C11orf86

Last updated
C11orf86
Identifiers
Aliases C11orf86 , chromosome 11 open reading frame 86
External IDs MGI: 1917111 HomoloGene: 52832 GeneCards: C11orf86
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001136485
NM_001353554

NM_027237

RefSeq (protein)

NP_001129957
NP_001340483

NP_081513

Location (UCSC) Chr 11: 66.98 – 66.98 Mb Chr 19: 4.55 – 4.55 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Chromosome 11 open reading frame 86, also known as C11orf86, is a protein-coding gene in humans. [5] It encodes for a protein known as uncharacterized protein C11orf86, [6] which is predicted to be a nuclear protein. The function of this protein is currently unknown.

Contents

Gene

Location

C11orf86 is located on the long arm of chromosome 11 at 11q13.2. It consists of 1732 base pairs, and is found on the plus strand. Gene neighbors of C11orf86 include uncharacterized LOC105369355, microRNA 6860, microRNA 3163, synaptotagmin 12, ras homolog family member D, and pyruvate carboxylase. [7]

NCBI Gene diagram showing the genes that neighbor C11orf86. C11orf86 - Gene Neighborhood.png
NCBI Gene diagram showing the genes that neighbor C11orf86.

Promoter

The program ElDorado, by Genomatix, identified the promoter region of C11orf86 on the positive strand from 66974707 to 66975464, for a total length of 758 base pairs. [8]

Expression

C11orf86 appears to be primarily expressed in the gastrointestinal tract. [9] Expression occurs in ascites, the intestine, the stomach, gastrointestinal tumors, and non-neoplasia. [10]

mRNA

AceView gene diagram of the alternative mRNA splice variants of human C11orf86. Gene diagram- Human C11orf86 alternative mRNAs.png
AceView gene diagram of the alternative mRNA splice variants of human C11orf86.

Alternative Splicing

According to AceView, transcription of the gene produces three different mRNAs, two of which are alternatively spliced variants, while the third is an unspliced form. [11] All three variants could possibly code for functional proteins. The transcript used for this article is made up of two exons, amounting to 1185 base pairs, and has the reference number NM_001136485.1. [12]

mRNA variantExonExon Size (bp)IntronIntron Size (bp)
a13621541
2829
b12491538
2251
c15510

Protein

General Properties

C11orf86 protein is 115 amino acids in length. [6] The molecular weight of C11orf86 is 13.2 kdal. [13] Its isoelectric point is predicted to be 11.9. [14]

1   MGTGLRSQSL REPRPSYGKL QEPWGRPQEG QLRRALSLRQ GQEKSRSQGL ERGTEGPDAT  61  AQERVPGSLG DTEQLIQAQR RGSRWWLRRY QQVRRRWESF VAIFPSVTLS QPASP 

Composition

The majority of the C11orf86 protein is composed of arginine (15.7%), glutamine (12.2%), serine (10.4%), glycine (10.4%), and leucine (9.6%). No cysteine, histidine, or asparagine residues are found in this protein. [13]

A  :  6( 5.2%); C  :  0( 0.0%); D  :  2( 1.7%); E  :  9( 7.8%); F  :  2( 1.7%) G  : 12(10.4%); H  :  0( 0.0%); I  :  2( 1.7%); K  :  2( 1.7%); L  : 11( 9.6%) M  :  1( 0.9%); N  :  0( 0.0%); P  :  9( 7.8%); Q  : 14(12.2%); R  : 18(15.7%) S  : 12(10.4%); T  :  5( 4.3%); V  :  4( 3.5%); W  :  4( 3.5%); Y  :  2( 1.7%) 

C11orf86 has no positive, negative, or mixed charge clusters. However, there is a higher presence of arginine, which is positively charged.

1   00000+0000 +-0+0000+0 0-000+00-0 00++0000+0 00-+0+0000 -+00-00-00  61  00-+000000 -0-000000+ +00+000++0 000+++0-00 0000000000 00000 

Domain

This protein is a part of the DUF4633 superfamily. Proteins that belong to this family are often between 94 and 123 amino acids in length. [15] This domain is found in bacteria, viruses, fungi, plants, insects, reptiles, birds, and mammals. [16]

Domain of unknown function, DUF4633, and the C11orf86 gene. C11orf86 - DUF4633.png
Domain of unknown function, DUF4633, and the C11orf86 gene.

