Search Results

Overview

Uniprot ID	Q9NY61
Protein Name	Protein AATF
Gene Name	AATF
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
145	KSRSHSAKTPGFSVQ
380	KTKLASGKLGKGFGA
383	LASGKLGKGFGAFER
58	LVVGSIRKLASASLL
69	ASLLDTDKRYCGKTT
74	TDKRYCGKTTSRKAW

Function

Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date

Protein Sequence

10 MAGPQPLALQ 20 LEQLLNPRPS 30 EADPEADPEE 40 ATAARVIDRF 50 DEGEDGEGDF 60 LVVGSIRKLA 70 SASLLDTDKR 80 YCGKTTSRKA 90 WNEDHWEQTL 100 PGSSDEEISD 110 EEGSGDEDSE 120 GLGLEEYDED 130 DLGAAEEQEC 140 GDHRESKKSR 150 SHSAKTPGFS 160 VQSISDFEKF 170 TKGMDDLGSS 180 EEEEDEESGM 190 EEGDDAEDSQ 200 GESEEDRAGD 210 RNSEDDGVVM 220 TFSSVKVSEE 230 VEKGRAVKNQ 240 IALWDQLLEG 250 RIKLQKALLT 260 TNQLPQPDVF 270 PLFKDKGGPE 280 FSSALKNSHK 290 ALKALLRSLV 300 GLQEELLFQY 310 PDTRYLVDGT 320 KPNAGSEEIS 330 SEDDELVEEK 340 KQQRRRVPAK 350 RKLEMEDYPS 360 FMAKRFADFT 370 VYRNRTLQKW 380 HDKTKLASGK 390 LGKGFGAFER 400 SILTQIDHIL 410 MDKERLLRRT 420 QTKRSVYRVL 430 GKPEPAAQPV 440 PESLPGEPEI 450 LPQAPANAHL 460 KDLDEEIFDD 470 DDFYHQLLRE 480 LIERKTSSLD 490 PNDQVAMGRQ 500 WLAIQKLRSK 510 IHKKVDRKAS 520 KGRKLRFHVL 530 SKLLSFMAPI 540 DHTTMNDDAR 550 TELYRSLFGQ 560 LHPPDEGHGD

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0032040	small-subunit processome
Cellular Component	GO:0005667	transcription regulator complex
Molecular Function	GO:0043522	leucine zipper domain binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0003713	transcription coactivator activity
Biological Process	GO:0030968	endoplasmic reticulum unfolded protein response
Biological Process	GO:0030490	maturation of SSU-rRNA
Biological Process	GO:0042274	ribosomal small subunit biogenesis

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] 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.

[3] 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.

[4] 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.