BCAR1_RAT - dbPTM
BCAR1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAR1_RAT
UniProt AC Q63767
Protein Name Breast cancer anti-estrogen resistance protein 1
Gene Name Bcar1
Organism Rattus norvegicus (Rat).
Sequence Length 968
Subcellular Localization Cell junction, focal adhesion. Cytoplasm. Localizes at focal adhesions and stress fibers. 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)..
Protein Sequence MKYLVSVGAGPARRAGGLEDVSWGPRVSRRPQSYRAARHVNESLPRSAFRVPAAHGASVTPSAALGSGLPETQPEAVCRGTEKPRFAEGCKPAASRDKNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAAPGPGPPATPPQPQPSLPQGVHTPVPPASQYSPMLPTAYQPQPDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGSPAQDIYQVPPSAGTGHDIYQVPPSLDTRSWEGTKPPAKVVVPTRVGQGYVYEASQAEQDEYDTPRHLLAPGSQDIYDVPPVRGLLPNQYGQEVYDTPPMAVKGPNGRDPLLDVYDVPPSVEKGLPPSNHHSVYDVPPSVSKDVPDGPLLREETYDVPPAFAKPKPFDPTRHPLILAAPPPDSPPAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGSVIDDGVYAVPPPAEREAPTDGKRLSASSTGSTRSSQSASSLEVVVPGREPLELEVAVETLARLQQGVSTTVAHLLDLVGSASGPGGWRSTSEPQEPPVQDLKAAVAAVHGAVHELLEFARSAVSSATHTSDRTLHAKLSRQLQKMEDVYQTLVVHGQVLDSGRGGPGFTLDDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKAPGPGPEGSSSLHLNPTDKASSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLEKGNIVRQGKGQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLVPGRTGGLGPSDRQLLLFYLEQCEANLTTLTDAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSKVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVDRVKELGHSTQQFRRVLGQLAAA
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-------MKYLVSVG
-------CCEEEEEC		6.09-
3Phosphorylation-----MKYLVSVGAG
-----CCEEEEECCC		15.8426022182
6Phosphorylation--MKYLVSVGAGPAR
--CCEEEEECCCCCH		16.5526022182
226PhosphorylationSKTQQGLYQAPGPNP
CCCCCCCCCCCCCCC		14.9522108457
237PhosphorylationGPNPQFQSPPAKQTS
CCCCCCCCCCCCCCC		33.8522108457
263PhosphorylationPSPATDLYQVPPGPG
CCCCCCCCCCCCCCC		15.4112972425
277PhosphorylationGSPAQDIYQVPPSAG
CCCHHHCEECCCCCC		16.2612972425
290PhosphorylationAGTGHDIYQVPPSLD
CCCCCCCCCCCCCCC		14.9812972425
332PhosphorylationSQAEQDEYDTPRHLL
HHCCCCCCCCCCCCC		33.1527097102
334PhosphorylationAEQDEYDTPRHLLAP
CCCCCCCCCCCCCCC		22.7127097102
343PhosphorylationRHLLAPGSQDIYDVP
CCCCCCCCCCCCCCC		24.5027097102
347PhosphorylationAPGSQDIYDVPPVRG
CCCCCCCCCCCCCCC		21.1227097102
365PhosphorylationNQYGQEVYDTPPMAV
CCCCCCCCCCCCCCC		17.2227097102
367PhosphorylationYGQEVYDTPPMAVKG
CCCCCCCCCCCCCCC		16.1727097102
385PhosphorylationRDPLLDVYDVPPSVE
CCCCCCCCCCCCCHH		15.7622108457
390PhosphorylationDVYDVPPSVEKGLPP
CCCCCCCCHHCCCCC		36.52-
404PhosphorylationPSNHHSVYDVPPSVS
CCCCCCCCCCCCCCC		17.7812972425
424PhosphorylationGPLLREETYDVPPAF
CCCCCCCCCCCCHHH		21.9227097102
425PhosphorylationPLLREETYDVPPAFA
CCCCCCCCCCCHHHC		20.4427097102
453PhosphorylationLAAPPPDSPPAEDVY
EECCCCCCCCHHHCC		38.2622108457
460PhosphorylationSPPAEDVYDVPPPAP
CCCHHHCCCCCCCCC		24.44-
470PhosphorylationPPPAPDLYDVPPGLR
CCCCCCCCCCCCCCC		23.44-
