Search Results

Overview

Uniprot IDP25440
Protein NameBromodomain-containing protein 2
Gene NameBRD2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
193 ELVVTIPKNSHKKGA
197 TIPKNSHKKGAKLAA
275 PPAQPLAKKKGVKRK
276 PAQPLAKKKGVKRKA
277 AQPLAKKKGVKRKAD
31 PEAAAPGKRIRKPSL
329 RPIKPPRKDLPDSQQ
343 QQHQSSKKGKLSEQL
585 APRPPQPKKSKKASG
589 PQPKKSKKASGSGGG
614 PSGGSGTKLPKKATK
617 GSGTKLPKKATKTAP
733 EELALEKKRELEKRL

Function

Chromatin reader protein that specifically recognizes and binds histone H4 acetylated at 'Lys-5' and 'Lys-12' (H4K5ac and H4K12ac, respectively), thereby controlling gene expression and remodeling chromatin structures (PubMed:17148447, PubMed:17848202, PubMed:18406326, PubMed:20048151, PubMed:20709061, PubMed:20871596). Recruits transcription factors and coactivators to target gene sites, and activates RNA polymerase II machinery for transcriptional elongation (PubMed:28262505). Plays a key role in genome compartmentalization via its association with CTCF and cohesin: recruited to chromatin by CTCF and promotes formation of topologically associating domains (TADs) via its ability to bind acetylated histones, contributing to CTCF boundary formation and enhancer insulation (PubMed:35410381). Also recognizes and binds acetylated non-histone proteins, such as STAT3 (PubMed:28262505). Involved in inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17: recognizes and binds STAT3 acetylated at 'Lys-87', promoting STAT3 recruitment to chromatin (PubMed:28262505). In addition to acetylated lysines, also recognizes and binds lysine residues on histones that are both methylated and acetylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation (PubMed:37731000). Specifically binds histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000)

Protein Sequence

10 MLQNVTPHNK 20 LPGEGNAGLL 30 GLGPEAAAPG 40 KRIRKPSLLY 50 EGFESPTMAS 60 VPALQLTPAN 70 PPPPEVSNPK 80 KPGRVTNQLQ 90 YLHKVVMKAL 100 WKHQFAWPFR 110 QPVDAVKLGL 120 PDYHKIIKQP 130 MDMGTIKRRL 140 ENNYYWAASE 150 CMQDFNTMFT 160 NCYIYNKPTD 170 DIVLMAQTLE 180 KIFLQKVASM 190 PQEEQELVVT 200 IPKNSHKKGA 210 KLAALQGSVT 220 SAHQVPAVSS 230 VSHTALYTPP 240 PEIPTTVLNI 250 PHPSVISSPL 260 LKSLHSAGPP 270 LLAVTAAPPA 280 QPLAKKKGVK 290 RKADTTTPTP 300 TAILAPGSPA 310 SPPGSLEPKA 320 ARLPPMRRES 330 GRPIKPPRKD 340 LPDSQQQHQS 350 SKKGKLSEQL 360 KHCNGILKEL 370 LSKKHAAYAW 380 PFYKPVDASA 390 LGLHDYHDII 400 KHPMDLSTVK 410 RKMENRDYRD 420 AQEFAADVRL 430 MFSNCYKYNP 440 PDHDVVAMAR 450 KLQDVFEFRY 460 AKMPDEPLEP 470 GPLPVSTAMP 480 PGLAKSSSES 490 SSEESSSESS 500 SEEEEEEDEE 510 DEEEEESESS 520 DSEEERAHRL 530 AELQEQLRAV 540 HEQLAALSQG 550 PISKPKRKRE 560 KKEKKKKRKA 570 EKHRGRAGAD 580 EDDKGPRAPR 590 PPQPKKSKKA 600 SGSGGGSAAL 610 GPSGFGPSGG 620 SGTKLPKKAT 630 KTAPPALPTG 640 YDSEEEEESR 650 PMSYDEKRQL 660 SLDINKLPGE 670 KLGRVVHIIQ 680 AREPSLRDSN 690 PEEIEIDFET 700 LKPSTLRELE 710 RYVLSCLRKK 720 PRKPYTIKKP 730 VGKTKEELAL 740 EKKRELEKRL 750 QDVSGQLNST 760 KKPPKKANEK 770 TESSSAQQVA 780 VSRLSASSSS 790 SDSSSSSSSS 800 SSSDTSDSDS G

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0140033 acetylation-dependent protein binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0140015 histone H3K14ac reader activity
Molecular Function GO:0140011 histone H4K12ac reader activity
Molecular Function GO:0140012 histone H4K5ac reader activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Biological Process GO:0140588 chromatin looping
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:2000330 positive regulation of T-helper 17 cell lineage commitment
Biological Process GO:0071168 protein localization to chromatin
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0007283 spermatogenesis

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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.