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Protein

Nucleolar protein 56

Gene

NOP56

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • histone methyltransferase binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • snoRNA binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Ribosome biogenesis

Enzyme and pathway databases

ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-6790901. rRNA modification in the nucleus.
R-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15911. NOP56.

Subcellular locationi

GO - Cellular componenti

  • box C/D snoRNP complex Source: BHF-UCL
  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • pre-snoRNP complex Source: BHF-UCL
  • small nucleolar ribonucleoprotein complex Source: BHF-UCL
  • small-subunit processome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 36 (SCA36)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. Caused by large hexanucleotide CGCCTG repeat expansions within intron 1. These expansions induce RNA foci and sequester the RNA-binding protein SRSF2. In addition, the transcription of MIR1292, a microRNA gene located just 19 bp 3' of the GGCCTG repeat, is significantly decreased.
Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA36 is characterized by complicated clinical features, with ataxia as the first symptom, followed by characteristic late-onset involvement of the motor neuron system. Ataxic symptoms, such as gait and truncal instability, ataxic dysarthria, and uncoordinated limbs, start in late forties to fifties. Characteristically, affected individuals exhibit tongue atrophy with fasciculation. Progression of motor neuron involvement is typically limited to the tongue and main proximal skeletal muscles in both upper and lower extremities.
See also OMIM:614153

Keywords - Diseasei

Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MalaCardsiNOP56.
MIMi614153. phenotype.
Orphaneti276198. Spinocerebellar ataxia type 36.
PharmGKBiPA164724063.

Polymorphism and mutation databases

BioMutaiNOP56.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Nucleolar protein 56PRO_0000219025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei466 – 4661PhosphoserineBy similarity
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei468 – 4681PhosphothreonineBy similarity
Modified residuei511 – 5111PhosphoserineCombined sources
Modified residuei519 – 5191PhosphoserineCombined sources
Modified residuei520 – 5201PhosphoserineCombined sources
Modified residuei537 – 5371PhosphoserineBy similarity
Cross-linki540 – 540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei561 – 5611N6-acetyllysineBy similarity
Modified residuei563 – 5631PhosphoserineCombined sources
Modified residuei569 – 5691PhosphoserineCombined sources
Modified residuei570 – 5701PhosphoserineCombined sources
Modified residuei579 – 5791PhosphoserineCombined sources
Modified residuei581 – 5811PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO00567.
MaxQBiO00567.
PaxDbiO00567.
PeptideAtlasiO00567.
PRIDEiO00567.

2D gel databases

SWISS-2DPAGEO00567.

PTM databases

iPTMnetiO00567.
PhosphoSiteiO00567.
SwissPalmiO00567.

Expressioni

Gene expression databases

BgeeiENSG00000101361.
ExpressionAtlasiO00567. baseline and differential.
GenevisibleiO00567. HS.

Organism-specific databases

HPAiCAB075757.
HPA049918.

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 NUFIP1.3 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • histone methyltransferase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115783. 263 interactions.
IntActiO00567. 153 interactions.
MINTiMINT-2997885.
STRINGi9606.ENSP00000370589.

Structurei

3D structure databases

ProteinModelPortaliO00567.
SMRiO00567. 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 – 589152Lys-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.
InParanoidiO00567.
KOiK14564.
OMAiTRVHFER.
OrthoDBiEOG091G06JZ.
PhylomeDBiO00567.
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.

O00567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLHVLFEH AVGYALLALK EVEEISLLQP QVEESVLNLG KFHSIVRLVA
60 70 80 90 100
FCPFASSQVA LENANAVSEG VVHEDLRLLL ETHLPSKKKK 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
VKIINDNATY CRLAQFIGNR RELNEDKLEK LEELTMDGAK 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 MKEAMVQAEE AAAEITRKLE KQEKKRLKKE
460 470 480 490 500
KKRLAALALA SSENSSSTPE ECEEMSEKPK KKKKQKPQEV PQENGMEDPS
510 520 530 540 550
ISFSKPKKKK SFSKEELMSS DLEETAGSTS IPKRKKSTPK EETVNDPEEA
560 570 580 590
GHRSGSKKKR KFSKEEPVSS GPEEAVGKSS SKKKKKFHKA SQED
Length:594
Mass (Da):66,050
Last modified:October 31, 2006 - v4
Checksum:i17D81E25DEBD052F
GO

