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Overview

Uniprot IDQ15424
Protein NameScaffold attachment factor B1
Gene NameSAFB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
294 DSLLAVVKREPAEQP
356 DSKEDGRKFDFDACN
423 TTRATDLKNLFSKYG
431 NLFSKYGKVVGAKVV
475 HKTELHGKMISVEKA
489 AKNEPVGKKTSDKRD
54 NVDSSGNKSVLMERL
568 ERTVVMDKSKGVPVI
570 TVVMDKSKGVPVISV
578 GVPVISVKTSGSKER
607 RSVVSFDKVKEPRKS
609 VVSFDKVKEPRKSRD
63 VLMERLKKAIEDEGG
728 DAYWPEAKRAALDER
83 EITSEGNKKTSKRSS
84 ITSEGNKKTSKRSSK
847 GMMDRDHKRWQGGER
87 EGNKKTSKRSSKGRK

Function

Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (PubMed:9671816). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (PubMed:12660241). Thereby acts as a negative regulator of cell proliferation (PubMed:12660241). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity)

Protein Sequence

10 MAETLSGLGD 20 SGAAGAAALS 30 SASSETGTRR 40 LSDLRVIDLR 50 AELRKRNVDS 60 SGNKSVLMER 70 LKKAIEDEGG 80 NPDEIEITSE 90 GNKKTSKRSS 100 KGRKPEEEGV 110 EDNGLEENSG 120 DGQEDVETSL 130 ENLQDIDIMD 140 ISVLDEAEID 150 NGSVADCVED 160 DDADNLQESL 170 SDSRELVEGE 180 MKELPEQLQE 190 HAIEDKETIN 200 NLDTSSSDFT 210 ILQEIEEPSL 220 EPENEKILDI 230 LGETCKSEPV 240 KEESSELEQP 250 FAQDTSSVGP 260 DRKLAEEEDL 270 FDSAHPEEGD 280 LDLASESTAH 290 AQSSKADSLL 300 AVVKREPAEQ 310 PGDGERTDCE 320 PVGLEPAVEQ 330 SSAASELAEA 340 SSEELAEAPT 350 EAPSPEARDS 360 KEDGRKFDFD 370 ACNEVPPAPK 380 ESSTSEGADQ 390 KMSSPEDDSD 400 TKRLSKEEKG 410 RSSCGRNFWV 420 SGLSSTTRAT 430 DLKNLFSKYG 440 KVVGAKVVTN 450 ARSPGARCYG 460 FVTMSTAEEA 470 TKCINHLHKT 480 ELHGKMISVE 490 KAKNEPVGKK 500 TSDKRDSDGK 510 KEKSSNSDRS 520 TNLKRDDKCD 530 RKDDAKKGDD 540 GSGEKSKDQD 550 DQKPGPSERS 560 RATKSGSRGT 570 ERTVVMDKSK 580 GVPVISVKTS 590 GSKERASKSQ 600 DRKSASREKR 610 SVVSFDKVKE 620 PRKSRDSESH 630 SRVRERSERE 640 QRMQAQWERE 650 ERERLEIARE 660 RLAFQRQRLE 670 RERMERERLE 680 RERMHVEHER 690 RREQERIHRE 700 REELRRQQEL 710 RYEQERRPAV 720 RRPYDLDRRD 730 DAYWPEAKRA 740 ALDERYHSDF 750 NRQDRFHDFD 760 HRDRGRYPDH 770 SVDRREGSRS 780 MMGEREGQHY 790 PERHGGPERH 800 GRDSRDGWGG 810 YGSDKRMSEG 820 RGLPPPPRRD 830 WGDHGRREDD 840 RSWQGTADGG 850 MMDRDHKRWQ 860 GGERSMSGHS 870 GPGHMMNRGG 880 MSGRGSFAPG 890 GASRGHPIPH 900 GGMQGGFGGQ 910 SRGSRPSDAR FTRRY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030496 midbody
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0043565 sequence-specific DNA binding
Biological Process GO:0006325 chromatin organization
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0030520 estrogen receptor 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] 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] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.