ANKRD24

ANKRD24
Identifiers
Aliases	ANKRD24 , ankyrin repeat domain 24
External IDs	MGI: 1890394 HomoloGene: 49885 GeneCards: ANKRD24
Gene location (Human)
Chr.	Chromosome 19 (human) [1]
End	4,224,814 bp [1]
Gene location (Mouse)
Chr.	Chromosome 10 (mouse) [2]
End	81,647,610 bp [2]
Orthologs
	170961
	70615
	ENSG00000089847
	ENSMUSG00000054708
	Q8TF21
	Q80VM7
	NM_133475
	NM_027480
	NP_597732
	NP_081756
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 12, 2019

Predicted tertiary structure of ANKRD24 using I-TASSER ANKRD24.jpg — Predicted tertiary structure of ANKRD24 using I-TASSER

Ankyrin repeat domain-containing protein 24 is a protein in humans that is coded for by the ANKRD24 gene.^[6] The gene is also known as KIAA1981^[7]. The protein's function in humans is currently unknown. ANKRD24 is in the protein family that contains ankyrin-repeat domains.

The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. Domains consisting of ankyrin tandem repeats mediate protein–protein interactions and are among the most common structural motifs in known proteins. They appear in bacterial, archaeal, and eukaryotic proteins, but are far more common in eukaryotes. Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia.

Gene

Locus

ANKRD24 gene neighborhood ANKRD24 gene neighborhood.png — ANKRD24 gene neighborhood

The gene is located on chromosome 19 at p13.3 on the forward strand.^[10]^[11] The gene is 4041 base pairs in length and contains 29 exons.^[9]^[12] The gene is neighbored by the gene SIRT6 that encodes for the Sirtuin-6 protein and the EBI3 gene that encodes for the Epstein-Barr virus induced gene 3 protein.^[13]

Sirtuins are a class of proteins that possess either mono-ADP-ribosyltransferase, or deacylase activity, including deacetylase, desuccinylase, demalonylase, demyristoylase and depalmitoylase activity. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2', the gene responsible for cellular regulation in yeast.

Epstein-Barr virus induced gene 3, also known as interleukin-27 subunit beta or IL-27B, is a protein which in humans is encoded by the EBI3 gene.

Expression

The expression pattern of ANKRD24 is uncharacterized. Under conditions of cell growth and proliferation, the expression levels increase. In germ line tumors, glioma, and prostate cancer, the expression is elevated relative to other disease states. During development, the expression level is elevated in the blastocyst stage. In adults, there are elevated levels of expression in the placenta, stomach, kidneys, and eye relative to other tissues.^[14] However, the results of experimental gene expression profiles are inconsistent relative to ANKRD24 expression, suggesting redundancy of the gene and its protein product.

Glioma A type of tumor that starts in the brain or spine

A glioma is a type of tumor that starts in the glial cells of the brain or the spine. Gliomas comprise about 30 percent of all brain tumors and central nervous system tumors, and 80 percent of all malignant brain tumors.

Prostate cancer is the development of cancer in the prostate, a gland in the male reproductive system. Most prostate cancers are slow growing; however, some grow relatively quickly. The cancer cells may spread from the prostate to other areas of the body, particularly the bones and lymph nodes. It may initially cause no symptoms. In later stages, it can lead to difficulty urinating, blood in the urine or pain in the pelvis, back, or when urinating. A disease known as benign prostatic hyperplasia may produce similar symptoms. Other late symptoms may include feeling tired due to low levels of red blood cells.

The blastocyst is a structure formed in the early development of mammals. It possesses an inner cell mass (ICM) which subsequently forms the embryo. The outer layer of the blastocyst consists of cells collectively called the trophoblast. This layer surrounds the inner cell mass and a fluid-filled cavity known as the blastocoel. The trophoblast gives rise to the placenta. The name "blastocyst" arises from the Greek βλαστός blastos and κύστις kystis.

mRNA

Alternative expression

13 transcription splice variants of ANKRD24 mRNA have been predicted.^[15]

Messenger RNA large family of RNA molecules that convey genetic information from DNA to the ribosome, where they specify the amino acid sequence of the protein products of gene expression

Messenger RNA (mRNA) is a large family of RNA molecules that convey genetic information from DNA to the ribosome, where they specify the amino acid sequence of the protein products of gene expression. RNA polymerase transcribes primary transcript mRNA into processed, mature mRNA. This mature mRNA is then translated into a polymer of amino acids: a protein, as summarized in the central dogma of molecular biology.

Protein

General features

The ANKRD24 protein is 1146 amino acids in length, has a molecular weight of 124kDa, and has an isoelectric point of 4.98.^[16] The secondary structure is predicted to consist of all alpha helices and to not contain any beta strands.^[17] The tertiary structure of the protein is predicted to be a helical twist.^[5]

The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I), although pI is also commonly seen, and is used in this article for brevity. The net charge on the molecule is affected by pH of its surrounding environment and can become more positively or negatively charged due to the gain or loss, respectively, of protons (H⁺).

The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group donates a hydrogen bond to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence.

