Search Results

Overview

Uniprot IDQ96ST3
Protein NamePaired amphipathic helix protein Sin3a
Gene NameSIN3A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1170 DKLECRFKLNSYKMV
396 LSKTTAEKVDSVRND
439 TGTTPPVKKKPKLLN
440 GTTPPVKKKPKLLNL
443 PPVKKKPKLLNLKDS
448 KPKLLNLKDSSMADA
457 SSMADASKHGGGTES
535 VHLETYPKERATEGI
563 SSYRALPKSYQQPKC
569 PKSYQQPKCTGRTPL
602 STFVSSKKTQYEEHI
865 GGSPPKSKLLFSNTA
875 FSNTAAQKLRGMDEV
937 VLGIKRDKSDSPAIQ

Function

Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (By similarity). Required for cortical neuron differentiation and callosal axon elongation (By similarity)

Protein Sequence

10 MKRRLDDQES 20 PVYAAQQRRI 30 PGSTEAFPHQ 40 HRVLAPAPPV 50 YEAVSETMQS 60 ATGIQYSVTP 70 SYQVSAMPQS 80 SGSHGPAIAA 90 VHSSHHHPTA 100 VQPHGGQVVQ 110 SHAHPAPPVA 120 PVQGQQQFQR 130 LKVEDALSYL 140 DQVKLQFGSQ 150 PQVYNDFLDI 160 MKEFKSQSID 170 TPGVISRVSQ 180 LFKGHPDLIM 190 GFNTFLPPGY 200 KIEVQTNDMV 210 NVTTPGQVHQ 220 IPTHGIQPQP 230 QPPPQHPSQP 240 SAQSAPAPAQ 250 PAPQPPPAKV 260 SKPSQLQAHT 270 PASQQTPPLP 280 PYASPRSPPV 290 QPHTPVTISL 300 GTAPSLQNNQ 310 PVEFNHAINY 320 VNKIKNRFQG 330 QPDIYKAFLE 340 ILHTYQKEQR 350 NAKEAGGNYT 360 PALTEQEVYA 370 QVARLFKNQE 380 DLLSEFGQFL 390 PDANSSVLLS 400 KTTAEKVDSV 410 RNDHGGTVKK 420 PQLNNKPQRP 430 SQNGCQIRRH 440 PTGTTPPVKK 450 KPKLLNLKDS 460 SMADASKHGG 470 GTESLFFDKV 480 RKALRSAEAY 490 ENFLRCLVIF 500 NQEVISRAEL 510 VQLVSPFLGK 520 FPELFNWFKN 530 FLGYKESVHL 540 ETYPKERATE 550 GIAMEIDYAS 560 CKRLGSSYRA 570 LPKSYQQPKC 580 TGRTPLCKEV 590 LNDTWVSFPS 600 WSEDSTFVSS 610 KKTQYEEHIY 620 RCEDERFELD 630 VVLETNLATI 640 RVLEAIQKKL 650 SRLSAEEQAK 660 FRLDNTLGGT 670 SEVIHRKALQ 680 RIYADKAADI 690 IDGLRKNPSI 700 AVPIVLKRLK 710 MKEEEWREAQ 720 RGFNKVWREQ 730 NEKYYLKSLD 740 HQGINFKQND 750 TKVLRSKSLL 760 NEIESIYDER 770 QEQATEENAG 780 VPVGPHLSLA 790 YEDKQILEDA 800 AALIIHHVKR 810 QTGIQKEDKY 820 KIKQIMHHFI 830 PDLLFAQRGD 840 LSDVEEEEEE 850 EMDVDEATGA 860 VKKHNGVGGS 870 PPKSKLLFSN 880 TAAQKLRGMD 890 EVYNLFYVNN 900 NWYIFMRLHQ 910 ILCLRLLRIC 920 SQAERQIEEE 930 NREREWEREV 940 LGIKRDKSDS 950 PAIQLRLKEP 960 MDVDVEDYYP 970 AFLDMVRSLL 980 DGNIDSSQYE 990 DSLREMFTIH 1000 AYIAFTMDKL 1010 IQSIVRQLQH 1020 IVSDEICVQV 1030 TDLYLAENNN 1040 GATGGQLNTQ 1050 NSRSLLESTY 1060 QRKAEQLMSD 1070 ENCFKLMFIQ 1080 SQGQVQLTIE 1090 LLDTEEENSD 1100 DPVEAERWSD 1110 YVERYMNSDT 1120 TSPELREHLA 1130 QKPVFLPRNL 1140 RRIRKCQRGR 1150 EQQEKEGKEG 1160 NSKKTMENVD 1170 SLDKLECRFK 1180 LNSYKMVYVI 1190 KSEDYMYRRT 1200 ALLRAHQSHE 1210 RVSKRLHQRF 1220 QAWVDKWTKE 1230 HVPREMAAET 1240 SKWLMGEGLE 1250 GLVPCTTTCD 1260 TETLHFVSIN 1270 KYRVKYGTVF KAP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000118 histone deacetylase complex
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0070822 Sin3-type complex
Cellular Component GO:0017053 transcription repressor complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0140416 transcription regulator inhibitor activity
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:1903351 cellular response to dopamine
Biological Process GO:0072736 cellular response to tert-butyl hydroperoxide
Biological Process GO:0021895 cerebral cortex neuron differentiation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0030336 negative regulation of cell migration
Biological Process GO:0042754 negative regulation of circadian rhythm
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:1900181 negative regulation of protein localization to nucleus
Biological Process GO:1902455 negative regulation of stem cell population maintenance
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0060633 negative regulation of transcription initiation by RNA polymerase II
Biological Process GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
Biological Process GO:0002230 positive regulation of defense response to virus by host
Biological Process GO:0045666 positive regulation of neuron differentiation
Biological Process GO:1902459 positive regulation of stem cell population maintenance
Biological Process GO:0030516 regulation of axon extension
Biological Process GO:0010817 regulation of hormone levels
Biological Process GO:0048511 rhythmic process
Biological Process GO:0060337 type I interferon-mediated signaling pathway

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] 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.

[6] 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.

[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.