dbPTM

RIN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RIN1_HUMAN
UniProt AC	Q13671
Protein Name	Ras and Rab interactor 1
Gene Name	RIN1
Organism	Homo sapiens (Human).
Sequence Length	783
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..
Protein Sequence	MESPGESGAGSPGAPSPSSFTTGHLAREKPAQDPLYDVPNASGGQAGGPQRPGRVVSLRERLLLTRPVWLQLQANAAAALHMLRTEPPGTFLVRKSNTRQCQALCMRLPEASGPSFVSSHYILESPGGVSLEGSELMFPDLVQLICAYCHTRDILLLPLQLPRAIHHAATHKELEAISHLGIEFWSSSLNIKAQRGPAGGPVLPQLKARSPQELDQGTGAALCFFNPLFPGDLGPTKREKFKRSFKVRVSTETSSPLSPPAVPPPPVPVLPGAVPSQTERLPPCQLLRRESSVGYRVPAGSGPSLPPMPSLQEVDCGSPSSSEEEGVPGSRGSPATSPHLGRRRPLLRSMSAAFCSLLAPERQVGRAAAALMQDRHTAAGQLVQDLLTQVRAGPEPQELQGIRQALSRARAMLSAELGPEKLLSPKRLEHVLEKSLHCSVLKPLRPILAARLRRRLAADGSLGRLAEGLRLARAQGPGAFGSHLSLPSPVELEQVRQKLLQLLRTYSPSAQVKRLLQACKLLYMALRTQEGEGAGADEFLPLLSLVLAHCDLPELLLEAEYMSELLEPSLLTGEGGYYLTSLSASLALLSGLGQAHTLPLSPVQELRRSLSLWEQRRLPATHCFQHLLRVAYQDPSSGCTSKTLAVPPEASIATLNQLCATKFRVTQPNTFGLFLYKEQGYHRLPPGALAHRLPTTGYLVYRRAEWPETQGAVTEEEGSGQSEARSRGEEQGCQGDGDAGVKASPRDIREQSETTAEGGQGQAQEGPAQPGEPEAEGSRAAEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESPGESG -------CCCCCCCC	11.82	20068231
3	Phosphorylation	-----MESPGESGAG -----CCCCCCCCCC	36.59	29255136
7	Phosphorylation	-MESPGESGAGSPGA -CCCCCCCCCCCCCC	39.60	29255136
11	Phosphorylation	PGESGAGSPGAPSPS CCCCCCCCCCCCCCC	21.45	29255136
16	Phosphorylation	AGSPGAPSPSSFTTG CCCCCCCCCCCCCCC	36.56	25159151
18	Phosphorylation	SPGAPSPSSFTTGHL CCCCCCCCCCCCCCC	42.28	28450419
19	Phosphorylation	PGAPSPSSFTTGHLA CCCCCCCCCCCCCCC	29.96	28450419
21	Phosphorylation	APSPSSFTTGHLARE CCCCCCCCCCCCCCC	33.54	28450419
22	Phosphorylation	PSPSSFTTGHLAREK CCCCCCCCCCCCCCC	22.16	28450419
29	Ubiquitination	TGHLAREKPAQDPLY CCCCCCCCCCCCCCC	39.85	21906983
29 (in isoform 1)	Ubiquitination	-	39.85	21906983
29 (in isoform 2)	Ubiquitination	-	39.85	21906983
35	Phosphorylation	EKPAQDPLYDVPNAS CCCCCCCCCCCCCCC	8.41	17016520
36	Phosphorylation	KPAQDPLYDVPNASG CCCCCCCCCCCCCCC	21.93	21945579
42	Phosphorylation	LYDVPNASGGQAGGP CCCCCCCCCCCCCCC	50.53	21945579
65	Phosphorylation	LRERLLLTRPVWLQL HHHHHHHHCHHHHHH	32.66	-
90	Phosphorylation	LRTEPPGTFLVRKSN HHCCCCCCEEEECCC	21.41	-
207	Ubiquitination	GPVLPQLKARSPQEL CCCCHHHHCCCHHHH	36.18	-
210	Phosphorylation	LPQLKARSPQELDQG CHHHHCCCHHHHCCC	35.48	29255136
218	Phosphorylation	PQELDQGTGAALCFF HHHHCCCCCEEEECC	20.29	29255136
236	Phosphorylation	FPGDLGPTKREKFKR CCCCCCCCHHHHHHH	40.72	24732914
237	Ubiquitination	PGDLGPTKREKFKRS CCCCCCCHHHHHHHH	62.79	-
244	Phosphorylation	KREKFKRSFKVRVST HHHHHHHHEEEEEEC	29.97	-
250	Phosphorylation	RSFKVRVSTETSSPL HHEEEEEECCCCCCC	15.23	28450419
251	Phosphorylation	SFKVRVSTETSSPLS HEEEEEECCCCCCCC	40.19	28176443
253	Phosphorylation	KVRVSTETSSPLSPP EEEEECCCCCCCCCC	34.29	28176443
254	Phosphorylation	VRVSTETSSPLSPPA EEEECCCCCCCCCCC	24.59	28450419
