ID NOP56_HUMAN Reviewed; 594 AA. AC O00567; Q2M3T6; Q9NQ05; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 4. DT 04-NOV-2026, entry version 226. DE RecName: Full=Nucleolar protein 56; DE AltName: Full=Nucleolar protein 5A; GN Name=NOP56 {ECO:0000312|HGNC:HGNC:15911}; Synonyms=NOL5A; 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] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND VARIANT THR-475. RC TISSUE=Cervix carcinoma; RX PubMed=9372940; DOI=10.1128/mcb.17.12.7088; RA Gautier T., Berges T., Tollervey D., Hurt E.; RT "Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and RT are required for ribosome biogenesis."; RL Mol. Cell. Biol. 17:7088-7098(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [4] RP PROTEIN SEQUENCE OF 21-41; 78-87; 91-99; 127-134; 191-202; 213-220; RP 231-240; 271-278; 289-333; 348-359; 405-415; 423-437 AND 541-553, RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V.; RL Submitted (AUG-2005) to UniProtKB. RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [6] RP ASSOCIATION WITH U14 BOX C/D SNORNA. RX PubMed=12417735; DOI=10.1128/mcb.22.23.8342-8352.2002; RA Watkins N.J., Dickmanns A., Luhrmann R.; RT "Conserved stem II of the box C/D motif is essential for nucleolar RT localization and is required, along with the 15.5K protein, for the RT hierarchical assembly of the box C/D snoRNP."; RL Mol. Cell. Biol. 22:8342-8352(2002). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRE-RIBOSOMAL RNP RP COMPLEX, INTERACTION WITH TCOF1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12777385; DOI=10.1074/jbc.m304304200; RA Hayano T., Yanagida M., Yamauchi Y., Shinkawa T., Isobe T., Takahashi N.; RT "Proteomic analysis of human Nop56p-associated pre-ribosomal RT ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar RT protein treacle responsible for Treacher Collins syndrome."; RL J. Biol. Chem. 278:34309-34319(2003). RN [8] RP FUNCTION IN BOX C/D SNORNA BIOGENESIS, ASSOCIATION WITH U3 BOX C/D SNORNA, RP AND SUBCELLULAR LOCATION. RX PubMed=15574333; DOI=10.1016/j.molcel.2004.11.012; RA Watkins N.J., Lemm I., Ingelfinger D., Schneider C., Hossbach M., RA Urlaub H., Luehrmann R.; RT "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large RT dynamic multiprotein complex."; RL Mol. Cell 16:789-798(2004). RN [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [11] RP ASSOCIATION WITH U8 BOX C/D SNORNA, AND INTERACTION WITH NUFIP1. RX PubMed=17636026; DOI=10.1128/mcb.01097-07; RA McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.; RT "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP RT assembly."; RL Mol. Cell. Biol. 27:6782-6793(2007). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-519; SER-520; RP SER-570; SER-579 AND SER-581, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE 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 [14] 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 [15] RP INTERACTION WITH RUVBL1 AND RUVBL2. RX PubMed=19620283; DOI=10.1128/mcb.00752-09; RA McKeegan K.S., Debieux C.M., Watkins N.J.; RT "Evidence that the AAA+ proteins TIP48 and TIP49 bridge interactions RT between 15.5K and the related NOP56 and NOP58 proteins during box C/D RT snoRNP biogenesis."; RL Mol. Cell. Biol. 29:4971-4981(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; SER-520 AND SER-569, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY RP 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 [18] RP INVOLVEMENT IN SCA36. RX PubMed=21683323; DOI=10.1016/j.ajhg.2011.05.015; RA Kobayashi H., Abe K., Matsuura T., Ikeda Y., Hitomi T., Akechi Y., Habu T., RA Liu W., Okuda H., Koizumi A.; RT "Expansion of intronic GGCCTG hexanucleotide repeat in NOP56 causes SCA36, RT a type of spinocerebellar ataxia accompanied by motor neuron involvement."; RL Am. J. Hum. Genet. 89:121-130(2011). