dbPTM

RGPA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RGPA1_MOUSE
UniProt AC	Q6GYP7
Protein Name	Ral GTPase-activating protein subunit alpha-1
Gene Name	Ralgapa1
Organism	Mus musculus (Mouse).
Sequence Length	2035
Subcellular Localization	Cytoplasm . Nucleus . Translocated to the nucleus, when associated with TCF3/E12.
Protein Description	Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB (By similarity). May interact with the HLH region of TCF3/isoform E12..
Protein Sequence	MFSKKPHGDVKKSTQKVLDTKKDALTRLKHLRIVIENAESIDLKQFFDQHFSHIYYVFFENFVTIEASLKQKGHKSQREELDAILFIFEKILQLLPERIHQRWQFHSIGLILKKLLHTGNSLKIRREGVRLFLLWLQALQDNCSKEQLWMFSCLIPGFSAPQSEYGPRTLDNLINPPLSLQETQVTIEEVTPLVPPQSGDKGQEDLTSYFLEALLKYIVIQVKSLEWKNKENQERGFSFLFSHFKKFYLPYIFPNICKENSLYHPVLDIPQIRPKPHYVMIKKDAETNETIYCTKEPFIQARVIVIRWLVSFWLEPKPHSGPNIPGMEGEVLPKNIQRAAASLVSREESKNDTVDKVDKSAEPEQSHSNTSTLTEREPSSSSLCSIDEEHLTDIEIVRRVFSSKRSNVNFVTEIFRQAFLLPICEAAAMRKVVKVYQEWIQQEEKPLFMQEPEDTAITCSDIPCSETVADHDSAIEDGEKREEENGTSTSEHVRNSSWTKNGSYQEAFHVCEEATEQNIQAGTQAVLQVFIINSSNIFLLEPANEIKNLLDEHTDMCKRILNIYRYMVVQVSMDKKTWEQMLLVLLRVTESVLKMSSQAFLQFQGKKSMTLAGRLAGPLFQTLIVAWIKANLNVYISRELWDDLLSVLSSLTYWEELATEWSLTMETLTKVLARNLYSLDLSDLPLDKLSEQKQKKHKGKGVGHEFQKVSVDKSFSRGWSRDQPGQAPMRQRSATTTGSPGTEKARSIVRQKTVDIDDAQILPRSTRVRHFSQSEDTGNEVFGALHEEQPLPRSSSTSDILEPFTVERAKVNKEDTSPKLPPLNSETGGNSANVPDLMDEFIAERLRSGNASTMTRRGSSPGSLEIPKDLPDILNKQNQMRPVDDPGVPSEWTSPASAGSSDLMSSDSHSDSFSAFQCEGRKFDNFGFGTDIGIPSSADVDLGSGHHQSTEEQEVASLTTLHLDSETSSLNQQAFSAEVATVTGSESASPVHSALGSRSQTPSPSTLSRAHIEQKDLQLDEKLHHSVLQTPDDLEISEFPSECCSVMAGGTLTGWHADVATVMWRRMLGILGDVNAIMDPEIHAQVFDYLCELWQNLAKIRDNLGISADNLTSPSPPVLIPPLRILTPWLFKATMLTDKYKQGKLHAYKLICNTMKRRQDVSPNRDFLTHFYNIMHCGLLHIDQDIVNTIIKHCSPQFFSLGLPGATMLIMDFIIAAGRVASSAFLNAPRVEAQVLLGSLVCFPNLYCELPALHPNIPDIAVSQFTDVKELIIKTVLSSARDEPSGPARCVALCSLGIWICEELVHESHHPQIKEALNVICVSLKFTNKTVAHVACNMLHMLVHYVPRLQIHQPQSPLKIIQILIATITHLLPSTEASSYEMDKRLVVSLLLCLLDWIMALPLKTLLQPVHATGAENDKTEKSVLNCIYKVLHGCVYGAQSFSNPKYFPISLSDLASVDYDPFMHLESLKEPEPLHSPDSERSSKLQPVTEVKTQMQQGLISIAARTVITHLVNHLGHYPMSGGPAMLTSQVCENHDNHYSESTELSPELFESPNIQFFVLNNTTLVSCIQIRSEESMPGGGLAAGLVSANSNVRIIVRDLSGKYSWDSAILYGPPIVSGLPEPTSFILSMSDQEKPEEPPTSNECLEDIAVKDGLSLQLRRFRETVPTWSTIREEEDVLDELLQYLGTTSPECLQRTGISLNVPAPQPLCISEKQENDVINAILKQYTEEKEFVEKHFNDLNMKASEQDEPTPQKPQSAFYYCRLLLSILGMNSWDKRRSFHLLKKNEKLLRELRNLDSRQCRETHKIAVFYVAEGQEDKYSILTNIGGSQAYEDFVAGLGWEVNLTNHCGFMGGLQKNRSTGLTTPYFATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHTRDYRRGIIPTEFGDVLIVIYPMKNHMFSIQIMKKPEVPFFGPLFDGAIVNGKVLPIMVRSTAINASRALKSLIPLYQNFYEERARYLQTIVQHHLEPTTFEDFAAQVFSPAPYHHFPADADH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
