BCAR3_HUMAN - dbPTM
BCAR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAR3_HUMAN
UniProt AC O75815
Protein Name Breast cancer anti-estrogen resistance protein 3
Gene Name BCAR3
Organism Homo sapiens (Human).
Sequence Length 825
Subcellular Localization
Protein Description May act as an adapter protein and couple activated growth factor receptors to a signaling pathway that regulates the proliferation in breast cancer cells. When overexpressed, it confers anti-estrogen resistance in breast cancer cell lines. May also be regulated by cellular adhesion to extracellular matrix proteins..
Protein Sequence MAAGKFASLPRNMPVNHQFPLASSMDLLSSRSPLAEHRPDAYQDVSIHGTLPRKKKGPPPIRSCDDFSHMGTLPHSKSPRQNSPVTQDGIQESPWQDRHGETFTFRDPHLLDPTVEYVKFSKERHIMDRTPEKLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLRCLEEHYGTSPGQAREGSLTKGRPDVAKRLSLTMGGVQAREQNLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGCKLPPQSSGVDTSPCPNSPVFRTGSEPALSPAVVRRVSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPSSPSAWLNSEANYCELNPAFATGCGRGAKLPSCAQGSHTELLTAKQNEAPGPRNSGVNYLILDDDDRERPWEPAAAQMEKGQWDKGEFVTPLLETVSSFRPNEFESKFLPPENKPLETAMLKRAKELFTNNDPKVIAQHVLSMDCRVARILGVSEEMRRNMGVSSGLELITLPHGHQLRLDIIERHNTMAIGIAVDILGCTGTLEDRAATLSKIIQVAVELKDSMGDLYSFSALMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKLLHEGRESTCVPPNNVSVPLLMPLVTLMERQAVTFEGTDMWEKNDQSCEIMLNHLATARFMAEAADSYRMNAERILAGFQPDEEMNEICKTEFQMRLLWGSKGAQVNQTERYEKFNQILTALSRKLEPPPVKQAEL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAGKFASL
------CCCCCCCCC		25.5622814378
5Methylation---MAAGKFASLPRN
---CCCCCCCCCCCC		32.79-
8PhosphorylationMAAGKFASLPRNMPV
CCCCCCCCCCCCCCC		41.8825394399
29PhosphorylationASSMDLLSSRSPLAE
CHHHHHHHCCCCHHH		30.8824719451
30PhosphorylationSSMDLLSSRSPLAEH
HHHHHHHCCCCHHHH		36.4324719451
32PhosphorylationMDLLSSRSPLAEHRP
HHHHHCCCCHHHHCC		26.6425159151
42PhosphorylationAEHRPDAYQDVSIHG
HHHCCCCCCCCCCCC		16.7821082442
46PhosphorylationPDAYQDVSIHGTLPR
CCCCCCCCCCCCCCC		19.7028442448
50PhosphorylationQDVSIHGTLPRKKKG
CCCCCCCCCCCCCCC		21.3030576142
55AcetylationHGTLPRKKKGPPPIR
CCCCCCCCCCCCCCC		65.3330587161
56AcetylationGTLPRKKKGPPPIRS
CCCCCCCCCCCCCCC		78.6230587167
63PhosphorylationKGPPPIRSCDDFSHM
CCCCCCCCCCCCCCC		23.7120068231
68PhosphorylationIRSCDDFSHMGTLPH
CCCCCCCCCCCCCCC		21.4020068231
72PhosphorylationDDFSHMGTLPHSKSP
CCCCCCCCCCCCCCC		29.5523403867
76PhosphorylationHMGTLPHSKSPRQNS
CCCCCCCCCCCCCCC		32.6520068231
78PhosphorylationGTLPHSKSPRQNSPV
CCCCCCCCCCCCCCC		28.4720201521
83PhosphorylationSKSPRQNSPVTQDGI
CCCCCCCCCCCCCCC		16.6522167270
86PhosphorylationPRQNSPVTQDGIQES
CCCCCCCCCCCCCCC		25.0722167270
93PhosphorylationTQDGIQESPWQDRHG
CCCCCCCCCCCCCCC		18.3123403867
104PhosphorylationDRHGETFTFRDPHLL
CCCCCEEEECCHHHC		25.77-
114PhosphorylationDPHLLDPTVEYVKFS
CHHHCCCCCEEEECC		26.1528152594
117PhosphorylationLLDPTVEYVKFSKER
HCCCCCEEEECCCHH		12.4721082442
119UbiquitinationDPTVEYVKFSKERHI
CCCCEEEECCCHHCC		42.91-
