Search Results

Overview

Uniprot IDP67809
Protein NameY-box-binding protein 1
Gene NameYBX1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
137 GVPVQGSKYAADRNH
301 NPKPQDGKETKAADP
81 FINRNDTKEDVFVHQ
92 FVHQTAIKKNNPRKY
93 VHQTAIKKNNPRKYL

Function

DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation (PubMed:10817758, PubMed:11698476, PubMed:14718551, PubMed:18809583, PubMed:31358969, PubMed:8188694). Predominantly acts as a RNA-binding protein: binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C) (PubMed:19561594, PubMed:31358969). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting the mRNA stability maintainer ELAVL1, thereby preventing mRNA decay (PubMed:10817758, PubMed:11698476, PubMed:31358969). Component of the CRD-mediated complex that promotes MYC mRNA stability (PubMed:19029303). Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs (PubMed:27559612, PubMed:29073095). Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (PubMed:28341602, PubMed:29073095). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs (PubMed:29712925). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (PubMed:12604611). Binds to TSC22D1 transcripts, thereby inhibiting their translation and negatively regulating TGF-beta-mediated transcription of COL1A2 (By similarity). Also able to bind DNA: regulates transcription of the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7' (PubMed:18809583). Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (PubMed:18809583, PubMed:8188694). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin (PubMed:14718551). Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair (PubMed:14718551). The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (PubMed:19483673)

Protein Sequence

10 MSSEAETQQP 20 PAAPPAAPAL 30 SAADTKPGTT 40 GSGAGSGGPG 50 GLTSAAPAGG 60 DKKVIATKVL 70 GTVKWFNVRN 80 GYGFINRNDT 90 KEDVFVHQTA 100 IKKNNPRKYL 110 RSVGDGETVE 120 FDVVEGEKGA 130 EAANVTGPGG 140 VPVQGSKYAA 150 DRNHYRRYPR 160 RRGPPRNYQQ 170 NYQNSESGEK 180 NEGSESAPEG 190 QAQQRRPYRR 200 RRFPPYYMRR 210 PYGRRPQYSN 220 PPVQGEVMEG 230 ADNQGAGEQG 240 RPVRQNMYRG 250 YRPRFRRGPP 260 RQRQPREDGN 270 EEDKENQGDE 280 TQGQQPPQRR 290 YRRNFNYRRR 300 RPENPKPQDG 310 KETKAADPPA 320 ENSSAPEAEQ GGAE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070937 CRD-mediated mRNA stability complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0071204 histone pre-mRNA 3'end processing complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000932 P-body
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0045202 synapse
Cellular Component GO:0005689 U12-type spliceosomal complex
Molecular Function GO:0062153 C5-methylcytidine-containing RNA reader activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0051020 GTPase binding
Molecular Function GO:0035198 miRNA binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003676 nucleic acid binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:1990837 sequence-specific double-stranded DNA binding
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0070934 CRD-mediated mRNA stabilization
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0048598 embryonic morphogenesis
Biological Process GO:0008544 epidermis development
Biological Process GO:1990428 miRNA transport
Biological Process GO:0006397 mRNA processing
Biological Process GO:0048255 mRNA stabilization
Biological Process GO:2000773 negative regulation of cellular senescence
Biological Process GO:1900152 negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Biological Process GO:0017148 negative regulation of translation
Biological Process GO:0051781 positive regulation of cell division
Biological Process GO:2000767 positive regulation of cytoplasmic translation
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:1903608 protein localization to cytoplasmic stress granule
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0010468 regulation of gene expression
Biological Process GO:0008380 RNA splicing
Biological Process GO:0050658 RNA transport
Biological Process GO:0051031 tRNA transport

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] 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.

[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.