Overview
| Uniprot ID | H0VJX3 |
| Protein Name | SAP domain-containing ribonucleoprotein |
| Gene Name | Sarnp |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 10 |
TETVELHKLKLAELK |
| 119 |
VPVSLESKKAARAAR |
| 149 |
KPMVNLDKLKERAQR |
| 17 |
KLKLAELKQECLARG |
| 31 |
GLETKGIKQDLINRL |
| 88 |
TVDVAAEKKVVKITS |
| 89 |
VDVAAEKKVVKITSE |
| 92 |
AAEKKVVKITSEMPQ |
Function
Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway. Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export
Protein Sequence
10
MATETVELHK
20
LKLAELKQEC
30
LARGLETKGI
40
KQDLINRLQA
50
YLEEHAEEEA
60
NEEDVLGDET
70
EEEEPKPIEL
80
PVKEEEPPEK
90
TVDVAAEKKV
100
VKITSEMPQT
110
ERMQKRAERF
120
NVPVSLESKK
130
AARAARFGIS
140
SVPTKGLSSD
150
TKPMVNLDKL
160
KERAQRFGLN
170
VSSISRKSED
180
DEKLKKRKER
190
FGIVTSSAGI
200
GTTEDTEAKK
210
RKRAERFGIA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0016973 |
poly(A)+ mRNA export from nucleus |
| Biological Process |
GO:0006417 |
regulation of translation |
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.