dbPTM

SOS1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SOS1_MOUSE
UniProt AC	Q62245
Protein Name	Son of sevenless homolog 1
Gene Name	Sos1
Organism	Mus musculus (Mouse).
Sequence Length	1319
Subcellular Localization
Protein Description	Promotes the exchange of Ras-bound GDP by GTP. Probably by promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3 in response to EGF (By similarity). 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. [PubMed: 10499589]
Protein Sequence	MQAQQLPYEFFSEENAPKWRGLLVPALKKVQGQVHPTLESNDDALQYVEELILQLLNMLCQAQPRSASDVEERVQKSFPHPIDKWAIADAQSAIEKRKRRNPLSLPAERIHHLLREVLGYKIDHQVSVYIVAVLEYISADILKLVGNYVRNIRHYEITKQDIKVAMCADKVLMDMFHQDVEDINILSLTDEEPSTSGEQTYYDLVKAFMAEIRQYIRELNLIIKVFREPFVSNSKLFSSNDVENIFSRIVDIHELSVKLLGHIEDTVEMTDEGSPHPLVGSCFEDLAEELAFDPYESYARDILRPGFHGHFLSQLSKPGAALYLQSIGEGFKEAVQYVLPRLLLAPVYHCLHYFELLKQLEEKSEDQEDKECMKQAITALLNVQSGMEKICSKSLAKRRLSESACRFYSQQMKGKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASSAEYRLKEKFFMRKVQINDKDDTSEYKHAFEIILKDGNSVIFSAKSAEEKNNWMAALISLQYRSTLERMLDVTVLQEEKEEQMRLPSAEVYRFAEPDSEENILFEENVQPKAGIPIIKAGTVLKLIERLTYHMYADPNFVRTFLTTYRSFCRPQELLSLLIERFEIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLNVCRHWVEHHFYDFERDADLLQRMEEFIGTVRGKAMKKWVESITKIIQRKKIARDNGPGHNITFQSSPPTVEWHISRPGHIETFDLLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNILKTEEGNPEVLRRHGKELINFSKRRRVAEITGEIQQYQNQPYCLRVEPDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIEPRHPKPLPRFPKKYSYPLKSPGVRPSNPRPGTMRHPTPLQQEPRKISYSRIPESETESTASAPNSPRTPLTPPPASGTSSNTDVCSVFDSDHSASPFHSRSASVSSISLSKGTDEVPVPPPVPPRRRPESAPAESSPSKIMSKHLDSPPAIPPRQPTSKAYSPRYSISDRTSISDPPESPPLLPPREPVRTPDVFSSSPLHLQPPPLGKKSDHGNAFFPNSPSPFTPPPPQTPSPHGTRRHLPSPPLTQEMDLHSIAGPPVPPRQSTSQLIPKLPPKTYKREHTHPSMHRDGPPLLENAHSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
238	Phosphorylation	VSNSKLFSSNDVENI CCCCCCCCCHHHHHH	38.37	20531401
239	Phosphorylation	SNSKLFSSNDVENIF CCCCCCCCHHHHHHH	29.70	20531401
401	Phosphorylation	SLAKRRLSESACRFY HHHHHHCCHHHHHHH	27.91	25521595
403	Phosphorylation	AKRRLSESACRFYSQ HHHHCCHHHHHHHHH	29.32	28066266
523	Phosphorylation	IILKDGNSVIFSAKS EEEECCCEEEEECCC	23.32	22817900
527	Phosphorylation	DGNSVIFSAKSAEEK CCCEEEEECCCHHHH	24.54	28285833
530	Phosphorylation	SVIFSAKSAEEKNNW EEEEECCCHHHHCCH	40.40	28285833
582	Phosphorylation	YRFAEPDSEENILFE EECCCCCCHHCCEEE	58.48	30635358
618	Phosphorylation	ERLTYHMYADPNFVR HHHHHHHHCCCHHHH	8.44	22817900
756	Phosphorylation	GHNITFQSSPPTVEW CCCCEECCCCCEEEE	40.39	26060331
757	Phosphorylation	HNITFQSSPPTVEWH CCCEECCCCCEEEEE	24.90	26060331
760	Phosphorylation	TFQSSPPTVEWHISR EECCCCCEEEEEECC	34.15	26060331