255	Phosphorylation	RVSTETSSPLSPPAV EEECCCCCCCCCCCC	36.96	26657352
258	Phosphorylation	TETSSPLSPPAVPPP CCCCCCCCCCCCCCC	32.02	26055452
276	Phosphorylation	VLPGAVPSQTERLPP CCCCCCCCCCCCCCC	43.04	27251275
278	Phosphorylation	PGAVPSQTERLPPCQ CCCCCCCCCCCCCCH	27.66	23090842
291	Phosphorylation	CQLLRRESSVGYRVP CHHHCCCCCCCCCCC	28.63	26055452
292	Phosphorylation	QLLRRESSVGYRVPA HHHCCCCCCCCCCCC	18.14	26055452
295	Phosphorylation	RRESSVGYRVPAGSG CCCCCCCCCCCCCCC	13.28	26356563
310	Phosphorylation	PSLPPMPSLQEVDCG CCCCCCCCCCCCCCC	36.11	20873877
318	Phosphorylation	LQEVDCGSPSSSEEE CCCCCCCCCCCCCCC	28.13	25137130
320	Phosphorylation	EVDCGSPSSSEEEGV CCCCCCCCCCCCCCC	48.47	25137130
321	Phosphorylation	VDCGSPSSSEEEGVP CCCCCCCCCCCCCCC	45.19	25137130
322	Phosphorylation	DCGSPSSSEEEGVPG CCCCCCCCCCCCCCC	54.05	25137130
330	Phosphorylation	EEEGVPGSRGSPATS CCCCCCCCCCCCCCC	27.65	20873877
333	Phosphorylation	GVPGSRGSPATSPHL CCCCCCCCCCCCCCC	15.39	30266825
336	Phosphorylation	GSRGSPATSPHLGRR CCCCCCCCCCCCCCC	46.29	30266825
337	Phosphorylation	SRGSPATSPHLGRRR CCCCCCCCCCCCCCH	16.66	29255136
349	Phosphorylation	RRRPLLRSMSAAFCS CCHHHHHHHHHHHHH	19.63	30266825
351	Phosphorylation	RPLLRSMSAAFCSLL HHHHHHHHHHHHHHH	20.07	29255136
356	Phosphorylation	SMSAAFCSLLAPERQ HHHHHHHHHHCCHHH	21.69	30266825
377	Phosphorylation	ALMQDRHTAAGQLVQ HHHHCHHHHHHHHHH	21.06	22817900
388	Phosphorylation	QLVQDLLTQVRAGPE HHHHHHHHHHHCCCC	32.11	22817900
407	Phosphorylation	QGIRQALSRARAMLS HHHHHHHHHHHHHHH	27.23	-
424	Phosphorylation	LGPEKLLSPKRLEHV HCHHHHCCHHHHHHH	38.52	21712546
435	Phosphorylation	LEHVLEKSLHCSVLK HHHHHHHHHCCHHHC	17.61	20873877
439	Phosphorylation	LEKSLHCSVLKPLRP HHHHHCCHHHCCHHH	21.53	20873877
451 (in isoform 2)	Ubiquitination	-	24.10	21906983
513 (in isoform 1)	Ubiquitination	-	25.83	21906983
513	Ubiquitination	YSPSAQVKRLLQACK CCHHHHHHHHHHHHH	25.83	2190698
523	Phosphorylation	LQACKLLYMALRTQE HHHHHHHHHHHHCCC	7.26	27642862
609	Phosphorylation	PVQELRRSLSLWEQR HHHHHHHHHHHHHHH	18.84	22617229
611	Phosphorylation	QELRRSLSLWEQRRL HHHHHHHHHHHHHCC	32.46	22617229
632	Phosphorylation	QHLLRVAYQDPSSGC HHHHHHHHCCCCCCC	15.59	21945579
643	Phosphorylation	SSGCTSKTLAVPPEA CCCCCCCCCCCCCCH	21.51	22210691
654	Phosphorylation	PPEASIATLNQLCAT CCCHHHHHHHHHHCC	25.27	22210691
662	Ubiquitination	LNQLCATKFRVTQPN HHHHHCCCCCCCCCC	16.79	-
664	Methylation	QLCATKFRVTQPNTF HHHCCCCCCCCCCCE	31.93	54558807
676	Phosphorylation	NTFGLFLYKEQGYHR CCEEEEEEECCCCCC	12.73	21945579
681	Phosphorylation	FLYKEQGYHRLPPGA EEEECCCCCCCCCCH	5.40	21945579
692	Methylation	PPGALAHRLPTTGYL CCCHHHHCCCCCCEE	36.43	24129315
695	Phosphorylation	ALAHRLPTTGYLVYR HHHHCCCCCCEEEEE	37.13	21945579
696	Phosphorylation	LAHRLPTTGYLVYRR HHHCCCCCCEEEEEE	23.14	21945579
698	Phosphorylation	HRLPTTGYLVYRRAE HCCCCCCEEEEEECC	7.30	21945579
