Serine/threonine-protein kinase 16 (STK16)

The protein contains 305 amino acids for an estimated molecular weight of 34656 Da.

 

Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. (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. 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.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 100%
Model score: 98

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VariantDescription
dbSNP:rs34799131
dbSNP:rs35947471
dbSNP:rs34282267
dbSNP:rs17849638
dbSNP:rs35454203

The reference OMIM entry for this protein is 604719

Serine/threonine protein kinase 16; stk16
Pkl12, mouse, homolog of
Transforming growth factor-beta-stimulated factor 1; tsf1
Tgfb-stimulated factor 1

CLONING

Protein kinases are a large family of proteins that share a homologous catalytic domain of 250 to 300 amino acids, which can be subdivided into 11 subdomains. By screening a mouse fetal liver cDNA library with primers from the catalytic domain of other serine/threonine protein kinases, Ligos et al. (1998) characterized a new member of the ser/thr kinase family, which they termed Pkl12 (protein kinase expressed in day 12 fetal liver). By in vitro kinase assay using enolase as substrate, they showed that Pkl12 can phosphorylate enolase and promote autophosphorylation, with a ser/thr specificity. They also constructed the human homolog, STK16, using several human ESTs with sequence similarity to the Pkl12 gene. The STK16 gene encodes a 310-amino acid protein that shares 94% identity with the mouse homolog. Because its size is very close to the minimal size for a core catalytic domain, the authors suggested that STK16 may constitute the catalytic subunit of a multisubunit kinase. By Northern blot analysis, Ligos et al. (1998) showed that both STK16 and Pkl12 are ubiquitously expressed at very low levels. Expression of an STK16 fusion protein showed that STK16 is localized with Golgi and Golgi-derived vesicles.

GENE FUNCTION

Ligos et al. (1998) showed that overexpression of STK16 leads to disorganization of the Golgi apparatus into vesicular structures, suggesting that STK16 is involved in the secretory pathway. By sequence walking in the EST database, followed by PCR of a fetal kidney cDNA library, Ohta et al. (2000) obtained a cDNA encoding STK16, which they termed TSF1. Western blot analysis of a rat pituitary cell line showed an increase of Tsf1 level after Tgfb (190180) treatment. Gel shift analysis indicated that Tsf1 is a sequence-specific DNA-binding factor that binds to GC-rich elements in vascular endothelial growth factor (VEGF; 192240) and type C natriuretic peptide (NPPC; 600296) promoters, independent of its kinase activity and Smad3 (603109) or Smad4 (600993). Tsf1 could not directly activate the Smad-dependent promoter of plasminogen activator inhibitor-1 (PAI1; 173360) but could enhance the transactivation function of Smad3 and Smad4. ... 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 25, 2017: Additional information
No protein expression data in P. Mayeux work for STK16

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604719 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

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