BARD1_MOUSE - dbPTM
BARD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BARD1_MOUSE
UniProt AC O70445
Protein Name BRCA1-associated RING domain protein 1
Gene Name Bard1
Organism Mus musculus (Mouse).
Sequence Length 765
Subcellular Localization Nucleus . Cytoplasm . Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs)
recruitment to DNA damage sites is mediated by the BRCA1-A complex.
Protein Description E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage..
Protein Sequence MPRRPPRVCSGNQPAPVPAMEPATDGLWAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHDNKDSKDNTSRASLFGDAERKKNSIKMWFSPRSKKVRYVVTKVSVQTQPQKAKDDKAQEASMYEFVSATPPVAVPKSAKTASRTSAKKHPKKSVAKINREENLRPETKDSRFDSKEELKEEKVVSCSQIPVMERPRVNGEIDLLASGSVVEPECSGSLTEVSLPLAEHIVSPDTVSKNEETPEKKVCVKDLRSGGSNGNRKGCHRPTTSTSDSCGSNIPSTSRGIGEPALLAENVVLVDCSSLPSGQLQVDVTLRRKSNASDDPLSLSPGTPPPLLNNSTHRQMMSSPSTVKLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNAVNIFGVRPVDYTDNENIRSLLLLPEENESFSTSQCSIVNTGQRKNGPLVFIGSGLSSQQQKMLSKLETVLKAKKCMEFDSTVTHVIVPDEEAQSTLKCMLGILSGCWILKFDWVKACLDSKVREQEEKYEVPGGPQRSRLNREQLLPKLFDGCYFFLGGNFKHHPRDDLLKLIAAAGGKVLSRKPKPDSDVTQTINTVAYHAKPESDQRFCTQYIVYEDLFNCHPERVRQGKVWMAPSTWLISCIMAFELLPLDS
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
119PhosphorylationNKDSKDNTSRASLFG
CCCCCCCCCHHHHHC		29.7129550500
120PhosphorylationKDSKDNTSRASLFGD
CCCCCCCCHHHHHCC		31.9129550500
123PhosphorylationKDNTSRASLFGDAER
CCCCCHHHHHCCHHH		24.1128066266
140PhosphorylationNSIKMWFSPRSKKVR
CCCEEEECCCCCCEE		12.1426643407
148PhosphorylationPRSKKVRYVVTKVSV
CCCCCEEEEEEEEEE		11.4020139300
179PhosphorylationMYEFVSATPPVAVPK
HHHHHHCCCCCCCCC		22.1825266776
187PhosphorylationPPVAVPKSAKTASRT
CCCCCCCCCCCCCCC		29.0023140645
190PhosphorylationAVPKSAKTASRTSAK
CCCCCCCCCCCCCCH		29.5823140645
192PhosphorylationPKSAKTASRTSAKKH
CCCCCCCCCCCCHHC		41.1223140645
194PhosphorylationSAKTASRTSAKKHPK
CCCCCCCCCCHHCCC		30.4623140645
195PhosphorylationAKTASRTSAKKHPKK
CCCCCCCCCHHCCCH		36.6623140645
237PhosphorylationEEKVVSCSQIPVMER
HHCCEECCCCCCCCC		24.5230482847
368PhosphorylationDVTLRRKSNASDDPL
EEEEECCCCCCCCCC		35.5026745281
371PhosphorylationLRRKSNASDDPLSLS
EECCCCCCCCCCCCC		46.9629550500
376PhosphorylationNASDDPLSLSPGTPP
CCCCCCCCCCCCCCC		31.9925266776
378PhosphorylationSDDPLSLSPGTPPPL
CCCCCCCCCCCCCCC		20.2226745281
381PhosphorylationPLSLSPGTPPPLLNN
CCCCCCCCCCCCCCC		35.6928973931
390PhosphorylationPPLLNNSTHRQMMSS
CCCCCCHHHHHHCCC		24.1729550500
396PhosphorylationSTHRQMMSSPSTVKL
HHHHHHCCCCCCEEE		33.4826745281
397PhosphorylationTHRQMMSSPSTVKLS
HHHHHCCCCCCEEEC		12.6526745281
399PhosphorylationRQMMSSPSTVKLSSG
HHHCCCCCCEEECCC		48.0228066266
400PhosphorylationQMMSSPSTVKLSSGM
HHCCCCCCEEECCCC		25.6628066266
415DimethylationPARKRNHRGETLLHI
CCCCCCCCCCCEEHH		48.47-
543PhosphorylationENESFSTSQCSIVNT
CCCCCCCCCCEECCC		28.1725266776
546PhosphorylationSFSTSQCSIVNTGQR
CCCCCCCEECCCCCC		23.18-
563PhosphorylationGPLVFIGSGLSSQQQ
CCEEEECCCCCHHHH		31.5725777480
566PhosphorylationVFIGSGLSSQQQKML
EEECCCCCHHHHHHH		29.6225777480
567PhosphorylationFIGSGLSSQQQKMLS
EECCCCCHHHHHHHH		36.7325777480
692PhosphorylationAAGGKVLSRKPKPDS
HCCCCEECCCCCCCC		41.0427357545
722PhosphorylationESDQRFCTQYIVYED
HHHCCCEEEEECHHH		22.99-
724PhosphorylationDQRFCTQYIVYEDLF
HCCCEEEEECHHHHH		3.68-
727PhosphorylationFCTQYIVYEDLFNCH
CEEEEECHHHHHCCC		8.31-
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 BARD1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BARD1_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 BARD1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHS_MOUSEPcbd1physical
20211142
BRCA1_HUMANBRCA1physical
9798686
P53_MOUSETrp53physical
11779501
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BARD1_MOUSE

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Related Literatures of Post-Translational Modification

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