Search Results
Overview
| Uniprot ID | P09405 |
|---|---|
| Protein Name | Nucleolin |
| Gene Name | Ncl |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 102 | KKNITPAKVIPTPGK |
| 109 | KVIPTPGKKGAAQAK |
| 116 | KKGAAQAKALVPTPG |
| 230 | KGKKTPAKVVPMKAK |
| 469 | SLYYTGEKGQRQERT |
| 478 | QRQERTGKTSTWSGE |
| 574 | PSKTLFVKGLSEDTT |
| 63 | ATTTPAKKVVVSQTK |
| 70 | KVVVSQTKKAAVPTP |
| 71 | VVVSQTKKAAVPTPA |
| 79 | AAVPTPAKKAAVTPG |
| 88 | AAVTPGKKAVATPAK |
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 (By similarity)
Protein Sequence
10
MVKLAKAGKT
20
HGEAKKMAPP
30
PKEVEEDSED
40
EEMSEDEDDS
50
SGEEEVVIPQ
60
KKGKKATTTP
70
AKKVVVSQTK
80
KAAVPTPAKK
90
AAVTPGKKAV
100
ATPAKKNITP
110
AKVIPTPGKK
120
GAAQAKALVP
130
TPGKKGAATP
140
AKGAKNGKNA
150
KKEDSDEDED
160
EEDEDDSDED
170
EDDEEEDEFE
180
PPIVKGVKPA
190
KAAPAAPASE
200
DEEDDEDEDD
210
EEDDDEEEED
220
DSEEEVMEIT
230
TAKGKKTPAK
240
VVPMKAKSVA
250
EEEDDEEEDE
260
DDEDEDDEEE
270
DDEDDDEEEE
280
EEEPVKAAPG
290
KRKKEMTKQK
300
EAPEAKKQKV
310
EGSEPTTPFN
320
LFIGNLNPNK
330
SVNELKFAIS
340
ELFAKNDLAV
350
VDVRTGTNRK
360
FGYVDFESAE
370
DLEKALELTG
380
LKVFGNEIKL
390
EKPKGRDSKK
400
VRAARTLLAK
410
NLSFNITEDE
420
LKEVFEDAME
430
IRLVSQDGKS
440
KGIAYIEFKS
450
EADAEKNLEE
460
KQGAEIDGRS
470
VSLYYTGEKG
480
QRQERTGKTS
490
TWSGESKTLV
500
LSNLSYSATK
510
ETLEEVFEKA
520
TFIKVPQNPH
530
GKPKGYAFIE
540
FASFEDAKEA
550
LNSCNKMEIE
560
GRTIRLELQG
570
SNSRSQPSKT
580
LFVKGLSEDT
590
TEETLKESFE
600
GSVRARIVTD
610
RETGSSKGFG
620
FVDFNSEEDA
630
KAAKEAMEDG
640
EIDGNKVTLD
650
WAKPKGEGGF
660
GGRGGGRGGF
670
GGRGGGRGGR
680
GGFGGRGRGG
690
FGGRGGFRGG
700
RGGGGDFKPQ
GKKTKFE
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005938 | cell cortex |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0001533 | cornified envelope |
| Cellular Component | GO:0036464 | cytoplasmic ribonucleoprotein granule |
| Cellular Component | GO:0001651 | dense fibrillar component |
| Cellular Component | GO:0001650 | fibrillar center |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0044547 | DNA topoisomerase binding |
| Molecular Function | GO:1990631 | ErbB-4 class receptor binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0043560 | insulin receptor substrate binding |
| Molecular Function | GO:0043236 | laminin binding |
| Molecular Function | GO:0048027 | mRNA 5'-UTR binding |
| Molecular Function | GO:0042731 | PH domain binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0042134 | rRNA primary transcript binding |
| Molecular Function | GO:0035368 | selenocysteine insertion sequence binding |
| Molecular Function | GO:0043565 | sequence-specific DNA binding |
| Molecular Function | GO:0005102 | signaling receptor binding |
| Molecular Function | GO:0003697 | single-stranded DNA binding |
| Molecular Function | GO:0042162 | telomeric DNA binding |
| Biological Process | GO:0001525 | angiogenesis |
| Biological Process | GO:0071364 | cellular response to epidermal growth factor stimulus |
| Biological Process | GO:1990830 | cellular response to leukemia inhibitory factor |
| Biological Process | GO:0071222 | cellular response to lipopolysaccharide |
| Biological Process | GO:0006897 | endocytosis |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0046627 | negative regulation of insulin receptor signaling pathway |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:0032755 | positive regulation of interleukin-6 production |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:1901838 | positive regulation of transcription of nucleolar large rRNA by RNA polymerase I |
| Biological Process | GO:0032760 | positive regulation of tumor necrosis factor production |
| Biological Process | GO:0050730 | regulation of peptidyl-tyrosine phosphorylation |
| Biological Process | GO:2000232 | regulation of rRNA processing |
Reference
[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.
[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.