UniProt ID | BARD1_HUMAN | |
---|---|---|
UniProt AC | Q99728 | |
Protein Name | BRCA1-associated RING domain protein 1 | |
Gene Name | BARD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 777 | |
Subcellular Localization |
Nucleus. During S phase of the cell cycle, colocalizes with BRCA1 into discrete subnuclear foci. 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 BRC |
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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 | MPDNRQPRNRQPRIRSGNEPRSAPAMEPDGRGAWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLRNLLHDNELSDLKEDKPRKSLFNDAGNKKNSIKMWFSPRSKKVRYVVSKASVQTQPAIKKDASAQQDSYEFVSPSPPADVSERAKKASARSGKKQKKKTLAEINQKWNLEAEKEDGEFDSKEESKQKLVSFCSQPSVISSPQINGEIDLLASGSLTESECFGSLTEVSLPLAEQIESPDTKSRNEVVTPEKVCKNYLTSKKSLPLENNGKRGHHNRLSSPISKRCRTSILSTSGDFVKQTVPSENIPLPECSSPPSCKRKVGGTSGRKNSNMSDEFISLSPGTPPSTLSSSSYRRVMSSPSAMKLLPNMAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVDYTDDESMKSLLLLPEKNESSSASHCSVMNTGQRRDGPLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAVQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQEEKYEIPEGPRRSRLNREQLLPKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYHARPDSDQRFCTQYIIYEDLCNYHPERVRQGKVWKAPSSWFIDCVMSFELLPLDS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
46 | Sumoylation | AALDRLEKLLRCSRC HHHHHHHHHHHCCCC | 58.37 | - | |
46 | Sumoylation | AALDRLEKLLRCSRC HHHHHHHHHHHCCCC | 58.37 | - | |
103 | O-linked_Glycosylation | KINRQLDSMIQLCSK HHHHHHHHHHHHHHH | 26.78 | 30379171 | |
110 | Ubiquitination | SMIQLCSKLRNLLHD HHHHHHHHHHHHHCC | 50.93 | - | |
124 | Acetylation | DNELSDLKEDKPRKS CCCHHHHCCCCCCHH | 69.71 | 20167786 | |
124 | Ubiquitination | DNELSDLKEDKPRKS CCCHHHHCCCCCCHH | 69.71 | - | |
130 | Ubiquitination | LKEDKPRKSLFNDAG HCCCCCCHHHCCCCC | 61.10 | - | |
139 | Ubiquitination | LFNDAGNKKNSIKMW HCCCCCCCCCCEEEE | 53.03 | - | |
144 | Sumoylation | GNKKNSIKMWFSPRS CCCCCCEEEEECCCC | 29.87 | - | |
144 | Sumoylation | GNKKNSIKMWFSPRS CCCCCCEEEEECCCC | 29.87 | - | |
148 | Phosphorylation | NSIKMWFSPRSKKVR CCEEEEECCCCCCEE | 12.14 | 21712546 | |
152 | Acetylation | MWFSPRSKKVRYVVS EEECCCCCCEEEEEE | 57.47 | 7338441 | |
160 | Ubiquitination | KVRYVVSKASVQTQP CEEEEEEHHHHHCCC | 32.83 | 21890473 | |
160 | Sumoylation | KVRYVVSKASVQTQP CEEEEEEHHHHHCCC | 32.83 | 28112733 | |
170 | Ubiquitination | VQTQPAIKKDASAQQ HHCCCCCCCCCCCCC | 46.86 | - | |
170 | Sumoylation | VQTQPAIKKDASAQQ HHCCCCCCCCCCCCC | 46.86 | - | |
170 | Sumoylation | VQTQPAIKKDASAQQ HHCCCCCCCCCCCCC | 46.86 | 28112733 | |
