SOS2_MOUSE
ID SOS2_MOUSE Reviewed; 1333 AA.
AC Q02384;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Son of sevenless homolog 2;
DE Short=SOS-2;
DE Short=mSOS-2;
GN Name=Sos2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-1333.
RC STRAIN=SWR/J; TISSUE=Eye;
RX PubMed=1631150; DOI=10.1073/pnas.89.14.6511;
RA Bowtell D.D., Fu P., Simon M.A., Senior P.V.;
RT "Identification of murine homologues of the Drosophila son of sevenless
RT gene: potential activators of ras.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6511-6515(1992).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1322, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP.
CC {ECO:0000250|UniProtKB:Q62245}.
CC -!- INTERACTION:
CC Q02384; Q8CBW3: Abi1; NbExp=2; IntAct=EBI-395573, EBI-375511;
CC Q02384; Q60631: Grb2; NbExp=5; IntAct=EBI-395573, EBI-1688;
CC -!- TISSUE SPECIFICITY: Expressed in most embryonic and adult tissues.
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DR EMBL; AC133949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z11664; CAA77732.1; -; mRNA.
DR PIR; S25714; S25714.
DR RefSeq; XP_006515698.1; XM_006515635.1.
DR PDB; 1GBR; NMR; -; B=1300-1314.
DR PDBsum; 1GBR; -.
DR AlphaFoldDB; Q02384; -.
DR SMR; Q02384; -.
DR BioGRID; 203395; 5.
DR IntAct; Q02384; 5.
DR STRING; 10090.ENSMUSP00000138793; -.
DR iPTMnet; Q02384; -.
DR PhosphoSitePlus; Q02384; -.
DR MaxQB; Q02384; -.
DR PaxDb; Q02384; -.
DR PeptideAtlas; Q02384; -.
DR PRIDE; Q02384; -.
DR ProteomicsDB; 261476; -.
DR Antibodypedia; 3885; 165 antibodies from 28 providers.
DR DNASU; 20663; -.
DR Ensembl; ENSMUST00000183277; ENSMUSP00000138793; ENSMUSG00000034801.
DR GeneID; 20663; -.
DR CTD; 6655; -.
DR MGI; MGI:98355; Sos2.
DR VEuPathDB; HostDB:ENSMUSG00000034801; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000158324; -.
DR HOGENOM; CLU_002744_0_0_1; -.
DR InParanoid; Q02384; -.
DR OrthoDB; 576110at2759; -.
DR PhylomeDB; Q02384; -.
DR TreeFam; TF317296; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 20663; 1 hit in 68 CRISPR screens.
DR ChiTaRS; Sos2; mouse.
DR EvolutionaryTrace; Q02384; -.
DR PRO; PR:Q02384; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q02384; protein.
DR Bgee; ENSMUSG00000034801; Expressed in saccule of membranous labyrinth and 253 other tissues.
DR ExpressionAtlas; Q02384; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0001782; P:B cell homeostasis; IGI:MGI.
DR GO; GO:0002260; P:lymphocyte homeostasis; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:2000973; P:regulation of pro-B cell differentiation; IGI:MGI.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IGI:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; IGI:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd00160; RhoGEF; 1.
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; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
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; PTHR23113; 1.
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; Guanine-nucleotide releasing factor; Methylation;
KW Reference proteome.
FT CHAIN 1..1333
FT /note="Son of sevenless homolog 2"
FT /id="PRO_0000068897"
FT DOMAIN 199..389
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 443..546
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 596..740
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 779..1018
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 1019..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1322
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 358
FT /note="Missing (in Ref. 2; CAA77732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1333 AA; 153127 MW; 5F687E3CFFCF7F1B CRC64;
MQQAPQPYEF FSEENSPKWR GLLVPALRKV QEQVHPTLSA NEESLYYIEE LIFQLLNKLC
MAQPRTVQDV EERVQKTFPH PIDKWAIADA QSAIEKRKRR NPLLLPVDKI HPSLKEVLGY
KVDYHVSLYI VAVLEYISAD ILKLAGNYVF NIRHYEISQQ DIKVSMCADK VLMDMFDQDD
DIGLVSLCED EPCSSGELNY YDLVRTEIAE ERQYLRELNM IIKVFREAFL LDRKLFKPSE
IEKIFSNISD IHELTVKLLG LIEDTVEMTD ESSPHPLAGS CFEDLAEEQA FDPYETLSQD
ILAPEFNDHF SKLMARPAVA LHFQSIADGF KEAVRYVLPR LMLVPVYHCW HYFELLKQLK
ACSEEQEDKE CLNQAITALM NLQGSMDRIY KQHSPRRRPG DPVCLFYNRQ LRSKHLAIKK
MNEIQKNIDG WEGKDIGQCC NEFIMEGPLT RIGAKHERHI FLFDGLMISC KPNHGQTRLP
GYSSAEYRLK EKFVMRKIQI CDKEDACEYR HAFELVSKDE NSVIFAAKSA EEKNNWMAAL
ISLHYRSTLD RMLDSVLLKE ENEQPLRLPS PDMYRFVVTD SEENIVFEDN LQSRSGIPII
KGGTVVKLIE RLTYHMYADP NFVRTFLTTY RSFCKPQELL NLLIERFEIP EPEPTEADKL
ALEKGEQPIS ADLKRFRKEY VQPVQLRVLN VFRHWVEHHY YDFERDLELL ERLESFISSV
RGKAMKKWVE SIAKIIKRKK QAQANGISHN ITFESSPPPV EWHISRTGQF ETFDLMTLHP
IEIARQLTLL ESDLYRKVQP SELVGSVWTK EDKEINSPNL LKMIRHTTNL TLWFEKCIVE
AENFEERVAV LSRIVEILQV FQDLNNFNGV LEIVSAVNSV SVYRLDHTFE ALQERKRRIL
DDAVELSQDH FKKYLVKLKS INPPCVPFFG IYLTNILKTE EGNSDFLKRK GKDLINFSKR
RKVAEITGEI QQYQNQPYCL RTEPEMRRFF ENLNPMGILS EKEFTDYLFN KSLEIEPRNC
KQPPRFPRKS TFSLKSPGIR PNAGRHGSTS GTLRGHPTPL EREPYKISFS RIAETELEST
VSAPTSPNTP STPPVSASSD HSVFLDVDLN SSCGSNTIFA PVLLPHSKTF FSSCGSLHKL
SEEPLIPPPL PPRKKFDHDA LNSKGAVKSD DDPPAIPPRQ PPPPKVKPRV PVLMGTFDGP
VPSPPPPPPR DPLPDTPPPV PLRPPEHFIN CPFNLQPPPL GHPHRDPDWL RDVSTCPNSP
STPPTTPSPR IPRSCHLLSS SHSSLAHLPA PPVPPRQNSS PLLPKLPPKT YKRELSHPPL
YRLPLLENAE TPQ