1006	Phosphorylation	NSMEKEFTDYLFNKS CHHHHHHHHHHHCCC	25.48	28066266
1008	Phosphorylation	MEKEFTDYLFNKSLE HHHHHHHHHHCCCCC	15.33	28066266
1064	Phosphorylation	QQEPRKISYSRIPES CCCCCCCCCCCCCCC	21.79	30387612
1071	Phosphorylation	SYSRIPESETESTAS CCCCCCCCCCCCCCC	44.45	25619855
1073	Phosphorylation	SRIPESETESTASAP CCCCCCCCCCCCCCC	44.51	25619855
1075	Phosphorylation	IPESETESTASAPNS CCCCCCCCCCCCCCC	36.37	25619855
1076	Phosphorylation	PESETESTASAPNSP CCCCCCCCCCCCCCC	20.57	25619855
1078	Phosphorylation	SETESTASAPNSPRT CCCCCCCCCCCCCCC	44.33	25521595
1082	Phosphorylation	STASAPNSPRTPLTP CCCCCCCCCCCCCCC	18.07	25521595
1085	Phosphorylation	SAPNSPRTPLTPPPA CCCCCCCCCCCCCCC	26.49	26643407
1088	Phosphorylation	NSPRTPLTPPPASGT CCCCCCCCCCCCCCC	34.65	26643407
1093	Phosphorylation	PLTPPPASGTSSNTD CCCCCCCCCCCCCCC	48.67	26643407
1095	Phosphorylation	TPPPASGTSSNTDVC CCCCCCCCCCCCCEE	26.87	26643407
1096	Phosphorylation	PPPASGTSSNTDVCS CCCCCCCCCCCCEEE	25.72	25293948
1097	Phosphorylation	PPASGTSSNTDVCSV CCCCCCCCCCCEEEC	43.52	25293948
1099	Phosphorylation	ASGTSSNTDVCSVFD CCCCCCCCCEEECCC	31.58	25777480
1103	Phosphorylation	SSNTDVCSVFDSDHS CCCCCEEECCCCCCC	26.18	25777480
1107	Phosphorylation	DVCSVFDSDHSASPF CEEECCCCCCCCCCC	26.26	25777480
1110	Phosphorylation	SVFDSDHSASPFHSR ECCCCCCCCCCCCCC	35.12	25777480
1112	Phosphorylation	FDSDHSASPFHSRSA CCCCCCCCCCCCCCC	30.98	25777480
1116	Phosphorylation	HSASPFHSRSASVSS CCCCCCCCCCCCCCE	28.45	25777480
1118	Phosphorylation	ASPFHSRSASVSSIS CCCCCCCCCCCCEEE	28.10	25619855
1120	Phosphorylation	PFHSRSASVSSISLS CCCCCCCCCCEEECC	24.63	25521595
1122	Phosphorylation	HSRSASVSSISLSKG CCCCCCCCEEECCCC	21.32	25521595
1123	Phosphorylation	SRSASVSSISLSKGT CCCCCCCEEECCCCC	17.65	25521595
1125	Phosphorylation	SASVSSISLSKGTDE CCCCCEEECCCCCCC	28.65	25619855
1127	Phosphorylation	SVSSISLSKGTDEVP CCCEEECCCCCCCCC	23.42	25619855
1147	Phosphorylation	PPRRRPESAPAESSP CCCCCCCCCCCCCCH	42.08	25521595
1152	Phosphorylation	PESAPAESSPSKIMS CCCCCCCCCHHHHHH	50.05	25521595
1153	Phosphorylation	ESAPAESSPSKIMSK CCCCCCCCHHHHHHH	25.38	26824392
1155	Phosphorylation	APAESSPSKIMSKHL CCCCCCHHHHHHHCC	36.44	21149613
1164	Phosphorylation	IMSKHLDSPPAIPPR HHHHCCCCCCCCCCC	38.86	26824392
1174	Phosphorylation	AIPPRQPTSKAYSPR CCCCCCCCCCCCCCC	34.22	25338131
1175	Phosphorylation	IPPRQPTSKAYSPRY CCCCCCCCCCCCCCC	23.21	26060331
1179	Phosphorylation	QPTSKAYSPRYSISD CCCCCCCCCCCCCCC	14.04	23684622
1182	Phosphorylation	SKAYSPRYSISDRTS CCCCCCCCCCCCCCC	17.46	-
1183	Phosphorylation	KAYSPRYSISDRTSI CCCCCCCCCCCCCCC	19.52	23684622
1185	Phosphorylation	YSPRYSISDRTSISD CCCCCCCCCCCCCCC	18.33	25338131
