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Overview

Uniprot IDP18846
Protein NameCyclic AMP-dependent transcription factor ATF-1
Gene NameATF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
239 RKKKEYVKCLENRVA
66 ARRPSYRKILKDLSS
69 PSYRKILKDLSSEDT

Function

This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation

Protein Sequence

10 MEDSHKSTTS 20 ETAPQPGSAV 30 QGAHISHIAQ 40 QVSSLSESEE 50 SQDSSDSIGS 60 SQKAHGILAR 70 RPSYRKILKD 80 LSSEDTRGRK 90 GDGENSGVSA 100 AVTSMSVPTP 110 IYQTSSGQYI 120 AIAPNGALQL 130 ASPGTDGVQG 140 LQTLTMTNSG 150 STQQGTTILQ 160 YAQTSDGQQI 170 LVPSNQVVVQ 180 TASGDMQTYQ 190 IRTTPSATSL 200 PQTVVMTSPV 210 TLTSQTTKTD 220 DPQLKREIRL 230 MKNREAAREC 240 RRKKKEYVKC 250 LENRVAVLEN 260 QNKTLIEELK 270 TLKDLYSNKS V

Gene Ontology

Classification GO ID Description
Cellular Component GO:1990590 ATF1-ATF4 transcription factor complex
Cellular Component GO:1990589 ATF4-CREB1 transcription factor complex
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific
Molecular Function GO:0003700 DNA-binding transcription factor activity
Molecular Function GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
Biological Process GO:0141156 cAMP/PKA signal transduction
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045740 positive regulation of DNA replication
Biological Process GO:0010976 positive regulation of neuron projection development
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0032025 response to cobalt ion
Biological Process GO:0014074 response to purine-containing compound

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 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.

[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] 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.

[6] 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.