Post-Translational Modification

C11orf86 is predicted to have nine possible phosphorylation sites, of which eight are serine, and one is threonine. [17] It is also predicted to have ten O-linked glycosylation sites. [18]

Secondary Structure

C11orf86 is primarily composed of random coil and alpha helices. [19] [20]

Sub-cellular Localization

This protein is predicted to be a nuclear protein. [21] There appears to be a bipartite nuclear localization sequence beginning at position 80. [22]

Homology

The C11orf86 protein is conserved in mammals, and orthologs can easily be traced back to marsupials, monotremes, and reptiles. No orthologs of C11orf86 appear to be present in plants, fungi, fish, amphibians, or birds. There are no paralogs of C11orf86. The table below shows some orthologs that were found using BLAST. [23] Dates of divergence were found from TimeTree, using the median molecular time estimate. [24]

Genus and SpeciesCommon NameAccession NumberProtein Length (aa)Percent Identity (%)Date of Divergence (mya)
Homo sapiensHumanNP_001129957.1115100
Macaca mulattaRhesus macaqueXP_001115236.11158927.3
Rattus norvegicusBrown ratNP_001102991.11237490.1
Bos taurusCattleNP_001070558.11227495.0
Equus caballusHorseXP_014585069.11137195.0
Mus musculusMouseNP_081513.11247190.1
Felis catusCatXP_003993784.11217095.0
Canis lupus familiarisDogXP_003639729.11216995.0
Sarcophilus harrisiiTasmanian devilXP_012408455.112040162.4
Ornithorhynchus anatinusPlatypusXP_007659213.111940169.7
Chrysemys picta belliiPainted turtleXP_008177865.113535320.5

Clinical Significance

A bipolar disorder association study identified C11orf86 as one of many genes found in a region of linkage disequilibrium on chromosome 11. Despite evidence of some association, C11orf86 was not found to be in an area of particular significance. [25] C11orf86 is down-regulated from non-neoplastic mucosa to adenomas and carcinomas, [26] down-regulated in renal cell carcinoma, [27] and harbors chromosomal gains that are significantly associated with pure mucinous subtypes in mucinous carcinoma. [28]

Related Research Articles

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<span class="mw-page-title-main">C2orf73</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">C16orf46</span> Human gene

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<span class="mw-page-title-main">C16orf86</span> Protein-coding gene in the species Homo sapiens

Uncharacterized protein C16orf86 is a protein in humans that is encoded by the C16orf86 gene. It is mostly made of alpha helices and it is expressed in the testes, but also in other tissues such as the kidney, colon, brain, fat, spleen, and liver. For the function of C16orf86, it is not well understood, however it could be a transcription factor in the nucleus that regulates G0/G1 in the cell cycle for tissues such as the kidney, brain, and skeletal muscles as mentioned in the DNA microarray data below in the gene level regulation section.

C11orf42 is an uncharacterized protein in homo sapiens that is encoded by the C11orf42 gene. It is also known as chromosome 11 open reading frame 42 and uncharacterized protein C11orf42, with no other aliases. The gene is mostly conserved in mammals, but it has also been found in rodents, reptiles, fish and worms.

<span class="mw-page-title-main">C16orf90</span> Protein-coding gene in the species Homo sapiens

C16orf90 or chromosome 16 open reading frame 90 produces uncharacterized protein C16orf90 in homo sapiens. C16orf90's protein has four predicted alpha-helix domains and is mildly expressed in the testes and lowly expressed throughout the body. While the function of C16orf90 is not yet well understood by the scientific community, it has suspected involvement in the biological stress response and apoptosis based on expression data from microarrays and post-translational modification data.

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<span class="mw-page-title-main">C17orf78</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">C9orf85</span> Protein-coding gene in the species Homo sapiens

Chromosome 9 open reading frame 85, commonly known as C9orf85, is a protein in Homo sapiens encoded by the C9orf85 gene. The gene is located at 9q21.13. When spliced, four different isoforms are formed. C9orf85 has a predicted molecular weight of 20.17 kdal. Isoelectric point was found to be 9.54. The function of the gene has not yet been confirmed, however it has been found to show high levels of expression in cells of high differentiation.

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