NOL8_HUMAN
ID NOL8_HUMAN Reviewed; 1167 AA.
AC Q76FK4; Q5TCC7; Q5TCC8; Q5TCD3; Q5TCD5; Q5TCD6; Q5TCD7; Q76D35; Q7L3E2;
AC Q9H586; Q9H795; Q9H7W7; Q9H9J6; Q9NWA4; Q9NWM4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Nucleolar protein 8;
DE AltName: Full=Nucleolar protein Nop132;
GN Name=NOL8 {ECO:0000312|HGNC:HGNC:23387}; Synonyms=C9orf34, NOP132;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD12268.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=15132771; DOI=10.1111/j.1349-7006.2004.tb03227.x;
RA Jinawath N., Furukawa Y., Nakamura Y.;
RT "Identification of NOL8, a nucleolar protein containing an RNA recognition
RT motif (RRM), which was overexpressed in diffuse-type gastric cancer.";
RL Cancer Sci. 95:430-435(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC99315.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 946-964,
RP FUNCTION, AND INTERACTION WITH NIP7; RRAGA; RRAGC AND RRAGD.
RX PubMed=14660641; DOI=10.1074/jbc.m305935200;
RA Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N., Nishimoto T.;
RT "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG
RT A/C/D.";
RL J. Biol. Chem. 279:8343-8350(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB14857.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic head {ECO:0000312|EMBL:BAA91479.1},
RC Hepatoma {ECO:0000312|EMBL:BAA91356.1},
RC Smooth muscle {ECO:0000312|EMBL:BAB15003.1}, and
RC Teratocarcinoma {ECO:0000312|EMBL:BAB14857.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH13788.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-1167 (ISOFORMS 1/2).
RC TISSUE=Colon {ECO:0000312|EMBL:AAH13788.2};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; THR-888 AND SER-890, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION, INTERACTION WITH DDX18 AND DDX47, AND SUBCELLULAR LOCATION.
RX PubMed=16963496; DOI=10.1093/nar/gkl603;
RA Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
RT "NOP132 is required for proper nucleolus localization of DEAD-box RNA
RT helicase DDX47.";
RL Nucleic Acids Res. 34:4593-4608(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-378; THR-381;
RP SER-837; SER-838; SER-843; SER-845; SER-1036; SER-1082; SER-1083; SER-1084
RP AND SER-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; THR-302; SER-304;
RP SER-378; THR-381; SER-837; THR-888; SER-1082; SER-1083 AND SER-1084, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; THR-888 AND SER-890, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; THR-302; SER-304;
RP SER-365; TYR-376; SER-378; THR-381; THR-888; SER-890; SER-1082; SER-1083;
RP SER-1084 AND SER-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-331; SER-365;
RP SER-378; THR-381; SER-432; SER-723; THR-888; SER-890 AND SER-1099, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837; SER-838; SER-843 AND
RP SER-845, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1057, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225; LYS-314 AND LYS-1057, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Plays an essential role in the survival of diffuse-type
CC gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47.
CC May be involved in regulation of gene expression at the post-
CC transcriptional level or in ribosome biogenesis in cancer cells.
CC {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:15132771,
CC ECO:0000269|PubMed:16963496}.
CC -!- SUBUNIT: Interacts with the GTP form of RRAGA, RRAGC and RRAGD.
CC Interacts with NIP7. Interacts with DDX18; the interaction is RNA-
CC dependent. Interacts with DDX47; the interaction is RNA-dependent.
CC {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:16963496}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15132771,
CC ECO:0000269|PubMed:16963496}. Note=Localizes in the nucleolar-
CC organizing region during ribosome biogenesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:15132771};
CC IsoId=Q76FK4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15164053};
CC IsoId=Q76FK4-2; Sequence=VSP_052055;
CC Name=4 {ECO:0000269|PubMed:15164053};
CC IsoId=Q76FK4-4; Sequence=VSP_052056;
CC -!- TISSUE SPECIFICITY: Expressed in various diffuse-type gastric cancers.
CC Detected at lower levels in skeletal muscle.
CC {ECO:0000269|PubMed:15132771}.
CC -!- INDUCTION: Up-regulated in diffuse-type gastric cancers.
CC {ECO:0000269|PubMed:15132771}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15132771}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91356.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91356.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14229.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB105104; BAD12268.1; -; mRNA.
DR EMBL; AB109030; BAC99315.1; -; mRNA.
DR EMBL; AK000743; BAA91356.1; ALT_SEQ; mRNA.
DR EMBL; AK001049; BAA91479.1; -; mRNA.
DR EMBL; AK022755; BAB14229.1; ALT_INIT; mRNA.
DR EMBL; AK024245; BAB14857.1; -; mRNA.
