dbPTM

RIN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RIN1_MOUSE
UniProt AC	Q921Q7
Protein Name	Ras and Rab interactor 1
Gene Name	Rin1
Organism	Mus musculus (Mouse).
Sequence Length	763
Subcellular Localization	Cytoplasm. Membrane. Cytoplasm, cytoskeleton. Some amount is membrane-associated..
Protein Description	Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis (By similarity)..
Protein Sequence	MEDPGETGAHPLGATNLNFVPGHQQKEKPSTDPLYDTPDTRGVQAGGSQQPARTVSLRERLLITRPVWLQLRANAAAALHVLRTEPPGTFLVRKSNTRQCQALCVRLPEASGPSFVSSHYIEESTGGVSLEGSELMFQDLVQLICGYCRTRAIHQAATHKELEAISHLGMEFWSSSLNTKDQQRPSEAPPIPRLKARSPQELDQGTGAALCFFNPLFPGDLGPTKREKFKRSFKVRVSTETSSPLSPPAVPPPPVPVLPGTSSSQTERLPPRQLLQRESSVGYRVPGSAASPCLPPLPSLQEVDCCSPSSSEEEGSSGSPTTSPRLSRPRHRRPLLRSMSSAFCSLLAPERQVGRAATMLMQNRYTAVGQLVQDLLTQVRAGPEPRELQGIRQALSRARAMLSAELGPEKLLPPERLELVLEKSLHRSVLKPLRPILAARLRRRLSADGSLGRLAEGFRLARTQGPGAFGSHLTLSSPVETEQVRQKLLQLLRAYSPSAQVKWLLQACKLLYTALKSQAGENAGADEFLPLLSLVLAQCDLPDLLLEAEYMSELLEPTLLTGEGGYYLTSLSASLALLSGLSQARALPLSPAQELQRSLALWEQRRLPATHSFQHLLRVAYQDPSTGCTSKTLAVPPGSSIATLSQLCATKFRVTQPDAFGLFLYKDQGYHRLPPEALAHRLPATGYLIYRRAERPETQGAVAEKAKTGSKGPEAGAWEEETGGLNREGKPRIAVDQEGKDQARGGHIGPEEQKAEGSQALEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDPGETG -------CCCCCCCC	13.71	-
30	Phosphorylation	HQQKEKPSTDPLYDT CCCCCCCCCCCCCCC	57.41	22499769
31	Phosphorylation	QQKEKPSTDPLYDTP CCCCCCCCCCCCCCC	50.60	22499769
35	Phosphorylation	KPSTDPLYDTPDTRG CCCCCCCCCCCCCCC	24.14	25521595
37	Phosphorylation	STDPLYDTPDTRGVQ CCCCCCCCCCCCCCC	14.98	23984901
40	Phosphorylation	PLYDTPDTRGVQAGG CCCCCCCCCCCCCCC	30.44	22499769
120	Phosphorylation	PSFVSSHYIEESTGG CCCHHCCCEEECCCC	16.39	22817900
147	Phosphorylation	LVQLICGYCRTRAIH HHHHHHHHHHHHHHH	3.70	22817900
198	Phosphorylation	IPRLKARSPQELDQG CCCCCCCCHHHHCCC	35.48	27087446
206	Phosphorylation	PQELDQGTGAALCFF HHHHCCCCCEEEECC	20.29	25619855
224	Phosphorylation	FPGDLGPTKREKFKR CCCCCCCCHHHHHHH	40.72	25777480
238	Phosphorylation	RSFKVRVSTETSSPL HHEEEEEECCCCCCC	15.23	25619855
239	Phosphorylation	SFKVRVSTETSSPLS HEEEEEECCCCCCCC	40.19	25619855
241	Phosphorylation	KVRVSTETSSPLSPP EEEEECCCCCCCCCC	34.29	25619855
242	Phosphorylation	VRVSTETSSPLSPPA EEEECCCCCCCCCCC	24.59	25619855
243	Phosphorylation	RVSTETSSPLSPPAV EEECCCCCCCCCCCC	36.96	25619855
246	Phosphorylation	TETSSPLSPPAVPPP CCCCCCCCCCCCCCC	32.02	25619855
261	Phosphorylation	PVPVLPGTSSSQTER CCCCCCCCCCCCCCC	24.40	25619855
262	Phosphorylation	VPVLPGTSSSQTERL CCCCCCCCCCCCCCC	33.63	25619855