114	Ubiquitination	SIGLILKKLLHTGNS HHHHHHHHHHHCCCC	53.49	-
342	Phosphorylation	NIQRAAASLVSREES HHHHHHHHHHCCHHH	25.28	29176673
345	Phosphorylation	RAAASLVSREESKND HHHHHHHCCHHHCCC	38.99	30352176
349	Phosphorylation	SLVSREESKNDTVDK HHHCCHHHCCCCCCC	31.82	29514104
368	Phosphorylation	AEPEQSHSNTSTLTE CCCCCCCCCCCCCCC	47.23	25195567
370	Phosphorylation	PEQSHSNTSTLTERE CCCCCCCCCCCCCCC	26.55	25521595
371	Phosphorylation	EQSHSNTSTLTEREP CCCCCCCCCCCCCCC	26.18	25521595
379	Phosphorylation	TLTEREPSSSSLCSI CCCCCCCCCCCCCCC	37.79	21183079
380	Phosphorylation	LTEREPSSSSLCSID CCCCCCCCCCCCCCC	34.36	21183079
381	Phosphorylation	TEREPSSSSLCSIDE CCCCCCCCCCCCCCH	31.50	21183079
382	Phosphorylation	EREPSSSSLCSIDEE CCCCCCCCCCCCCHH	35.03	21183079
385	Phosphorylation	PSSSSLCSIDEEHLT CCCCCCCCCCHHHCC	38.07	21183079
682	Phosphorylation	NLYSLDLSDLPLDKL HCCCCCCCCCCHHHH	36.45	21183079
710	Phosphorylation	GHEFQKVSVDKSFSR CCCCEEEECCCCCCC	31.47	26824392
714	Phosphorylation	QKVSVDKSFSRGWSR EEEECCCCCCCCCCC	24.80	29514104
720	Phosphorylation	KSFSRGWSRDQPGQA CCCCCCCCCCCCCCC	28.89	26239621
733	Phosphorylation	QAPMRQRSATTTGSP CCCCCCCCCCCCCCC	22.94	23608596
735	Phosphorylation	PMRQRSATTTGSPGT CCCCCCCCCCCCCCH	26.57	28542873
736	Phosphorylation	MRQRSATTTGSPGTE CCCCCCCCCCCCCHH	28.95	29550500
737	Phosphorylation	RQRSATTTGSPGTEK CCCCCCCCCCCCHHH	31.16	25521595
739	Phosphorylation	RSATTTGSPGTEKAR CCCCCCCCCCHHHHH	20.33	25521595
742	Phosphorylation	TTTGSPGTEKARSIV CCCCCCCHHHHHHHH	37.38	29899451
753	Phosphorylation	RSIVRQKTVDIDDAQ HHHHHHCCCCCCCCC	18.31	25521595
766	Phosphorylation	AQILPRSTRVRHFSQ CCCCCCCCEEEEEEC	34.17	-
772	Phosphorylation	STRVRHFSQSEDTGN CCEEEEEECCCCCCC	27.03	25521595
774	Phosphorylation	RVRHFSQSEDTGNEV EEEEEECCCCCCCCE	35.92	27087446
777	Phosphorylation	HFSQSEDTGNEVFGA EEECCCCCCCCEEHH	37.54	27742792
794	Phosphorylation	EEQPLPRSSSTSDIL CCCCCCCCCCCCCCC	27.05	24925903
795	Phosphorylation	EQPLPRSSSTSDILE CCCCCCCCCCCCCCC	38.63	24925903
796	Phosphorylation	QPLPRSSSTSDILEP CCCCCCCCCCCCCCC	32.93	24925903
797	Phosphorylation	PLPRSSSTSDILEPF CCCCCCCCCCCCCCC	32.16	24925903
798	Phosphorylation	LPRSSSTSDILEPFT CCCCCCCCCCCCCCE	25.30	24925903
805	Phosphorylation	SDILEPFTVERAKVN CCCCCCCEEEECCCC	31.97	25619855
816	Phosphorylation	AKVNKEDTSPKLPPL CCCCCCCCCCCCCCC	48.28	25293948
817	Phosphorylation	KVNKEDTSPKLPPLN CCCCCCCCCCCCCCC	32.15	25293948
