Search Results

Overview

Uniprot IDO00268
Protein NameTranscription initiation factor TFIID subunit 4
Gene NameTAF4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1019 IGPRKKRKVDCPGPG
817 AQAAAAQKNKLKEPG
819 AAAAQKNKLKEPGGG
821 AAQKNKLKEPGGGSF

Function

The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:10594036, PubMed:33795473, PubMed:8942982). TAF4 may maintain an association between the TFIID and TFIIA complexes, while bound to the promoter, together with TBP, during PIC assembly (PubMed:33795473). Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone (PubMed:9192867)

Protein Sequence

10 MAAGSDLLDE 20 VFFNSEVDEK 30 VVSDLVGSLE 40 SQLAASAAHH 50 HHLAPRTPEV 60 RAAAAGALGN 70 HVVSGSPAGA 80 AGAGPAAPAE 90 GAPGAAPEPP 100 PAGRARPGGG 110 GPQRPGPPSP 120 RRPLVPAGPA 130 PPAAKLRPPP 140 EGSAGSCAPV 150 PAAAAVAAGP 160 EPAPAGPAKP 170 AGPAALAARA 180 GPGPGPGPGP 190 GPGPGPGKPA 200 GPGAAQTLNG 210 SAALLNSHHA 220 AAPAVSLVNN 230 GPAALLPLPK 240 PAAPGTVIQT 250 PPFVGAAAPP 260 APAAPSPPAA 270 PAPAAPAAAP 280 PPPPPAPATL 290 ARPPGHPAGP 300 PTAAPAVPPP 310 AAAQNGGSAG 320 AAPAPAPAAG 330 GPAGVSGQPG 340 PGAAAAAPAP 350 GVKAESPKRV 360 VQAAPPAAQT 370 LAASGPASTA 380 ASMVIGPTMQ 390 GALPSPAAVP 400 PPAPGTPTGL 410 PKGAAGAVTQ 420 SLSRTPTATT 430 SGIRATLTPT 440 VLAPRLPQPP 450 QNPTNIQNFQ 460 LPPGMVLVRS 470 ENGQLLMIPQ 480 QALAQMQAQA 490 HAQPQTTMAP 500 RPATPTSAPP 510 VQISTVQAPG 520 TPIIARQVTP 530 TTIIKQVSQA 540 QTTVQPSATL 550 QRSPGVQPQL 560 VLGGAAQTAS 570 LGTATAVQTG 580 TPQRTVPGAT 590 TTSSAATETM 600 ENVKKCKNFL 610 STLIKLASSG 620 KQSTETAANV 630 KELVQNLLDG 640 KIEAEDFTSR 650 LYRELNSSPQ 660 PYLVPFLKRS 670 LPALRQLTPD 680 SAAFIQQSQQ 690 QPPPPTSQAT 700 TALTAVVLSS 710 SVQRTAGKTA 720 ATVTSALQPP 730 VLSLTQPTQV 740 GVGKQGQPTP 750 LVIQQPPKPG 760 ALIRPPQVTL 770 TQTPMVALRQ 780 PHNRIMLTTP 790 QQIQLNPLQP 800 VPVVKPAVLP 810 GTKALSAVSA 820 QAAAAQKNKL 830 KEPGGGSFRD 840 DDDINDVASM 850 AGVNLSEESA 860 RILATNSELV 870 GTLTRSCKDE 880 TFLLQAPLQR 890 RILEIGKKHG 900 ITELHPDVVS 910 YVSHATQQRL 920 QNLVEKISET 930 AQQKNFSYKD 940 DDRYEQASDV 950 RAQLKFFEQL 960 DQIEKQRKDE 970 QEREILMRAA 980 KSRSRQEDPE 990 QLRLKQKAKE 1000 MQQQELAQMR 1010 QRDANLTALA 1020 AIGPRKKRKV 1030 DCPGPGSGAE 1040 GSGPGSVVPG 1050 SSGVGTPRQF 1060 TRQRITRVNL 1070 RDLIFCLENE 1080 RETSHSLLLY KAFLK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0071339 MLL1 complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0005669 transcription factor TFIID complex
Cellular Component GO:0033276 transcription factor TFTC complex
Molecular Function GO:0017162 aryl hydrocarbon receptor binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0046982 protein heterodimerization activity
Biological Process GO:0006352 DNA-templated transcription initiation
Biological Process GO:0042789 mRNA transcription by RNA polymerase II
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0060261 positive regulation of transcription initiation by RNA polymerase II
Biological Process GO:0006282 regulation of DNA repair
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0051123 RNA polymerase II preinitiation complex assembly
Biological Process GO:0006366 transcription by RNA polymerase II
Biological Process GO:0006367 transcription initiation at RNA polymerase II promoter

Reference

[1] 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.

[2] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[3] 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.