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Overview

Uniprot IDQ9Y5B9
Protein NameFACT complex subunit SPT16
Gene NameSUPT16H
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1021 RSMSRKRKASVHSSG
1043 RHSSAPPKKKRK***
185 GELNLMKKAASITSE
424 VLTSVKKKVKNVGIF
426 TSVKKKVKNVGIFLK
479 EKRRAHQKELAAQLN
490 AQLNEEAKRRLTEQK
497 KRRLTEQKGEQQIQK
504 KGEQQIQKARKSNVS
513 RKSNVSYKNPSLMPK
92 LKQIANTKGNENANG

Function

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II)

Protein Sequence

10 MAVTLDKDAY 20 YRRVKRLYSN 30 WRKGEDEYAN 40 VDAIVVSVGV 50 DEEIVYAKST 60 ALQTWLFGYE 70 LTDTIMVFCD 80 DKIIFMASKK 90 KVEFLKQIAN 100 TKGNENANGA 110 PAITLLIREK 120 NESNKSSFDK 130 MIEAIKESKN 140 GKKIGVFSKD 150 KFPGEFMKSW 160 NDCLNKEGFD 170 KIDISAVVAY 180 TIAVKEDGEL 190 NLMKKAASIT 200 SEVFNKFFKE 210 RVMEIVDADE 220 KVRHSKLAES 230 VEKAIEEKKY 240 LAGADPSTVE 250 MCYPPIIQSG 260 GNYNLKFSVV 270 SDKNHMHFGA 280 ITCAMGIRFK 290 SYCSNLVRTL 300 MVDPSQEVQE 310 NYNFLLQLQE 320 ELLKELRHGV 330 KICDVYNAVM 340 DVVKKQKPEL 350 LNKITKNLGF 360 GMGIEFREGS 370 LVINSKNQYK 380 LKKGMVFSIN 390 LGFSDLTNKE 400 GKKPEEKTYA 410 LFIGDTVLVD 420 EDGPATVLTS 430 VKKKVKNVGI 440 FLKNEDEEEE 450 EEEKDEAEDL 460 LGRGSRAALL 470 TERTRNEMTA 480 EEKRRAHQKE 490 LAAQLNEEAK 500 RRLTEQKGEQ 510 QIQKARKSNV 520 SYKNPSLMPK 530 EPHIREMKIY 540 IDKKYETVIM 550 PVFGIATPFH 560 IATIKNISMS 570 VEGDYTYLRI 580 NFYCPGSALG 590 RNEGNIFPNP 600 EATFVKEITY 610 RASNIKAPGE 620 QTVPALNLQN 630 AFRIIKEVQK 640 RYKTREAEEK 650 EKEGIVKQDS 660 LVINLNRSNP 670 KLKDLYIRPN 680 IAQKRMQGSL 690 EAHVNGFRFT 700 SVRGDKVDIL 710 YNNIKHALFQ 720 PCDGEMIIVL 730 HFHLKNAIMF 740 GKKRHTDVQF 750 YTEVGEITTD 760 LGKHQHMHDR 770 DDLYAEQMER 780 EMRHKLKTAF 790 KNFIEKVEAL 800 TKEELEFEVP 810 FRDLGFNGAP 820 YRSTCLLQPT 830 SSALVNATEW 840 PPFVVTLDEV 850 ELIHFERVQF 860 HLKNFDMVIV 870 YKDYSKKVTM 880 INAIPVASLD 890 PIKEWLNSCD 900 LKYTEGVQSL 910 NWTKIMKTIV 920 DDPEGFFEQG 930 GWSFLEPEGE 940 GSDAEEGDSE 950 SEIEDETFNP 960 SEDDYEEEEE 970 DSDEDYSSEA 980 EESDYSKESL 990 GSEEESGKDW 1000 DELEEEARKA 1010 DRESRYEEEE 1020 EQSRSMSRKR 1030 KASVHSSGRG 1040 SNRGSRHSSA PPKKKRK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035101 FACT complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0031491 nucleosome binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006281 DNA repair
Biological Process GO:0006260 DNA replication
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0006337 nucleosome disassembly
Biological Process GO:0032786 positive regulation of DNA-templated transcription, elongation
Biological Process GO:0032784 regulation of DNA-templated transcription elongation
Biological Process GO:0006366 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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[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.