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

loading...

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.

TOP