Search Results

Overview

Uniprot IDQ96RL1
Protein NameBRCA1-A complex subunit RAP80
Gene NameUIMC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
245 GRGSAFLKAVQGSGD
31 TTSSVSVKRKRRLED
372 RASDWHSKTKDFQES
428 SVAALTSKRSLVLMP
544 RQKEAKTKSDSGTAA
607 ACSTVEGKWQQRLKN
697 DCLVDFKKQVTVQPG

Function

Ubiquitin-binding protein (PubMed:24627472). Specifically recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19328070, Ref.38). Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1

Protein Sequence

10 MPRRKKKVKE 20 VSESRNLEKK 30 DVETTSSVSV 40 KRKRRLEDAF 50 IVISDSDGEE 60 PKEENGLQKT 70 KTKQSNRAKC 80 LAKRKIAQMT 90 EEEQFALALK 100 MSEQEAREVN 110 SQEEEEEELL 120 RKAIAESLNS 130 CRPSDASATR 140 SRPLATGPSS 150 QSHQEKTTDS 160 GLTEGIWQLV 170 PPSLFKGSHI 180 SQGNEAEERE 190 EPWDHTEKTE 200 EEPVSGSSGS 210 WDQSSQPVFE 220 NVNVKSFDRC 230 TGHSAEHTQC 240 GKPQESTGRG 250 SAFLKAVQGS 260 GDTSRHCLPT 270 LADAKGLQDT 280 GGTVNYFWGI 290 PFCPDGVDPN 300 QYTKVILCQL 310 EVYQKSLKMA 320 QRQLLNKKGF 330 GEPVLPRPPS 340 LIQNECGQGE 350 QASEKNECIS 360 EDMGDEDKEE 370 RQESRASDWH 380 SKTKDFQESS 390 IKSLKEKLLL 400 EEEPTTSHGQ 410 SSQGIVEETS 420 EEGNSVPASQ 430 SVAALTSKRS 440 LVLMPESSAE 450 EITVCPETQL 460 SSSETFDLER 470 EVSPGSRDIL 480 DGVRIIMADK 490 EVGNKEDAEK 500 EVAISTFSSS 510 NQVSCPLCDQ 520 CFPPTKIERH 530 AMYCNGLMEE 540 DTVLTRRQKE 550 AKTKSDSGTA 560 AQTSLDIDKN 570 EKCYLCKSLV 580 PFREYQCHVD 590 SCLQLAKADQ 600 GDGPEGSGRA 610 CSTVEGKWQQ 620 RLKNPKEKGH 630 SEGRLLSFLE 640 QSEHKTSDAD 650 IKSSETGAFR 660 VPSPGMEEAG 670 CSREMQSSFT 680 RRDLNESPVK 690 SFVSISEATD 700 CLVDFKKQVT 710 VQPGSRTRTK AGRGRRRKF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070531 BRCA1-A complex
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0070530 K63-linked polyubiquitin modification-dependent protein binding
Molecular Function GO:0061649 ubiquitin-modified histone reader activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0140861 DNA repair-dependent chromatin remodeling
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0007095 mitotic G2 DNA damage checkpoint signaling
Biological Process GO:0044818 mitotic G2/M transition checkpoint
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0045739 positive regulation of DNA repair
Biological Process GO:0006282 regulation of DNA repair
Biological Process GO:0010212 response to ionizing radiation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.