dbPTM

RAI3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAI3_HUMAN
UniProt AC	Q8NFJ5
Protein Name	Retinoic acid-induced protein 3
Gene Name	GPRC5A
Organism	Homo sapiens (Human).
Sequence Length	357
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cytoplasmic vesicle membrane Multi-pass membrane protein . Localized in perinuclear vesicles, probably Golgi-associated vesicles.
Protein Description	Orphan receptor. Could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. This retinoic acid-inducible GPCR provide evidence for a possible interaction between retinoid and G-protein signaling pathways. Functions as a negative modulator of EGFR signaling (By similarity). May act as a lung tumor suppressor. [PubMed: 18000218]
Protein Sequence	MATTVPDGCRNGLKSKYYRLCDKAEAWGIVLETVATAGVVTSVAFMLTLPILVCKVQDSNRRKMLPTQFLFLLGVLGIFGLTFAFIIGLDGSTGPTRFFLFGILFSICFSCLLAHAVSLTKLVRGRKPLSLLVILGLAVGFSLVQDVIAIEYIVLTMNRTNVNVFSELSAPRRNEDFVLLLTYVLFLMALTFLMSSFTFCGSFTGWKRHGAHIYLTMLLSIAIWVAWITLLMLPDFDRRWDDTILSSALAANGWVFLLAYVSPEFWLLTKQRNPMDYPVEDAFCKPQLVKKSYGVENRAYSQEEITQGFEETGDTLYAPYSTHFQLQNQPPQKEFSIPRAHAWPSPYKDYEVKKEGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	S-palmitoylation	ATTVPDGCRNGLKSK CCCCCCCCCCCCHHH	3.89	19801377
59	Phosphorylation	LVCKVQDSNRRKMLP HHEEECCCCHHCCCH	18.36	23401153
158	N-linked_Glycosylation	EYIVLTMNRTNVNVF HHHECCCCCCCCCEE	42.25	UniProtKB CARBOHYD
169	Phosphorylation	VNVFSELSAPRRNED CCEEHHHCCCCCCHH	31.98	24719451
277	Phosphorylation	KQRNPMDYPVEDAFC CCCCCCCCCCCCCCC	11.70	28152594
284	S-palmitoylation	YPVEDAFCKPQLVKK CCCCCCCCCHHHHCH	7.24	19801377
285	Acetylation	PVEDAFCKPQLVKKS CCCCCCCCHHHHCHH	29.37	26051181
285	Ubiquitination	PVEDAFCKPQLVKKS CCCCCCCCHHHHCHH	29.37	21963094
290	2-Hydroxyisobutyrylation	FCKPQLVKKSYGVEN CCCHHHHCHHHCCCC	44.59	-
290	Ubiquitination	FCKPQLVKKSYGVEN CCCHHHHCHHHCCCC	44.59	27667366
291	Ubiquitination	CKPQLVKKSYGVENR CCHHHHCHHHCCCCC	41.24	22817900
292	Phosphorylation	KPQLVKKSYGVENRA CHHHHCHHHCCCCCC	22.77	28152594
293	Phosphorylation	PQLVKKSYGVENRAY HHHHCHHHCCCCCCC	33.79	28152594
300	Phosphorylation	YGVENRAYSQEEITQ HCCCCCCCCHHHHHH	13.98	21955146
301	Phosphorylation	GVENRAYSQEEITQG CCCCCCCCHHHHHHC	30.08	25159151
306	Phosphorylation	AYSQEEITQGFEETG CCCHHHHHHCCHHHC	26.39	21955146
312	Phosphorylation	ITQGFEETGDTLYAP HHHCCHHHCCCEEEC	32.91	25159151
315	Phosphorylation	GFEETGDTLYAPYST CCHHHCCCEEECCCC	24.02	21082442
317	Phosphorylation	EETGDTLYAPYSTHF HHHCCCEEECCCCCE	13.97	30175587
320	Phosphorylation	GDTLYAPYSTHFQLQ CCCEEECCCCCEECC	20.30	25311788
321	Phosphorylation	DTLYAPYSTHFQLQN CCEEECCCCCEECCC	17.85	30175587
322	Phosphorylation	TLYAPYSTHFQLQNQ CEEECCCCCEECCCC	22.36	21082442
333	Ubiquitination	LQNQPPQKEFSIPRA CCCCCCCCCCCCCCC	67.51	21906983
336	Phosphorylation	QPPQKEFSIPRAHAW CCCCCCCCCCCCCCC	32.54	25463755
345	Phosphorylation	PRAHAWPSPYKDYEV CCCCCCCCCCCCCCC	30.11	22167270
347	Phosphorylation	AHAWPSPYKDYEVKK CCCCCCCCCCCCCCC	22.34	25159151
348	2-Hydroxyisobutyrylation	HAWPSPYKDYEVKKE CCCCCCCCCCCCCCC	58.16	-
348	Ubiquitination	HAWPSPYKDYEVKKE CCCCCCCCCCCCCCC	58.16	23000965
350	Phosphorylation	WPSPYKDYEVKKEGS CCCCCCCCCCCCCCC	20.62	21945579
353	Ubiquitination	PYKDYEVKKEGS--- CCCCCCCCCCCC---	32.92	23000965
354	Ubiquitination	YKDYEVKKEGS---- CCCCCCCCCCC----	72.92	23000965
357	Phosphorylation	YEVKKEGS------- CCCCCCCC-------	37.83	28152594

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
317	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
320	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
347	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
350	Y	Phosphorylation	Kinase	EGFR	P00533	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAI3_HUMAN !!

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 RAI3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
T2FB_HUMAN	GTF2F2	physical	22939629

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
DB00755	Tretinoin

Regulatory Network of RAI3_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-345, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345; TYR-347 ANDTYR-350, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND MASSSPECTROMETRY.	16565220 [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-347 AND TYR-350, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-317, AND MASSSPECTROMETRY.	17389395 [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-317; TYR-320; TYR-347AND TYR-350, AND MASS SPECTROMETRY.	18083107 [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-317, AND MASSSPECTROMETRY.	15951569 [Abstract]