485PhosphorylationRPGPGTLYDVPRERV
CCCCCCCCCCCHHHC		18.0927097102
508PhosphorylationSVIDDGVYAVPPPAE
CEECCCEEECCCCCC		13.8622108457
526PhosphorylationPTDGKRLSASSTGST
CCCCCCCCCCCCCCC		30.0928432305
528PhosphorylationDGKRLSASSTGSTRS
CCCCCCCCCCCCCCC		25.6728432305
529PhosphorylationGKRLSASSTGSTRSS
CCCCCCCCCCCCCCC		36.1828432305
530PhosphorylationKRLSASSTGSTRSSQ
CCCCCCCCCCCCCCC		32.4328432305
532PhosphorylationLSASSTGSTRSSQSA
CCCCCCCCCCCCCCC		22.2728432305
533PhosphorylationSASSTGSTRSSQSAS
CCCCCCCCCCCCCCC		35.6028432305
535PhosphorylationSSTGSTRSSQSASSL
CCCCCCCCCCCCCEE		32.5827097102
536PhosphorylationSTGSTRSSQSASSLE
CCCCCCCCCCCCEEE		25.5127097102
538PhosphorylationGSTRSSQSASSLEVV
CCCCCCCCCCEEEEE		31.8727097102
540PhosphorylationTRSSQSASSLEVVVP
CCCCCCCCEEEEEEC		40.4827097102
650PhosphorylationLQKMEDVYQTLVVHG
HHHHHHHHHHHEECC		14.22-
737PhosphorylationIQSRPLPSPPKFTSQ
CCCCCCCCCCCCCCC		62.6122673903
751PhosphorylationQDSPDGQYENSEGGW
CCCCCCCCCCCCCCC		23.708621540
762PhosphorylationEGGWMEDYDYVHLQG
CCCCCCCCCEEEECC		8.8916245368
764PhosphorylationGWMEDYDYVHLQGKE
CCCCCCCEEEECCHH		5.419360983
896PhosphorylationKLVFIGDTLSRQAKA
EEEEECCHHHHHHHH		22.7823984901
898PhosphorylationVFIGDTLSRQAKAAD
EEECCHHHHHHHHHH		25.1623984901
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
226YPhosphorylationKinaseSRCQ9WUD9
Uniprot
226YPhosphorylationKinaseSRCP00523
PSP
263YPhosphorylationKinasePTK2O35346
GPS
263YPhosphorylationKinaseSRCP00523
PSP
277YPhosphorylationKinaseSRCP00523
PSP
290YPhosphorylationKinaseSRCP00523
PSP
332YPhosphorylationKinaseSRCP00523
PSP
347YPhosphorylationKinaseABL1-Uniprot
347YPhosphorylationKinaseABL1E9PT20
GPS
347YPhosphorylationKinaseSRCP00523
PSP
365YPhosphorylationKinaseSRCP00523
PSP
385YPhosphorylationKinaseSRCP00523
PSP
404YPhosphorylationKinaseSRCP00523
PSP
485YPhosphorylationKinaseSRCP00523
PSP
508YPhosphorylationKinaseSRCP00523
PSP
508YPhosphorylationKinaseSRCQ9WUD9
PSP
762YPhosphorylationKinasePTK2O35346
GPS
764YPhosphorylationKinasePTK2O35346
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAR1_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P85A_RATPik3r1physical
12692262
FYN_RATFynphysical
11181827
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BCAR1_RAT

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylation of Crk-associated substrates by focaladhesion kinase. A putative mechanism for the integrin-mediatedtyrosine phosphorylation of Crk-associated substrates.";
Tachibana K., Urano T., Fujita H., Ohashi Y., Kamiguchi K., Iwata S.,Hirai H., Morimoto C.;
J. Biol. Chem. 272:29083-29090(1997).
Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES BY PTK2/FAK1.
"Evidence that SH2 domains promote processive phosphorylation byprotein-tyrosine kinases.";
Mayer B.J., Hirai H., Sakai R.;
Curr. Biol. 5:296-305(1995).
Cited for: PHOSPHORYLATION AT TYR-347 BY ABL1.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory