Protein PALS2 (MPP6)

The protein contains 540 amino acids for an estimated molecular weight of 61117 Da.

 

No function (updated: June 2, 2021)

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. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. 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.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 33%
Model score: 0
No model available.

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The reference OMIM entry for this protein is 606959

Membrane protein, palmitoylated 6; mpp6
Veli-associated maguk 1; vam1
Protein associated with lin7 2, mouse, homolog of; pals2

DESCRIPTION

Members of the peripheral membrane-associated guanylate kinase (MAGUK) family function in tumor suppression and receptor clustering by forming multiprotein complexes containing distinct sets of transmembrane, cytoskeletal, and cytoplasmic signaling proteins. All MAGUKs contain a PDZ-SH3-GUK core and are divided into 4 subfamilies, DLG-like (see DLG1; 601014), ZO1-like (see TJP1; 601009), p55-like (see MPP1; 305360), and LIN2-like (see CASK; 300172), based on their size and the presence of additional domains. MPP6 is a member of the p55-like MAGUK subfamily (Tseng et al., 2001).

CLONING

By searching an EST database with DLG2 (603583) as the probe, followed by PCR of a brain cDNA library and 5-prime RACE, Tseng et al. (2001) obtained a cDNA encoding MPP6, which they called VAM1 for VELI (603380)-associated MAGUK-1. The deduced 540-amino acid protein has a single PDZ domain, a central SH3 domain, and a C-terminal GUK domain, resembling other members of the p55 MAGUK subfamily. Like MPP1, MPP6 also contains a protein 4.1 (EPB41; 130500)-binding domain with its characteristic KKKK sequence, as well as a leucine zipper and 2 phosphorylation sites. Northern blot analysis revealed expression of an abundant 2.3-kb transcript and a minor 4.2-kb transcript only in testis. RT-PCR analysis detected predominant expression in testis, with lower amounts in ovary, prostate, thymus, small intestine, and several other tissues; VELI has a similar expression pattern. GST pull-down and mutation analyses indicated that a domain N-terminal of the PDZ region of VAM1 contains the minimal VELI-binding sequence. No binding between VAM1 and EPB41 was detected. Kamberov et al. (2000) cloned and characterized the mouse Mpp5 (606958) and Mpp6 genes, which they called Pals1 and Pals2, respectively. The Pals proteins bind to mouse Lin7 (VELI) through a region N-terminal to their PDZ domains.

GENE STRUCTURE

By genomic sequence analysis, Tseng et al. (2001) determined that the MPP6 gene contains 12 exons and spans 115 kb.

MAPPING

Using FISH, Tseng et al. (2001) mapped the MPP6 gene to chromosome 7p21-p15. Kamberov et al. (2000) mapped the mouse Pals2 gene to chromosome 6. ... More on the omim web site

Subscribe to this protein entry history

July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.

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 606959 was added.