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Protein

Nucleolar protein 56

Gene

Nop56

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis

Enzyme and pathway databases

ReactomeiR-MMU-6791226. Major pathway of rRNA processing in the nucleolus.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar protein 56
Alternative name(s):
Nucleolar protein 5A
Gene namesi
Name:Nop56
Synonyms:Nol5a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914384. Nop56.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Nucleolar protein 56PRO_0000219027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei314 – 3141PhosphoserineBy similarity
Modified residuei465 – 4651PhosphoserineCombined sources
Modified residuei466 – 4661PhosphoserineCombined sources
Modified residuei467 – 4671PhosphothreonineCombined sources
Modified residuei513 – 5131PhosphoserineCombined sources
Modified residuei522 – 5221PhosphoserineCombined sources
Modified residuei528 – 5281PhosphoserineCombined sources
Cross-linki531 – 531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei536 – 5361PhosphoserineCombined sources
Modified residuei543 – 5431PhosphoserineCombined sources
Modified residuei545 – 5451PhosphothreonineCombined sources
Modified residuei546 – 5461PhosphothreonineCombined sources
Modified residuei552 – 5521N6-acetyllysineCombined sources
Modified residuei554 – 5541PhosphoserineCombined sources
Modified residuei565 – 5651N6-acetyllysineCombined sources
Modified residuei567 – 5671PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D6Z1.
MaxQBiQ9D6Z1.
PaxDbiQ9D6Z1.
PeptideAtlasiQ9D6Z1.
PRIDEiQ9D6Z1.

PTM databases

iPTMnetiQ9D6Z1.
PhosphoSiteiQ9D6Z1.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in the central nervous system (CNS), including cerebral cortex and cerebellum, and spleen. In the CNS, expressed in Purkinje cells of the cerebellum, as well as in motor neurons of the hypoglossal nucleus and in the spinal cord anterior horn (at protein level).1 Publication

Gene expression databases

BgeeiQ9D6Z1.
CleanExiMM_NOL5A.
ExpressionAtlasiQ9D6Z1. baseline and differential.
GenevisibleiQ9D6Z1. MM.

Interactioni

Subunit structurei

Part of a large pre-ribosomal ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA species. Within this complex directly interacts with TCOF1 in an RNA-independent manner. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles; the core proteins SNU13, NOP56, NOP58 and FBL assemble stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP56 with NUFIP1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211966. 4 interactions.
IntActiQ9D6Z1. 7 interactions.
MINTiMINT-1868279.
STRINGi10090.ENSMUSP00000099487.

Structurei

3D structure databases

ProteinModelPortaliQ9D6Z1.
SMRiQ9D6Z1. Positions 148-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini292 – 410119NopPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi438 – 576139Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the NOP5/NOP56 family.Curated
Contains 1 Nop domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2572. Eukaryota.
COG1498. LUCA.
GeneTreeiENSGT00550000075068.
HOGENOMiHOG000196309.
InParanoidiQ9D6Z1.
KOiK14564.
OMAiMETNMPE.
OrthoDBiEOG7T7GT0.
PhylomeDBiQ9D6Z1.
TreeFamiTF105713.

Family and domain databases

InterProiIPR012974. NOP5_N.
IPR002687. Nop_dom.
IPR012976. NOSIC.
[Graphical view]
PfamiPF01798. Nop. 1 hit.
PF08156. NOP5NT. 1 hit.
[Graphical view]
SMARTiSM00931. NOSIC. 1 hit.
[Graphical view]
SUPFAMiSSF89124. SSF89124. 1 hit.
PROSITEiPS51358. NOP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D6Z1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLHVLFEH AVGYALLALK EVEEISLLLP QVEECVLNLG KFHNVVRLVA
60 70 80 90 100
FCPFSSSQVA LENANAVSEG VVHEDLRLLL ETYLPSKKKK VLLGVGDPKI
110 120 130 140 150
GAAIQEELGY NCQTGGVIAE ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH
160 170 180 190 200
SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK DINTFSMRVR EWYGYHFPEL
210 220 230 240 250
VKIVNDNATY CRLAQFIGNR RELNEEKLEK LEEITMDGAK AKAILDASRS
260 270 280 290 300
SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI
310 320 330 340 350
GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL
360 370 380 390 400
IFHSTFIGRA AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ
410 420 430 440 450
VEERLSFYET GEIPRKNLDV MKEAVVQAEE AAAEITRKLE KQEKKRLKKE
460 470 480 490 500
KKRLAALALA SSENSSTPEE CEEVNEKSKK KKKLKPQENG MEDPPVSLPK
510 520 530 540 550
SKKKKAPKEE LASDLEEMAT SSAKRKKSSP KEEVASEPEE AASPTTPKKK
560 570 580
RKFSEEPEVA ANFTKSSTKK KKKSQKAQED
Length:580
Mass (Da):64,464
Last modified:May 16, 2003 - v2
Checksum:i60AA1D43E349ADD7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701Q → K in BAC37015 (PubMed:16141072).Curated
Sequence conflicti182 – 1821I → V in BAB27647 (PubMed:16141072).Curated
Sequence conflicti436 – 4361T → A in AAH21355 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009799 mRNA. Translation: BAB26511.1.
AK011481 mRNA. Translation: BAB27647.3.
AK077795 mRNA. Translation: BAC37015.1.
AK150258 mRNA. Translation: BAE29417.1.
BC002231 mRNA. Translation: AAH02231.1.
BC021355 mRNA. Translation: AAH21355.1.
CCDSiCCDS16737.1.
RefSeqiNP_077155.2. NM_024193.2.
UniGeneiMm.29363.