Sequence cautioni

The sequence CAA72789 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171L → V in CAA72789 (PubMed:9372940).Curated
Sequence conflicti427 – 4271Q → QAE in CAA72789 (PubMed:9372940).Curated
Sequence conflicti555 – 5551G → R in CAA72789 (PubMed:9372940).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211I → V.
Corresponds to variant rs2273137 [ dbSNP | Ensembl ].
VAR_028793
Natural varianti475 – 4751M → T.1 Publication
Corresponds to variant rs6753 [ dbSNP | Ensembl ].
VAR_028794
Natural varianti576 – 5761V → A.
Corresponds to variant rs5856 [ dbSNP | Ensembl ].
VAR_014471

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12065 mRNA. Translation: CAA72789.1. Different initiation.
AL049712 Genomic DNA. Translation: CAC01444.2.
BC104791 mRNA. Translation: AAI04792.1.
BC104793 mRNA. Translation: AAI04794.1.
CCDSiCCDS13030.1.
RefSeqiNP_006383.2. NM_006392.3.
UniGeneiHs.376064.

Genome annotation databases

EnsembliENST00000329276; ENSP00000370589; ENSG00000101361.
GeneIDi10528.
KEGGihsa:10528.
UCSCiuc002wgh.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12065 mRNA. Translation: CAA72789.1. Different initiation.
AL049712 Genomic DNA. Translation: CAC01444.2.
BC104791 mRNA. Translation: AAI04792.1.
BC104793 mRNA. Translation: AAI04794.1.
CCDSiCCDS13030.1.
RefSeqiNP_006383.2. NM_006392.3.
UniGeneiHs.376064.

3D structure databases

ProteinModelPortaliO00567.
SMRiO00567. Positions 148-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115783. 263 interactions.
IntActiO00567. 153 interactions.
MINTiMINT-2997885.
STRINGi9606.ENSP00000370589.

PTM databases

iPTMnetiO00567.
PhosphoSiteiO00567.
SwissPalmiO00567.

Polymorphism and mutation databases

BioMutaiNOP56.

2D gel databases

SWISS-2DPAGEO00567.

Proteomic databases

EPDiO00567.
MaxQBiO00567.
PaxDbiO00567.
PeptideAtlasiO00567.
PRIDEiO00567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329276; ENSP00000370589; ENSG00000101361.
GeneIDi10528.
KEGGihsa:10528.
UCSCiuc002wgh.4. human.

Organism-specific databases

CTDi10528.
GeneCardsiNOP56.
HGNCiHGNC:15911. NOP56.
HPAiCAB075757.
HPA049918.
MalaCardsiNOP56.
MIMi614153. phenotype.
614154. gene.
neXtProtiNX_O00567.
Orphaneti276198. Spinocerebellar ataxia type 36.
PharmGKBiPA164724063.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2572. Eukaryota.
COG1498. LUCA.
GeneTreeiENSGT00550000075068.
HOGENOMiHOG000196309.
InParanoidiO00567.
KOiK14564.
OMAiTRVHFER.
OrthoDBiEOG091G06JZ.
PhylomeDBiO00567.
TreeFamiTF105713.

Enzyme and pathway databases

ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-6790901. rRNA modification in the nucleus.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus.

Miscellaneous databases

ChiTaRSiNOP56. human.
GeneWikiiNOL5A.
GenomeRNAii10528.
PROiO00567.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101361.
ExpressionAtlasiO00567. baseline and differential.
GenevisibleiO00567. HS.

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...

Entry informationi

Entry nameiNOP56_HUMAN
AccessioniPrimary (citable) accession number: O00567
Secondary accession number(s): Q2M3T6, Q9NQ05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2006
Last modified: September 7, 2016
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.