O00567 (NOP56_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleolar protein 56

Alternative name(s):
Nucleolar protein 5A

Gene names

Name:	NOP56
Synonyms:	NOL5A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Ref.6
Subunit structure	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. Interacts with NOP1 and NOP58. Ref.6
Subcellular location	Nucleus › nucleolus. Cytoplasm By similarity Ref.4 Ref.5 Ref.6.
Involvement in disease	Defects in NOP56 are the cause of spinocerebellar ataxia type 36 (SCA36) [MIM:614153]. A 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. Note=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. Ref.13
Sequence similarities	Belongs to the NOP5/NOP56 family. Contains 1 Nop domain.
Sequence caution	The sequence CAA72789.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Ribosome biogenesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Neurodegeneration Spinocerebellar ataxia
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW rRNA processing Traceable author statement. Source: ProtInc
Cellular component	box C/D snoRNP complex Non-traceable author statement. Source: BHF-UCL cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell pre-snoRNP complex Inferred from direct assay. Source: BHF-UCL
Molecular function	protein binding Inferred from physical interaction. Source: BHF-UCL snoRNA binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 594	594	Nucleolar protein 56		PRO_0000219025
Regions
	Domain	263 – 411	149	Nop
	Compositional bias	438 – 589	152	Lys-rich
Amino acid modifications
	Modified residue	406	1	Phosphoserine Ref.8
	Modified residue	467	1	Phosphoserine By similarity
	Modified residue	468	1	Phosphothreonine By similarity
	Modified residue	511	1	Phosphoserine Ref.11
	Modified residue	519	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	520	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	563	1	Phosphoserine By similarity
	Modified residue	569	1	Phosphoserine Ref.9 Ref.12
	Modified residue	570	1	Phosphoserine Ref.9 Ref.11 Ref.12
	Modified residue	579	1	Phosphoserine Ref.11
	Modified residue	581	1	Phosphoserine Ref.11
Natural variations
	Natural variant	121	1	I → V. Corresponds to variant rs2273137 [ dbSNP | Ensembl ].		VAR_028793
	Natural variant	475	1	M → T. Ref.1 Corresponds to variant rs6753 [ dbSNP | Ensembl ].		VAR_028794
	Natural variant	576	1	V → A. Corresponds to variant rs5856 [ dbSNP | Ensembl ].		VAR_014471
Experimental info
	Sequence conflict	17	1	L → V in CAA72789. Ref.1
	Sequence conflict	427	1	Q → QAE in CAA72789. Ref.1
	Sequence conflict	555	1	G → R in CAA72789. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O00567 [UniParc]. Last modified October 31, 2006. Version 4. Checksum: 17D81E25DEBD052F	FASTA	594	66,050
	10 20 30 40 50 60 MVLLHVLFEH AVGYALLALK EVEEISLLQP QVEESVLNLG KFHSIVRLVA FCPFASSQVA 70 80 90 100 110 120 LENANAVSEG VVHEDLRLLL ETHLPSKKKK VLLGVGDPKI GAAIQEELGY NCQTGGVIAE 130 140 150 160 170 180 ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK 190 200 210 220 230 240 DINTFSMRVR EWYGYHFPEL VKIINDNATY CRLAQFIGNR RELNEDKLEK LEELTMDGAK 250 260 270 280 290 300 AKAILDASRS SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI 310 320 330 340 350 360 GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL IFHSTFIGRA 370 380 390 400 410 420 AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ VEERLSFYET GEIPRKNLDV 430 440 450 460 470 480 MKEAMVQAEE AAAEITRKLE KQEKKRLKKE KKRLAALALA SSENSSSTPE ECEEMSEKPK 490 500 510 520 530 540 KKKKQKPQEV PQENGMEDPS ISFSKPKKKK SFSKEELMSS DLEETAGSTS IPKRKKSTPK 550 560 570 580 590 EETVNDPEEA GHRSGSKKKR KFSKEEPVSS GPEEAVGKSS SKKKKKFHKA SQED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis." Gautier T., Berges T., Tollervey D., Hurt E. Mol. Cell. Biol. 17:7088-7098(1997) [PubMed: 9372940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-475. Tissue: Cervix carcinoma.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	Bienvenut W.V. Submitted (AUG-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 21-41; 78-87; 91-99; 127-134; 191-202; 213-220; 231-240; 271-278; 289-333; 348-359; 405-415; 423-437 AND 541-553, SUBCELLULAR LOCATION, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed: 12429849] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome." Hayano T., Yanagida M., Yamauchi Y., Shinkawa T., Isobe T., Takahashi N. J. Biol. Chem. 278:34309-34319(2003) [PubMed: 12777385] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRE-RIBOSOMAL RNP COMPLEX, INTERACTION WITH TCOF1, MASS SPECTROMETRY.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-520, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[9]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; SER-520; SER-569 AND SER-570, MASS SPECTROMETRY. Tissue: Prostate cancer.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-520, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-519; SER-520; SER-570; SER-579 AND SER-581, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; SER-520; SER-569 AND SER-570, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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: 21683323] [Abstract] Cited for: INVOLVEMENT IN SCA36.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12065 mRNA. Translation: CAA72789.1. Different initiation. AL049712 Genomic DNA. Translation: CAC01444.2. BC104791 mRNA. Translation: AAI04792.1. BC104793 mRNA. Translation: AAI04794.1.
IPI	IPI00411937.
RefSeq	NP_006383.2. NM_006392.3.
UniGene	Hs.376064.
3D structure databases
ProteinModelPortal	O00567.
SMR	O00567. Positions 6-411.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00567. 9 interactions.
STRING	O00567.
PTM databases
PhosphoSite	O00567.
2D gel databases
SWISS-2DPAGE	O00567.
Proteomic databases
PRIDE	O00567.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000329276; ENSP00000370589; ENSG00000101361.
GeneID	10528.
KEGG	hsa:10528.
NMPDR	fig|9606.3.peg.19735.
UCSC	uc002wgh.1. human.
Organism-specific databases
CTD	10528.
GeneCards	GC20P002681.
H-InvDB	HIX0015577.
HGNC	HGNC:15911. NOP56.
MIM	614153. phenotype. 614154. gene.
neXtProt	NX_O00567.
PharmGKB	PA164724063.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG611715.
InParanoid	O00567.
OMA	NHIIQAI.
OrthoDB	EOG41G342.
PhylomeDB	O00567.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	O00567.
Bgee	O00567.
Genevestigator	O00567.
GermOnline	ENSG00000101361. Homo sapiens.
Family and domain databases
InterPro	IPR012974. NOP5_N. IPR012976. NOSIC. IPR002687. SnoRNA-bd_dom. [Graphical view]
KO	K14564.
Pfam	PF01798. Nop. 1 hit. PF08156. NOP5NT. 1 hit. PF08060. NOSIC. 1 hit. [Graphical view]
SMART	SM00931. NOSIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	39942.
SOURCE	Search...

Entry information

Entry name

NOP56_HUMAN

Accession

Primary (citable) accession number: O00567
Secondary accession number(s): Q2M3T6, Q9NQ05

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 31, 2006
Last modified:	January 25, 2012
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.