BCAS3_HUMAN - dbPTM
BCAS3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAS3_HUMAN
UniProt AC Q9H6U6
Protein Name Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470}
Gene Name BCAS3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470}
Organism Homo sapiens (Human).
Sequence Length 928
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motil
Protein Description Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin..
Protein Sequence MNEAMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGTPLTEEKEKIVWVRFENADLNDTSRNLEFHEIHSTGNEPPLLIMIGYSDGMQVWSIPISGEAQELFSVRHGPIRAARILPAPQFGAQKCDNFAEKRPLLGVCKSIGSSGTSPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVISAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVAIHSNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLNSQDSYNNFTNNNPGNPRLSPLPSLMVVMPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKPPPQISPSKSMGGEFCVAAIFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMMEPRPLSTAPKISDDTPLEMMTSPRASWTLVRTPQWNELQPPFNANHPLLLAADAVQYYQFLLAGLVPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFQFKTIHPSGQTTVISSSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRPVSDRRGVSTVIDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHTEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP
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
1Acetylation-------MNEAMATD
-------CCCCCCCC
10.3722814378
9PhosphorylationNEAMATDSPRRPSRC
CCCCCCCCCCCCCCC
18.8929759185
14PhosphorylationTDSPRRPSRCTGGVV
CCCCCCCCCCCCCEE
37.8720068231
73PhosphorylationENADLNDTSRNLEFH
CCCCCCCCCCCEEEE
28.63-
97PhosphorylationPLLIMIGYSDGMQVW
CEEEEEECCCCCEEE
7.8322210691
98PhosphorylationLLIMIGYSDGMQVWS
EEEEEECCCCCEEEE
23.6022210691
105PhosphorylationSDGMQVWSIPISGEA
CCCCEEEEEEECCCH
21.4522210691
145UbiquitinationKCDNFAEKRPLLGVC
CCCCHHHHCCCHHHH
56.75-
145 (in isoform 8)Ubiquitination-56.75-
154PhosphorylationPLLGVCKSIGSSGTS
CCHHHHHHCCCCCCC
27.3625627689
157PhosphorylationGVCKSIGSSGTSPPY
HHHHHCCCCCCCCCE
24.7525627689
158PhosphorylationVCKSIGSSGTSPPYC
HHHHCCCCCCCCCEE
40.6625627689
160PhosphorylationKSIGSSGTSPPYCCV
HHCCCCCCCCCEEEE
39.7525627689
161PhosphorylationSIGSSGTSPPYCCVD
HCCCCCCCCCEEEEE
27.6625627689
171PhosphorylationYCCVDLYSLRTGEMV
EEEEEEEECCCCCCE
20.7624719451
180PhosphorylationRTGEMVKSIQFKTPI
CCCCCEEEEEECCCE
15.37-
184UbiquitinationMVKSIQFKTPIYDLH
CEEEEEECCCEEECC
36.70-
215AcetylationFDSCTFTKKFFVTSC
CCCCCCEEEEEEEEE
43.3125953088
215MalonylationFDSCTFTKKFFVTSC
CCCCCCEEEEEEEEE
43.3126320211
215SumoylationFDSCTFTKKFFVTSC
CCCCCCEEEEEEEEE
43.3125114211
215UbiquitinationFDSCTFTKKFFVTSC
CCCCCCEEEEEEEEE
43.31-
215 (in isoform 8)Malonylation-43.3126320211
246AcetylationWLAYAENKLIRCHQS
HHHHHHHCEEEEECC
36.4730587173
275PhosphorylationTVISAAKTLKSGLTM
HHHHHHHHHHHCCCH
34.39-
288PhosphorylationTMVGKVVTQLTGTLP
CHHHHHHHHHHCCCC
22.35-
326 (in isoform 6)Phosphorylation-35.5825849741
328 (in isoform 6)Phosphorylation-40.5129116813
445PhosphorylationGGQPCVRTHMSPRVV
CCCCCCCCCCCHHHH
11.0926437602
