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Nucleolar protein 56

 
Known also as: Nucleolar protein 5A

Known abbreviations: NOP56, NOL5A

 

FUNCTION:
 
Involved in the early to middle stages of 60S ribosomal subunit biogenesis. 
 
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. 
 
CELLULAR LOCALIZATION:
 
Nucleus › nucleolus. Cytoplasm (By similarity)
 
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. 



This protein can be a part of a given complexes: Activities in which Nucleolar protein 56 is involved: Pathways in which Nucleolar protein 56 is involved:

NCBI GI number(s): 32483374
343183410
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O00567 O00567
BRENDA - -
KEGG hsa:10528 hsa:10528
PFAM: PF01798
PF08156
PF08060
PF01798
PF08156
PF08060
InterPro: IPR012974
IPR012976
IPR002687
IPR012974
IPR012976
IPR002687
CATH: - -
SCOP: - -


Protein sequence:
MVLLHVLFEHAVGYALLALKEVEEISLLQPQVEESVLNLGKFHSIVRLVA
FCPFASSQVALENANAVSEGVVHEDLRLLLETHLPSKKKKVLLGVGDPKI
GAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGH
SYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPEL
VKIINDNATYCRLAQFIGNRRELNEDKLEKLEELTMDGAKAKAILDASRS
SMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALI
GEAVGARLIAHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGL
IFHSTFIGRAAAKNKGRISRYLANKCSIASRIDCFSEVPTSVFGEKLREQ
VEERLSFYETGEIPRKNLDVMKEAMVQAEEAAAEITRKLEKQEKKRLKKE
KKRLAALALASSENSSSTPEECEEMSEKPKKKKKQKPQEVPQENGMEDPS
ISFSKPKKKKSFSKEELMSSDLEETAGSTSIPKRKKSTPKEETVNDPEEA
GHRSGSKKKRKFSKEEPVSSGPEEAVGKSSSKKKKKFHKASQED

Nucleolar protein 56 (Homo sapiens) is product of expression of NOP56 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell 2008-08-08 (31) 18691976
Phosphoproteome analysis of the human mitotic spindle. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R Proc Natl Acad Sci U S A 2006-04-04 (103) 16565220
Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S Electrophoresis 2007-06-01 (28) 17487921
Functional proteomic analysis of human nucleolus. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ Mol Biol Cell 2002-11-01 (13) 12429849
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 1997-12-01 (17) 9372940
The DNA sequence and comparative analysis of human chromosome 20. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, K Nature 2001-01-01 (414) 11780052
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 2003-09-05 (278) 12777385
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 2011-07-15 (89) 21683323



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Last modification of this entry: Sept. 25, 2012.

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