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Cleavage and polyadenylation specificity factor subunit 4

 
Known also as: Cleavage and polyadenylation specificity factor 30 kDa subunit, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1, No arches homolog

Known abbreviations: Neb-1, CPSF4, CPSF30, NAR, NEB1

 

FUNCTION:
 
Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U). 
 
SUBUNIT STRUCTURE:
 
Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with FIP1L1. Association with influenza A virus NS1 blocks processing of pre-mRNAs, thereby preventing nuclear export of host cell mRNAs. 
 
CELLULAR LOCALIZATION:
 
Nucleus.



This protein can be a part of a given complexes: Activities in which Cleavage and polyadenylation specificity factor subunit 4 is involved: Pathways in which Cleavage and polyadenylation specificity factor subunit 4 is involved:

NCBI GI number(s): 125987603
125987602
5729939
125987601
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O95639 O95639
BRENDA - -
KEGG hsa:10898 hsa:10898
PFAM: PF00642
PF00098
PF00642
PF00098
InterPro: IPR000571
IPR001878
IPR000571
IPR001878
CATH: - -
SCOP: - -
Solved crystal structures: 2D9N
2RHK
[PDB] [details]
[PDB] [details]


Protein sequence:
MQEIIASVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEFFLKAACG
KGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYS
KFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVN
YLVGFCPEGPSCKFMHPRFELPMGTTEQPPLPQQTQPPAKQSNNPPLQRS
SSLIQLTSQNSSPNQQRTPQVIGVMQSQNSSAGNRGPRPLEQVTCYKCGE
KGHYANRCTKGHLAFLSGQ

Cleavage and polyadenylation specificity factor subunit 4 (Homo sapiens) is product of expression of CPSF4 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
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
Human chromosome 7: DNA sequence and biology. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R Science 2003-05-02 (300) 12690205
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
The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA. Laishram RS, Anderson RA EMBO J 2010-12-15 (29) 21102410
The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins. Barabino SM, Hubner W, Jenny A, Minvielle-Sebastia L, Keller W Genes Dev 1997-07-01 (11) 9224719
Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM Mol Cell 1998-06-01 (1) 9651582



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

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