Protein phosphatase 1B (PPM1B)

The protein contains 479 amino acids for an estimated molecular weight of 52643 Da.

 

Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. (updated: April 1, 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. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  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: 81%
Model score: 78

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The reference OMIM entry for this protein is 603770

Protein phosphatase, magnesium/manganese-dependent, 1b; ppm1b
Protein phosphatase, magnesium-dependent, 1b
Protein phosphatase, magnesium-dependent, 1, beta isoform
Protein phosphatase 2c, beta isoform, formerly; pp2cb, formerly

CLONING

Protein phosphorylation/dephosphorylation is a major mechanism for regulating cellular functions. PP2C, 1 of 4 major groups of serine/threonine phosphatases in eukaryotic cells, is distinguished from the other groups by its absolute requirement for magnesium or manganese and its insensitivity to the tumor promoter okadaic acid. Marley et al. (1998) cloned human liver cDNAs encoding a novel PP2C-beta isoform, which they named PP2C-beta-X. The deduced 479-amino acid protein shows high sequence similarity to other mammalian PP2C-beta isoforms but has an extended and unique C-terminal portion. Recombinant PP2C-beta-X expressed in bacteria is indistinguishable from recombinant human PP2C-alpha (PPM1A; 606108) in its cation dependence and its insensitivity to okadaic acid. By Northern blot analysis, the authors demonstrated that both PP2C-beta-X and PP2C-alpha are widely expressed, with the most abundant expression detected in heart and skeletal muscle. Parvari et al. (2001) identified PPM1B as one of the genes affected by a homozygous deletion of 179 kb on chromosome 2, which results in the 2p21 deletion syndrome (606407). By EST database analysis, Parvari et al. (2005) identified 7 PPM1B splice variants, some of which differ only in noncoding regions. The longest deduced protein contains 479 amino acids, and its N-terminal half has a phosphatase catalytic domain. RT-PCR showed that expression of each variant was tissue specific.

GENE STRUCTURE

Parvari et al. (2005) determined that the PPM1B gene contains 6 exons, the first of which is noncoding.

MAPPING

By genomic sequence analysis, Parvari et al. (2001) mapped the PPM1B gene to chromosome 2p16. Parvari et al. (2005) refined the mapping to chromosome 2p21.

MOLECULAR GENETICS

Parvari et al. (2001, 2005) identified PPM1B as one of the genes deleted in the homozygous 2p21 deletion syndrome (606407).

NOMENCLATURE

The symbol PP2CB, formerly used for PPM1B, now refers to a gene that maps to chromosome 8p21 (see 176916). ... 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

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603770 was added.

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed