C20orf144

Chromosome 20 open reading frame 144 (c20orf144) is a human protein-encoding gene.^[3] The human c20orf144 protein consists of 153 amino acids, with the first 150 amino acids being characterized as part of the Bcl-2 like protein of testis (Bclt) family (pfam 15318).^[4]

C20orf144
Identifiers
Aliases	C20orf144, dJ63M2.6, chromosome 20 open reading frame 144
External IDs	HomoloGene: 76810; GeneCards: C20orf144; OMA:C20orf144 - orthologs
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q11.22 Start 33,662,327 bp[1] End 33,665,619 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right testis left testis testicle sural nerve stromal cell of endometrium right adrenal cortex left ovary left adrenal gland left adrenal cortex right ovary n/a More reference expression data BioGPS n/a
Orthologs Species Human Mouse Entrez 128864 n/a Ensembl ENSG00000149609 n/a UniProt Q9BQM9 n/a RefSeq (mRNA) NM_080825 n/a RefSeq (protein) NP_543015 n/a Location (UCSC) Chr 20: 33.66 – 33.67 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Gene

The c20orf144 gene is located on the plus strand at 20q11.22 and spans 3,293 base pairs.^[5] The gene contains two exons.^[3] Of the plus strand, 572 nucleotides are antisense to parts of the human genes PXMP4 and NECAB3.^[6] Other gene neighbors include ACTL10 and CBFA2T2.^[7]

Transcript

The encoded mRNA is 522 nucleotides in length (Accession: NM_080825) and there are no identified alternative splicings.^[8] Human c20orf144 mRNA expression is enriched in the testis, specifically in the early and late spermatids.^[9]

Protein

The human c20orf144 gene encodes a protein of 153 amino acids in length, and there are three disordered regions (Accession: NP_543015.1).^[4] Amino acids 1-150 are a part of the Bclt protein family which is predicted to be involved in apoptosis.^[10] The molecular weight is 17.2kDa and the theoretical isoelectric point is 11.47.^[11] There are 21 more lysines and arginines, which are positively charged, than there are aspartates and glutamates, which are negatively charged.

Annotated conceptual translation of human C20orf144 mRNA and protein.^[4]

The tertiary protein structure, produced by AlphaFold,^[12] predicts the presence of 3 α helices, and the absence of β sheets in human c20orf144.

AlphaFold^[12] structure prediction of human C20orf144. The predicted alpha helices are shown in spherical form.

Cellular localization

Analysis of the localization of human c20orf144 and many mammalian orthologs predicts localization of c20orf144 in the nucleus, with 78.3% confidence for the human protein.^[13]

Post translational modifications

Table 1. Predicted Post Translation Modifications of Human C20orf144

Modification	Modification Site in Human C20orf144
N-Myristoylation[13][14]	2G
Protein Kinase C Phosphorylation[15]	6S
Casein Kinase 2 Phosphorylation[15]	87S
Non-Specific Phosphorylation[15]	117S
O-Glycosylation[16]	117S
Protein Kinase C Phosphorylation[15]	123S

Evolution and orthologs

The rate of evolution of C20orf144 in comparison to the rates of evolution of Cytochrome C and Fibrinogen Alpha Chain.

The evolutionary rate of C20orf144 is comparable to the high rate of evolution of fibrinogen alpha chain, suggesting the protein is evolving quickly.

Orthologs of the c20orf144 gene in Homo sapiens are found in many mammals excluding monotremes.^[17] As shown in Table 2, marsupials are the most distantly related organisms to humans in which proteins encoded by human c20orf144 gene orthologs are found, suggesting that C20orf144 first appeared approximately 160 million years ago.

Table 2. Proteins encoded by the orthologs of the c20orf144 gene in humans.

Genus and Species	Common Name	Order	Protein Accession #	Median Date of Divergence (MYA)[18]	Sequence Length	Sequence Identity (%)	Sequence Similarity (%)
Homo sapiens	Human	Primata	NP_543015.1	0	153	100	100
Macaca mulatta	Rhesus Monkey	Primata	XP_001105397.1	28.9	153	86.3	90.8
Piliocolobus tephrosceles	Ugandan Red Colobus	Primata	XP_023076213.1	28.9	141	63.7	66.1
Jaculus jaculus	Lesser Egyptian Jerboa	Rodentia	XP_045011648.1	87	176	46.4	55.8
Myodes glareolus	Bank Vole	Rodentia	XP_048287479.1	87	197	42.1	51.8
Mus musculus	House Mouse	Rodentia	NP_083581.1	87	197	41.4	49.8
Camelus ferus	Wild Bactrian Camel	Artiodactyla	XP_032318023.1	94	174	54	64.4
Equus caballus	Domestic Horse	Perissodactyla	XP_023482143.1	94	178	45.7	56
Monodon monoceros	Narwhal	Artiodactyla	XP_029075207.1	94	181	42.9	50.5
Physeter catodon	Sperm Whale	Artiodactyla	XP_023984368.1	94	148	40.8	48.4
Prionailurus bengalensis	Leopard Cat	Carnivora	XP_043458511.1	94	179	52	60.9
Ursus arctos	Brown Bear	Carnivora	XP_026358671.1	94	184	51.6	61.4
Eumetopias jubatus	Steller Sea Lion	Carnivora	XP_027974622.1	94	184	47.3	58.1
Rousettus aegyptiacus	Egyptian Fruit Bat	Chiroptera	XP_016017694.2	94	175	51.4	62.7
Rhinolophus ferrumenquinum	Greater Horseshoe Bat	Chiroptera	XP_032951343.1	94	191	40.2	51.5
Pteropus vampyrus	Large Flying Fox	Chiroptera	XP_023377960.1	94	209	40	50.5
Choloepus didactylus	Southern Two-Toed Sloth	Pilosa	XP_037668100.1	99	188	47.9	57.4
Gracilinanus agilis	Agile Gracile Mouse Opossum	Didelphimorphia	XP_044517537.1	160	169	37.9	49.7
Dromiciops gliroides	Monito del Monte	Microbiotheria	XP_043845608.1	160	170	37	50.8
Sarcophilus harrisii	Tasmanian Devil	Dasyuromorphia	XP_031809718.1	160	160	36.4	50

Clinical significance

In a study of 28 breast cancer patients, missense mutations in c20orf144 were found in approximately 33% of patients, suggesting a potential role for c20orf144 in the development of breast cancer.^[19] Furthermore, c20orf144 is listed in primary renal proximal tubule epithelial cells as a top candidate hit in an siRNA screen, which silences targeted genes.^[20] The silencing of c20orf144 in cells exposed to Shiga toxin resulted in metabolic activity that was greater than or equal to 90% of that in a typical cell.