121PhosphorylationTVEYVKFSKERHIMD
CCEEEECCCHHCCCC		28.0828152594
122UbiquitinationVEYVKFSKERHIMDR
CEEEECCCHHCCCCC		63.00-
130PhosphorylationERHIMDRTPEKLKKE
HHCCCCCCHHHHHHH		31.3817001009
145PhosphorylationLEEELLLSSEDLRSH
HHHHHCCCCHHHHHH		31.4825072903
146PhosphorylationEEELLLSSEDLRSHA
HHHHCCCCHHHHHHH		34.7925072903
164PhosphorylationGRIPRQVSENLVQRD
CCCCHHHHHHHHHCC		16.6627251275
179PhosphorylationGDFLVRDSLSSPGNF
CCEEEEECCCCCCCE		21.4223663014
181PhosphorylationFLVRDSLSSPGNFVL
EEEEECCCCCCCEEE		38.1423663014
182PhosphorylationLVRDSLSSPGNFVLT
EEEECCCCCCCEEEE		41.9625159151
189PhosphorylationSPGNFVLTCQWKNLA
CCCCEEEEEEECHHH		9.4320068231
204PhosphorylationQHFKINRTVLRLSEA
HHHCCCHHHHHHHHH		21.2830576142
209PhosphorylationNRTVLRLSEAYSRVQ
CHHHHHHHHHHHHHH		17.4726356563
212PhosphorylationVLRLSEAYSRVQYQF
HHHHHHHHHHHHHEE		7.9228102081
213PhosphorylationLRLSEAYSRVQYQFE
HHHHHHHHHHHHEEE		32.7828152594
242PhosphorylationVGNRRPISQQSGAII
ECCCCCCCCCCCCEE		25.5024114839
245PhosphorylationRRPISQQSGAIIFQP
CCCCCCCCCCEEEEE		23.6624114839
266PhosphorylationLRCLEEHYGTSPGQA
CHHHHHHHCCCCCCC		25.9421945579
268PhosphorylationCLEEHYGTSPGQARE
HHHHHHCCCCCCCCC		25.2821945579
269PhosphorylationLEEHYGTSPGQAREG
HHHHHCCCCCCCCCC		23.7521945579
277PhosphorylationPGQAREGSLTKGRPD
CCCCCCCCCCCCCCC		28.2824719451
290PhosphorylationPDVAKRLSLTMGGVQ
CCHHHHHCCHHCHHH		26.3130266825
292PhosphorylationVAKRLSLTMGGVQAR
HHHHHCCHHCHHHHH		15.4723927012
315PhosphorylationLLRNKEKSGSQPACL
CCCCCCCCCCCCCHH		44.7823403867
317PhosphorylationRNKEKSGSQPACLDH
CCCCCCCCCCCHHHH		39.8325849741
332PhosphorylationMQDRRALSLKAHQSE
HHHHHHHHCCCCCCC		27.1724719451
334MethylationDRRALSLKAHQSESY
HHHHHHCCCCCCCCC		40.2124129315
338PhosphorylationLSLKAHQSESYLPIG
HHCCCCCCCCCCCCC		20.7421945579
340PhosphorylationLKAHQSESYLPIGCK
CCCCCCCCCCCCCCC		36.9021945579
341PhosphorylationKAHQSESYLPIGCKL
CCCCCCCCCCCCCCC		16.6721945579
352PhosphorylationGCKLPPQSSGVDTSP
CCCCCCCCCCCCCCC		34.5323090842
353PhosphorylationCKLPPQSSGVDTSPC
CCCCCCCCCCCCCCC		37.2723090842
357PhosphorylationPQSSGVDTSPCPNSP
CCCCCCCCCCCCCCC		31.9622199227
358PhosphorylationQSSGVDTSPCPNSPV
CCCCCCCCCCCCCCC		21.7525159151
363PhosphorylationDTSPCPNSPVFRTGS
CCCCCCCCCCCCCCC		13.9525159151
368PhosphorylationPNSPVFRTGSEPALS
CCCCCCCCCCCCCCC		33.3330266825
370PhosphorylationSPVFRTGSEPALSPA
CCCCCCCCCCCCCHH		39.5330266825
375PhosphorylationTGSEPALSPAVVRRV
CCCCCCCCHHHHHHH		16.9625159151
383PhosphorylationPAVVRRVSSDARAGE
HHHHHHHCCCCHHHH		22.2328655764
395PhosphorylationAGEALRGSDSQLCPK
HHHHHCCCCCCCCCC		27.8828857561
397PhosphorylationEALRGSDSQLCPKPP
HHHCCCCCCCCCCCC		27.1027794612
417PhosphorylationVPFLKVPSSPSAWLN
CCEEECCCCHHHHHC		58.8426356563
418PhosphorylationPFLKVPSSPSAWLNS
CEEECCCCHHHHHCC		19.4626356563
420PhosphorylationLKVPSSPSAWLNSEA
EECCCCHHHHHCCCC		33.7426356563
425PhosphorylationSPSAWLNSEANYCEL
CHHHHHCCCCCCEEC		35.6027259358
429PhosphorylationWLNSEANYCELNPAF
HHCCCCCCEECCHHH		8.3727259358
