Overview
| Uniprot ID | H0UWA3 |
|---|
| Protein Name | - |
|---|
| Gene Name | Hnrnpc |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 157 |
ARAVVPSKRQRVSGN |
| 176 |
GKSGFNSKSGQRGSS |
| 190 |
SSKSGKLKGDDLQAI |
| 224 |
KIEKEQSKQAVEMKN |
| 244 |
EQTSTSLKKDETNVK |
| 42 |
AIFSKYGKIVGCSVH |
| 8 |
MASNVTNKTDPRSMN |
| 89 |
INLAAEPKVNRGKAG |
Function
Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing
Protein Sequence
10
MASNVTNKTD
20
PRSMNSRVFI
30
GNLNTLVVKK
40
SDVEAIFSKY
50
GKIVGCSVHK
60
GFAFVQYVNE
70
RNARAAVAGE
80
DGRMIAGQVL
90
DINLAAEPKV
100
NRGKAGVKRS
110
AAEMYGSVPE
120
HPSPSPLLSS
130
SFDLDYDFQR
140
DYYDRMYSYP
150
ARVPPPPPIA
160
RAVVPSKRQR
170
VSGNTSRRGK
180
SGFNSKSGQR
190
GSSSKSGKLK
200
GDDLQAIKKE
210
LTQIKQKVDS
220
LLESLEKIEK
230
EQSKQAVEMK
240
NDKSEEEQTS
250
TSLKKDETNV
260
KMESEGAADD
270
SAEEGDLLDD
280
DENEDRADDQ
290
LELIKDDEKE
300
AEEGEDDRDS
ANGEDDS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0045120 |
pronucleus |
| Cellular Component |
GO:1990904 |
ribonucleoprotein complex |
| Molecular Function |
GO:0003729 |
mRNA binding |
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.