Search Results
Overview
| Uniprot ID | Q76FK4 |
|---|---|
| Protein Name | Nucleolar protein 8 |
| Gene Name | NOL8 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1070 | VETVKPGKIVWQEDP |
| 145 | HKNWVVSKFGRVLPV |
| 156 | VLPVLHLKNQHKRKI |
| 266 | CDSITPSKSSPVPVS |
| 279 | VSDTQKLKNLPFKTS |
| 284 | KLKNLPFKTSGLETA |
| 292 | TSGLETAKKRNSISD |
| 293 | SGLETAKKRNSISDD |
| 357 | SLIGLGIKNRVSCHD |
| 395 | KKNVAKVKNSTEFSQ |
| 426 | ELSDHCIKLQKRKSN |
| 443 | SALSHGLKSLNRKSP |
| 518 | PETTTQCKFDRGSKS |
| 574 | KPKFQAFKGVGCLYE |
| 721 | SSGLTSLKKSPKVSS |
| 722 | SGLTSLKKSPKVSSK |
Function
Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells
Protein Sequence
10
MKVNRETKRL
20
YVGGLSQDIS
30
EADLQNQFSR
40
FGEVSDVEII
50
TRKDDQGNPQ
60
KVFAYINISV
70
AEADLKKCMS
80
VLNKTKWKGG
90
TLQIQLAKES
100
FLHRLAQERE
110
AAKAKKEEST
120
TGNANLLEKT
130
GGVDFHMKAV
140
PGTEVPGHKN
150
WVVSKFGRVL
160
PVLHLKNQHK
170
RKIIKYDPSK
180
YCHNLKKIGE
190
DFSNTIPISS
200
LTWELEGGND
210
PMSKKRRGEF
220
SDFHGPPKKI
230
IKVQKDESST
240
GSLAMSTRPR
250
RVIERPPLTQ
260
QQAAQKRTCD
270
SITPSKSSPV
280
PVSDTQKLKN
290
LPFKTSGLET
300
AKKRNSISDD
310
DTDSEDELRM
320
MIAKEENLQR
330
TTQPSINESE
340
SDPFEVVRDD
350
FKSGVHKLHS
360
LIGLGIKNRV
370
SCHDSDDDIM
380
RNDREYDSGD
390
TDEIIAMKKN
400
VAKVKNSTEF
410
SQMEKSTKKT
420
SFKNRENCEL
430
SDHCIKLQKR
440
KSNVESALSH
450
GLKSLNRKSP
460
SHSSSSEDAD
470
SASELADSEG
480
GEEYNAMMKN
490
CLRVNLTLAD
500
LEQLAGSDLK
510
VPNEDTKSDG
520
PETTTQCKFD
530
RGSKSPKTPT
540
GLRRGRQCIR
550
PAEIVASLLE
560
GEENTCGKQK
570
PKENNLKPKF
580
QAFKGVGCLY
590
EKESMKKSLK
600
DSVASNNKDQ
610
NSMKHEDPSI
620
ISMEDGSPYV
630
NGSLGEVTPC
640
QHAKKANGPN
650
YIQPQKRQTT
660
FESQDRKAVS
670
PSSSEKRSKN
680
PISRPLEGKK
690
SLSLSAKTHN
700
IGFDKDSCHS
710
TTKTEASQEE
720
RSDSSGLTSL
730
KKSPKVSSKD
740
TREIKTDFSL
750
SISNSSDVSA
760
KDKHAEDNEK
770
RLAALEARQK
780
AKEVQKKLVH
790
NALANLDGHP
800
EDKPTHIIFG
810
SDSECETEET
820
STQEQSHPGE
830
EWVKESMGKT
840
SGKLFDSSDD
850
DESDSEDDSN
860
RFKIKPQFEG
870
RAGQKLMDLQ
880
SHFGTDDRFR
890
MDSRFLETDS
900
EEEQEEVNEK
910
KTAEEEELAE
920
EKKKALNVVQ
930
SVLQINLSNS
940
TNRGSVAAKK
950
FKDIIHYDPT
960
KQDHATYERK
970
RDDKPKESKA
980
KRKKKREEAE
990
KLPEVSKEMY
1000
YNIAMDLKEI
1010
FQTTKYTSEK
1020
EEGTPWNEDC
1030
GKEKPEEIQD
1040
PAALTSDAEQ
1050
PSGFTFSFFD
1060
SDTKDIKEET
1070
YRVETVKPGK
1080
IVWQEDPRLQ
1090
DSSSEEEDVT
1100
EETDHRNSSP
1110
GEASLLEKET
1120
TRFFFFSKND
1130
ERLQGSDLFW
1140
RGVGSNMSRN
1150
SWEARTTNLR
1160
MDCRKKHKDA
KRKMKPK
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005730 | nucleolus |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:1902570 | protein localization to nucleolus |
| Biological Process | GO:0006364 | rRNA processing |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.