CPLM-015397

Genbank Nucleotide ID

Pre-mRNA 3'-end-processing factor FIP1

Protein Synonyms/Alias

hFip1; FIP1-like 1 protein; Factor interacting with PAP; Rearranged in hypereosinophilia

Homo sapiens (Human)

Position	Peptide	Type	References
123	APVNLNIKTGGRVYG	ubiquitination	[1, 2, 3, 4, 5]
135	VYGTTGTKVKGVDLD	ubiquitination	[3]
235	DGRFNLFKVQQGRTG	ubiquitination	[5]
246	GRTGNSEKETALPST	ubiquitination	[3, 5]
254	ETALPSTKAEFTSPP	ubiquitination	[3, 5]
294	KANSSVGKWQDRYGR	acetylation	[6]
294	KANSSVGKWQDRYGR	ubiquitination	[3]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

Functional Description

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays 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. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex.

REGION 1 356 Necessary for stimulating PAPOLA
REGION 1 111 Sufficient for interaction with PAPOLA.
REGION 137 243 Sufficient for interaction with CPSF4.
REGION 443 594 Sufficient for interaction with CPSF1 and
MOD_RES 85 85 Phosphoserine.
MOD_RES 87 87 Phosphoserine.
MOD_RES 89 89 Phosphoserine.
MOD_RES 259 259 Phosphoserine.
MOD_RES 294 294 N6-acetyllysine.
MOD_RES 304 304 Phosphoserine.
MOD_RES 426 426 Phosphotyrosine.
MOD_RES 492 492 Phosphoserine.
MOD_RES 494 494 Phosphothreonine.
MOD_RES 496 496 Phosphoserine.
MOD_RES 500 500 Phosphoserine.
MOD_RES 554 554 Phosphoserine.

Acetylation; Alternative splicing; Complete proteome; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:Compara.
GO:0005634; C:nucleus; IDA:HPA.
GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.