DR EMBL; AK024786; BAB15003.1; ALT_INIT; mRNA.
DR EMBL; AL136097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013788; AAH13788.2; -; mRNA.
DR CCDS; CCDS47993.1; -. [Q76FK4-1]
DR CCDS; CCDS59135.1; -. [Q76FK4-2]
DR CCDS; CCDS83384.1; -. [Q76FK4-4]
DR RefSeq; NP_001243323.1; NM_001256394.1. [Q76FK4-2]
DR RefSeq; NP_001317651.1; NM_001330722.1. [Q76FK4-4]
DR RefSeq; NP_060418.4; NM_017948.5. [Q76FK4-1]
DR RefSeq; XP_006717229.1; XM_006717166.3. [Q76FK4-1]
DR RefSeq; XP_006717230.1; XM_006717167.3. [Q76FK4-1]
DR RefSeq; XP_006717232.1; XM_006717169.3. [Q76FK4-2]
DR RefSeq; XP_006717233.1; XM_006717170.3. [Q76FK4-2]
DR RefSeq; XP_011517126.1; XM_011518824.2. [Q76FK4-2]
DR RefSeq; XP_016870365.1; XM_017014876.1. [Q76FK4-4]
DR AlphaFoldDB; Q76FK4; -.
DR SMR; Q76FK4; -.
DR BioGRID; 120364; 109.
DR IntAct; Q76FK4; 30.
DR MINT; Q76FK4; -.
DR STRING; 9606.ENSP00000441140; -.
DR GlyGen; Q76FK4; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q76FK4; -.
DR PhosphoSitePlus; Q76FK4; -.
DR BioMuta; NOL8; -.
DR DMDM; 74758950; -.
DR EPD; Q76FK4; -.
DR jPOST; Q76FK4; -.
DR MassIVE; Q76FK4; -.
DR MaxQB; Q76FK4; -.
DR PaxDb; Q76FK4; -.
DR PeptideAtlas; Q76FK4; -.
DR PRIDE; Q76FK4; -.
DR ProteomicsDB; 68665; -. [Q76FK4-1]
DR ProteomicsDB; 68666; -. [Q76FK4-2]
DR ProteomicsDB; 68668; -. [Q76FK4-4]
DR Antibodypedia; 43737; 117 antibodies from 22 providers.
DR DNASU; 55035; -.
DR Ensembl; ENST00000358855.8; ENSP00000351723.4; ENSG00000198000.12. [Q76FK4-2]
DR Ensembl; ENST00000442668.7; ENSP00000401177.2; ENSG00000198000.12. [Q76FK4-1]
DR Ensembl; ENST00000535387.5; ENSP00000441300.1; ENSG00000198000.12. [Q76FK4-4]
DR Ensembl; ENST00000542053.5; ENSP00000440709.1; ENSG00000198000.12. [Q76FK4-2]
DR Ensembl; ENST00000545558.5; ENSP00000441140.1; ENSG00000198000.12. [Q76FK4-1]
DR GeneID; 55035; -.
DR KEGG; hsa:55035; -.
DR MANE-Select; ENST00000442668.7; ENSP00000401177.2; NM_017948.6; NP_060418.4.
DR UCSC; uc064uhl.1; human. [Q76FK4-1]
DR CTD; 55035; -.
DR DisGeNET; 55035; -.
DR GeneCards; NOL8; -.
DR HGNC; HGNC:23387; NOL8.
DR HPA; ENSG00000198000; Low tissue specificity.
DR MIM; 611534; gene.
DR neXtProt; NX_Q76FK4; -.
DR OpenTargets; ENSG00000198000; -.
DR PharmGKB; PA134918056; -.
DR VEuPathDB; HostDB:ENSG00000198000; -.
DR eggNOG; KOG4365; Eukaryota.
DR GeneTree; ENSGT00390000004860; -.
DR HOGENOM; CLU_008415_0_0_1; -.
DR InParanoid; Q76FK4; -.
DR OMA; HKRNIMK; -.
DR OrthoDB; 442365at2759; -.
DR PhylomeDB; Q76FK4; -.
DR TreeFam; TF323283; -.
DR PathwayCommons; Q76FK4; -.
DR SignaLink; Q76FK4; -.
DR BioGRID-ORCS; 55035; 589 hits in 1085 CRISPR screens.
DR ChiTaRS; NOL8; human.
DR GeneWiki; NOL8; -.
DR GenomeRNAi; 55035; -.
DR Pharos; Q76FK4; Tbio.
DR PRO; PR:Q76FK4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q76FK4; protein.
DR Bgee; ENSG00000198000; Expressed in calcaneal tendon and 194 other tissues.
DR ExpressionAtlas; Q76FK4; baseline and differential.
