CPLM-002814

Genbank Nucleotide ID

Heterogeneous nuclear ribonucleoprotein A1

Protein Synonyms/Alias

hnRNP A1; Helix-destabilizing protein; Single-strand RNA-binding protein; hnRNP core protein A1

Homo sapiens (Human)

Position	Peptide	Type	References
3	*****MSKSESPKEP	acetylation	[1]
3	*****MSKSESPKEP	ubiquitination	[2, 3, 4]
8	MSKSESPKEPEQLRK	ubiquitination	[2, 4, 5, 6]
15	KEPEQLRKLFIGGLS	ubiquitination	[4, 6, 7]
52	VMRDPNTKRSRGFGF	ubiquitination	[3, 4, 5]
78	AMNARPHKVDGRVVE	ubiquitination	[3, 4, 6]
105	PGAHLTVKKIFVGGI	ubiquitination	[3, 4]
106	GAHLTVKKIFVGGIK	ubiquitination	[4]
113	KIFVGGIKEDTEEHH	acetylation	[1]
113	KIFVGGIKEDTEEHH	ubiquitination	[4]
144	MTDRGSGKKRGFAFV	acetylation	[8]
166	VDKIVIQKYHTVNGH	acetylation	[8]
166	VDKIVIQKYHTVNGH	ubiquitination	[6]
183	EVRKALSKQEMASAS	ubiquitination	[4, 6]
329	SSNFGPMKGGNFGGR	ubiquitination	[5]
350	GGGQYFAKPRNQGGY	acetylation	[1, 9, 10]
350	GGGQYFAKPRNQGGY	ubiquitination	[2, 3, 4, 5, 6, 7, 11]

[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] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[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] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[9] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[10] Proteome-wide prediction of acetylation substrates.
Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
[11] 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]

Functional Description

Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.

DOMAIN 14 97 RRM 1.
DOMAIN 105 184 RRM 2.
REGION 4 94 Globular A domain.
REGION 95 185 Globular B domain.
REGION 218 240 RNA-binding RGG-box.
REGION 320 357 Nuclear targeting sequence (M9).
MOD_RES 2 2 N-acetylserine.
MOD_RES 2 2 Phosphoserine.
MOD_RES 3 3 N6-acetyllysine.
MOD_RES 4 4 Phosphoserine.
MOD_RES 6 6 Phosphoserine.
MOD_RES 192 192 Phosphoserine; by MKNK2.
MOD_RES 194 194 Asymmetric dimethylarginine; alternate
MOD_RES 194 194 Dimethylated arginine; alternate.
MOD_RES 199 199 Phosphoserine.
MOD_RES 206 206 Dimethylated arginine; alternate.
MOD_RES 206 206 Omega-N-methylarginine; alternate.
MOD_RES 225 225 Dimethylated arginine; alternate.
MOD_RES 225 225 Omega-N-methylarginine; alternate.
MOD_RES 350 350 N6-acetyllysine.
MOD_RES 362 362 Phosphoserine; by MKNK2.
MOD_RES 363 363 Phosphoserine; by MKNK2.
MOD_RES 364 364 Phosphoserine; by MKNK2.
MOD_RES 365 365 Phosphoserine.
MOD_RES 368 368 Phosphoserine.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Isopeptide bond; Methylation; mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; Transport; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO:0005737; C:cytoplasm; IDA:HGNC.
GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0005654; C:nucleoplasm; IDA:HGNC.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003697; F:single-stranded DNA binding; IDA:HGNC.
GO:0003727; F:single-stranded RNA binding; IC:HGNC.
GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO:0051170; P:nuclear import; IDA:HGNC.
GO:0006405; P:RNA export from nucleus; IC:HGNC.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

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