BCAR1_MOUSE - dbPTM
BCAR1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAR1_MOUSE
UniProt AC Q61140
Protein Name Breast cancer anti-estrogen resistance protein 1
Gene Name Bcar1
Organism Mus musculus (Mouse).
Sequence Length 874
Subcellular Localization Cell junction, focal adhesion. Cytoplasm. Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation..
Protein Description Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration (By similarity). Has been shown to be essential in cardiovascular development during embryogenesis..
Protein Sequence MTVPNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPVGPGPGPPATPPQPQPSLPQGVHAPVPPASQYSPMLPTAYQPQSDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGSPAQDIYQVPPSAGIGHDIYQVPPSLDTRGWEGTKPPAKVVVPTRVGQGYVYEAAQTEQDEYDTPRHLLAPGPQDIYDVPPVRGLLPNQYGQEVYDTPPMAVKGPNGRDPLLDVYDVPPSVEKGLLSSSHHSVYDVPPSVSKDVPDGPLLREETYDVPPAFAKPKPFDPTRHPLILAAPPPDSPAAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGSVVDDGVYAVPPPAEREAPTDGKRLSASSTGSTRSSQSASSLEVVVPGREPLELEVAVESLARLQQGVSTTVAHLLDLVGSASGPGGWRGTSEPQEPPAQDLKAAVAAVHGAVHELLEFARGAVSNATHTSDRTLHAKLSRQLQKMEDVYQTLVVHGQVLDSGRGSPGFTPEDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKAPGPGPEGSSSLHPNPTDKASSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLERGNIMRQGKGQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLVPGRTGGLGPSDRQLLLFYLEQCEANLTTLTDAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSQVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVDRVKELGHSTQQFRRVLGQLAAA
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-------MTVPNVLA
-------CCHHHHHH		8.43-
12PhosphorylationNVLAKALYDNVAESP
HHHHHHHHHHHCCCC		15.4418563927
119PhosphorylationQPQSDNVYLVPTPSK
CCCCCCEEEECCCCC		14.29-
127PhosphorylationLVPTPSKTQQGLYQA
EECCCCCCCCCCCCC		30.3825619855
132PhosphorylationSKTQQGLYQAPGPNP
CCCCCCCCCCCCCCC		14.9525619855
143PhosphorylationGPNPQFQSPPAKQTS
CCCCCCCCCCCCCCC		33.8525619855
169PhosphorylationPSPATDLYQVPPGPG
CCCCCCCCCCCCCCC		15.4120430882
196PhosphorylationAGIGHDIYQVPPSLD
CCCCCCCCCCCCCCC		14.98-
226PhosphorylationPTRVGQGYVYEAAQT
ECCCCCCCEEECCCC		7.6222499769
228PhosphorylationRVGQGYVYEAAQTEQ
CCCCCCEEECCCCCC		7.4322499769
233PhosphorylationYVYEAAQTEQDEYDT
CEEECCCCCCCCCCC		30.7822499769
238PhosphorylationAQTEQDEYDTPRHLL
CCCCCCCCCCCCHHC		33.1525521595
240PhosphorylationTEQDEYDTPRHLLAP
CCCCCCCCCCHHCCC		22.7122499769
253PhosphorylationAPGPQDIYDVPPVRG
CCCCCCCCCCCCCCC		21.1226824392
266PhosphorylationRGLLPNQYGQEVYDT
CCCCCCCCCCCCCCC		27.6722499769
271PhosphorylationNQYGQEVYDTPPMAV
CCCCCCCCCCCCCCC		17.2222499769
273PhosphorylationYGQEVYDTPPMAVKG
CCCCCCCCCCCCCCC		16.1722499769
291PhosphorylationRDPLLDVYDVPPSVE
CCCCCCCCCCCCCHH		15.7620116462
296PhosphorylationDVYDVPPSVEKGLLS
CCCCCCCCHHHCCCC		36.52-
303PhosphorylationSVEKGLLSSSHHSVY
CHHHCCCCCCCCCCC		34.5322499769
304PhosphorylationVEKGLLSSSHHSVYD
HHHCCCCCCCCCCCC		33.3922499769
305PhosphorylationEKGLLSSSHHSVYDV
HHCCCCCCCCCCCCC		23.1122499769
308PhosphorylationLLSSSHHSVYDVPPS
CCCCCCCCCCCCCCC		19.5622499769
310PhosphorylationSSSHHSVYDVPPSVS
CCCCCCCCCCCCCCC		17.7820116462
315PhosphorylationSVYDVPPSVSKDVPD
CCCCCCCCCCCCCCC		32.7122499769
317PhosphorylationYDVPPSVSKDVPDGP
CCCCCCCCCCCCCCC		27.7222499769
330PhosphorylationGPLLREETYDVPPAF
CCCCCCCCCCCCHHH		21.9222499769
331PhosphorylationPLLREETYDVPPAFA
CCCCCCCCCCCHHHC		20.4422499769
366PhosphorylationSPAAEDVYDVPPPAP
