KCTD20 (6p21.31), C6orf69, dJ108k11.3. BTBD10:n kaltainen ja edistää haiman betasolukasvua.

https://www.ncbi.nlm.nih.gov/gene/222658

Official Symbol

KCTD20

Official Full Name

potassium channel tetramerization domain containing 20

Also known as

C6orf69; dJ108K11.3

Expression

Ubiquitous expression in fat (RPKM 16.9), gall bladder (RPKM 16.8) and 25 other tissues See more

    CDS             1..253
                     /gene="KCTD20"
                     /gene_synonym="C6orf69; dJ108K11.3"
                     /coded_by="NM_001286579.2:159..920"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS69096.1"
                     /db_xref="GeneID:222658"
                     /db_xref="HGNC:HGNC:21052"
                     /db_xref="MIM:615932"
ORIGIN      
        1 mnvhrgsdsd rllrqeascl vddtlavaqe keanslassg phnltyplgp rnegallhel
       61 sndgahkqfd hyleelilpi mvgcakkger echivvltde dsvdwdedhp ppmgeeysqi
      121 lyssklyrff kyienrdvak tvlkerglkn irigiegypt ckekikrrpg grseviynyv
      181 qrpfiqmswe keegksrhvd fqcvrskslt nlvaagddvl edqeilmhhp pqvdeldrln
      241 aplsqmasnd fqd
//

 BTB/POZ domain-containing protein KCTD20 isoform c [Homo sapiens]

NCBI Reference Sequence:

NM_001286580.1

Pleckstrin homology-like domain

The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.

Related articles in PubMed

1. Kctd20 promotes the development of non-small cell lung cancer through activating Fak/AKT pathway and predicts poor overall survival of patients. Zhang X, et al. Mol Carcinog, 2017 Sep. PMID 28398603
2. KCTD20, a relative of BTBD10, is a positive regulator of Akt. Nawa M, et al. BMC Biochem, 2013 Oct 24. PMID 24156551, Free PMC Article
   BMC Biochem. 2013 Oct 24;14:27. doi: 10.1186/1471-2091-14-27.
   KCTD20, a relative of BTBD10, is a positive regulator of Akt.
   
   Nawa M, Matsuoka M¹.Department of Pharmacology, Tokyo Medical University, 6-1-1 Shinjuku, Shinjuku-ku, Tokyo 160-8042, Japan.  

   Abstract BACKGROUND:

   BTBD10 binds to Akt and protein phosphatase 2A (PP2A) and inhibits the PP2A-mediated dephosphorylation of Akt, thereby keeping Akt activated. Previous studies have suggested that BTBD10 plays an important role in preventing motor neuronal death and accelerating the growth of pancreatic beta cells. Because levels of BTBD10 expression are much lower in many non-nervous tissues than nervous tissues, there may be a relative of BTBD10 that has BTBD10-like function in non-neuronal cells. RESULTS:
   A 419-amino-acid BTBD10-like protein, named KCTD20 (potassium channel tetramerization protein domain containing 20), was to found to bind to all Akt isoforms and PP2A. Overexpression of KCTD20 increased Akt phosphorylation at Thr308, as BTBD10 did, which suggests that KCTD20 as well as BTBD10 positively regulates the function of Akt. KCTD20 was ubiquitously expressed in non-nervous as well as nervous tissues. CONCLUSIONS:
   KCTD20 is a positive regulator of Akt and may play an important role in regulating the death and growth of some non-nervous and nervous cells.
3. Protein phosphatase 1γ isoforms linked interactions in the brain. Esteves SL, et al. J Mol Neurosci, 2013 May. PMID 23080069    Protein phosphorylation occurs primarily on serine, threonine, and tyrosine residues, through the antagonistic actions of protein kinases and phosphatases. The catalytic subunit of protein phosphatase 1 (PP1), a major Ser/Thr-phosphatase, associates with a large variety of regulatory subunits that define substrate specificity and determine specific cellular pathway responses. PP1 has been shown to bind to different proteins in the brain in order to execute key and differential functions. This work reports the identification of proteins expressed in the human brain that interact with PP1γ1 and PP1γ2 isoforms by the yeast two-hybrid method. An extensive search of PP1-binding motifs was performed for the proteins identified, revealing already known PP1 regulators but also novel interactors. Moreover, our results were integrated with the data of PP1γ interacting proteins from several public web databases, permitting the development of physical maps of the novel interactions. The PP1γ interactome thus obtained allowed for the identification of novel PP1 interacting proteins, supporting novel functions of PP1γ isoforms in the human brain.
4. Protein phosphatase 1α interacting proteins in the human brain. Esteves SL, et al. OMICS, 2012 Jan-Feb. PMID 22321011, Free PMC Article
5. Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. Brajenovic M, et al. J Biol Chem, 2004 Mar 26. PMID 14676191

See all (17) citations in PubMed