Heterogeneous nuclear ribonucleoprotein A/B (HNRNPAB)

The protein contains 332 amino acids for an estimated molecular weight of 36225 Da.

 

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. (updated: March 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 57%
Model score: 29

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The reference OMIM entry for this protein is 602688

Heterogeneous nuclear ribonucleoprotein a/b; hnrnpab
Apolipoprotein b mrna-editing enzyme, catalytic polypeptide 1-binding protein 1
Apobec1-binding protein 1; abbp1
Hnrpab

CLONING

Apolipoprotein B (APOB; 107730) mRNA editing is an intranuclear function and is mediated by a multiprotein editosome complex (see APOBEC1; 600130). Using the yeast 2-hybrid system, Lau et al. (1997) identified an APOBEC1-binding protein (ABBP1) that interacts with APOB mRNA. The ABBP1 cDNA encodes a 331-amino acid protein that is identical to the human type A/B heterogeneous nuclear ribonucleoprotein (hnRNP) reported by Khan et al. (1991), except for a 47-residue insertion in its C-terminal region. Khan et al. (1991) identified the type A/B hnRNP as an RNA-binding protein of unknown function in HeLa cells. Northern blot analysis indicated that ABBP1 mRNA is distributed in multiple human tissues as an approximately 2-kb transcript. The 47-amino acid insertion of ABBP1 is encoded by an alternatively spliced exon.

GENE FUNCTION

Lau et al. (1997) found that ABBP1 contains typical RNP-type RNA-binding motifs in its N-terminal half and glycine-rich motifs, which house the APOBEC1-binding region, in its C-terminal region. ABBP1 binds to APOB mRNA transcripts around the editing site and can be UV-crosslinked to them. Editing is inhibited by ABBP1 immunodepletion or antisense ABBP1 cDNA transfection. ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602688 was added.