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Cleavage stimulation factor subunit 3

 
Known also as: CF-1 77 kDa subunit, Cleavage stimulation factor 77 kDa subunit, CSTF 77 kDa subunit

Known abbreviations: CSTF3, CstF-77

 

FUNCTION:
 
One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs.
 
SUBUNIT STRUCTURE:
 
Homodimer. The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF3 directly interacts with CSTF1 and CSTF2. Interacts with FIP1L1.
 
CELLULAR LOCALIZATION:
 
Nucleus.



This protein can be a part of a given complexes: Activities in which Cleavage stimulation factor subunit 3 is involved: Pathways in which Cleavage stimulation factor subunit 3 is involved:

NCBI GI number(s): 75709187
75709186
75709189
75709188
75709185
4557495
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q12996 Q12996
BRENDA - -
KEGG hsa:1479 hsa:1479
PFAM: PF05843
PF05843
InterPro: IPR003107
IPR008847
IPR011990
IPR003107
IPR008847
IPR011990
CATH: - -
SCOP: - -


Protein sequence:
MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKA
RKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDL
WKCYLSYVRETKGKLPSYKEKMAQAYDFALDKIGMEIMSYQIWVDYINFL
KGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIH
LAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVD
MWKKYIQWEKSNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQY
LEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYE
ESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEGIKSGRMIFKK
AREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAY
IDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLAS
ILKVEKRRFTAFKEEYEGKETALLVDRYKFMDLYPCSASELKALGYKDVS
RAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPP
GLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPN
TVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAV
VPPVHDIYRARQQKRIR

Cleavage stimulation factor subunit 3 (Homo sapiens) is product of expression of CSTF3 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
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
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
Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J Proteomics 2008-04-01 (8) 18318008
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
Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase. Kaufmann I, Martin G, Friedlein A, Langen H, Keller W EMBO J 2004-01-11 (23) 14749727
A polyadenylation factor subunit is the human homologue of the Drosophila suppressor of forked protein. Takagaki Y, Manley JL Nature 1994-12-01 (372) 7984242
Complex protein interactions within the human polyadenylation machinery identify a novel component. Takagaki Y, Manley JL Mol Cell Biol 2000-03-01 (20) 10669729



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

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