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-570, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-519; SER-520; RP SER-563; SER-569 AND SER-570, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND SER-563, AND RP 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 [23] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-359, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-540, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-540, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-230; LYS-240; LYS-540 AND RP LYS-564, AND 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). RN [27] RP INTERACTION WITH NOP2; FBL; RUVBL1 AND NUFIP1. RX PubMed=36161484; DOI=10.1093/nar/gkac817; RA Liao H., Gaur A., McConie H., Shekar A., Wang K., Chang J.T., Breton G., RA Denicourt C.; RT "Human NOP2/NSUN1 regulates ribosome biogenesis through non-catalytic RT complex formation with box C/D snoRNPs."; RL Nucleic Acids Res. 50:10695-10716(2022). RN [28] RP FUNCTION, AND IDENTIFICATION AS PART OF A BOX C/D SMALL NUCLEOLAR RP RIBONUCLEOPROTEIN (SNORNP) COMPLEX. RX PubMed=39570315; DOI=10.1073/pnas.2406961121; RA Zhang D., Li B., Xu H., Li J., Ma C., Ge W., Lu C., Cao X.; RT "Identification of FBLL1 as a neuron-specific RNA 2'-O-methyltransferase RT mediating neuronal differentiation."; RL Proc. Natl. Acad. Sci. U.S.A. 121:e2406961121-e2406961121(2024). RN [29] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION, SUBUNIT, AND SUBCELLULAR RP LOCATION. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). CC -!- FUNCTION: Involved in the early to middle stages of 60S ribosomal CC subunit biogenesis. Required for the biogenesis of box C/D snoRNAs such CC U3, U8 and U14 snoRNAs (PubMed:12777385, PubMed:15574333). Part of the CC small subunit (SSU) processome, first precursor of the small eukaryotic CC ribosomal subunit. During the assembly of the SSU processome in the CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and CC ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (PubMed:34516797). Core component of box C/D small CC nucleolar ribonucleoprotein (snoRNP) complexes that function in CC methylation of multiple sites on ribosomal RNAs (rRNAs) and messenger CC RNAs (mRNAs) (PubMed:12777385, PubMed:39570315). CC {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333, CC ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:39570315}. CC -!- SUBUNIT: Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, CC that consists of at least 62 ribosomal proteins, 45 nonribosomal CC proteins and both pre-rRNA and mature rRNA species. Within this complex CC directly interacts with TCOF1 in an RNA-independent manner. Core CC component of box C/D small nucleolar ribonucleoprotein (snoRNP) CC particles; the core proteins SNU13, NOP56, NOP58 and FBL or FBLL1 CC assemble stepwise onto the snoRNA. Interacts with NOP1 and NOP58. CC Interacts with NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge CC the association of NOP56 with NUFIP1. Part of the small subunit (SSU) CC processome, composed of more than 70 proteins and the RNA chaperone CC small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Interacts with NOP2 CC and FBL (PubMed:36161484). {ECO:0000269|PubMed:12777385, CC ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:19620283, CC ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36161484, CC ECO:0000269|PubMed:39570315}. CC -!- INTERACTION: CC O00567; O43818: RRP9; NbExp=2; IntAct=EBI-396034, EBI-2115327; CC O00567; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-396034, EBI-742426; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, CC ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:34516797, CC ECO:0000269|PubMed:9372940}. Cytoplasm {ECO:0000250|UniProtKB:Q9D6Z1}. CC Nucleus, nucleoplasm {ECO:0000305|PubMed:15574333}. CC -!- DISEASE: Spinocerebellar ataxia 36 (SCA36) [MIM:614153]: A form of CC spinocerebellar ataxia, a clinically and genetically heterogeneous CC group of cerebellar disorders. Patients show progressive incoordination CC of gait and often poor coordination of hands, speech and eye movements, CC due to degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. SCA36 is characterized by complicated CC clinical features, with ataxia as the first symptom, followed by CC characteristic late-onset involvement of the motor neuron system. CC Ataxic symptoms, such as gait and truncal instability, ataxic CC dysarthria, and uncoordinated limbs, start in late forties to fifties. CC Characteristically, affected individuals exhibit tongue atrophy with CC fasciculation. Progression of motor neuron involvement is typically CC limited to the tongue and main proximal skeletal muscles in both upper CC and lower extremities. {ECO:0000269|PubMed:21683323}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC Caused by large hexanucleotide CGCCTG repeat expansions within intron CC 1. These expansions induce RNA foci and sequester the RNA-binding CC protein SRSF2. In addition, the transcription of MIR1292, a microRNA CC gene located just 19 bp 3' of the GGCCTG repeat, is significantly CC decreased. CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA72789.