701	Phosphorylation	PTTGYLVYRRAEWPE CCCCEEEEEECCCCC	7.56	21945579
719	Phosphorylation	AVTEEEGSGQSEARS CCCCCCCCCCCHHHH	36.62	26852163
722	Phosphorylation	EEEGSGQSEARSRGE CCCCCCCCHHHHHHH	36.43	26852163
742	Ubiquitination	GDGDAGVKASPRDIR CCCCCCCCCCHHHHH	42.08	-
744	Phosphorylation	GDAGVKASPRDIREQ CCCCCCCCHHHHHHH	18.10	30576142

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
36	Y	Phosphorylation	Kinase	ABL1	P00519	Uniprot
36	Y	Phosphorylation	Kinase	ABL2	P42684	Uniprot
292	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
292	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
292	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
351	S	Phosphorylation	Kinase	PRKD1	Q15139	Uniprot
351	S	Phosphorylation	Kinase	PKD1	P98161	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
351	S	Phosphorylation		11784866
Phosphorylation at Ser-351 by PRKD1 induces interaction with 14-3-3 proteins.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNDS_HUMAN	RALGDS	physical	10545207
AFAD_HUMAN	MLLT4	physical	10545207
STAM2_HUMAN	STAM2	physical	17403676
STAM2_HUMAN	STAM2	physical	22976291
ABL2_HUMAN	ABL2	physical	15886098
CACO2_HUMAN	CALCOCO2	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
ANS1B_HUMAN	ANKS1B	physical	25814554
RASK_HUMAN	KRAS	physical	28514442
ANS1A_HUMAN	ANKS1A	physical	28514442
ABL2_HUMAN	ABL2	physical	28514442
RASN_HUMAN	NRAS	physical	28514442
RASH_HUMAN	HRAS	physical	28514442
RRAS_HUMAN	RRAS	physical	28514442
1433Z_HUMAN	YWHAZ	physical	28514442
ISCA1_HUMAN	ISCA1	physical	28514442
1433E_HUMAN	YWHAE	physical	28514442
RRAS2_HUMAN	RRAS2	physical	28514442
1433G_HUMAN	YWHAG	physical	28514442
1433F_HUMAN	YWHAH	physical	28514442
ABL1_HUMAN	ABL1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of RIN1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; THR-251; SER-258;SER-337; SER-351 AND SER-609, AND MASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-337, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"The RAS effector RIN1 directly competes with RAF and is regulated by14-3-3 proteins."; Wang Y., Waldron R.T., Dhaka A., Patel A., Riley M.M., Rozengurt E.,Colicelli J.; Mol. Cell. Biol. 22:916-926(2002). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-351, AND MUTAGENESIS OFSER-351.	11784866 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-632, AND MASSSPECTROMETRY.	17053785 [Abstract]
"RIN1 is an ABL tyrosine kinase activator and a regulator ofepithelial-cell adhesion and migration."; Hu H., Bliss J.M., Wang Y., Colicelli J.; Curr. Biol. 15:815-823(2005). Cited for: FUNCTION, INTERACTION WITH ABL1 AND ABL2, AND PHOSPHORYLATION ATTYR-36.	15886098 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASSSPECTROMETRY.	15951569 [Abstract]

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