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Nucleolar protein 58
 
Known also as: Nucleolar protein 5

Known abbreviations: NOP58, NOL5, NOP5, HSPC120

FUNCTION:

Required for 60S ribosomal subunit biogenesis (By similarity.)
 
SUBUNIT STRUCTURE:
 
Interacts with NOLC1/Nopp140 By similarity. Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles.
 
CELLULAR LOCALIZATION:
 
Nucleus › nucleolus. 
 
TISSUE SPECIFICITY:
 
Ubiquitous.
 
POST-TRANSLATIONAL MODIFICATION:
 
Sumoylation is essential for high-affinity binding to snoRNAs.


This protein can be a part of a given complexes: Activities in which Nucleolar protein 58 is involved: Pathways in which Nucleolar protein 58 is involved:
NCBI GI number(s): 7706254
34222329
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9Y2X3 Q9Y2X3
BRENDA - -
KEGG hsa:51602 hsa:51602
PFAM: PF01798
PF08156
PF08060
PF01798
PF08156
PF08060
InterPro: IPR012974
IPR012976
IPR002687
 IPR012974
IPR012976
IPR002687
CATH: - -
SCOP: - -


Protein sequence:
MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKF
QDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKE
KLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYR
LKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISD
NLTYCKCLQKVGDRKNYASAKLSELLPEEVEAEVKAAAEISMGTEVSEED
ICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIA
HAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQT
SPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGVENRAKLEARLRTLED
RGIRKISGTGKALAKTEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEQVDK
EDEITEKKAKKAKIKVKVEEEEEEKVAEEEETSVKKKKKRGKKKHIKEEP
LSEEEPCTSTAIASPEKKKKKKKKRENED

Nucleolar protein 58 (Homo sapiens) is product of expression of NOP58 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
Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M Nature 2005-04-07 (434) 15815621
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
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
The full-ORF clone resource of the German cDNA Consortium. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I BMC Genomics 2007-01-01 (8) 17974005
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
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res 2008-03-01 (7) 18220336
Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Wang B, Malik R, Nigg EA, Korner R Anal Chem 2008-12-15 (80) 19007248
Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J J Proteome Res 2008-12-01 (7) 19367720
Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z Genome Res 2000-10-01 (10) 11042152
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
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
Isolation and characterization of a novel PDGF-induced human gene. Nelson SA, Santora KE, LaRochelle WJ Gene 2000-07-25 (253) 10925205
Human Nop5/Nop58 is a component common to the box C/D small nucleolar ribonucleoproteins. Lyman SK, Gerace L, Baserga SJ RNA 1999-12-01 (5) 10606270
A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58. Westman BJ, Verheggen C, Hutten S, Lam YW, Bertrand E, Lamond AI Mol Cell 2010-08-27 (39) 20797632


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