CPLM-005498

Genbank Nucleotide ID

Splicing factor U2AF 65 kDa subunit

Protein Synonyms/Alias

U2 auxiliary factor 65 kDa subunit; hU2AF(65); hU2AF65; U2 snRNP auxiliary factor large subunit

Homo sapiens (Human)

Position	Peptide	Type	References
70	KPLTRGAKEEHGGLI	acetylation	[1, 2, 3]
225	IFQGQSLKIRRPHDY	ubiquitination	[4]
286	LTSFGPLKAFNLVKD	ubiquitination	[5, 6]
413	CSKYGLVKSIEIPRP	ubiquitination	[7]
462	ANRVVVTKYCDPDSY	acetylation	[1]
462	ANRVVVTKYCDPDSY	ubiquitination	[8]

[1] 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]
[2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[3] 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]
[4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[5] 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]
[6] 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]
[7] 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]
[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]

Functional Description

Necessary for the splicing of pre-mRNA. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10.

DOMAIN 149 231 RRM 1.
DOMAIN 259 337 RRM 2.
DOMAIN 385 466 RRM 3.
MOD_RES 2 2 N-acetylserine.
MOD_RES 2 2 Phosphoserine.
MOD_RES 15 15 5-hydroxylysine; by JMJD6.
MOD_RES 70 70 N6-acetyllysine.
MOD_RES 79 79 Phosphoserine.
MOD_RES 276 276 5-hydroxylysine; by JMJD6.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Hydroxylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Spliceosome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0005681; C:spliceosomal complex; IDA:HGNC.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO:0000398; P:mRNA splicing, via spliceosome; IC:HGNC.
GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.

IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.
IPR006529; U2AF_lg.