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Cleavage and polyadenylation specificity factor subunit 7

 
Known also as: Cleavage and polyadenylation specificity factor 59 kDa subunit, CPSF 59 kDa subunit, Pre-mRNA cleavage factor Im 59 kDa subunit

Known abbreviations: CPSF7, CFIm59

 

FUNCTION:
 
Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3' processing. Binds to cleavage and polyadenylation RNA substrates. 
 
SUBUNIT STRUCTURE:
 
Component of the cleavage factor Im (CFIm) complex, composed of, at least, NUDT21/CPSF5 and CPSF6 or CPSF7. Within the cleavage factor Im complex, the NUDT21/CPSF5 homodimer is at the core of a heterotetramer, and is clasped by two additional subunits (CPSF6 or CPSF7). Interacts with NUDT21/CPSF5. 
 
CELLULAR LOCALIZATION:
 
Nucleus (Probable)



This protein can be a part of a given complexes: Activities in which Cleavage and polyadenylation specificity factor subunit 7 is involved: Pathways in which Cleavage and polyadenylation specificity factor subunit 7 is involved:

NCBI GI number(s): 209862881
217035103
217035107
217035106
217035102
217035101
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q8N684 Q8N684
BRENDA - -
KEGG hsa:79869 hsa:79869
PFAM: PF00076
PF00076
InterPro: IPR012677
IPR000504
IPR012677
IPR000504
CATH: - -
SCOP: - -
Solved crystal structures: 3N9U
[PDB] [details]


Protein sequence:
MSEGVDLIDIYADEEFNQDPEFNNTDQIDLYDDVLTATSQPSDDRSSSTE
PPPPVRQEPSPKPNNKTPAILYTYSGLRNRRAAVYVGSFSWWTTDQQLIQ
VIRSIGVYDVVELKFAENRANGQSKGYAEVVVASENSVHKLLELLPGKVL
NGEKVDVRPATRQNLSQFEAQARKRECVRVPRGGIPPRAHSRDSSDSADG
RATPSENLVPSSARVDKPPSVLPYFNRPPSALPLMGLPPPPIPPPPPLSS
SFGVPPPPPGIHYQHLMPPPPRLPPHLAVPPPGAIPPALHLNPAFFPPPN
ATVGPPPDTYMKASAPYNHHGSRDSGPPPSTVSEAEFEDIMKRNRAISSS
AISKAVSGASAGDYSDAIETLLTAIAVIKQSRVANDERCRVLISSLKDCL
HGIEAKSYSVGASGSSSRKRHRSRERSPSRSRESSRRHRDLLHNEDRHDD
YFQERNREHERHRDRERDRHH

Cleavage and polyadenylation specificity factor subunit 7 (Homo sapiens) is product of expression of CPSF7 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
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
Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD J Proteome Res 2007-11-01 (6) 17924679
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A Proc Natl Acad Sci U S A 2007-01-13 (104) 17287340
Human chromosome 11 DNA sequence and analysis including novel gene identification. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y Nature 2006-03-23 (440) 16554811
Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. Kim S, Yamamoto J, Chen Y, Aida M, Wada T, Handa H, Yamaguchi Y Genes Cells 2010-09-01 (15) 20695905
Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors. Ruegsegger U, Beyer K, Keller W J Biol Chem 1996-03-15 (271) 8626397
Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC Anal Chem 2004-05-15 (76) 15144186



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

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