CCCHHHCCCCCCCCC		24.4415592455
376PhosphorylationPPPAPDLYDVPPGLR
CCCCCCCCCCCCCCC		23.4415592455
389PhosphorylationLRRPGPGTLYDVPRE
CCCCCCCCCCCCCHH		25.8622499769
391PhosphorylationRPGPGTLYDVPRERV
CCCCCCCCCCCHHHC		18.0926824392
407PhosphorylationPPEVADGSVVDDGVY
CHHHCCCCEECCCEE		21.3722499769
414PhosphorylationSVVDDGVYAVPPPAE
CEECCCEEECCCCCC		13.8620442405
426PhosphorylationPAEREAPTDGKRLSA
CCCCCCCCCCCCCCC		65.5126160508
432PhosphorylationPTDGKRLSASSTGST
CCCCCCCCCCCCCCC		30.0926824392
434PhosphorylationDGKRLSASSTGSTRS
CCCCCCCCCCCCCCC		25.6725263469
435PhosphorylationGKRLSASSTGSTRSS
CCCCCCCCCCCCCCC		36.1829472430
436PhosphorylationKRLSASSTGSTRSSQ
CCCCCCCCCCCCCCC		32.4324899341
438PhosphorylationLSASSTGSTRSSQSA
CCCCCCCCCCCCCCC		22.2724899341
439PhosphorylationSASSTGSTRSSQSAS
CCCCCCCCCCCCCCC		35.6028066266
441PhosphorylationSSTGSTRSSQSASSL
CCCCCCCCCCCCCEE		32.5826370283
444PhosphorylationGSTRSSQSASSLEVV
CCCCCCCCCCEEEEE		31.8726370283
540PhosphorylationATHTSDRTLHAKLSR
CCCCCCHHHHHHHHH		28.0821454597
556PhosphorylationLQKMEDVYQTLVVHG
HHHHHHHHHHHEECC		14.2217242355
558PhosphorylationKMEDVYQTLVVHGQV
HHHHHHHHHEECCEE		12.11-
568PhosphorylationVHGQVLDSGRGSPGF
ECCEECCCCCCCCCC		26.6519060867
572PhosphorylationVLDSGRGSPGFTPED
ECCCCCCCCCCCHHH		22.0820415495
576PhosphorylationGRGSPGFTPEDLDRL
CCCCCCCCHHHHHHH		31.5120415495
638PhosphorylationDKASSIQSRPLPSPP
CCCCCCCCCCCCCCC		33.9126824392
643PhosphorylationIQSRPLPSPPKFTSQ
CCCCCCCCCCCCCCC		62.6126824392
648PhosphorylationLPSPPKFTSQDSPDG
CCCCCCCCCCCCCCC		31.4426643407
649PhosphorylationPSPPKFTSQDSPDGQ
CCCCCCCCCCCCCCC		34.8126643407
652PhosphorylationPKFTSQDSPDGQYEN
CCCCCCCCCCCCCCC		19.7726643407
657PhosphorylationQDSPDGQYENSEGGW
CCCCCCCCCCCCCCC		23.7026643407
660PhosphorylationPDGQYENSEGGWMED
CCCCCCCCCCCCCCC		26.1926643407
668PhosphorylationEGGWMEDYDYVHLQG
CCCCCCCCCEEEECC		8.8918515860
670PhosphorylationGWMEDYDYVHLQGKE
CCCCCCCEEEECCHH		5.4118515860
697UbiquitinationGNIMRQGKGQLELQQ
CCHHHCCCCHHHHHH		34.84-
706UbiquitinationQLELQQLKQFERLEQ
HHHHHHHHHHHHHHH		48.91-
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
132YPhosphorylationKinaseSRCP05480
GPS
169YPhosphorylationKinaseSRCP05480
GPS
183YPhosphorylationKinaseSRCP05480
GPS
196YPhosphorylationKinaseSRCP05480
GPS
238YPhosphorylationKinaseSRCP05480
GPS
253YPhosphorylationKinaseABL1P00520
GPS
253YPhosphorylationKinaseSRCP05480
GPS
271YPhosphorylationKinaseSRCP05480
GPS
291YPhosphorylationKinaseSRCP05480
GPS
310YPhosphorylationKinaseSRCP05480
GPS
331YPhosphorylationKinaseSRCP05480
GPS
366YPhosphorylationKinaseSRCP05480
GPS
376YPhosphorylationKinaseSRCP05480
GPS
391YPhosphorylationKinaseSRCP05480
GPS
414YPhosphorylationKinaseSRCP05480
GPS
668YPhosphorylationKinaseSRC64-PhosphoELM
668YPhosphorylationKinaseSRCP05480
PSP
668YPhosphorylationKinasePTK2P34152-2
GPS
668YPhosphorylationKinaseFAK1P34152
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAR1_MOUSE !!
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 BCAR1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC_MOUSESrcphysical
11038351
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BCAR1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238 AND TYR-253, ANDMASS SPECTROMETRY.
"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-132; TYR-228; TYR-331;TYR-366 AND TYR-414, AND MASS SPECTROMETRY.

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