171 | Ubiquitination | QTQPAIKKDASAQQD HCCCCCCCCCCCCCC | 53.03 | - | |
174 | Phosphorylation | PAIKKDASAQQDSYE CCCCCCCCCCCCCCC | 36.42 | 26074081 | |
179 | Phosphorylation | DASAQQDSYEFVSPS CCCCCCCCCCCCCCC | 23.40 | 22199227 | |
180 | Phosphorylation | ASAQQDSYEFVSPSP CCCCCCCCCCCCCCC | 22.98 | 26074081 | |
184 | Phosphorylation | QDSYEFVSPSPPADV CCCCCCCCCCCCCCH | 25.61 | 25159151 | |
186 | Phosphorylation | SYEFVSPSPPADVSE CCCCCCCCCCCCHHH | 35.69 | 25159151 | |
192 | Phosphorylation | PSPPADVSERAKKAS CCCCCCHHHHHHHHH | 23.16 | 30576142 | |
217 | Sumoylation | TLAEINQKWNLEAEK HHHHHHHHHCHHHHH | 33.29 | - | |
217 | Ubiquitination | TLAEINQKWNLEAEK HHHHHHHHHCHHHHH | 33.29 | - | |
217 | Sumoylation | TLAEINQKWNLEAEK HHHHHHHHHCHHHHH | 33.29 | - | |
224 | Ubiquitination | KWNLEAEKEDGEFDS HHCHHHHHCCCCCCC | 69.06 | - | |
244 | Phosphorylation | QKLVSFCSQPSVISS HHHHHHHCCCCCCCC | 43.02 | - | |
250 | Phosphorylation | CSQPSVISSPQINGE HCCCCCCCCCCCCCE | 33.53 | 26074081 | |
251 | Phosphorylation | SQPSVISSPQINGEI CCCCCCCCCCCCCEE | 15.08 | 26074081 | |
279 | Phosphorylation | FGSLTEVSLPLAEQI HCCCEEEEHHHHHHC | 20.31 | 26074081 | |
288 | Phosphorylation | PLAEQIESPDTKSRN HHHHHCCCCCCCCCC | 29.70 | 26074081 | |
291 | Phosphorylation | EQIESPDTKSRNEVV HHCCCCCCCCCCCCC | 34.01 | 26074081 | |
293 | Phosphorylation | IESPDTKSRNEVVTP CCCCCCCCCCCCCCH | 42.29 | 26552605 | |
299 | Phosphorylation | KSRNEVVTPEKVCKN CCCCCCCCHHHHHHH | 30.79 | 23401153 | |
305 | Sumoylation | VTPEKVCKNYLTSKK CCHHHHHHHHHCCCC | 52.17 | - | |
305 | Sumoylation | VTPEKVCKNYLTSKK CCHHHHHHHHHCCCC | 52.17 | - | |
307 | Phosphorylation | PEKVCKNYLTSKKSL HHHHHHHHHCCCCCC | 9.24 | - | |
311 | Acetylation | CKNYLTSKKSLPLEN HHHHHCCCCCCCCCC | 40.94 | 25953088 | |
313 | Phosphorylation | NYLTSKKSLPLENNG HHHCCCCCCCCCCCC | 38.67 | 25159151 | |
329 | Phosphorylation | RGHHNRLSSPISKRC CCCCCCCCCCHHHHH | 30.72 | 30266825 | |
330 | Phosphorylation | GHHNRLSSPISKRCR CCCCCCCCCHHHHHH | 30.74 | 23401153 | |
333 | Phosphorylation | NRLSSPISKRCRTSI CCCCCCHHHHHHHHH | 19.89 | 20068231 | |
338 | Phosphorylation | PISKRCRTSILSTSG CHHHHHHHHHHHCCC | 24.60 | 23186163 | |
339 | Phosphorylation | ISKRCRTSILSTSGD HHHHHHHHHHHCCCC | 11.37 | 23186163 | |
342 | Phosphorylation | RCRTSILSTSGDFVK HHHHHHHHCCCCHHH | 20.89 | 29116813 | |
343 | Phosphorylation | CRTSILSTSGDFVKQ HHHHHHHCCCCHHHC | 33.03 | 23186163 | |
344 | Phosphorylation | RTSILSTSGDFVKQT HHHHHHCCCCHHHCC | 32.75 | 21815630 | |
351 | Phosphorylation | SGDFVKQTVPSENIP CCCHHHCCCCCCCCC | 28.77 | 26552605 | |