Genome annotation databases

EnsembliENSMUST00000103198; ENSMUSP00000099487; ENSMUSG00000027405.
GeneIDi67134.
KEGGimmu:67134.
UCSCiuc008mil.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009799 mRNA. Translation: BAB26511.1.
AK011481 mRNA. Translation: BAB27647.3.
AK077795 mRNA. Translation: BAC37015.1.
AK150258 mRNA. Translation: BAE29417.1.
BC002231 mRNA. Translation: AAH02231.1.
BC021355 mRNA. Translation: AAH21355.1.
CCDSiCCDS16737.1.
RefSeqiNP_077155.2. NM_024193.2.
UniGeneiMm.29363.

3D structure databases

ProteinModelPortaliQ9D6Z1.
SMRiQ9D6Z1. Positions 148-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211966. 4 interactions.
IntActiQ9D6Z1. 7 interactions.
MINTiMINT-1868279.
STRINGi10090.ENSMUSP00000099487.

PTM databases

iPTMnetiQ9D6Z1.
PhosphoSiteiQ9D6Z1.

Proteomic databases

EPDiQ9D6Z1.
MaxQBiQ9D6Z1.
PaxDbiQ9D6Z1.
PeptideAtlasiQ9D6Z1.
PRIDEiQ9D6Z1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103198; ENSMUSP00000099487; ENSMUSG00000027405.
GeneIDi67134.
KEGGimmu:67134.
UCSCiuc008mil.1. mouse.

Organism-specific databases

CTDi10528.
MGIiMGI:1914384. Nop56.

Phylogenomic databases

eggNOGiKOG2572. Eukaryota.
COG1498. LUCA.
GeneTreeiENSGT00550000075068.
HOGENOMiHOG000196309.
InParanoidiQ9D6Z1.
KOiK14564.
OMAiMETNMPE.
OrthoDBiEOG7T7GT0.
PhylomeDBiQ9D6Z1.
TreeFamiTF105713.

Enzyme and pathway databases

ReactomeiR-MMU-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

ChiTaRSiNop56. mouse.
PROiQ9D6Z1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D6Z1.
CleanExiMM_NOL5A.
ExpressionAtlasiQ9D6Z1. baseline and differential.
GenevisibleiQ9D6Z1. MM.

Family and domain databases

InterProiIPR012974. NOP5_N.
IPR002687. Nop_dom.
IPR012976. NOSIC.
[Graphical view]
PfamiPF01798. Nop. 1 hit.
PF08156. NOP5NT. 1 hit.
[Graphical view]
SMARTiSM00931. NOSIC. 1 hit.
[Graphical view]
SUPFAMiSSF89124. SSF89124. 1 hit.
PROSITEiPS51358. NOP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryo, Thymus and Tongue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  3. "Box C/D snoRNA-associated proteins: two pairs of evolutionarily ancient proteins and possible links to replication and transcription."
    Newman D.R., Kuhn J.F., Shanab G.M., Maxwell E.S.
    RNA 6:861-879(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH U14 BOX C/D SNORNA.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-467; SER-513; SER-536 AND SER-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-536, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 AND SER-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465; SER-466; THR-467; SER-513; SER-522; SER-528; SER-536; SER-543; THR-545; THR-546 AND SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "Expansion of intronic GGCCTG hexanucleotide repeat in NOP56 causes SCA36, a type of spinocerebellar ataxia accompanied by motor neuron involvement."
    Kobayashi H., Abe K., Matsuura T., Ikeda Y., Hitomi T., Akechi Y., Habu T., Liu W., Okuda H., Koizumi A.
    Am. J. Hum. Genet. 89:121-130(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-552 AND LYS-565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNOP56_MOUSE
AccessioniPrimary (citable) accession number: Q9D6Z1
Secondary accession number(s): Q3UD45
, Q8BVL1, Q8VDT2, Q99LT8, Q9CT15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 16, 2003
Last modified: July 6, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.