NOL8_MOUSE
ID NOL8_MOUSE Reviewed; 1147 AA.
AC Q3UHX0; Q059P5; Q504M4; Q8CDJ7; Q9CUR0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nucleolar protein 8;
GN Name=Nol8 {ECO:0000312|MGI:MGI:1918180};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE27736.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE27736.1};
RC TISSUE=Embryonic liver {ECO:0000312|EMBL:BAE27736.1}, and
RC Testis {ECO:0000312|EMBL:BAC26701.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH94941.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas {ECO:0000312|EMBL:AAH94941.1};
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1063; SER-1064 AND SER-1065,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-306; SER-364;
RP SER-365; THR-367; THR-777; SER-783; SER-787; SER-819; SER-820; SER-825;
RP SER-1063; SER-1064; SER-1065 AND SER-1080, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes
CC in the nucleolar-organizing region during ribosome biogenesis.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3UHX0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q3UHX0-2; Sequence=VSP_052057;
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q76FK4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC26701.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK029961; BAC26701.1; ALT_INIT; mRNA.
DR EMBL; AK147172; BAE27736.1; -; mRNA.
DR EMBL; AK014994; BAB29660.1; ALT_INIT; mRNA.
DR EMBL; BC094941; AAH94941.1; -; mRNA.
DR EMBL; BC125575; AAI25576.1; -; mRNA.
DR EMBL; BC125579; AAI25580.1; -; mRNA.
DR RefSeq; NP_001258326.1; NM_001271397.1.
DR RefSeq; XP_006517019.2; XM_006516956.3. [Q3UHX0-1]
DR AlphaFoldDB; Q3UHX0; -.
DR SMR; Q3UHX0; -.
DR BioGRID; 214353; 2.
DR STRING; 10090.ENSMUSP00000021824; -.
DR iPTMnet; Q3UHX0; -.
DR PhosphoSitePlus; Q3UHX0; -.
DR EPD; Q3UHX0; -.
DR jPOST; Q3UHX0; -.
DR MaxQB; Q3UHX0; -.
DR PaxDb; Q3UHX0; -.
DR PeptideAtlas; Q3UHX0; -.
DR PRIDE; Q3UHX0; -.
DR ProteomicsDB; 252986; -. [Q3UHX0-1]
DR ProteomicsDB; 252987; -. [Q3UHX0-2]
DR Antibodypedia; 43737; 117 antibodies from 22 providers.
DR Ensembl; ENSMUST00000221142; ENSMUSP00000152552; ENSMUSG00000021392. [Q3UHX0-1]
DR Ensembl; ENSMUST00000223467; ENSMUSP00000152878; ENSMUSG00000021392. [Q3UHX0-1]
DR GeneID; 70930; -.
DR KEGG; mmu:70930; -.
DR UCSC; uc033glk.1; mouse. [Q3UHX0-1]
DR CTD; 55035; -.
DR MGI; MGI:1918180; Nol8.
DR VEuPathDB; HostDB:ENSMUSG00000021392; -.
DR eggNOG; KOG4365; Eukaryota.
DR GeneTree; ENSGT00390000004860; -.
DR InParanoid; Q3UHX0; -.
DR OMA; HKRNIMK; -.
DR OrthoDB; 442365at2759; -.
DR PhylomeDB; Q3UHX0; -.
DR BioGRID-ORCS; 70930; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Nol8; mouse.
DR PRO; PR:Q3UHX0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UHX0; protein.
DR Bgee; ENSMUSG00000021392; Expressed in animal zygote and 237 other tissues.
DR ExpressionAtlas; Q3UHX0; baseline and differential.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:1902570; P:protein localization to nucleolus; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISS: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; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..1147
FT /note="Nucleolar protein 8"
FT /id="PRO_0000239444"
FT DOMAIN 8..89
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 379..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 868..898
FT /evidence="ECO:0000255"
FT COILED 937..963
FT /evidence="ECO:0000255"
FT COMPBIAS 483..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT CROSSLNK 1038
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q76FK4"
FT VAR_SEQ 1..848
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052057"
FT CONFLICT 383
FT /note="S -> R (in Ref. 1; BAC26701)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="D -> G (in Ref. 1; BAE27736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1147 AA; 128635 MW; 53949DB71021DB38 CRC64;
MQGNREMKRL FVGGLGQGIS ETDLQNQFGR FGEVSDVEII TRKDDQGNSQ KVFAYVNIQI
TEADLKKCMS ILNKTKWKGG TLQIQLAKES FLHRLAQERE DAKAKKEKST TGNPTLLEKM
GAVDFHMKAV PGTEVPGHKN WVVSKFGRVL PVLHLKNQQK HKIMKYDPSK YCHNIKKIPE
NLTETTPIAE LTWELEGGND PMSKKRRGEF SDFHIPPQKV KKVQKSNDPM ESKVSNIGLR
TNQVMEKNKS THPVTAHGTA PSTVNPSKQL LVSSSGTQKP KHVVFHNSDF EIIWNKSSMS
DDDVDSEDEL KMMIAKEENR EKPGHSSVNE SEHDTFEVVR DDFKSNIHKL SSSVSLGNNH
EYDSSDTDEI IAMKTKNAKV KNSAESSQPE RTVSKKSSFQ KIEPSNDCIK VQGINSNKES
ALCHGVKFVN PKFPPDSSGS DSEESEEDEE YKVLMENCPR VSLTLADLEQ LAGSHRKFPG
KDSETNGPQN DSHCKFDTTS KNPKTSGDLY NGRQQCILPE EIVASLLEDE NTYSKQKSEE
DILKPKFQAF KGIGCLYAKE SVDKTLKENI AFNTGGGHHS SLKHEDHNRS LMENGSKCVN
GSSSKLTSCQ PAKKVNDPNH IQPPKRQCTF ENQNHKVMSS TSCDKGSTNP LPGPLPLKAK
TSLHLSANSH KVDSDGDACH WPESRKALEK ERTNLSNLES LEKSSKVSPR EDPQKSPAGF
SLSDSNASCI NAKDKQAEDN QKRLAALAAW QKAREVQKKL VHSALANLDG HPEDKKTHIV
FASDNESETE ETSTQEQSCP EKELMKESVS KSPGKLFDSS DDEDSDSKED STRFSIKPQF
EGRAGQKLMD LQSQFGSDER FRMDSRFLES DSEDEKKELN EDKVNEDELA AEKKKTLNVV
QSVLNINVNN PTNKGSVAAK KFKDIVHYDP TKHDHAIYER KQEDKEKESK ATRKKKKEEA
EKLPEVSQDM YYNIAADLKE IFQSMSNTDE KEEDVPRTEA GAREGTGKIR NAETLACEPE
QTTGFTFSFF DSATKDEKDA TYRIELVKHG KIVCPNDPRF QDSSSEEEDI AEEADHSKPS
PGEAVPENEA IRFFFFSEND DRLRGSNLFW SGMGGSISRN SWEARTSSLL LECRKKHKEA
KRKVKAN
