Search Results

Overview

Uniprot IDQ9H4L7
Protein NameSWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1
Gene NameSMARCAD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
321 SRSQNYPKNATKTKL
335 LKQKFSMKAQNGFNK
346 GFNKKRKKNVFNPKR
77 ETPDNERKASISYFK
84 KASISYFKNQRGIQY

Function

Protein that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization (PubMed:22960744, PubMed:21820097). Combines the ATP-dependent ability to exchange histones, with the chaperone-like ATP-independent activity to deposit histones and assemble nucleosomes (PubMed:21820097). Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs (PubMed:22960744). Required for the restoration of heterochromatin organization after replication (PubMed:21549307). Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing (PubMed:21549307)

Protein Sequence

10 MNLFNLDRFR 20 FEKRNKIEEA 30 PEATPQPSQP 40 GPSSPISLSA 50 EEENAEGEVS 60 RANTPDSDIT 70 EKTEDSSVPE 80 TPDNERKASI 90 SYFKNQRGIQ 100 YIDLSSDSED 110 VVSPNCSNTV 120 QEKTFNKDTV 130 IIVSEPSEDE 140 ESQGLPTMAR 150 RNDDISELED 160 LSELEDLKDA 170 KLQTLKELFP 180 QRSDNDLLKL 190 IESTSTMDGA 200 IAAALLMFGD 210 AGGGPRKRKL 220 SSSSEPYEED 230 EFNDDQSIKK 240 TRLDHGEESN 250 ESAESSSNWE 260 KQESIVLKLQ 270 KEFPNFDKQE 280 LREVLKEHEW 290 MYTEALESLK 300 VFAEDQDMQY 310 VSQSEVPNGK 320 EVSSRSQNYP 330 KNATKTKLKQ 340 KFSMKAQNGF 350 NKKRKKNVFN 360 PKRVVEDSEY 370 DSGSDVGSSL 380 DEDYSSGEEV 390 MEDGYKGKIL 400 HFLQDASIGE 410 LTLIPQCSQK 420 KAQKITELRP 430 FNSWEALFTK 440 MSKTNGLSED 450 LIWHCKTLIQ 460 ERDVVIRLMN 470 KCEDISNKLT 480 KQVTMLTGNG 490 GGWNIEQPSI 500 LNQSLSLKPY 510 QKVGLNWLAL 520 VHKHGLNGIL 530 ADEMGLGKTI 540 QAIAFLAYLY 550 QEGNNGPHLI 560 VVPASTIDNW 570 LREVNLWCPT 580 LKVLCYYGSQ 590 EERKQIRFNI 600 HSRYEDYNVI 610 VTTYNCAISS 620 SDDRSLFRRL 630 KLNYAIFDEG 640 HMLKNMGSIR 650 YQHLMTINAN 660 NRLLLTGTPV 670 QNNLLELMSL 680 LNFVMPHMFS 690 SSTSEIRRMF 700 SSKTKSADEQ 710 SIYEKERIAH 720 AKQIIKPFIL 730 RRVKEEVLKQ 740 LPPKKDRIEL 750 CAMSEKQEQL 760 YLGLFNRLKK 770 SINNLEKNTE 780 MCNVMMQLRK 790 MANHPLLHRQ 800 YYTAEKLKEM 810 SQLMLKEPTH 820 CEANPDLIFE 830 DMEVMTDFEL 840 HVLCKQYRHI 850 NNFQLDMDLI 860 LDSGKFRVLG 870 CILSELKQKG 880 DRVVLFSQFT 890 MMLDILEVLL 900 KHHQHRYLRL 910 DGKTQISERI 920 HLIDEFNTDM 930 DIFVFLLSTK 940 AGGLGINLTS 950 ANVVILHDID 960 CNPYNDKQAE 970 DRCHRVGQTK 980 EVLVIKLISQ 990 GTIEESMLKI 1000 NQQKLKLEQD 1010 MTTVDEGDEG 1020 SMPADIATLL KTSMGL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0043596 nuclear replication fork
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
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:0140674 ATP-dependent histone chaperone activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140750 nucleosome array spacer activity
Molecular Function GO:0043130 ubiquitin binding
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0051304 chromosome separation
Biological Process GO:0000729 DNA double-strand break processing
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0000018 regulation of DNA recombination

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] 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.