442MethylationAFATGCGRGAKLPSC
HHHCCCCCCCCCCCC		46.0724129315
448PhosphorylationGRGAKLPSCAQGSHT
CCCCCCCCCCCCCCC		32.3027251275
453PhosphorylationLPSCAQGSHTELLTA
CCCCCCCCCCHHEEC		18.3728857561
455PhosphorylationSCAQGSHTELLTAKQ
CCCCCCCCHHEECCC		29.9928857561
459PhosphorylationGSHTELLTAKQNEAP
CCCCHHEECCCCCCC		44.4224719451
471PhosphorylationEAPGPRNSGVNYLIL
CCCCCCCCCCCEEEE		45.4525159151
475PhosphorylationPRNSGVNYLILDDDD
CCCCCCCEEEECCCC		7.8527642862
541MalonylationTAMLKRAKELFTNND
HHHHHHHHHHHHCCC		60.0126320211
541AcetylationTAMLKRAKELFTNND
HHHHHHHHHHHHCCC		60.0126051181
541UbiquitinationTAMLKRAKELFTNND
HHHHHHHHHHHHCCC		60.01-
617PhosphorylationAVDILGCTGTLEDRA
HHHHHCCCCCHHHHH		31.2519690332
619PhosphorylationDILGCTGTLEDRAAT
HHHCCCCCHHHHHHH		14.6022817900
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 BCAR3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAR3_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 BCAR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYTC_HUMANTARSphysical
17353931
PABP1_HUMANPABPC1physical
17353931
IMDH2_HUMANIMPDH2physical
17353931
SYIC_HUMANIARSphysical
17353931
CASL_HUMANNEDD9physical
12517963
BCAR1_HUMANBCAR1physical
12517963
A4_HUMANAPPphysical
21832049
IMA5_HUMANKPNA1physical
21988832
RPR1A_HUMANRPRD1Aphysical
21988832
IRS1_HUMANIRS1physical
25814554
AGR3_HUMANAGR3physical
25640309
ATAD2_HUMANATAD2physical
25640309
BAP1_HUMANBAP1physical
25640309
BEX1_HUMANBEX1physical
25640309
BEX2_HUMANBEX2physical
25640309
CASZ1_HUMANCASZ1physical
25640309
CCL5_HUMANCCL5physical
25640309
CYTM_HUMANCST6physical
25640309
DKK3_HUMANDKK3physical
25640309
ESIP1_HUMANEPSTI1physical
25640309
ERRFI_HUMANERRFI1physical
25640309
GLCE_HUMANGLCEphysical
25640309
GREB1_HUMANGREB1physical
25640309
HXC6_HUMANHOXC6physical
25640309
MTA3_HUMANMTA3physical
25640309
OSGI1_HUMANOSGIN1physical
25640309
PDLI2_HUMANPDLIM2physical
25640309
PRD14_HUMANPRDM14physical
25640309
HOP2_HUMANPSMC3IPphysical
25640309
SPB5_HUMANSERPINB5physical
25640309
THRSP_HUMANTHRSPphysical
25640309
VPS45_HUMANVPS45physical
25640309
NSD3_HUMANWHSC1L1physical
25640309
BCAR1_HUMANBCAR1physical
28514442
CASL_HUMANNEDD9physical
28514442
GAST_HUMANGASTphysical
28514442
DEF5_HUMANDEFA5physical
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 BCAR3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-32; SER-83; SER-290;SER-358; SER-363 AND SER-375, AND MASS SPECTROMETRY.
"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-290, AND MASSSPECTROMETRY.
"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-182 AND SER-375, ANDMASS SPECTROMETRY.
"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 THR-130, AND MASSSPECTROMETRY.
"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-212 AND TYR-266, ANDMASS SPECTROMETRY.
"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-266, AND MASSSPECTROMETRY.

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