BCAS1_MOUSE - dbPTM
BCAS1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAS1_MOUSE
UniProt AC Q80YN3
Protein Name Breast carcinoma-amplified sequence 1 homolog
Gene Name Bcas1
Organism Mus musculus (Mouse).
Sequence Length 633
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MGNQMSVPLRPGDQEHDPGADTCKVTSDNECVQNGNPVVLSTRVIQHYEEVDLGISSSKDNVATSSPKTMEAQAVGDASGKNLGKEAKTKAPAARSHFFLTLSRPVPGRPGDQGTDSSAASGRFDVSPSAAPENKDPSEHGALPVAAAPGQAPDKTPGCPEAKQQTLPATGPLAPSPPESQAEAPAQDKDFGFLNRFFKLDKGRESAPVNSQPKEAKGSEDPEQATEAPAVPGNPHGVSAGEDIVDSEQRGQDVDTLSYSVPGDPEVPGTTKEDPQVVDTTENSSSIMSFFKTLVSPNKTETKKDPEDTKATKADSVCDGHAAGQKMSETQAKSKKKRLDSPRLGLSFRKLFRHKDTENSPTTSANLKSDKANFTPQETRGKTKATKSCSPPPPPPEPTSEGRDSGKEKAGPTSLPLGKLFWKKSVKEDTLSTGAEENAVCESPVETVRLEEVESSLQTVDLSEETQPEPTDVKVKEESKPRKTPLMAFLRQMSVRSSEGIPRSEESNVKDSSCQTSNSVEKTPSPPEPEPAGTAQKNKETSSSKDKKSVDKKSATENSKQKNGKQEVREPAPCVQPPTVEANAMQTGDKTPKKSEKRRQSLGGFLKGLGPKRMSDAQVQTDPVSIGPVGKSK
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
127PhosphorylationASGRFDVSPSAAPEN
CCCCCCCCCCCCCCC		18.25-
206PhosphorylationKLDKGRESAPVNSQP
CCCCCCCCCCCCCCC		36.1921454597
211PhosphorylationRESAPVNSQPKEAKG
CCCCCCCCCCCCCCC		48.3621454597
258PhosphorylationGQDVDTLSYSVPGDP
CCCCCCCCEECCCCC		19.9025521595
293PhosphorylationSIMSFFKTLVSPNKT
HHHHHHHHHCCCCCC		27.5122324799
296PhosphorylationSFFKTLVSPNKTETK
HHHHHHCCCCCCCCC		26.3528066266
300PhosphorylationTLVSPNKTETKKDPE
HHCCCCCCCCCCCHH		56.3728066266
303UbiquitinationSPNKTETKKDPEDTK
CCCCCCCCCCHHHCC		49.28-
313UbiquitinationPEDTKATKADSVCDG
HHHCCCCHHHHHHCH		55.87-
316PhosphorylationTKATKADSVCDGHAA
CCCCHHHHHHCHHHH		29.5121930439
326UbiquitinationDGHAAGQKMSETQAK
CHHHHHHHHCHHHHH		43.40-
328PhosphorylationHAAGQKMSETQAKSK
HHHHHHHCHHHHHHH		44.5222817900
330PhosphorylationAGQKMSETQAKSKKK
HHHHHCHHHHHHHHH		26.9022817900
341PhosphorylationSKKKRLDSPRLGLSF
HHHHHCCCCCCCHHH		19.2622324799
347PhosphorylationDSPRLGLSFRKLFRH
CCCCCCHHHHHHHCC		22.6222324799
357PhosphorylationKLFRHKDTENSPTTS
HHHCCCCCCCCCCCC		41.7029899451
360PhosphorylationRHKDTENSPTTSANL
CCCCCCCCCCCCCCC		19.8625521595
363PhosphorylationDTENSPTTSANLKSD
CCCCCCCCCCCCCCC		29.2629899451
364PhosphorylationTENSPTTSANLKSDK
CCCCCCCCCCCCCCC		20.0325521595
368UbiquitinationPTTSANLKSDKANFT
CCCCCCCCCCCCCCC		57.3122790023
369PhosphorylationTTSANLKSDKANFTP
CCCCCCCCCCCCCCC		47.7329899451
371UbiquitinationSANLKSDKANFTPQE
CCCCCCCCCCCCCHH		52.93-
375PhosphorylationKSDKANFTPQETRGK
CCCCCCCCCHHCCCC		24.7025521595
379PhosphorylationANFTPQETRGKTKAT
CCCCCHHCCCCCCCC		39.2025521595
388PhosphorylationGKTKATKSCSPPPPP
CCCCCCCCCCCCCCC		18.5728066266
390PhosphorylationTKATKSCSPPPPPPE
CCCCCCCCCCCCCCC		47.7525521595