DR Genevisible; Q76FK4; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; IMP:BHF-UCL.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR CDD; cd12226; RRM_NOL8; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034138; NOP8_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW rRNA processing; Ubl conjugation.
FT CHAIN 1..1167
FT /note="Nucleolar protein 8"
FT /id="PRO_0000239443"
FT DOMAIN 8..89
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 223..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 753..779
FT /evidence="ECO:0000255"
FT COILED 886..924
FT /evidence="ECO:0000255"
FT COMPBIAS 248..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHX0"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHX0"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 888
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1057
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15164053"
FT /id="VSP_052055"
FT VAR_SEQ 787..824
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15164053"
FT /id="VSP_052056"
FT VARIANT 470
FT /note="G -> E (in dbSNP:rs58545014)"
FT /id="VAR_061830"
FT VARIANT 748
FT /note="V -> L (in dbSNP:rs2236344)"
FT /id="VAR_052211"
FT VARIANT 841
FT /note="D -> E (in dbSNP:rs15717)"
FT /id="VAR_052212"
FT VARIANT 988
FT /note="E -> D (in dbSNP:rs34224798)"
FT /id="VAR_052213"
FT VARIANT 1021
FT /note="G -> S (in dbSNP:rs921122)"
FT /id="VAR_052214"
FT CONFLICT 69
FT /note="M -> I (in Ref. 2; BAC99315 and 3; BAA91479)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="S -> G (in Ref. 3; BAB14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="K -> E (in Ref. 3; BAB14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="C -> W (in Ref. 2; BAC99315 and 3; BAA91356)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="E -> G (in Ref. 3; BAB14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="S -> G (in Ref. 3; BAB14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="I -> L (in Ref. 2; BAC99315 and 3; BAA91356)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="K -> R (in Ref. 2; BAC99315 and 3; BAA91356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1167 AA; 131616 MW; 6E64780D6F0E7415 CRC64;
MKVNRETKRL YVGGLSQDIS EADLQNQFSR FGEVSDVEII TRKDDQGNPQ KVFAYINISV
AEADLKKCMS VLNKTKWKGG TLQIQLAKES FLHRLAQERE AAKAKKEEST TGNANLLEKT
GGVDFHMKAV PGTEVPGHKN WVVSKFGRVL PVLHLKNQHK RKIIKYDPSK YCHNLKKIGE
DFSNTIPISS LTWELEGGND PMSKKRRGEF SDFHGPPKKI IKVQKDESST GSLAMSTRPR
RVIERPPLTQ QQAAQKRTCD SITPSKSSPV PVSDTQKLKN LPFKTSGLET AKKRNSISDD
DTDSEDELRM MIAKEENLQR TTQPSINESE SDPFEVVRDD FKSGVHKLHS LIGLGIKNRV
SCHDSDDDIM RNDREYDSGD TDEIIAMKKN VAKVKNSTEF SQMEKSTKKT SFKNRENCEL
SDHCIKLQKR KSNVESALSH GLKSLNRKSP SHSSSSEDAD SASELADSEG GEEYNAMMKN
CLRVNLTLAD LEQLAGSDLK VPNEDTKSDG PETTTQCKFD RGSKSPKTPT GLRRGRQCIR
PAEIVASLLE GEENTCGKQK PKENNLKPKF QAFKGVGCLY EKESMKKSLK DSVASNNKDQ
NSMKHEDPSI ISMEDGSPYV NGSLGEVTPC QHAKKANGPN YIQPQKRQTT FESQDRKAVS
PSSSEKRSKN PISRPLEGKK SLSLSAKTHN IGFDKDSCHS TTKTEASQEE RSDSSGLTSL
KKSPKVSSKD TREIKTDFSL SISNSSDVSA KDKHAEDNEK RLAALEARQK AKEVQKKLVH
NALANLDGHP EDKPTHIIFG SDSECETEET STQEQSHPGE EWVKESMGKT SGKLFDSSDD
DESDSEDDSN RFKIKPQFEG RAGQKLMDLQ SHFGTDDRFR MDSRFLETDS EEEQEEVNEK
KTAEEEELAE EKKKALNVVQ SVLQINLSNS TNRGSVAAKK FKDIIHYDPT KQDHATYERK
RDDKPKESKA KRKKKREEAE KLPEVSKEMY YNIAMDLKEI FQTTKYTSEK EEGTPWNEDC
GKEKPEEIQD PAALTSDAEQ PSGFTFSFFD SDTKDIKEET YRVETVKPGK IVWQEDPRLQ
DSSSEEEDVT EETDHRNSSP GEASLLEKET TRFFFFSKND ERLQGSDLFW RGVGSNMSRN
SWEARTTNLR MDCRKKHKDA KRKMKPK
