Search Results
Overview
| Uniprot ID | H0UVA7 |
|---|---|
| Protein Name | Nucleolin |
| Gene Name | NCL |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | KKTVTPAKAVVAPGK |
| 115 | KKGAALGKAVVATPG |
| 123 | AVVATPGKKGTVTPA |
| 229 | KGKKAPAKAAPVKAK |
| 401 | DARTLLAKNLPYKVT |
| 406 | LAKNLPYKVTQDELK |
| 432 | VSKDGKSKGIAYIEF |
| 470 | SLYYTGEKGQNQDYR |
| 480 | NQDYRGGKNSTWSGE |
| 548 | EALNSCNKREIEGRT |
| 575 | NARSQPSKTLFVKGL |
| 580 | PSKTLFVKGLSEETT |
| 61 | AAVTPAKKAVASPVK |
| 613 | DRETGSSKGFGFVDF |
| 68 | KAVASPVKKVAVATP |
| 69 | AVASPVKKVAVATPA |
| 77 | VAVATPAKKAAVTPG |
Function
Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats
Protein Sequence
10
MVKLAKAGKN
20
QSDPKKMAPP
30
PKEVEESDDE
40
EMSDDEDDSS
50
GEEVVIPQKK
60
SKKAAVTPAK
70
KAVASPVKKV
80
AVATPAKKAA
90
VTPGKKAAAA
100
TPAKKTVTPA
110
KAVVAPGKKG
120
AALGKAVVAT
130
PGKKGTVTPA
140
KGAKNGKNAK
150
KEDSDEDEED
160
GDSDEEDDDE
170
EEEEEEDEEF
180
EPKVMKAVAA
190
APASEDEDED
200
DDDDDDDDEE
210
EDDDDDEDDD
220
SEEEAMETTP
230
AKGKKAPAKA
240
APVKAKSMAE
250
EEDDDEDDDD
260
EDEDEDDEED
270
EDEEEEEEEE
280
EEEEPVKEAP
290
GKRKKDMTKQ
300
KAAPEAKKQK
310
MEGTEPTTAF
320
NLFVGNLNSS
330
KSPSELKTGI
340
SEVFAKNDLT
350
TVDVRIGTNR
360
KFGYVDFESA
370
EDLEKALELT
380
GLKVFGSEIK
390
LEKPKGKDSK
400
KDRDARTLLA
410
KNLPYKVTQD
420
ELKEVFEDAL
430
EIRLVSKDGK
440
SKGIAYIEFK
450
TEADAEKTFE
460
EKQGTEIDGR
470
SVSLYYTGEK
480
GQNQDYRGGK
490
NSTWSGESKT
500
LYLSNLSYSA
510
TEETLQEVFE
520
KATFIKVPQN
530
QNGKSKGYAF
540
IEFASFEDAK
550
EALNSCNKRE
560
IEGRTIRLEL
570
QGPRGSPNAR
580
SQPSKTLFVK
590
GLSEETTEET
600
LKESFDGSIG
610
ARIVTDRETG
620
SSKGFGFVDF
630
NTEEDAKAAK
640
EAMEDGEIDG
650
NKVTLDWAKP
660
KGEGGFGGRG
670
GGRGGFGGRG
680
GGRGGRGGFG
690
GRGRGGFGGR
700
GGFRGGRGGG
710
GDHKPQGKKT
KFE
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005938 | cell cortex |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0001533 | cornified envelope |
| Cellular Component | GO:0036464 | cytoplasmic ribonucleoprotein granule |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0044547 | DNA topoisomerase binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0043560 | insulin receptor substrate binding |
| Molecular Function | GO:0048027 | mRNA 5'-UTR binding |
| Molecular Function | GO:0042731 | PH domain binding |
| Molecular Function | GO:0042162 | telomeric DNA binding |
| Biological Process | GO:0001525 | angiogenesis |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:1901838 | positive regulation of transcription of nucleolar large rRNA by RNA polymerase I |
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.