399PhosphorylationPPPPPEPTSEGRDSG
CCCCCCCCCCCCCCC		37.4429899451
400PhosphorylationPPPPEPTSEGRDSGK
CCCCCCCCCCCCCCC		49.0929899451
405PhosphorylationPTSEGRDSGKEKAGP
CCCCCCCCCCCCCCC		50.8625521595
413PhosphorylationGKEKAGPTSLPLGKL
CCCCCCCCCCCHHHH		41.8129899451
414PhosphorylationKEKAGPTSLPLGKLF
CCCCCCCCCCHHHHH		30.9922817900
419UbiquitinationPTSLPLGKLFWKKSV
CCCCCHHHHHHCCCC		48.4722790023
425PhosphorylationGKLFWKKSVKEDTLS
HHHHHCCCCCCCCCC		34.3922817900
430PhosphorylationKKSVKEDTLSTGAEE
CCCCCCCCCCCCCHH		24.5722807455
432PhosphorylationSVKEDTLSTGAEENA
CCCCCCCCCCCHHHC		27.2125521595
433PhosphorylationVKEDTLSTGAEENAV
CCCCCCCCCCHHHCC		43.4519060867
443PhosphorylationEENAVCESPVETVRL
HHHCCCCCCCEEEEH		29.1725521595
447PhosphorylationVCESPVETVRLEEVE
CCCCCCEEEEHHHHH		15.9128066266
484PhosphorylationEESKPRKTPLMAFLR
CCCCCCCCHHHHHHH		23.9622817900
494PhosphorylationMAFLRQMSVRSSEGI
HHHHHHHHCCCCCCC		13.1725521595
497PhosphorylationLRQMSVRSSEGIPRS
HHHHHCCCCCCCCCC		30.5025521595
498PhosphorylationRQMSVRSSEGIPRSE
HHHHCCCCCCCCCCH		29.3122324799
504PhosphorylationSSEGIPRSEESNVKD
CCCCCCCCHHCCCCC		40.1220415495
507PhosphorylationGIPRSEESNVKDSSC
CCCCCHHCCCCCCCC		42.7620415495
512PhosphorylationEESNVKDSSCQTSNS
HHCCCCCCCCCCCCC		27.5620415495
513PhosphorylationESNVKDSSCQTSNSV
HCCCCCCCCCCCCCC		22.0029899451
516PhosphorylationVKDSSCQTSNSVEKT
CCCCCCCCCCCCCCC		33.9124925903
517PhosphorylationKDSSCQTSNSVEKTP
CCCCCCCCCCCCCCC		10.9624925903
519PhosphorylationSSCQTSNSVEKTPSP
CCCCCCCCCCCCCCC		31.2729899451
523PhosphorylationTSNSVEKTPSPPEPE
CCCCCCCCCCCCCCC		18.5925521595
525PhosphorylationNSVEKTPSPPEPEPA
CCCCCCCCCCCCCCC		59.3225521595
537AcetylationEPAGTAQKNKETSSS
CCCCCCCCCCCCCCC		68.477713415
579PhosphorylationAPCVQPPTVEANAMQ
CCCCCCCCCCHHHHC		37.3520415495
587PhosphorylationVEANAMQTGDKTPKK
CCHHHHCCCCCCCCH		33.9720415495
591PhosphorylationAMQTGDKTPKKSEKR
HHCCCCCCCCHHHHH		45.1125521595
601PhosphorylationKSEKRRQSLGGFLKG
HHHHHHHHHHHHHHC		27.4625521595
615PhosphorylationGLGPKRMSDAQVQTD
CCCCCCCCCCCCCCC		33.5525521595
621PhosphorylationMSDAQVQTDPVSIGP
CCCCCCCCCCCCCCC		43.3324925903
625PhosphorylationQVQTDPVSIGPVGKS
CCCCCCCCCCCCCCC		27.5024925903
631UbiquitinationVSIGPVGKSK-----
CCCCCCCCCC-----		56.1322790023
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 BCAS1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAS1_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 BCAS1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BCAS1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BCAS1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND MASSSPECTROMETRY.

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