Search Results

Overview

Uniprot IDQ9NYF8
Protein NameBcl-2-associated transcription factor 1
Gene NameBCLAF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
303 PSRRSPAKTIAPQNA
332 GGDQETAKTGKFLKR
335 QETAKTGKFLKRFTD
413 EDYRQFRKSVLADQG
421 SVLADQGKSFATASH
437 NTEEEGLKYKSKVSL
439 EEEGLKYKSKVSLKG
441 EGLKYKSKVSLKGNR
445 YKSKVSLKGNRESDG
457 SDGFREEKNYKLKET
462 EEKNYKLKETGYVVE
475 VERPSTTKDKHKEED
477 RPSTTKDKHKEEDKN
492 SERITVKKETQSPEQ
517 DYSPPLHKNLDAREK
536 EESPLRIKMIASDSH
548 DSHRPEVKLKMAPVP
550 HRPEVKLKMAPVPLD
567 NRPASLTKDRLLAST
580 STLVHSVKKEQEFRS
593 RSIFDHIKLPQASKS
676 AGEERVFKEENQKGD
681 VFKEENQKGDKKLRC
728 RKQEKTPKDYKEYKS
731 EKTPKDYKEYKSYKD
734 PKDYKEYKSYKDDSK
737 YKEYKSYKDDSKHKR
778 KEREEEFKTHHEMKE
831 TTFQKRPKEEEWDPE
842 WDPEYTPKSKKYFLH
844 PEYTPKSKKYFLHDD
845 EYTPKSKKYFLHDDR
891 SPKWTHDKYQGDGIV

Function

Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA

Protein Sequence

10 MGRSNSRSHS 20 SRSKSRSQSS 30 SRSRSRSHSR 40 KKRYSSRSRS 50 RTYSRSRSRD 60 RMYSRDYRRD 70 YRNNRGMRRP 80 YGYRGRGRGY 90 YQGGGGRYHR 100 GGYRPVWNRR 110 HSRSPRRGRS 120 RSRSPKRRSV 130 SSQRSRSRSR 140 RSYRSSRSPR 150 SSSSRSSSPY 160 SKSPVSKRRG 170 SQEKQTKKAE 180 GEPQEESPLK 190 SKSQEEPKDT 200 FEHDPSESID 210 EFNKSSATSG 220 DIWPGLSAYD 230 NSPRSPHSPS 240 PIATPPSQSS 250 SCSDAPMLST 260 VHSAKNTPSQ 270 HSHSIQHSPE 280 RSGSGSVGNG 290 SSRYSPSQNS 300 PIHHIPSRRS 310 PAKTIAPQNA 320 PRDESRGRSS 330 FYPDGGDQET 340 AKTGKFLKRF 350 TDEESRVFLL 360 DRGNTRDKEA 370 SKEKGSEKGR 380 AEGEWEDQEA 390 LDYFSDKESG 400 KQKFNDSEGD 410 DTEETEDYRQ 420 FRKSVLADQG 430 KSFATASHRN 440 TEEEGLKYKS 450 KVSLKGNRES 460 DGFREEKNYK 470 LKETGYVVER 480 PSTTKDKHKE 490 EDKNSERITV 500 KKETQSPEQV 510 KSEKLKDLFD 520 YSPPLHKNLD 530 AREKSTFREE 540 SPLRIKMIAS 550 DSHRPEVKLK 560 MAPVPLDDSN 570 RPASLTKDRL 580 LASTLVHSVK 590 KEQEFRSIFD 600 HIKLPQASKS 610 TSESFIQHIV 620 SLVHHVKEQY 630 FKSAAMTLNE 640 RFTSYQKATE 650 EHSTRQKSPE 660 IHRRIDISPS 670 TLRKHTRLAG 680 EERVFKEENQ 690 KGDKKLRCDS 700 ADLRHDIDRR 710 RKERSKERGD 720 SKGSRESSGS 730 RKQEKTPKDY 740 KEYKSYKDDS 750 KHKREQDHSR 760 SSSSSASPSS 770 PSSREEKESK 780 KEREEEFKTH 790 HEMKEYSGFA 800 GVSRPRGTFF 810 RIRGRGRARG 820 VFAGTNTGPN 830 NSNTTFQKRP 840 KEEEWDPEYT 850 PKSKKYFLHD 860 DRDDGVDYWA 870 KRGRGRGTFQ 880 RGRGRFNFKK 890 SGSSPKWTHD 900 KYQGDGIVED 910 EEETMENNEE 920 KKDRRKEEKE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016592 mediator complex
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003712 transcription coregulator activity
Biological Process GO:0006915 apoptotic process
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0048255 mRNA stabilization
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:2000144 positive regulation of DNA-templated transcription initiation
Biological Process GO:2001244 positive regulation of intrinsic apoptotic signaling pathway
Biological Process GO:0045944 positive 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] 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.

[4] 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.

[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.