dbPTM

RCAS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RCAS1_HUMAN
UniProt AC	O00559
Protein Name	Receptor-binding cancer antigen expressed on SiSo cells
Gene Name	EBAG9
Organism	Homo sapiens (Human).
Sequence Length	213
Subcellular Localization	Golgi apparatus membrane Single-pass type III membrane protein . According to PubMed:10426319, it also exists as a soluble form which has the same biological activities. The existence of such soluble form is however uncertain.
Protein Description	May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases..
Protein Sequence	MAITQFRLFKFCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGIPDGSTGFSSRLAATQDLPFIHQSSELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKLADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-palmitoylation	QFRLFKFCTCLATVF HHHHHHHHHHHHHHH	2.43	29575903
14	S-palmitoylation	RLFKFCTCLATVFSF HHHHHHHHHHHHHHH	2.27	29575903
20	Phosphorylation	TCLATVFSFLKRLIC HHHHHHHHHHHHHHH	25.90	24719451
36	Phosphorylation	SGRGRKLSGDQITLP CCCCCCCCCCCEECC	43.27	19664994
41	Phosphorylation	KLSGDQITLPTTVDY CCCCCCEECCCEECC	22.50	22167270
44	Phosphorylation	GDQITLPTTVDYSSV CCCEECCCEECCCCC	42.43	23927012
45	O-linked_Glycosylation	DQITLPTTVDYSSVP CCEECCCEECCCCCC	14.94	OGP
45	Phosphorylation	DQITLPTTVDYSSVP CCEECCCEECCCCCC	14.94	23927012
48	Phosphorylation	TLPTTVDYSSVPKQT ECCCEECCCCCCCCC	9.86	23927012
49	Phosphorylation	LPTTVDYSSVPKQTD CCCEECCCCCCCCCC	22.01	23927012
50	Phosphorylation	PTTVDYSSVPKQTDV CCEECCCCCCCCCCH	35.89	23927012
55	Phosphorylation	YSSVPKQTDVEEWTS CCCCCCCCCHHHCCC	48.41	27251275
61	Phosphorylation	QTDVEEWTSWDEDAP CCCHHHCCCCCCCCC	24.18	22199227
62	Phosphorylation	TDVEEWTSWDEDAPT CCHHHCCCCCCCCCC	33.34	22199227
82	Phosphorylation	GGNGNVATQQNSLEQ CCCCCCCCCCCCHHH	26.80	28450419
86	Phosphorylation	NVATQQNSLEQLEPD CCCCCCCCHHHHCCC	29.01	25159151
94	Phosphorylation	LEQLEPDYFKDMTPT HHHHCCCHHHCCCHH	24.20	28450419
99	Phosphorylation	PDYFKDMTPTIRKTQ CCHHHCCCHHHCEEC	27.67	21815630
101	Phosphorylation	YFKDMTPTIRKTQKI HHHCCCHHHCEECEE	25.01	-
112	Ubiquitination	TQKIVIKKREPLNFG ECEEEEECCCCCCCC	51.36	-
124	Phosphorylation	NFGIPDGSTGFSSRL CCCCCCCCCCHHHHH	32.51	28555341
125	Phosphorylation	FGIPDGSTGFSSRLA CCCCCCCCCHHHHHH	48.01	28555341
128	Phosphorylation	PDGSTGFSSRLAATQ CCCCCCHHHHHHHCC	18.85	28555341
134	Phosphorylation	FSSRLAATQDLPFIH HHHHHHHCCCCCEEE	19.60	24275569
184 (in isoform 2)	Phosphorylation	-	33.99	-
191 (in isoform 2)	Phosphorylation	-	52.73	-
202	Acetylation	KEAQRLMKKEQNKIG HHHHHHHHHHHHHHC	58.72	7461927
213	Phosphorylation	NKIGVKLS------- HHHCCCCC-------	32.24	24719451

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 RCAS1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RCAS1_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 RCAS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RCAS1_HUMAN !!

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 RCAS1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-86, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-36, 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-36, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-41 AND TYR-48,AND MASS SPECTROMETRY.	15144186 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, AND MASSSPECTROMETRY.	15592455 [Abstract]