UniProt Accession

 ROAA_HUMAN; Q99729; B3KNN5; D3DWP7; Q04150; Q8N7U3; Q9BQ99 

Genbank Protein ID

 M65028; U76713; AK054600; AK097657; CH471165; CH471165; CH471165; BC001616; BC002625; BC004561; BC009359; BC036708 

Genbank Nucleotide ID

 AAA36575.1; AAC50956.1; BAG51397.1; BAC05134.1; EAW53843.1; EAW53844.1; EAW53845.1; AAH01616.1; AAH02625.1; AAH04561.1; AAH09359.1; AAH36708.1 

Protein Name

 Heterogeneous nuclear ribonucleoprotein A/B 

Protein Synonyms/Alias

 hnRNP A/B; APOBEC1-binding protein 1; ABBP-1 

Gene Name

 HNRNPAB 

Gene Synonyms/Alias

 ABBP1; HNRPAB 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
83	LSWDTSKKDLKDYFT	ubiquitination	[1, 2]
86	DTSKKDLKDYFTKFG	ubiquitination	[1]
91	DLKDYFTKFGEVVDC	ubiquitination	[1]
101	EVVDCTIKMDPNTGR	ubiquitination	[1, 2]
118	GFGFILFKDAASVEK	ubiquitination	[1]
125	KDAASVEKVLDQKEH	ubiquitination	[1]
130	VEKVLDQKEHRLDGR	ubiquitination	[1]
154	MKKDPVKKIFVGGLN	ubiquitination	[1]
169	PESPTEEKIREYFGE	ubiquitination	[1, 2]
232	EIKVAQPKEVYQQQQ	ubiquitination	[1, 2]
330	GGHQNNYKPY*****	acetylation	[3, 4]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 

Functional Description

 Binds single-stranded RNA. Has a high affinity for G- rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site. 

Sequence Annotation

 DOMAIN 69 154 RRM 1.
 DOMAIN 153 233 RRM 2.
 MOD_RES 77 77 Phosphoserine (By similarity).
 MOD_RES 242 242 Phosphoserine.
 MOD_RES 245 245 Dimethylated arginine; alternate.
 MOD_RES 245 245 Omega-N-methylarginine; alternate.
 MOD_RES 322 322 Dimethylated arginine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 332 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; ISS:HGNC.
 GO:0005634; C:nucleus; ISS:HGNC.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0003729; F:mRNA binding; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:HGNC. 

Interpro

 IPR012956; CARG-binding_factor_N.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF08143; CBFNT
 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS