Welcome! Click here to login or here to register.
Home
Pathways
Proteins
Catalytic RNA molecules
Enzymatic complexes
Structures
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

U3 small nucleolar RNA-interacting protein 2

 
Known also as: RRP9 homolog, U3 small nucleolar ribonucleoprotein-associated 55 kDa protein, U3 snoRNP-associated 55 kDa protein

Known abbreviations: RRP9, RNU3IP2, U355K, U3-55K

 

FUNCTION:
 
Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA.
 
SUBUNIT STRUCTURE:
 
Interacts specifically with the U3 small nucleolar RNA (U3 snoRNA). Binds a sub-fragment of the U3 snoRNA surrounding the B/C motif (3UBC). This association with the U3BC RNA is dependent on the binding of a protein called 15.5K to the box B/C motif. The association of the protein with the U3BC RNA was found to be also dependent on a conserved RNA structure that flanks the box B/C motif. 
 
CELLULAR LOCALIZATION:
 
Nucleus › nucleolus 
 
DOMAIN: 
 
The WD domains are required for nucleolar localization and U3 small nucleolar RNAs binding.



This protein can be a part of a given complexes: Activities in which U3 small nucleolar RNA-interacting protein 2 is involved: Pathways in which U3 small nucleolar RNA-interacting protein 2 is involved:

NCBI GI number(s): 4759276
51871124
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O43818 O43818
BRENDA - -
KEGG hsa:9136 hsa:9136
PFAM: PF00400
PF00400
InterPro: IPR020472
IPR015943
IPR001680
IPR019775
IPR017986
IPR020472
IPR015943
IPR001680
IPR019775
IPR017986
CATH: - -
SCOP: - -


Protein sequence:
MSATAAARKRGKPASGAGAGAGAGKRRRKADSAGDRGKSKGGGKMNEEIS
SDSESESLAPRKPEEEEEEELEETAQEKKLRLAKLYLEQLRQQEEEKAEA
RAFEEDQVAGRLKEDVLEQRGRLQKLVAKEIQAPASADIRVLRGHQLSIT
CLVVTPDDSAIFSAAKDCSIIKWSVESGRKLHVIPRAKKGAEGKPPGHSS
HVLCMAISSDGKYLASGDRSKLILIWEAQSCQHLYTFTGHRDAVSGLAFR
RGTHQLYSTSHDRSVKVWNVAENSYVETLFGHQDAVAALDALSRECCVTA
GGRDGTVRVWKIPEESQLVFYGHQGSIDCIHLINEEHMVSGADDGSVALW
GLSKKRPLALQREAHGLRGEPGLEQPFWISSVAALLNTDLVATGSHSSCV
RLWQCGEGFRQLDLLCDIPLVGFINSLKFSSSGDFLVAGVGQEHRLGRWW
RIKEARNSVCIIPLRRVPVPPAAGS

U3 small nucleolar RNA-interacting protein 2 (Homo sapiens) is product of expression of RRP9 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
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
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
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
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
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
The consensus coding sequences of human breast and colorectal cancers. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE Science 2006-10-13 (314) 16959974
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
cDNA cloning and characterization of the human U3 small nucleolar ribonucleoprotein complex-associated 55-kilodalton protein. Pluk H, Soffner J, Luhrmann R, van Venrooij WJ Mol Cell Biol 1998-02-01 (18) 9418896
Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k. Lukowiak AA, Granneman S, Mattox SA, Speckmann WA, Jones K, Pluk H, Venrooij WJ, Terns RM, Terns MP Nucleic Acids Res 2000-09-15 (28) 10982864
The hU3-55K protein requires 15.5K binding to the box B/C motif as well as flanking RNA elements for its association with the U3 small nucleolar RNA in Vitro. Granneman S, Pruijn GJ, Horstman W, van Venrooij WJ, Luhrmann R, Watkins NJ J Biol Chem 2002-12-13 (277) 12381732



Add your own comment!


There are no comments yet.

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

Welcome stranger! Click here to login or here to register.