848	Phosphorylation	FIAERLRSGNASTMT HHHHHHHCCCCCCCC	40.78	25338131
859 (in isoform 2)	Phosphorylation	-	31.39	19144319
859	Phosphorylation	STMTRRGSSPGSLEI CCCCCCCCCCCCCCC	31.39	26824392
860	Phosphorylation	TMTRRGSSPGSLEIP CCCCCCCCCCCCCCC	35.78	25521595
863	Phosphorylation	RRGSSPGSLEIPKDL CCCCCCCCCCCCCCH	26.64	27742792
969	Phosphorylation	HLDSETSSLNQQAFS EECCCCCHHHHHCCE	38.47	-
985	Phosphorylation	EVATVTGSESASPVH EEEEECCCCCCCCCH	21.00	-
989	Phosphorylation	VTGSESASPVHSALG ECCCCCCCCCHHHCC	36.41	-
993	Phosphorylation	ESASPVHSALGSRSQ CCCCCCHHHCCCCCC	25.98	-
999	Phosphorylation	HSALGSRSQTPSPST HHHCCCCCCCCCHHH	39.85	23527152
1001	Phosphorylation	ALGSRSQTPSPSTLS HCCCCCCCCCHHHHC	27.29	25521595
1003	Phosphorylation	GSRSQTPSPSTLSRA CCCCCCCCHHHHCHH	34.57	25521595
1005	Phosphorylation	RSQTPSPSTLSRAHI CCCCCCHHHHCHHHH	46.44	25521595
1006	Phosphorylation	SQTPSPSTLSRAHIE CCCCCHHHHCHHHHH	31.94	23737553
1008	Phosphorylation	TPSPSTLSRAHIEQK CCCHHHHCHHHHHHH	27.75	23737553
1477	Phosphorylation	KEPEPLHSPDSERSS CCCCCCCCCCCHHCC	37.78	25521595
1480	Phosphorylation	EPLHSPDSERSSKLQ CCCCCCCCHHCCCCC	37.99	25521595
1589	Phosphorylation	GLAAGLVSANSNVRI CCCEEEEECCCCCEE	27.12	26026062
1592	Phosphorylation	AGLVSANSNVRIIVR EEEEECCCCCEEEEE	36.10	26026062
1781	Phosphorylation	NSWDKRRSFHLLKKN CCCCHHHHHHHHHHH	22.50	21743459
1806	Phosphorylation	DSRQCRETHKIAVFY CHHHHHHHHCEEEEE	14.76	22871156
1813	Phosphorylation	THKIAVFYVAEGQED HHCEEEEEEECCCCC	7.67	22871156
1882	Phosphorylation	VEVIFHVSTRMPSDS EEEEEEEECCCCCCC	11.17	-
1883	Phosphorylation	EVIFHVSTRMPSDSD EEEEEEECCCCCCCC	29.87	-
1941	Phosphorylation	PMKNHMFSIQIMKKP ECCCCEEEEEEECCC	13.15	-
2070	Phosphorylation	------------------------------------------ ------------------------------------------		-

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
Oops, there are no upstream regulatory protein records of RGPA1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RGPA1_MOUSE !!

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 RGPA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TFE2_MOUSE	Tcf3	physical	12200424

Drug and Disease Associations

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

Regulatory Network of RGPA1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-860; SER-999AND THR-1001, AND MASS SPECTROMETRY.	19367708 [Abstract]
"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-859 AND SER-860, ANDMASS SPECTROMETRY.	17242355 [Abstract]