354 | Phosphorylation | FVKQTVPSENIPLPE HHHCCCCCCCCCCCC | 38.65 | 26552605 | |
363 | Phosphorylation | NIPLPECSSPPSCKR CCCCCCCCCCCCCCC | 44.19 | 23401153 | |
364 | Phosphorylation | IPLPECSSPPSCKRK CCCCCCCCCCCCCCC | 53.11 | 22167270 | |
367 | Phosphorylation | PECSSPPSCKRKVGG CCCCCCCCCCCCCCC | 35.34 | 22167270 | |
371 | Acetylation | SPPSCKRKVGGTSGR CCCCCCCCCCCCCCC | 30.63 | 20167786 | |
381 | Phosphorylation | GTSGRKNSNMSDEFI CCCCCCCCCCCCCCC | 36.62 | 22199227 | |
384 | Phosphorylation | GRKNSNMSDEFISLS CCCCCCCCCCCCCCC | 37.93 | 28634120 | |
389 | Phosphorylation | NMSDEFISLSPGTPP CCCCCCCCCCCCCCC | 28.28 | 28450419 | |
391 | Phosphorylation | SDEFISLSPGTPPST CCCCCCCCCCCCCCC | 17.94 | 25159151 | |
394 | Phosphorylation | FISLSPGTPPSTLSS CCCCCCCCCCCCCCC | 35.10 | 25159151 | |
397 | Phosphorylation | LSPGTPPSTLSSSSY CCCCCCCCCCCCHHH | 43.09 | 28450419 | |
398 | Phosphorylation | SPGTPPSTLSSSSYR CCCCCCCCCCCHHHH | 36.11 | 28450419 | |
400 | Phosphorylation | GTPPSTLSSSSYRRV CCCCCCCCCHHHHHH | 28.41 | 28450419 | |
401 | Phosphorylation | TPPSTLSSSSYRRVM CCCCCCCCHHHHHHH | 26.81 | 28450419 | |
402 | Phosphorylation | PPSTLSSSSYRRVMS CCCCCCCHHHHHHHC | 28.19 | 28450419 | |
403 | Phosphorylation | PSTLSSSSYRRVMSS CCCCCCHHHHHHHCC | 25.30 | 28450419 | |
404 | Phosphorylation | STLSSSSYRRVMSSP CCCCCHHHHHHHCCH | 12.37 | 28450419 | |
409 | Phosphorylation | SSYRRVMSSPSAMKL HHHHHHHCCHHHHHH | 35.92 | 30266825 | |
410 | Phosphorylation | SYRRVMSSPSAMKLL HHHHHHCCHHHHHHC | 12.55 | 30266825 | |
412 | Phosphorylation | RRVMSSPSAMKLLPN HHHHCCHHHHHHCCC | 42.83 | 30266825 | |
423 | Sumoylation | LLPNMAVKRNHRGET HCCCCCCCCCCCCCE | 37.63 | - | |
423 | Ubiquitination | LLPNMAVKRNHRGET HCCCCCCCCCCCCCE | 37.63 | 21890473 | |
423 | Sumoylation | LLPNMAVKRNHRGET HCCCCCCCCCCCCCE | 37.63 | 28112733 | |
430 | Phosphorylation | KRNHRGETLLHIASI CCCCCCCEEEEEEEE | 37.13 | - | |
443 | Phosphorylation | SIKGDIPSVEYLLQN EECCCCCCHHHHHHC | 28.10 | - | |
446 | Phosphorylation | GDIPSVEYLLQNGSD CCCCCHHHHHHCCCC | 15.57 | - | |
457 | Ubiquitination | NGSDPNVKDHAGWTP CCCCCCHHCCCCCCH | 50.89 | - | |
484 | Ubiquitination | VELLLQHKALVNTTG HHHHHHCHHHHCCCC | 30.38 | - | |
496 | Phosphorylation | TTGYQNDSPLHDAAK CCCCCCCCCHHHHHH | 36.59 | 25159151 | |
538 | Phosphorylation | VDYTDDESMKSLLLL CCCCCCHHHHHHEEC | 38.21 | 26074081 | |
541 | Phosphorylation | TDDESMKSLLLLPEK CCCHHHHHHEECCCC | 18.66 | 26074081 | |
548 | Ubiquitination | SLLLLPEKNESSSAS HHEECCCCCCCCCCC | 65.16 | - | |
548 | Sumoylation | SLLLLPEKNESSSAS HHEECCCCCCCCCCC | 65.16 | - | |
