Overview
| Uniprot ID | H0V4H8 |
|---|
| Protein Name | Heterogeneous nuclear ribonucleoprotein K |
|---|
| Gene Name | - |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 31 |
MEEEQAFKRSRNTDE |
Function
One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction. As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation
Protein Sequence
10
METEQPEETF
20
PNTETNGKRP
30
AEDMEEEQAF
40
KRSRNTDEMV
50
ELRILLQSKN
60
AGAVIGKGGK
70
NIKALRTDYN
80
ASVSVPDSSG
90
PERILSISAD
100
IETIGEILKK
110
IIPTLEEYQH
120
YKGSDFDCEL
130
RLLIHQSLAG
140
GIIGVKGAKI
KELRE
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0002102 |
podosome |
| Cellular Component |
GO:0005681 |
spliceosomal complex |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0006397 |
mRNA processing |
| Biological Process |
GO:0008380 |
RNA splicing |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.