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y12065; CAA72789.1; ALT_INIT; mRNA. DR EMBL; AL049712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC104791; AAI04792.1; -; mRNA. DR EMBL; BC104793; AAI04794.1; -; mRNA. DR CCDS; CCDS13030.1; -. DR RefSeq; NP_006383.2; NM_006392.4. DR PDB; 7MQ8; EM; 3.60 A; SA=1-594. DR PDB; 7MQ9; EM; 3.87 A; SA=1-594. DR PDB; 7MQA; EM; 2.70 A; SA=1-594. DR AlphaFoldDB; O00567; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR SMR; O00567; -. DR BioGRID; 115783; 644. DR ComplexPortal; CPX-2511; Small ribosomal subunit processome. DR ComplexPortal; CPX-26377; Box C/D snoRNA-Guided RNP methyltransferase complex, FBLL1 variant. DR ComplexPortal; CPX-26423; Box C/D snoRNA-guided RNP methyltransferase complex, FBL variant. DR CORUM; O00567; -. DR FunCoup; O00567; 3121. DR IntAct; O00567; 254. DR STRING; 9606.ENSP00000370589; -. DR BindingDB; O00567; -. DR ChEMBL; CHEMBL6066335; -. DR GlyConnect; O00567; 1 N-Linked glycan (1 site). DR GlyCosmos; O00567; 4 sites, 4 glycans. DR GlyGen; O00567; 4 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (3 sites). DR iPTMnet; O00567; -. DR MetOSite; O00567; -. DR PhosphoSitePlus; O00567; -. DR SwissPalm; O00567; -. DR BioMuta; NOP56; -. DR jPOST; O00567; -. DR MassIVE; O00567; -. DR PaxDb; 9606-ENSP00000370589; -. DR PeptideAtlas; O00567; -. DR ProteomicsDB; 47980; -. DR Pumba; O00567; -. DR Antibodypedia; 23219; 146 antibodies from 29 providers. DR DNASU; 10528; -. DR Ensembl; ENST00000329276.10; ENSP00000370589.3; ENSG00000101361.18. DR GeneID; 10528; -. DR KEGG; hsa:10528; -. DR MANE-Select; ENST00000329276.10; ENSP00000370589.3; NM_006392.4; NP_006383.2. DR UCSC; uc002wgh.4; human. DR AGR; HGNC:15911; -. DR ClinPGx; PA164724063; -. DR CTD; 10528; -. DR DisGeNET; 10528; -. DR GeneCards; NOP56; -. DR GeneReviews; NOP56; -. DR HGNC; HGNC:15911; NOP56. DR HPA; ENSG00000101361; Low tissue specificity. DR MalaCards; NOP56; -. DR MIM; 614153; phenotype. DR MIM; 614154; gene. DR OpenTargets; ENSG00000101361; -. DR Orphanet; 276198; Spinocerebellar ataxia type 36. DR VEuPathDB; HostDB:ENSG00000101361; -. DR eggNOG; KOG2573; Eukaryota. DR GeneTree; ENSGT00940000153534; -. DR HOGENOM; CLU_015495_4_0_1; -. DR InParanoid; O00567; -. DR OMA; AAELNCN; -. DR OrthoDB; 6780543at2759; -. DR PAN-GO; O00567; 3 GO annotations based on evolutionary models. DR PhylomeDB; O00567; -. DR PathwayCommons; O00567; -. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; O00567; -. DR SIGNOR; O00567; -. DR Agora; ENSG00000101361; -. DR BioGRID-ORCS; 10528; 805 hits in 1163 CRISPR screens. DR CD-CODE; 08386919; Dense Fibrillar Component. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 6F24707C; Cajal body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; NOP56; human. DR GeneWiki; NOL5A; -. DR GenomeRNAi; 10528; -. DR Pharos; O00567; Tbio. DR PRO; PR:O00567; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O00567; protein. DR Bgee; ENSG00000101361; Expressed in cervix squamous epithelium and 209 other cell types or tissues. DR ExpressionAtlas; O00567; baseline and differential. DR GO; GO:0031428; C:box C/D methylation guide snoRNP complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IPI:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IDA:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:1990226; F:histone methyltransferase binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0030515; F:snoRNA binding; IDA:BHF-UCL. DR GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal. DR GO; GO:0016556; P:mRNA modification; NAS:ComplexPortal. DR GO; GO:0030182; P:neuron differentiation; NAS:ComplexPortal. