NOP56_MOUSE
ID NOP56_MOUSE Reviewed; 580 AA.
AC Q9D6Z1; Q3UD45; Q8BVL1; Q8VDT2; Q99LT8; Q9CT15;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Nucleolar protein 56;
DE AltName: Full=Nucleolar protein 5A;
GN Name=Nop56; Synonyms=Nol5a;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, Thymus, and Tongue;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 ASSOCIATION WITH U14 BOX C/D SNORNA.
RX PubMed=10864044; DOI=10.1017/s1355838200992446;
RA Newman D.R., Kuhn J.F., Shanab G.M., Maxwell E.S.;
RT "Box C/D snoRNA-associated proteins: two pairs of evolutionarily ancient
RT proteins and possible links to replication and transcription.";
RL RNA 6:861-879(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-467; SER-513;
RP SER-536 AND SER-543, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-536, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-554, AND
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 AND SER-543, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465; SER-466; THR-467;
RP SER-513; SER-522; SER-528; SER-536; SER-543; THR-545; THR-546 AND SER-554,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-552 AND LYS-565, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:21683323}. Nucleus, nucleoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the
CC central nervous system (CNS), including cerebral cortex and cerebellum,
CC and spleen. In the CNS, expressed in Purkinje cells of the cerebellum,
CC as well as in motor neurons of the hypoglossal nucleus and in the
CC spinal cord anterior horn (at protein level).
CC {ECO:0000269|PubMed:21683323}.
CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
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DR EMBL; AK009799; BAB26511.1; -; mRNA.
DR EMBL; AK011481; BAB27647.3; -; mRNA.
DR EMBL; AK077795; BAC37015.1; -; mRNA.
DR EMBL; AK150258; BAE29417.1; -; mRNA.
DR EMBL; BC002231; AAH02231.1; -; mRNA.
DR EMBL; BC021355; AAH21355.1; -; mRNA.
DR CCDS; CCDS16737.1; -.
DR RefSeq; NP_077155.2; NM_024193.2.
DR AlphaFoldDB; Q9D6Z1; -.
DR SMR; Q9D6Z1; -.
DR BioGRID; 211966; 14.
DR CORUM; Q9D6Z1; -.
DR IntAct; Q9D6Z1; 11.
DR STRING; 10090.ENSMUSP00000099487; -.
DR iPTMnet; Q9D6Z1; -.
DR PhosphoSitePlus; Q9D6Z1; -.
DR SwissPalm; Q9D6Z1; -.
DR EPD; Q9D6Z1; -.
DR jPOST; Q9D6Z1; -.
DR MaxQB; Q9D6Z1; -.
DR PaxDb; Q9D6Z1; -.
DR PeptideAtlas; Q9D6Z1; -.
DR PRIDE; Q9D6Z1; -.
DR ProteomicsDB; 293703; -.
DR Antibodypedia; 23219; 128 antibodies from 26 providers.
DR DNASU; 67134; -.
DR Ensembl; ENSMUST00000103198; ENSMUSP00000099487; ENSMUSG00000027405.
DR GeneID; 67134; -.
DR KEGG; mmu:67134; -.
DR UCSC; uc008mil.1; mouse.
DR CTD; 10528; -.
DR MGI; MGI:1914384; Nop56.
DR VEuPathDB; HostDB:ENSMUSG00000027405; -.
DR eggNOG; KOG2573; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR HOGENOM; CLU_015495_4_1_1; -.
DR InParanoid; Q9D6Z1; -.
DR OMA; DNYMFAK; -.
DR OrthoDB; 632707at2759; -.
DR PhylomeDB; Q9D6Z1; -.
DR TreeFam; TF105713; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 67134; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Nop56; mouse.
DR PRO; PR:Q9D6Z1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D6Z1; protein.
DR Bgee; ENSMUSG00000027405; Expressed in embryonic post-anal tail and 73 other tissues.
DR ExpressionAtlas; Q9D6Z1; baseline and differential.
DR Genevisible; Q9D6Z1; MM.
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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISO:MGI.
DR GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IPI:MGI.
DR GO; GO:0030515; F:snoRNA binding; ISO:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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 Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW Ubl conjugation.
FT CHAIN 1..580
FT /note="Nucleolar protein 56"
FT /id="PRO_0000219027"
FT DOMAIN 292..410
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 458..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT MOD_RES 359
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT CROSSLNK 531
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00567"
FT CONFLICT 170
FT /note="Q -> K (in Ref. 1; BAC37015)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> V (in Ref. 1; BAB27647)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="T -> A (in Ref. 2; AAH21355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 64464 MW; 60AA1D43E349ADD7 CRC64;
MVLLHVLFEH AVGYALLALK EVEEISLLLP QVEECVLNLG KFHNVVRLVA FCPFSSSQVA
LENANAVSEG VVHEDLRLLL ETYLPSKKKK VLLGVGDPKI GAAIQEELGY NCQTGGVIAE
ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK
DINTFSMRVR EWYGYHFPEL VKIVNDNATY CRLAQFIGNR RELNEEKLEK LEEITMDGAK
AKAILDASRS SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI
GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL IFHSTFIGRA
AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ VEERLSFYET GEIPRKNLDV
MKEAVVQAEE AAAEITRKLE KQEKKRLKKE KKRLAALALA SSENSSTPEE CEEVNEKSKK
KKKLKPQENG MEDPPVSLPK SKKKKAPKEE LASDLEEMAT SSAKRKKSSP KEEVASEPEE
AASPTTPKKK RKFSEEPEVA ANFTKSSTKK KKKSQKAQED
