NOP56_HUMAN
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 03-AUG-2022, entry version 206.
DE RecName: Full=Nucleolar protein 56;
DE AltName: Full=Nucleolar protein 5A;
GN Name=NOP56; 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).
CC -!- FUNCTION: Involved in the early to middle stages of 60S ribosomal
CC subunit biogenesis. Core component of box C/D small nucleolar
CC ribonucleoprotein (snoRNP) particles. Required for the biogenesis of
CC box C/D snoRNAs such U3, U8 and U14 snoRNAs.
CC {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333}.
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 assemble
CC stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with
CC NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association
CC of NOP56 with NUFIP1. {ECO:0000269|PubMed:12777385,
CC ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:19620283}.
CC -!- INTERACTION:
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:9372940}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9D6Z1}. Nucleus, nucleoplasm
CC {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};
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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_006392.3.
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 PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; O00567; -.
DR SMR; O00567; -.
DR BioGRID; 115783; 554.
DR CORUM; O00567; -.
DR IntAct; O00567; 215.
DR MINT; O00567; -.
DR STRING; 9606.ENSP00000370589; -.
DR GlyConnect; 1580; 1 N-Linked glycan (1 site).
DR GlyGen; O00567; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; O00567; -.
DR MetOSite; O00567; -.
DR PhosphoSitePlus; O00567; -.
DR SwissPalm; O00567; -.
DR BioMuta; NOP56; -.
DR SWISS-2DPAGE; O00567; -.
DR EPD; O00567; -.
DR jPOST; O00567; -.
DR MassIVE; O00567; -.
DR MaxQB; O00567; -.
DR PaxDb; O00567; -.
DR PeptideAtlas; O00567; -.
DR PRIDE; O00567; -.
DR ProteomicsDB; 47980; -.
DR Antibodypedia; 23219; 128 antibodies from 26 providers.
DR DNASU; 10528; -.
DR Ensembl; ENST00000329276.10; ENSP00000370589.3; ENSG00000101361.17.
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 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 neXtProt; NX_O00567; -.
DR OpenTargets; ENSG00000101361; -.
DR Orphanet; 276198; Spinocerebellar ataxia type 36.
DR PharmGKB; PA164724063; -.
DR VEuPathDB; HostDB:ENSG00000101361; -.
DR eggNOG; KOG2573; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR HOGENOM; CLU_015495_4_0_1; -.
DR InParanoid; O00567; -.
DR OMA; DNYMFAK; -.
DR OrthoDB; 632707at2759; -.
DR PhylomeDB; O00567; -.
DR TreeFam; TF105713; -.
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 BioGRID-ORCS; 10528; 763 hits in 1080 CRISPR screens.
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 207 other tissues.
DR ExpressionAtlas; O00567; baseline and differential.
DR Genevisible; O00567; HS.
DR GO; GO:0031428; C:box C/D RNP complex; IBA:GO_Central.
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; TAS:ProtInc.
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; IBA:GO_Central.
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:0006364; P:rRNA processing; TAS:ProtInc.
DR Gene3D; 1.10.246.90; -; 1.
DR InterPro; IPR045056; Nop56/Nop58.
DR InterPro; IPR012974; NOP5_N.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR PANTHER; PTHR10894; PTHR10894; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF08156; NOP5NT; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 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 Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW 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 471..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..568
FT /note="Basic and acidic 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"
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
