UniProt Accession

 CPSF1_HUMAN; Q10570; Q96AF0 

Genbank Protein ID

 U37012; BC017232 

Genbank Nucleotide ID

 AAC50293.1; AAH17232.1 

Protein Name

 Cleavage and polyadenylation specificity factor subunit 1 

Protein Synonyms/Alias

 Cleavage and polyadenylation specificity factor 160 kDa subunit; CPSF 160 kDa subunit 

Gene Name

 CPSF1 

Gene Synonyms/Alias

 CPSF160 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
52	RDAEALTKNDRSTEG	ubiquitination	[1, 2, 3]
99	DALLLSFKDAKLSVV	ubiquitination	[2, 3]
102	LLSFKDAKLSVVEYD	ubiquitination	[2]
116	DPGTHDLKTLSLHYF	ubiquitination	[1, 2]
364	VRAFHFDKAAASVLT	ubiquitination	[2]
395	LGNSLLLKYTEKLQE	ubiquitination	[1, 2, 3, 4, 5, 6]
399	LLLKYTEKLQEPPAS	ubiquitination	[1, 2, 3]
551	KEEEDNPKGEGTEQE	ubiquitination	[1]
686	HHRLALHKPPLHHQS	ubiquitination	[2]
759	GSLFSPSKEEARRSS	ubiquitination	[1, 2, 3]
809	WRLVFLVKNFPVGQR	ubiquitination	[2, 7, 8, 9]
847	QGELPLVKEVLLVAL	ubiquitination	[2]
893	GNLKVRFKKVPHNIN	ubiquitination	[2]
894	NLKVRFKKVPHNINF	ubiquitination	[2]
1055	PRMTGEEKEFETIER	ubiquitination	[1, 2, 6]
1104	WEHVTCMKTVSLRSE	ubiquitination	[2, 3, 4]
1118	EETVSGLKGYVAAGT	ubiquitination	[1, 2, 4]
1157	EPGQPLTKNKFKVLY	ubiquitination	[1, 2, 3, 6]
1159	GQPLTKNKFKVLYEK	ubiquitination	[2]
1161	PLTKNKFKVLYEKEQ	ubiquitination	[2, 6, 7, 9]
1166	KFKVLYEKEQKGPVT	ubiquitination	[1, 2, 6]
1241	LRYQEESKTLSLVSR	ubiquitination	[1, 2, 6, 7, 9]
1326	ATEGLSKKSVVWENK	ubiquitination	[2, 6]
1421	ERSELAKKIGTTPDI	ubiquitination	[1, 2, 6]

Reference

 [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] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

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. This subunit is involved in the RNA recognition step of the polyadenylation reaction. 

Sequence Annotation

 MOTIF 893 908 Nuclear localization signal (Potential).  

Keyword

 Complete proteome; mRNA processing; Nucleus; Reference proteome; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1443 AA 

Protein Sequence

Gene Ontology

 GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
 GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
 GO:0006379; P:mRNA cleavage; IDA:UniProtKB.
 GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
 GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 

Interpro

 IPR004871; Cleavage/polyA-sp_fac_asu_C. 

Pfam

 PF03178; CPSF_A 

SMART

  

PROSITE

  

PRINTS