448PhosphorylationPCVRTHMSPRVVNRM
CCCCCCCCHHHHHHH
11.2726437602
456PhosphorylationPRVVNRMSRFQKSAG
HHHHHHHHHHHHHCC
27.0624719451
461PhosphorylationRMSRFQKSAGLEEIE
HHHHHHHHCCHHHHH
19.4525159151
472PhosphorylationEEIEQELTSKQGGRC
HHHHHHHHHCCCCCC
32.8826074081
473PhosphorylationEIEQELTSKQGGRCS
HHHHHHHHCCCCCCC
35.2926074081
474UbiquitinationIEQELTSKQGGRCSP
HHHHHHHCCCCCCCC
47.962190698
474 (in isoform 1)Ubiquitination-47.9621906983
474 (in isoform 2)Ubiquitination-47.9621906983
474 (in isoform 3)Ubiquitination-47.9621906983
480PhosphorylationSKQGGRCSPVPGLSS
HCCCCCCCCCCCCCC
27.8023401153
486PhosphorylationCSPVPGLSSSPSGSP
CCCCCCCCCCCCCCC
34.3823401153
487PhosphorylationSPVPGLSSSPSGSPL
CCCCCCCCCCCCCCC
51.8422167270
488PhosphorylationPVPGLSSSPSGSPLH
CCCCCCCCCCCCCCC
21.5123401153
490PhosphorylationPGLSSSPSGSPLHGK
CCCCCCCCCCCCCCC
54.5822167270
492PhosphorylationLSSSPSGSPLHGKLN
CCCCCCCCCCCCCCC
28.7322167270
500PhosphorylationPLHGKLNSQDSYNNF
CCCCCCCCCCCCCCC
45.8923401153
503PhosphorylationGKLNSQDSYNNFTNN
CCCCCCCCCCCCCCC
23.3225159151
504PhosphorylationKLNSQDSYNNFTNNN
CCCCCCCCCCCCCCC
23.5528450419
508PhosphorylationQDSYNNFTNNNPGNP
CCCCCCCCCCCCCCC
38.8828450419
518PhosphorylationNPGNPRLSPLPSLMV
CCCCCCCCCCCCEEE
26.1828857561
522PhosphorylationPRLSPLPSLMVVMPL
CCCCCCCCEEEEEEH
36.4624043423
555 (in isoform 2)Phosphorylation-9.1725849741
555 (in isoform 3)Phosphorylation-9.1725849741
555 (in isoform 7)Phosphorylation-9.1725849741
557 (in isoform 2)Phosphorylation-1.9029116813
557 (in isoform 3)Phosphorylation-1.9029116813
557 (in isoform 7)Phosphorylation-1.9029116813
570PhosphorylationVKPPPQISPSKSMGG
CCCCCCCCCCCCCCC
20.2030266825
572PhosphorylationPPPQISPSKSMGGEF
CCCCCCCCCCCCCCE
30.4820873877
574PhosphorylationPQISPSKSMGGEFCV
CCCCCCCCCCCCEEE
27.3127251275
599UbiquitinationFANNAGLKREKDQSK
HHCCCCCCCCCCCCC
58.56-
614PhosphorylationQVVVESLYIISCYGT
HHHHEEEEHHHHHHH
12.8925850435
617PhosphorylationVESLYIISCYGTLVE
HEEEEHHHHHHHHHH
7.5425850435
619PhosphorylationSLYIISCYGTLVEHM
EEEHHHHHHHHHHHH
13.3225850435
621PhosphorylationYIISCYGTLVEHMME
EHHHHHHHHHHHHHC
10.9325850435
648PhosphorylationDTPLEMMTSPRASWT
CCCCHHHCCCCCCEE
33.98-
649PhosphorylationTPLEMMTSPRASWTL
CCCHHHCCCCCCEEE
8.42-
706PhosphorylationGPITRHGSYDSLASD
CCCCCCCCHHCCCCC
21.4630108239
707PhosphorylationPITRHGSYDSLASDH
CCCCCCCHHCCCCCC
17.7230108239
709PhosphorylationTRHGSYDSLASDHSG
CCCCCHHCCCCCCCC
20.0130108239
712PhosphorylationGSYDSLASDHSGQED
CCHHCCCCCCCCCCC
40.9430108239
715PhosphorylationDSLASDHSGQEDEEW
HCCCCCCCCCCCHHH
47.3530108239
724PhosphorylationQEDEEWLSQVEIVTH
CCCHHHHHCEEEEEE
33.0023312004
730PhosphorylationLSQVEIVTHTGPHRR
HHCEEEEEECCCCCC
21.2723312004
732PhosphorylationQVEIVTHTGPHRRLW
CEEEEEECCCCCCEE
42.9423312004
801PhosphorylationPVRSDPVSMPGSSRP
ECCCCCCCCCCCCCC
25.3428348404
805PhosphorylationDPVSMPGSSRPVSDR
CCCCCCCCCCCCCCC
19.8028555341
806PhosphorylationPVSMPGSSRPVSDRR
CCCCCCCCCCCCCCC
46.6628555341
816PhosphorylationVSDRRGVSTVIDAAS
CCCCCCCCCHHHHCC
21.5629255136