1188	Phosphorylation	RYSISDRTSISDPPE CCCCCCCCCCCCCCC	35.09	25777480
1189	Phosphorylation	YSISDRTSISDPPES CCCCCCCCCCCCCCC	22.46	25777480
1191	Phosphorylation	ISDRTSISDPPESPP CCCCCCCCCCCCCCC	43.78	28066266
1196	Phosphorylation	SISDPPESPPLLPPR CCCCCCCCCCCCCCC	37.28	26824392
1208	Phosphorylation	PPREPVRTPDVFSSS CCCCCCCCCCCCCCC	24.87	26060331
1213	Phosphorylation	VRTPDVFSSSPLHLQ CCCCCCCCCCCCCCC	29.74	26643407
1214	Phosphorylation	RTPDVFSSSPLHLQP CCCCCCCCCCCCCCC	25.22	26643407
1215	Phosphorylation	TPDVFSSSPLHLQPP CCCCCCCCCCCCCCC	30.22	26824392
1228	Phosphorylation	PPPLGKKSDHGNAFF CCCCCCCCCCCCCCC	38.02	22817900
1238	Phosphorylation	GNAFFPNSPSPFTPP CCCCCCCCCCCCCCC	27.30	26060331
1240	Phosphorylation	AFFPNSPSPFTPPPP CCCCCCCCCCCCCCC	32.25	22817900
1243	Phosphorylation	PNSPSPFTPPPPQTP CCCCCCCCCCCCCCC	37.97	27742792
1249	Phosphorylation	FTPPPPQTPSPHGTR CCCCCCCCCCCCCCC	31.35	21659605
1251	Phosphorylation	PPPPQTPSPHGTRRH CCCCCCCCCCCCCCC	32.68	26824392
1255	Phosphorylation	QTPSPHGTRRHLPSP CCCCCCCCCCCCCCC	22.84	26824392
1261	Phosphorylation	GTRRHLPSPPLTQEM CCCCCCCCCCCCCCC	45.57	25521595
1265	Phosphorylation	HLPSPPLTQEMDLHS CCCCCCCCCCCCHHH	28.40	21082442
1272	Phosphorylation	TQEMDLHSIAGPPVP CCCCCHHHCCCCCCC	22.79	18846507
1318	Phosphorylation	PLLENAHSS------ CCCCCCCCC------	35.02	25619855
1319	Phosphorylation	LLENAHSS------- CCCCCCCC-------	34.08	25619855

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1120	S	Phosphorylation	Kinase	RPS6KA3	P18654	Uniprot
1147	S	Phosphorylation	Kinase	RPS6KA3	P18654	Uniprot
1182	Y	Phosphorylation	Kinase	ABL1	P00519	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
1120	S	Phosphorylation	-
Phosphorylation at Ser-1120 and Ser-1147 by RPS6KA3 create YWHAB and YWHAE binding sites and which contribute to the negative regulation of EGF-induced MAPK1/3 phosphorylation.
1147	S	Phosphorylation	-
Phosphorylation at Ser-1120 and Ser-1147 by RPS6KA3 create YWHAB and YWHAE binding sites and which contribute to the negative regulation of EGF-induced MAPK1/3 phosphorylation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SOS1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPY1_MOUSE	Spry1	physical	11585837
SPY2_MOUSE	Spry2	physical	11585837
SPY2_MOUSE	Spry2	physical	16339969
SPY4_MOUSE	Spry4	physical	16339969
GRB2_MOUSE	Grb2	physical	10373493

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SOS1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1078 AND SER-1082, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082, AND MASSSPECTROMETRY.	17114649 [Abstract]

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