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0000451; P:rRNA 2'-O-methylation; NAS:ComplexPortal. DR GO; GO:0006364; P:rRNA processing; TAS:ProtInc. DR FunFam; 1.10.246.90:FF:000001; Nucleolar protein 56; 1. DR FunFam; 1.10.287.4070:FF:000002; Nucleolar protein 56; 1. DR Gene3D; 1.10.287.4070; -; 1. DR Gene3D; 1.10.246.90; Nop domain; 1. DR InterPro; IPR045056; Nop56/Nop58. DR InterPro; IPR012974; NOP58/56_N. DR InterPro; IPR042239; Nop_C. DR InterPro; IPR002687; Nop_dom. DR InterPro; IPR036070; Nop_dom_sf. DR InterPro; IPR012976; NOSIC. DR PANTHER; PTHR10894; NUCLEOLAR PROTEIN 5 NUCLEOLAR PROTEIN NOP5 NOP58; 1. DR PANTHER; PTHR10894:SF0; NUCLEOLAR PROTEIN 56; 1. DR Pfam; PF01798; Nop; 1. DR Pfam; PF08156; NOP5NT; 1. DR SMART; SM00931; NOSIC; 1. DR SUPFAM; SSF89124; Nop domain; 1. DR PROSITE; PS51358; NOP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Methylation; Neurodegeneration; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Ribonucleoprotein; KW Ribosome biogenesis; Spinocerebellar ataxia; Ubl conjugation. FT CHAIN 1..594 FT /note="Nucleolar protein 56" FT /id="PRO_0000219025" FT DOMAIN 292..410 FT /note="Nop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690" FT REGION 458..594 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 458..469 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..504 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 580..594 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 359 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 466 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D6Z1" FT MOD_RES 467 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D6Z1" FT MOD_RES 468 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D6Z1" FT MOD_RES 511 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 519 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 520 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 537 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D6Z1" FT MOD_RES 561 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D6Z1" FT MOD_RES 563 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 570 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 579 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 87 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 230 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 540 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 564 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 121 FT /note="I -> V (in dbSNP:rs2273137)" FT /id="VAR_028793" FT VARIANT 475 FT /note="M -> T (in dbSNP:rs6753)" FT /evidence="ECO:0000269|PubMed:9372940" FT /id="VAR_028794" FT VARIANT 576 FT /note="V -> A (in dbSNP:rs5856)" FT /id="VAR_014471" FT CONFLICT 17 FT /note="L -> V (in Ref. 1; CAA72789)" FT /evidence="ECO:0000305" FT CONFLICT 427 FT /note="Q -> QAE (in Ref. 1; CAA72789)" FT /evidence="ECO:0000305" FT CONFLICT 555 FT /note="G -> R (in Ref. 1; CAA72789)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 11..19 FT /evidence="ECO:0007829|PDB:7MQA" FT TURN 25..28 FT /evidence="ECO:0007829|PDB:7MQA" FT TURN 30..33 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 34..37 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 39..45 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 57..69 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 74..83 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 118..127 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 129..132 FT /evidence="ECO:0007829|PDB:7MQA" FT TURN 133..136 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 141..157 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 166..196 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 207..216 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 226..234 FT /evidence="ECO:0007829|PDB:7MQA" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 238..249 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 258..292 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 294..300 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 302..312 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 315..320 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 323..329 FT /evidence="ECO:0007829|PDB:7MQA" FT TURN 330..337 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 365..385 FT /evidence="ECO:0007829|PDB:7MQA" FT HELIX 392..410 FT /evidence="ECO:0007829|PDB:7MQA" SQ SEQUENCE 594 AA; 66050 MW; 17D81E25DEBD052F CRC64; MVLLHVLFEH AVGYALLALK EVEEISLLQP QVEESVLNLG KFHSIVRLVA FCPFASSQVA LENANAVSEG VVHEDLRLLL ETHLPSKKKK VLLGVGDPKI GAAIQEELGY NCQTGGVIAE ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK DINTFSMRVR EWYGYHFPEL VKIINDNATY CRLAQFIGNR RELNEDKLEK LEELTMDGAK AKAILDASRS SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL IFHSTFIGRA AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ VEERLSFYET GEIPRKNLDV MKEAMVQAEE AAAEITRKLE KQEKKRLKKE KKRLAALALA SSENSSSTPE ECEEMSEKPK KKKKQKPQEV PQENGMEDPS ISFSKPKKKK SFSKEELMSS DLEETAGSTS IPKRKKSTPK EETVNDPEEA GHRSGSKKKR KFSKEEPVSS GPEEAVGKSS SKKKKKFHKA SQED //