263	Phosphorylation	PVLPGTSSSQTERLP CCCCCCCCCCCCCCC	26.72	25619855
264	Phosphorylation	VLPGTSSSQTERLPP CCCCCCCCCCCCCCH	40.67	25619855
266	Phosphorylation	PGTSSSQTERLPPRQ CCCCCCCCCCCCHHH	25.64	25619855
279	Phosphorylation	RQLLQRESSVGYRVP HHHHCCCCCCCCCCC	32.29	25521595
280	Phosphorylation	QLLQRESSVGYRVPG HHHCCCCCCCCCCCC	18.14	18779572
319	Phosphorylation	EEEGSSGSPTTSPRL CCCCCCCCCCCCCCC	22.48	-
323	Phosphorylation	SSGSPTTSPRLSRPR CCCCCCCCCCCCCCC	15.53	-
338	Phosphorylation	HRRPLLRSMSSAFCS HHHHHHHHHHHHHHH	24.00	27087446
340	Phosphorylation	RPLLRSMSSAFCSLL HHHHHHHHHHHHHHH	21.55	25521595
341	Phosphorylation	PLLRSMSSAFCSLLA HHHHHHHHHHHHHHC	19.40	27087446
345	Phosphorylation	SMSSAFCSLLAPERQ HHHHHHHHHHCCHHH	21.69	25619855
403	Phosphorylation	SRARAMLSAELGPEK HHHHHHHHHHHCHHH	13.45	25338131
446	Phosphorylation	ARLRRRLSADGSLGR HHHHHHHCCCCCHHH	23.62	26824392
450	Phosphorylation	RRLSADGSLGRLAEG HHHCCCCCHHHHHHC	28.35	28066266
590	Phosphorylation	QARALPLSPAQELQR HHCCCCCCHHHHHHH	19.09	25521595
598	Phosphorylation	PAQELQRSLALWEQR HHHHHHHHHHHHHHH	12.67	-
612	Phosphorylation	RRLPATHSFQHLLRV HCCCCCCCHHHHHHH	23.42	29899451
621	Phosphorylation	QHLLRVAYQDPSTGC HHHHHHHHCCCCCCC	15.59	22817900
648	S-palmitoylation	IATLSQLCATKFRVT HHHHHHHHCCCCCCC	3.33	28680068
670	Phosphorylation	FLYKDQGYHRLPPEA EEECCCCCCCCCHHH	4.33	29514104
681	Methylation	PPEALAHRLPATGYL CHHHHHHCCCCCCEE	36.44	-
690	Phosphorylation	PATGYLIYRRAERPE CCCCEEEEEECCCCC	7.46	-
758	Phosphorylation	EEQKAEGSQALEE-- HHHHHCHHHHHCC--	12.09	29514104

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
35	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
35	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
35	Y	Phosphorylation	Kinase	ABL2	P42684	GPS
35	Y	Phosphorylation	Kinase	ABL2	Q4JIM5	Uniprot
340	S	Phosphorylation	Kinase	PRKD1	Q62101	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
340	S	Phosphorylation		-
Phosphorylation at Ser-340 by PRKD1 induces interaction with 14-3-3 proteins (By similarity).

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 RIN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
1433E_MOUSE	Ywhae	physical	9144171

Drug and Disease Associations

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

Regulatory Network of RIN1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-590, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASSSPECTROMETRY.	18034455 [Abstract]

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