Overview
| Uniprot ID | H0VTS7 |
|---|
| Protein Name | Heterogeneous nuclear ribonucleoprotein D-like |
|---|
| Gene Name | HNRNPDL |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 294 |
EIKVAQPKEVYRQQQ |
| 76 |
LAGGAAIKGGRRRRP |
| 91 |
DLFRRHFKSSSIQRF |
Function
Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes. Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter. Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence
Protein Sequence
10
MEVPPRLAHV
20
PPPLFPAAPA
30
PLASRSLSHW
40
RPRAPRQLAP
50
LLPSLAAGSA
60
RQGARRAPRH
70
VTAQQPSRLA
80
GGAAIKGGRR
90
RRPDLFRRHF
100
KSSSIQRFRC
110
RHHPRDPDCR
120
EFAEGSKINA
130
SKNQQDDGYR
140
TKMFIGGLSW
150
DTSKKDLTEY
160
LSRFGEVVDC
170
TIKTDPVTGR
180
SRGFGFVLFK
190
DAASVDKVLE
200
LKEHKLDGKL
210
IDPKRAKALK
220
GKEPPKKVFV
230
GGLSPDTSEE
240
QIKEYFGAFG
250
EIENIELPMD
260
TKTNERRGFC
270
FITYTDEEPV
280
KKLLESRYHQ
290
IGSGKCEIKV
300
AQPKEVYRQQ
310
QQQQKGGRGA
320
AAGGRGGTRG
330
RGRGQGQNWN
340
QGFNNYYDQG
350
YGNYNSAYGG
360
DQNYSGYGGY
370
DYTGYNYGNY
380
GYGQGYADYS
390
GQQSTYGKAS
400
RGGGNHQNNY
QPY
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0008143 |
poly(A) binding |
| Molecular Function |
GO:0034046 |
poly(G) binding |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0010468 |
regulation of gene expression |
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.