817PhosphorylationSDRRGVSTVIDAASG
CCCCCCCCHHHHCCC
21.0529255136
823PhosphorylationSTVIDAASGTFDRSV
CCHHHHCCCCCCCEE
39.8329255136
825PhosphorylationVIDAASGTFDRSVTL
HHHHCCCCCCCEEEH
21.6229255136
829PhosphorylationASGTFDRSVTLLEVC
CCCCCCCEEEHHHHH
22.6922617229
831PhosphorylationGTFDRSVTLLEVCGS
CCCCCEEEHHHHHCC
27.2025278378
838PhosphorylationTLLEVCGSWPEGFGL
EHHHHHCCCCCCCCC
34.0422617229
849PhosphorylationGFGLRHMSSMEHTEE
CCCCCCHHHHCCCHH
22.0223927012
850PhosphorylationFGLRHMSSMEHTEEG
CCCCCHHHHCCCHHH
22.1823927012
854PhosphorylationHMSSMEHTEEGLRER
CHHHHCCCHHHHHHH
23.5623312004
854 (in isoform 3)Phosphorylation-23.5625849741
854 (in isoform 7)Phosphorylation-23.5625849741
856 (in isoform 3)Phosphorylation-65.7625849741
856 (in isoform 7)Phosphorylation-65.7625849741
862 (in isoform 3)Phosphorylation-4.3022199227
862 (in isoform 7)Phosphorylation-4.3022199227
866SulfoxidationRERLADAMAESPSRD
HHHHHHHHHHCCCCC
4.3521406390
869PhosphorylationLADAMAESPSRDVVG
HHHHHHHCCCCCCCC
20.7319664994
869 (in isoform 8)Phosphorylation-20.7325849741
871PhosphorylationDAMAESPSRDVVGSG
HHHHHCCCCCCCCCC
50.8530266825
871 (in isoform 8)Phosphorylation-50.8525849741
877PhosphorylationPSRDVVGSGTELQRE
CCCCCCCCCCCEEEE
30.8220058876
877 (in isoform 8)Phosphorylation-30.8222199227
879PhosphorylationRDVVGSGTELQREGS
CCCCCCCCCEEEECC
34.9129978859
886PhosphorylationTELQREGSIETLSNS
CCEEEECCEEECCCC
16.7030266825
889PhosphorylationQREGSIETLSNSSGS
EEECCEEECCCCCCC
33.5430266825
891PhosphorylationEGSIETLSNSSGSTS
ECCEEECCCCCCCCC
41.9330266825
893PhosphorylationSIETLSNSSGSTSGS
CEEECCCCCCCCCCC
32.4730266825
893 (in isoform 3)Phosphorylation-32.4729507054
894PhosphorylationIETLSNSSGSTSGSI
EEECCCCCCCCCCCC
40.8023403867
896PhosphorylationTLSNSSGSTSGSIPR
ECCCCCCCCCCCCCC
22.7330266825
897PhosphorylationLSNSSGSTSGSIPRN
CCCCCCCCCCCCCCC
40.4029255136
898PhosphorylationSNSSGSTSGSIPRNF
CCCCCCCCCCCCCCC
32.0430266825
900PhosphorylationSSGSTSGSIPRNFDG
CCCCCCCCCCCCCCC
29.2330266825
908PhosphorylationIPRNFDGYRSPLPTN
CCCCCCCCCCCCCCC
15.1227251275
908 (in isoform 8)Phosphorylation-15.1229507054
910PhosphorylationRNFDGYRSPLPTNES
CCCCCCCCCCCCCCC
23.4627251275
914PhosphorylationGYRSPLPTNESQPLS
CCCCCCCCCCCCCCC
60.3428122231
917PhosphorylationSPLPTNESQPLSLFP
CCCCCCCCCCCCCCC
38.8928348404
921PhosphorylationTNESQPLSLFPTGFP
CCCCCCCCCCCCCCC
34.3528348404

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 BCAS3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAS3_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 BCAS3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CP070_HUMANC16orf70physical
25416956
ESR1_HUMANESR1physical
17505058
PELP1_HUMANPELP1physical
17505058
KAT2B_HUMANKAT2Bphysical
17505058

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 BCAS3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-886, AND MASSSPECTROMETRY.
"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-480 AND SER-488, ANDMASS SPECTROMETRY.

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