CPLM-008459

Genbank Nucleotide ID

Heterogeneous nuclear ribonucleoprotein A3

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
4	****MEVKPPPGRPQ	acetylation	[1, 2, 3]
4	****MEVKPPPGRPQ	ubiquitination	[3, 4, 5, 6, 7]
29	GEEGHDPKEPEQLRK	acetylation	[3, 8]
36	KEPEQLRKLFIGGLS	ubiquitination	[4, 7]
57	SLREHFEKWGTLTDC	ubiquitination	[3, 4, 7, 9]
73	VMRDPQTKRSRGFGF	ubiquitination	[6, 10, 11]
118	VSREDSVKPGAHLTV	ubiquitination	[3, 5, 6, 10]
126	PGAHLTVKKIFVGGI	acetylation	[3]
126	PGAHLTVKKIFVGGI	ubiquitination	[3, 6]
127	GAHLTVKKIFVGGIK	ubiquitination	[6]
134	KIFVGGIKEDTEEYN	acetylation	[3, 8]
134	KIFVGGIKEDTEEYN	ubiquitination	[3, 6, 10]
148	NLRDYFEKYGKIETI	acetylation	[1, 3, 8]
148	NLRDYFEKYGKIETI	ubiquitination	[3, 4, 5, 6, 7, 10]
151	DYFEKYGKIETIEVM	acetylation	[8]
151	DYFEKYGKIETIEVM	ubiquitination	[3, 4, 5, 6, 7, 10]
187	VDKIVVQKYHTINGH	acetylation	[2]
199	NGHNCEVKKALSKQE	acetylation	[3]
200	GHNCEVKKALSKQEM	ubiquitination	[6]
204	EVKKALSKQEMQSAG	ubiquitination	[6]

[1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[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] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[9] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[10] 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]
[11] 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]

Functional Description

Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing.

DOMAIN 35 118 RRM 1.
DOMAIN 126 205 RRM 2.
MOD_RES 52 52 Dimethylated arginine; alternate.
MOD_RES 52 52 Omega-N-methylarginine; alternate.
MOD_RES 134 134 N6-acetyllysine.
MOD_RES 246 246 Dimethylated arginine.
MOD_RES 350 350 Phosphoserine.
MOD_RES 355 355 Phosphoserine (By similarity).
MOD_RES 358 358 Phosphoserine.
MOD_RES 360 360 Phosphotyrosine.
MOD_RES 364 364 Phosphotyrosine.
MOD_RES 366 366 Phosphoserine.
MOD_RES 370 370 Phosphoserine.

Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003723; F:RNA binding; TAS:ProtInc.
GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.

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