Search Results

Overview

Uniprot IDO60264
Protein NameSWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
Gene NameSMARCA5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1036 KPSTQKRKMDGAPDG
132 PRIKKDEKQNLLSVG
647 QNLNKIGKDEMLQMI
694 EMNEKLSKMGESSLR
739 EPPKRERKANYAVDA
758 ALRVSEPKAPKAPRP
929 DTKIGRYKAPFHQLR

Function

ATPase that possesses intrinsic ATP-dependent nucleosome-remodeling activity (PubMed:12972596, PubMed:28801535). Catalytic subunit of 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; this may require intact histone H4 tails (PubMed:10880450, PubMed:12198550, PubMed:12434153, PubMed:12972596, PubMed:23911928, PubMed:28801535). Within the ISWI chromatin-remodeling complexes, slides edge- and center-positioned histone octamers away from their original location on the DNA template (PubMed:28801535). Catalytic activity and histone octamer sliding propensity is regulated and determined by components of the ISWI chromatin-remodeling complexes (PubMed:28801535). The BAZ1A/ACF1-, BAZ1B/WSTF-, BAZ2A/TIP5- and BAZ2B-containing ISWI chromatin-remodeling complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template in an ATP-dependent manner (PubMed:14759371, PubMed:15543136, PubMed:28801535). The CECR2- and RSF1-containing ISWI chromatin-remodeling complexes do not have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Binds to core histones together with RSF1, and is required for the assembly of regular nucleosome arrays by the RSF-5 ISWI chromatin-remodeling complex (PubMed:12972596). Involved in DNA replication and together with BAZ1A/ACF1 is required for replication of pericentric heterochromatin in S-phase (PubMed:12434153). Probably plays a role in repression of RNA polymerase I dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter (By similarity). Essential component of the WICH-5 ISWI chromatin-remodeling complex (also called the WICH complex), a chromatin-remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure (PubMed:11980720, PubMed:15543136). The WICH-5 ISWI chromatin-remodeling complex regulates the transcription of various genes, has a role in RNA polymerase I transcription (By similarity). Within the B-WICH complex has a role in RNA polymerase III transcription (PubMed:16603771). Mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes (By similarity). Essential component of NoRC-5 ISWI chromatin-remodeling complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity)

Protein Sequence

10 MSSAAEPPPP 20 PPPESAPSKP 30 AASIASGGSN 40 SSNKGGPEGV 50 AAQAVASAAS 60 AGPADAEMEE 70 IFDDASPGKQ 80 KEIQEPDPTY 90 EEKMQTDRAN 100 RFEYLLKQTE 110 LFAHFIQPAA 120 QKTPTSPLKM 130 KPGRPRIKKD 140 EKQNLLSVGD 150 YRHRRTEQEE 160 DEELLTESSK 170 ATNVCTRFED 180 SPSYVKWGKL 190 RDYQVRGLNW 200 LISLYENGIN 210 GILADEMGLG 220 KTLQTISLLG 230 YMKHYRNIPG 240 PHMVLVPKST 250 LHNWMSEFKR 260 WVPTLRSVCL 270 IGDKEQRAAF 280 VRDVLLPGEW 290 DVCVTSYEML 300 IKEKSVFKKF 310 NWRYLVIDEA 320 HRIKNEKSKL 330 SEIVREFKTT 340 NRLLLTGTPL 350 QNNLHELWSL 360 LNFLLPDVFN 370 SADDFDSWFD 380 TNNCLGDQKL 390 VERLHMVLRP 400 FLLRRIKADV 410 EKSLPPKKEV 420 KIYVGLSKMQ 430 REWYTRILMK 440 DIDILNSAGK 450 MDKMRLLNIL 460 MQLRKCCNHP 470 YLFDGAEPGP 480 PYTTDMHLVT 490 NSGKMVVLDK 500 LLPKLKEQGS 510 RVLIFSQMTR 520 VLDILEDYCM 530 WRNYEYCRLD 540 GQTPHDERQD 550 SINAYNEPNS 560 TKFVFMLSTR 570 AGGLGINLAT 580 ADVVILYDSD 590 WNPQVDLQAM 600 DRAHRIGQTK 610 TVRVFRFITD 620 NTVEERIVER 630 AEMKLRLDSI 640 VIQQGRLVDQ 650 NLNKIGKDEM 660 LQMIRHGATH 670 VFASKESEIT 680 DEDIDGILER 690 GAKKTAEMNE 700 KLSKMGESSL 710 RNFTMDTESS 720 VYNFEGEDYR 730 EKQKIAFTEW 740 IEPPKRERKA 750 NYAVDAYFRE 760 ALRVSEPKAP 770 KAPRPPKQPN 780 VQDFQFFPPR 790 LFELLEKEIL 800 FYRKTIGYKV 810 PRNPELPNAA 820 QAQKEEQLKI 830 DEAESLNDEE 840 LEEKEKLLTQ 850 GFTNWNKRDF 860 NQFIKANEKW 870 GRDDIENIAR 880 EVEGKTPEEV 890 IEYSAVFWER 900 CNELQDIEKI 910 MAQIERGEAR 920 IQRRISIKKA 930 LDTKIGRYKA 940 PFHQLRISYG 950 TNKGKNYTEE 960 EDRFLICMLH 970 KLGFDKENVY 980 DELRQCIRNS 990 PQFRFDWFLK 1000 SRTAMELQRR 1010 CNTLITLIER 1020 ENMELEEKEK 1030 AEKKKRGPKP 1040 STQKRKMDGA 1050 PDGRGRKKKL KL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0090537 CERF complex
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005677 chromatin silencing complex
Cellular Component GO:0000793 condensed chromosome
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016589 NURF complex
Cellular Component GO:0005721 pericentric heterochromatin
Cellular Component GO:0031213 RSF complex
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140658 ATP-dependent chromatin remodeler activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0004386 helicase activity
Molecular Function GO:0140751 histone octamer slider activity
Molecular Function GO:0140750 nucleosome array spacer activity
Molecular Function GO:0031491 nucleosome binding
Biological Process GO:0140374 antiviral innate immune response
Biological Process GO:0006325 chromatin organization
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006346 DNA methylation-dependent constitutive heterochromatin formation
Biological Process GO:0006281 DNA repair
Biological Process GO:0006352 DNA-templated transcription initiation
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:1905213 negative regulation of mitotic chromosome condensation
Biological Process GO:0016479 negative regulation of transcription by RNA polymerase I
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0045740 positive regulation of DNA replication
Biological Process GO:0045943 positive regulation of transcription by RNA polymerase I
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045945 positive regulation of transcription by RNA polymerase III
Biological Process GO:0000183 rDNA heterochromatin formation
Biological Process GO:0006275 regulation of DNA replication
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0006357 regulation of transcription by RNA polymerase II

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] 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] 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.

[6] 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.