Search Results

Overview

Uniprot IDQ92922
Protein NameSWI/SNF complex subunit SMARCC1
Gene NameSMARCC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
345 ESRKKSGKKGQASLY
346 SRKKSGKKGQASLYG
354 GQASLYGKRRSQKEE
387 IEEVVLPKNVNLKKD
392 LPKNVNLKKDSENTP
393 PKNVNLKKDSENTPV
608 LRTDIYSKKTLAKSK
609 RTDIYSKKTLAKSKG
880 ALASAATKAKHLAAV
882 ASAATKAKHLAAVEE

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. May stimulate the ATPase activity of the catalytic subunit of the complex (PubMed:10078207, PubMed:29374058). 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)

Protein Sequence

10 MAAAAGGGGP 20 GTAVGATGSG 30 IAAAAAGLAV 40 YRRKDGGPAT 50 KFWESPETVS 60 QLDSVRVWLG 70 KHYKKYVHAD 80 APTNKTLAGL 90 VVQLLQFQED 100 AFGKHVTNPA 110 FTKLPAKCFM 120 DFKAGGALCH 130 ILGAAYKYKN 140 EQGWRRFDLQ 150 NPSRMDRNVE 160 MFMNIEKTLV 170 QNNCLTRPNI 180 YLIPDIDLKL 190 ANKLKDIIKR 200 HQGTFTDEKS 210 KASHHIYPYS 220 SSQDDEEWLR 230 PVMRKEKQVL 240 VHWGFYPDSY 250 DTWVHSNDVD 260 AEIEDPPIPE 270 KPWKVHVKWI 280 LDTDIFNEWM 290 NEEDYEVDEN 300 RKPVSFRQRI 310 STKNEEPVRS 320 PERRDRKASA 330 NARKRKHSPS 340 PPPPTPTESR 350 KKSGKKGQAS 360 LYGKRRSQKE 370 EDEQEDLTKD 380 MEDPTPVPNI 390 EEVVLPKNVN 400 LKKDSENTPV 410 KGGTVADLDE 420 QDEETVTAGG 430 KEDEDPAKGD 440 QSRSVDLGED 450 NVTEQTNHII 460 IPSYASWFDY 470 NCIHVIERRA 480 LPEFFNGKNK 490 SKTPEIYLAY 500 RNFMIDTYRL 510 NPQEYLTSTA 520 CRRNLTGDVC 530 AVMRVHAFLE 540 QWGLVNYQVD 550 PESRPMAMGP 560 PPTPHFNVLA 570 DTPSGLVPLH 580 LRSPQVPAAQ 590 QMLNFPEKNK 600 EKPVDLQNFG 610 LRTDIYSKKT 620 LAKSKGASAG 630 REWTEQETLL 640 LLEALEMYKD 650 DWNKVSEHVG 660 SRTQDECILH 670 FLRLPIEDPY 680 LENSDASLGP 690 LAYQPVPFSQ 700 SGNPVMSTVA 710 FLASVVDPRV 720 ASAAAKAALE 730 EFSRVREEVP 740 LELVEAHVKK 750 VQEAARASGK 760 VDPTYGLESS 770 CIAGTGPDEP 780 EKLEGAEEEK 790 MEADPDGQQP 800 EKAENKVENE 810 TDEGDKAQDG 820 ENEKNSEKEQ 830 DSEVSEDTKS 840 EEKETEENKE 850 LTDTCKERES 860 DTGKKKVEHE 870 ISEGNVATAA 880 AAALASAATK 890 AKHLAAVEER 900 KIKSLVALLV 910 ETQMKKLEIK 920 LRHFEELETI 930 MDREKEALEQ 940 QRQQLLTERQ 950 NFHMEQLKYA 960 ELRARQQMEQ 970 QQHGQNPQQA 980 HQHSGGPGLA 990 PLGAAGHPGM 1000 MPHQQPPPYP 1010 LMHHQMPPPH 1020 PPQPGQIPGP 1030 GSMMPGQHMP 1040 GRMIPTVAAN 1050 IHPSGSGPTP 1060 PGMPPMPGNI 1070 LGPRVPLTAP 1080 NGMYPPPPQQ 1090 QPPPPPPADG 1100 VPPPPAPGPP ASAAP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
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:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0016514 SWI/SNF complex
Cellular Component GO:0001741 XY body
Molecular Function GO:0003682 chromatin binding
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:0045596 negative regulation of cell differentiation
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:0008284 positive regulation of cell population proliferation
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:1902459 positive regulation of stem cell population maintenance
Biological Process GO:0045582 positive regulation of T cell differentiation
Biological Process GO:0030850 prostate gland development
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 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] 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.

[3] 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.

[4] 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.

[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] 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.