Search Results

Overview

Uniprot IDQ8TAQ2
Protein NameSWI/SNF complex subunit SMARCC2
Gene NameSMARCC2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
317 EAKKKNAKKGPSTPY
318 AKKKNAKKGPSTPYT
326 GPSTPYTKSKRGHRE
328 STPYTKSKRGHREEE
365 PKTVNTKKDSESAPV
584 LRTDMYTKKNVPSKS
585 RTDMYTKKNVPSKSK
874 AAAAVKAKHLAAVEE

Function

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:11018012). Can stimulate the ATPase activity of the catalytic subunit of these complexes (PubMed:10078207). May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells (PubMed:12192000). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Critical regulator of myeloid differentiation, controlling granulocytopoiesis and the expression of genes involved in neutrophil granule formation (By similarity)

Protein Sequence

10 MAVRKKDGGP 20 NVKYYEAADT 30 VTQFDNVRLW 40 LGKNYKKYIQ 50 AEPPTNKSLS 60 SLVVQLLQFQ 70 EEVFGKHVSN 80 APLTKLPIKC 90 FLDFKAGGSL 100 CHILAAAYKF 110 KSDQGWRRYD 120 FQNPSRMDRN 130 VEMFMTIEKS 140 LVQNNCLSRP 150 NIFLCPEIEP 160 KLLGKLKDII 170 KRHQGTVTED 180 KNNASHVVYP 190 VPGNLEEEEW 200 VRPVMKRDKQ 210 VLLHWGYYPD 220 SYDTWIPASE 230 IEASVEDAPT 240 PEKPRKVHAK 250 WILDTDTFNE 260 WMNEEDYEVN 270 DDKNPVSRRK 280 KISAKTLTDE 290 VNSPDSDRRD 300 KKGGNYKKRK 310 RSPSPSPTPE 320 AKKKNAKKGP 330 STPYTKSKRG 340 HREEEQEDLT 350 KDMDEPSPVP 360 NVEEVTLPKT 370 VNTKKDSESA 380 PVKGGTMTDL 390 DEQEDESMET 400 TGKDEDENST 410 GNKGEQTKNP 420 DLHEDNVTEQ 430 THHIIIPSYA 440 AWFDYNSVHA 450 IERRALPEFF 460 NGKNKSKTPE 470 IYLAYRNFMI 480 DTYRLNPQEY 490 LTSTACRRNL 500 AGDVCAIMRV 510 HAFLEQWGLI 520 NYQVDAESRP 530 TPMGPPPTSH 540 FHVLADTPSG 550 LVPLQPKTPQ 560 QTSASQQMLN 570 FPDKGKEKPT 580 DMQNFGLRTD 590 MYTKKNVPSK 600 SKAAASATRE 610 WTEQETLLLL 620 EALEMYKDDW 630 NKVSEHVGSR 640 TQDECILHFL 650 RLPIEDPYLE 660 DSEASLGPLA 670 YQPIPFSQSG 680 NPVMSTVAFL 690 ASVVDPRVAS 700 AAAKSALEEF 710 SKMKEEVPTA 720 LVEAHVRKVE 730 EAAKVTGKAD 740 PAFGLESSGI 750 AGTTSDEPER 760 IEESGNDEAR 770 VEGQATDEKK 780 EPKEPREGGG 790 AIEEEAKEKT 800 SEAPKKDEEK 810 GKEGDSEKES 820 EKSDGDPIVD 830 PEKEKEPKEG 840 QEEVLKEVVE 850 SEGERKTKVE 860 RDIGEGNLST 870 AAAAALAAAA 880 VKAKHLAAVE 890 ERKIKSLVAL 900 LVETQMKKLE 910 IKLRHFEELE 920 TIMDREREAL 930 EYQRQQLLAD 940 RQAFHMEQLK 950 YAEMRARQQH 960 FQQMHQQQQQ 970 PPPALPPGSQ 980 PIPPTGAAGP 990 PAVHGLAVAP 1000 ASVVPAPAGS 1010 GAPPGSLGPS 1020 EQIGQAGSTA 1030 GPQQQQPAGA 1040 PQPGAVPPGV 1050 PPPGPHGPSP 1060 FPNQQTPPSM 1070 MPGAVPGSGH 1080 PGVAGNAPLG 1090 LPFGMPPPPP 1100 PPAPSIIPFG 1110 SLADSISINL 1120 PAPPNLHGHH 1130 HHLPFAPGTL 1140 PPPNLPVSMA 1150 NPLHPNLPAT 1160 TTMPSSLPLG 1170 PGLGSAAAQS 1180 PAIVAAVQGN 1190 LLPSASPLPD 1200 PGTPLPPDPT 1210 APSPGTVTPV PPPQ

Gene Ontology

Classification GO ID Description
Biological Process GO:0045582 positive regulation of T cell differentiation
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0071565 nBAF complex
Cellular Component GO:0071564 npBAF complex
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0016514 SWI/SNF complex
Molecular Function GO:0042393 histone binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0007399 nervous system development
Biological Process GO:0006337 nucleosome disassembly
Biological Process GO:0045597 positive regulation of cell differentiation
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:2000781 positive regulation of double-strand break repair
Biological Process GO:0045663 positive regulation of myoblast differentiation
Biological Process GO:0070316 regulation of G0 to G1 transition
Biological Process GO:2000045 regulation of G1/S transition of mitotic cell cycle
Biological Process GO:0030071 regulation of mitotic metaphase/anaphase transition
Biological Process GO:2000819 regulation of nucleotide-excision repair
Biological Process GO:0006357 regulation of transcription by RNA polymerase II

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[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] 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.

[5] 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.

[6] 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.

[7] 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.