Search Results

Overview

Uniprot IDQ9UHB7
Protein NameAF4/FMR2 family member 4
Gene NameAFF4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
107 GGSHQSSKWTPVGPA
297 SSKAHLTKLKIPSQP
299 KAHLTKLKIPSQPLD
363 NFGTGEQKRYNPSKT
538 RDSKTIQKGSESGRG
822 PAGPVPSKDPKTEHG
825 PVPSKDPKTEHGSRK

Function

Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression

Protein Sequence

10 MNREDRNVLR 20 MKERERRNQE 30 IQQGEDAFPP 40 SSPLFAEPYK 50 VTSKEDKLSS 60 RIQSMLGNYD 70 EMKDFIGDRS 80 IPKLVAIPKP 90 TVPPSADEKS 100 NPNFFEQRHG 110 GSHQSSKWTP 120 VGPAPSTSQS 130 QKRSSGLQSG 140 HSSQRTSAGS 150 SSGTNSSGQR 160 HDRESYNNSG 170 SSSRKKGQHG 180 SEHSKSRSSS 190 PGKPQAVSSL 200 NSSHSRSHGN 210 DHHSKEHQRS 220 KSPRDPDANW 230 DSPSRVPFSS 240 GQHSTQSFPP 250 SLMSKSNSML 260 QKPTAYVRPM 270 DGQESMEPKL 280 SSEHYSSQSH 290 GNSMTELKPS 300 SKAHLTKLKI 310 PSQPLDASAS 320 GDVSCVDEIL 330 KEMTHSWPPP 340 LTAIHTPCKT 350 EPSKFPFPTK 360 ESQQSNFGTG 370 EQKRYNPSKT 380 SNGHQSKSML 390 KDDLKLSSSE 400 DSDGEQDCDK 410 TMPRSTPGSN 420 SEPSHHNSEG 430 ADNSRDDSSS 440 HSGSESSSGS 450 DSESESSSSD 460 SEANEPSQSA 470 SPEPEPPPTN 480 KWQLDNWLNK 490 VNPHKVSPAS 500 SVDSNIPSSQ 510 GYKKEGREQG 520 TGNSYTDTSG 530 PKETSSATPG 540 RDSKTIQKGS 550 ESGRGRQKSP 560 AQSDSTTQRR 570 TVGKKQPKKA 580 EKAAAEEPRG 590 GLKIESETPV 600 DLASSMPSSR 610 HKAATKGSRK 620 PNIKKESKSS 630 PRPTAEKKKY 640 KSTSKSSQKS 650 REIIETDTSS 660 SDSDESESLP 670 PSSQTPKYPE 680 SNRTPVKPSS 690 VEEEDSFFRQ 700 RMFSPMEEKE 710 LLSPLSEPDD 720 RYPLIVKIDL 730 NLLTRIPGKP 740 YKETEPPKGE 750 KKNVPEKHTR 760 EAQKQASEKV 770 SNKGKRKHKN 780 EDDNRASESK 790 KPKTEDKNSA 800 GHKPSSNRES 810 SKQSAAKEKD 820 LLPSPAGPVP 830 SKDPKTEHGS 840 RKRTISQSSS 850 LKSSSNSNKE 860 TSGSSKNSSS 870 TSKQKKTEGK 880 TSSSSKEVKE 890 KAPSSSSNCP 900 PSAPTLDSSK 910 PRRTKLVFDD 920 RNYSADHYLQ 930 EAKKLKHNAD 940 ALSDRFEKAV 950 YYLDAVVSFI 960 ECGNALEKNA 970 QESKSPFPMY 980 SETVDLIKYT 990 MKLKNYLAPD 1000 ATAADKRLTV 1010 LCLRCESLLY 1020 LRLFKLKKEN 1030 ALKYSKTLTE 1040 HLKNSYNNSQ 1050 APSPGLGSKA 1060 VGMPSPVSPK 1070 LSPGNSGNYS 1080 SGASSASASG 1090 SSVTIPQKIH 1100 QMAASYVQVT 1110 SNFLYATEIW 1120 DQAEQLSKEQ 1130 KEFFAELDKV 1140 MGPLIFNASI 1150 MTDLVRYTRQ 1160 GLHWLRQDAK LIS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000791 euchromatin
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0032783 super elongation complex
Cellular Component GO:0008023 transcription elongation factor complex
Molecular Function GO:0003712 transcription coregulator activity
Biological Process GO:0006354 DNA-templated transcription elongation
Biological Process GO:0050877 nervous system process
Biological Process GO:0006355 regulation of DNA-templated transcription

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] 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.