.
FT   HELIX       307    316       {ECO:0000244|PDB:1DBH}.
FT   HELIX       320    327       {ECO:0000244|PDB:1DBH}.
FT   HELIX       331    337       {ECO:0000244|PDB:1DBH}.
FT   HELIX       339    342       {ECO:0000244|PDB:1DBH}.
FT   HELIX       345    363       {ECO:0000244|PDB:1DBH}.
FT   HELIX       367    379       {ECO:0000244|PDB:1DBH}.
FT   HELIX       381    392       {ECO:0000244|PDB:1DBH}.
FT   HELIX       394    402       {ECO:0000244|PDB:1DBH}.
FT   HELIX       420    426       {ECO:0000244|PDB:1DBH}.
FT   STRAND      429    431       {ECO:0000244|PDB:1DBH}.
FT   HELIX       437    439       {ECO:0000244|PDB:1DBH}.
FT   STRAND      444    452       {ECO:0000244|PDB:1DBH}.
FT   TURN        453    456       {ECO:0000244|PDB:1AWE}.
FT   STRAND      459    473       {ECO:0000244|PDB:1DBH}.
FT   HELIX       480    482       {ECO:0000244|PDB:1AWE}.
FT   STRAND      487    496       {ECO:0000244|PDB:1DBH}.
FT   STRAND      500    503       {ECO:0000244|PDB:1DBH}.
FT   STRAND      507    509       {ECO:0000244|PDB:1DBH}.
FT   STRAND      512    516       {ECO:0000244|PDB:1DBH}.
FT   TURN        519    521       {ECO:0000244|PDB:1AWE}.
FT   STRAND      524    527       {ECO:0000244|PDB:1DBH}.
FT   HELIX       531    545       {ECO:0000244|PDB:1DBH}.
FT   TURN        546    549       {ECO:0000244|PDB:1DBH}.
FT   TURN        572    574       {ECO:0000244|PDB:1NVV}.
FT   HELIX       576    578       {ECO:0000244|PDB:1NVV}.
FT   TURN        583    585       {ECO:0000244|PDB:1NVV}.
FT   STRAND      586    588       {ECO:0000244|PDB:1NVV}.
FT   STRAND      590    592       {ECO:0000244|PDB:3KSY}.
FT   STRAND      601    604       {ECO:0000244|PDB:1NVV}.
FT   HELIX       606    613       {ECO:0000244|PDB:1NVV}.
FT   STRAND      616    618       {ECO:0000244|PDB:1NVX}.
FT   HELIX       621    630       {ECO:0000244|PDB:1NVV}.
FT   HELIX       631    633       {ECO:0000244|PDB:1NVV}.
FT   HELIX       637    648       {ECO:0000244|PDB:1NVV}.
FT   HELIX       657    663       {ECO:0000244|PDB:1NVV}.
FT   TURN        664    666       {ECO:0000244|PDB:1NVV}.
FT   HELIX       672    680       {ECO:0000244|PDB:1NVV}.
FT   HELIX       682    699       {ECO:0000244|PDB:1NVV}.
FT   HELIX       702    706       {ECO:0000244|PDB:1NVV}.
FT   HELIX       708    720       {ECO:0000244|PDB:1NVV}.
FT   HELIX       724    742       {ECO:0000244|PDB:1NVV}.
FT   STRAND      764    766       {ECO:0000244|PDB:1NVX}.
FT   HELIX       771    773       {ECO:0000244|PDB:1NVV}.
FT   TURN        776    778       {ECO:0000244|PDB:1NVV}.
FT   HELIX       781    797       {ECO:0000244|PDB:1NVV}.
FT   HELIX       801    803       {ECO:0000244|PDB:1NVV}.
FT   HELIX       805    810       {ECO:0000244|PDB:1NVV}.
FT   HELIX       814    817       {ECO:0000244|PDB:1NVV}.
FT   HELIX       819    840       {ECO:0000244|PDB:1NVV}.
FT   HELIX       845    864       {ECO:0000244|PDB:1NVV}.
FT   HELIX       868    878       {ECO:0000244|PDB:1NVV}.
FT   HELIX       881    884       {ECO:0000244|PDB:1NVV}.
FT   HELIX       887    891       {ECO:0000244|PDB:1NVV}.
FT   HELIX       895    921       {ECO:0000244|PDB:1NVV}.
FT   HELIX       931    942       {ECO:0000244|PDB:1NVV}.
FT   STRAND      946    950       {ECO:0000244|PDB:1NVV}.
FT   STRAND      953    957       {ECO:0000244|PDB:1NVV}.
FT   HELIX       958    973       {ECO:0000244|PDB:1NVV}.
FT   HELIX       985    992       {ECO:0000244|PDB:1NVV}.
FT   TURN        996    999       {ECO:0000244|PDB:1NVV}.
FT   HELIX      1002   1016       {ECO:0000244|PDB:1NVV}.
FT   STRAND     1020   1022       {ECO:0000244|PDB:3KSY}.
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
//
DBGET integrated database retrieval system