Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4)

The protein contains 131 amino acids for an estimated molecular weight of 13810 Da.

 

Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.', 'Isoform 2 binds to double-stranded DNA. (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. 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: 98%
Model score: 99

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VariantDescription
dbSNP:rs6525589
dbSNP:rs7058353

The reference OMIM entry for this protein is 300252

Peptidyl-prolyl cis/trans isomerase, nima-interacting, 4; pin4
Parvulin 14; par14
Epvh

The peptidyl-prolyl cis/trans isomerase protein family (PPIases) consists of the cyclophilin (e.g., PPIA; 123840), FK506-binding protein (FKBPs, e.g., FKBP1A; 186945), and parvulin subfamilies. PPIases have diverse functions, but in general they are implicated in the folding, transport, or assembly of proteins. The human parvulin PIN1 (601052) is implicated in the regulation of mitosis through interaction with CDC25 (157680) and polo-like kinase-1 (PLX1; see 602098).

CLONING

By searching an EST database using human PIN1 and E. coli parvulin sequences as probes, followed by screening a lung cDNA library, Uchida et al. (1999) isolated a cDNA encoding PIN4, which they called PAR14 (parvulin-14). Using a similar method, Rulten et al. (1999) isolated a cDNA encoding PIN4, which they called EPVH (eukaryotic parvulin homolog). Sequence analysis predicted that the 131-amino acid PIN4 protein contains a PPIase domain preceded by a 40-amino acid glycine- and lysine-rich N-terminal sequence. PIN4, however, lacks a WW domain, a nuclear localization motif, and residues required for phosphoprotein interactions. Multiple-tissue Northern blot analysis detected variable expression of an approximately 1.0-kb PIN4 transcript in all tissues tested, with notably lower expression in neuronal tissue. Transmission electron microscopy demonstrated preferential localization of PIN4 in the mitochondrial matrix. Functional analysis failed to show PPIase activity, possibly due to proteolytic degradation or different substrate requirements.

MAPPING

The International Radiation Hybrid Mapping Consortium mapped the PIN4 gene to Xq13 (TMAP sts-H61973). ... 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

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

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300252 was added.