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Overview

Uniprot IDQ9UIF9
Protein NameBromodomain adjacent to zinc finger domain protein 2A
Gene NameBAZ2A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1746 PKRGQKRKSGYSLNF
1786 EEGLSPSKRRRLSMR
680 RGRPPKVKITELLNK
687 KITELLNKTDNRPLK
695 TDNRPLKKLEAQETL

Function

Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity). In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription (By similarity). Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (By similarity). Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity)

Protein Sequence

10 MEMEANDHFN 20 FTGLPPAPAA 30 SGLKPSPSSG 40 EGLYTNGSPM 50 NFPQQGKSLN 60 GDVNVNGLST 70 VSHTTTSGIL 80 NSAPHSSSTS 90 HLHHPSVAYD 100 CLWNYSQYPS 110 ANPGSNLKDP 120 PLLSQFSGGQ 130 YPLNGILGGS 140 RQPSSPSHNT 150 NLRAGSQEFW 160 ANGTQSPMGL 170 NFDSQELYDS 180 FPDQNFEVMP 190 NGPPSFFTSP 200 QTSPMLGSSI 210 QTFAPSQEVG 220 SGIHPDEAAE 230 KEMTSVVAEN 240 GTGLVGSLEL 250 EEEQPELKMC 260 GYNGSVPSVE 270 SLHQEVSVLV 280 PDPTVSCLDD 290 PSHLPDQLED 300 TPILSEDSLE 310 PFNSLAPEPV 320 SGGLYGIDDT 330 ELMGAEDKLP 340 LEDSPVISAL 350 DCPSLNNATA 360 FSLLADDSQT 370 STSIFASPTS 380 PPVLGESVLQ 390 DNSFDLNNGS 400 DAEQEEMETQ 410 SSDFPPSLTQ 420 PAPDQSSTIQ 430 LHPATSPAVS 440 PTTSPAVSLV 450 VSPAASPEIS 460 PEVCPAASTV 470 VSPAVFSVVS 480 PASSAVLPAV 490 SLEVPLTASV 500 TSPKASPVTS 510 PAAAFPTASP 520 ANKDVSSFLE 530 TTADVEEITG 540 EGLTASGSGD 550 VMRRRIATPE 560 EVRLPLQHGW 570 RREVRIKKGS 580 HRWQGETWYY 590 GPCGKRMKQF 600 PEVIKYLSRN 610 VVHSVRREHF 620 SFSPRMPVGD 630 FFEERDTPEG 640 LQWVQLSAEE 650 IPSRIQAITG 660 KRGRPRNTEK 670 AKTKEVPKVK 680 RGRGRPPKVK 690 ITELLNKTDN 700 RPLKKLEAQE 710 TLNEEDKAKI 720 AKSKKKMRQK 730 VQRGECQTTI 740 QGQARNKRKQ 750 ETKSLKQKEA 760 KKKSKAEKEK 770 GKTKQEKLKE 780 KVKREKKEKV 790 KMKEKEEVTK 800 AKPACKADKT 810 LATQRRLEER 820 QRQQMILEEM 830 KKPTEDMCLT 840 DHQPLPDFSR 850 VPGLTLPSGA 860 FSDCLTIVEF 870 LHSFGKVLGF 880 DPAKDVPSLG 890 VLQEGLLCQG 900 DSLGEVQDLL 910 VRLLKAALHD 920 PGFPSYCQSL 930 KILGEKVSEI 940 PLTRDNVSEI 950 LRCFLMAYGV 960 EPALCDRLRT 970 QPFQAQPPQQ 980 KAAVLAFLVH 990 ELNGSTLIIN 1000 EIDKTLESMS 1010 SYRKNKWIVE 1020 GRLRRLKTVL 1030 AKRTGRSEVE 1040 MEGPEECLGR 1050 RRSSRIMEET 1060 SGMEEEEEEE 1070 SIAAVPGRRG 1080 RRDGEVDATA 1090 SSIPELERQI 1100 EKLSKRQLFF 1110 RKKLLHSSQM 1120 LRAVSLGQDR 1130 YRRRYWVLPY 1140 LAGIFVEGTE 1150 GNLVPEEVIK 1160 KETDSLKVAA 1170 HASLNPALFS 1180 MKMELAGSNT 1190 TASSPARARG 1200 RPRKTKPGSM 1210 QPRHLKSPVR 1220 GQDSEQPQAQ 1230 LQPEAQLHAP 1240 AQPQPQLQLQ 1250 LQSHKGFLEQ 1260 EGSPLSLGQS 1270 QHDLSQSAFL 1280 SWLSQTQSHS 1290 SLLSSSVLTP 1300 DSSPGKLDPA 1310 PSQPPEEPEP 1320 DEAESSPDPQ 1330 ALWFNISAQM 1340 PCNAAPTPPP 1350 AVSEDQPTPS 1360 PQQLASSKPM 1370 NRPSAANPCS 1380 PVQFSSTPLA 1390 GLAPKRRAGD 1400 PGEMPQSPTG 1410 LGQPKRRGRP 1420 PSKFFKQMEQ 1430 RYLTQLTAQP 1440 VPPEMCSGWW 1450 WIRDPEMLDA 1460 MLKALHPRGI 1470 REKALHKHLN 1480 KHRDFLQEVC 1490 LRPSADPIFE 1500 PRQLPAFQEG 1510 IMSWSPKEKT 1520 YETDLAVLQW 1530 VEELEQRVIM 1540 SDLQIRGWTC 1550 PSPDSTREDL 1560 AYCEHLSDSQ 1570 EDITWRGRGR 1580 EGLAPQRKTT 1590 NPLDLAVMRL 1600 AALEQNVERR 1610 YLREPLWPTH 1620 EVVLEKALLS 1630 TPNGAPEGTT 1640 TEISYEITPR 1650 IRVWRQTLER 1660 CRSAAQVCLC 1670 LGQLERSIAW 1680 EKSVNKVTCL 1690 VCRKGDNDEF 1700 LLLCDGCDRG 1710 CHIYCHRPKM 1720 EAVPEGDWFC 1730 TVCLAQQVEG 1740 EFTQKPGFPK 1750 RGQKRKSGYS 1760 LNFSEGDGRR 1770 RRVLLRGRES 1780 PAAGPRYSEE 1790 GLSPSKRRRL 1800 SMRNHHSDLT 1810 FCEIILMEME 1820 SHDAAWPFLE 1830 PVNPRLVSGY 1840 RRIIKNPMDF 1850 STMRERLLRG 1860 GYTSSEEFAA 1870 DALLVFDNCQ 1880 TFNEDDSEVG 1890 KAGHIMRRFF 1900 ESRWEEFYQG KQANL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005677 chromatin silencing complex
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005634 nucleus
Cellular Component GO:0033553 rDNA heterochromatin
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0140046 histone H4K16ac reader activity
Molecular Function GO:0016922 nuclear receptor binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0000183 rDNA heterochromatin formation
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0001188 RNA polymerase I preinitiation complex assembly

Reference

[1] 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.

[2] 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.