548 | Sumoylation | SLLLLPEKNESSSAS HHEECCCCCCCCCCC | 65.16 | 28112733 | |
551 | Phosphorylation | LLPEKNESSSASHCS ECCCCCCCCCCCCCE | 38.70 | 26552605 | |
552 | Phosphorylation | LPEKNESSSASHCSV CCCCCCCCCCCCCEE | 24.60 | 26552605 | |
553 | Phosphorylation | PEKNESSSASHCSVM CCCCCCCCCCCCEEC | 42.97 | 26552605 | |
555 | Phosphorylation | KNESSSASHCSVMNT CCCCCCCCCCEECCC | 27.29 | 26552605 | |
558 | Phosphorylation | SSSASHCSVMNTGQR CCCCCCCEECCCCCC | 20.98 | 26552605 | |
562 | Phosphorylation | SHCSVMNTGQRRDGP CCCEECCCCCCCCCC | 19.32 | 26552605 | |
586 | Phosphorylation | SEQQKMLSELAVILK HHHHHHHHHHHHHHH | 27.37 | - | |
596 | Ubiquitination | AVILKAKKYTEFDST HHHHHHHHCCCCCCC | 63.36 | - | |
650 | Ubiquitination | KVCEQEEKYEIPEGP HHHHHHHHCCCCCCC | 47.64 | - | |
660 | Phosphorylation | IPEGPRRSRLNREQL CCCCCCCCCCCHHHH | 42.26 | 17081983 | |
688 | Ubiquitination | GTFKHHPKDNLIKLV CCCCCCCCCCEEEEE | 55.69 | - | |
704 | Phosphorylation | AGGGQILSRKPKPDS CCCCCCCCCCCCCCC | 39.63 | 27251275 | |
714 | Phosphorylation | PKPDSDVTQTINTVA CCCCCCHHHHEEEEE | 25.61 | 16651405 | |
719 | Phosphorylation | DVTQTINTVAYHARP CHHHHEEEEEHHCCC | 11.58 | 24719451 | |
734 | Phosphorylation | DSDQRFCTQYIIYED CCCCCCEEEEEHHHH | 22.99 | 16651405 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
148 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
148 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
251 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
251 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
288 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
288 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
299 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
299 | T | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
714 | T | Phosphorylation | Kinase | ATM | Q13315 | GPS |
714 | T | Phosphorylation | Kinase | ATR | Q13535 | GPS |
734 | T | Phosphorylation | Kinase | ATM | Q13315 | GPS |
734 | T | Phosphorylation | Kinase | ATR | Q13535 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | BRCA1 | P38398 | PMID:19117993 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BARD1_HUMAN !! |
* 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_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"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-186; SER-391 ANDTHR-394, AND MASS SPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, 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-148; SER-391 ANDTHR-394, AND MASS SPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-423, AND MASSSPECTROMETRY. |