Composition

ANKRD24 has a relatively high composition of alanine (15.0%), glutamic acid (13.5%), and leucine (11.0%) and a relatively low composition of cysteine (1.5%), phenylalanine (0.7%), tryptophan (0.2%), and tyrosine (0.8%). The protein contains positive run clusters that could be nuclear localization signals. The protein does not have any significant negative charge clusters and no significant charge patterns.^[18]

Alanine (symbol Ala or A) is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently, its IUPAC systematic name is 2-aminopropanoic acid, and it is classified as a nonpolar, aliphatic α-amino acid. Under biological conditions, it exists in its zwitterionic form with its amine group protonated (as −NH₃⁺) and its carboxyl group deprotonated (as −CO₂⁻). It is non-essential to humans as it can be synthesised metabolically and does not need to be present in the diet. It is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG).

Glutamic acid is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is non-essential in humans, meaning the body can synthesize it. It is also an excitatory neurotransmitter, in fact the most abundant one, in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons.

Leucine (symbol Leu or L) is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH₃⁺ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO⁻ form under biological conditions), and a side chain isobutyl group, making it a non-polar aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG.

Subcellular localization

The ANKRD24 protein is predicted to localize in the nucleus of cells.^[19]

Domains

ANKRD24 is in the protein family that contains ankyrin-repeat domains. Ankyrin repeats are known for mediating protein-protein interactions.^[20] The protein also contains two coiled-coil regions.^[21]

Post-translational modification

ANKRD24 is predicted to undergo C-mannosylation.^[22]

Interacting proteins

ANKRD24 is predicted to interact with disks large homolog 4 (DLG4), eukaryotic translation elongation factor 1-alpha 1 (EEF1A1), unc-119 homolog A (UNC119), replication timing regulatory factor 1 (RIF1), protein kinase C and casein kinase substrate in neurons 1 (PACSIN1), nuclear factor NF-kappa-B p105 subunit (NFKB1), cholest-5-ene-3β,7α-diol 3β-dehydrogenase (HSD3B7), lethal giant larvae homolog 2 (L2GL2), and glucocorticoid induced 1 (GLC)CI1.^[23]^[24]^[25]^[26] No characterization of these interactions has yet to be observed.^[27]

Homology

ANKRD24 has no human paralogs. Orthologous proteins are found in other organisms. The following table represents some of the orthologs found using searches in BLAST ^[29] and BLAT.^[30] However, this list is not exhaustive for the orthologs of ANKRD24 and is only meant to display the wide diversity of species for which orthologs of ANKRD24 can be found.

	Genus species	Common Name	Date of Divergence (MYA)^[31]	Accession # (Nucleotide)	Accession # (Protein)	Sequence Length (bp)	Sequence Length (aa)	E value	Sequence Identity (%)	Sequence Similarity (%)
1	Homo sapiens	Humans	0	NM_133475.1	NP_597732.1	4041	1146		100	100
2	Nomascus leucogenys	Northern white-cheeked gibbon	19.9	XM_012503370.1	XP_012358824.1	3675	1165	0	95	96
3	Otolemur garnettii	Small-eared galago	75.9	XM_012804592.1	XP_012660046.1	4181	1035	0	83	87
4	Trichechus manatus latirostris	Florida Manatee	105	XM_004378459.1	]	3354	1117	0	81	86
5	Eptesicus fuscus	Big brown bat	97.5	XM_008150610.1	XP_008148832.1	3369	1122	0	80	84
6	Ailuropoda melanoleuca	Giant panda	97.5	XM_002928471.2	XP_002928517.1	3729	1116	0	80	84
7	Loxodonta africana	African savanna elephant	105	XM_003421925.2	XP_003421973.1	4049	1345	0	79	85
8	Octodon degus	Degu	90.9	XM_004632746.1	XP_004632803.1	3381	1126	0	79	84
9	Chrysochloris asiatica	Cape golden mole	105	XM_006869037.1	XP_006869099.1	3747	1248	0	78	85
10	Orcinus orca	Killer Whale	97.5	XM_004277648.2	XP_004277696.1	3482	1079	0	77	82
11	Chelonia mydas	Green sea turle	320.5	XM_007072230.1	XP_007072292	3051	1016	9.00E-178	63	77
12	Ficedula albicollis	Collared flycatcher	320.5	XM_005060250.1	XP_005060307	1885	621	2.00E-171	60	74
13	Gekko Japonicus	Japanese gecko	320.5	XM_015410656.1	XP_015266142	3057	1019	3.00E-175	58	75
14	Python bivittatus	Burmese python	320.5	XM_007434390	XP_007434452	3192	1063	1.00E-167	58	75
15	Falco cherrug	Saker falcon	320.5	XM_014277718.1	XP_014133193	1431	476	0	57	71
16	Stegastes partitus	Bicolor damselfish	429.6	XM_008295305.1	XP_008293527.1	3629	1095	2.00E-90	41	55
17	Trichomonas vaginalis G3	Trichomonas vaginalis	2040	XM_001329224.1	XP_001329259	774	257	2.00E-24	34	54
18	Ciona intestinalis	Vase tunicate	733	XM_009863371.1	XP_009861673	3156	956	9.00E-24	32	48
19	Talaromyces stipitatus	Fungi	1302.5	XM_002486774.1	XP_002486819.1	3216	1071	3.00E-18	32	51
20	Cryptococcus neoformans	Yeast	1302.5	XM_012197089.1	XP_012052479.1	943	236	3.00E-16	32	51

Related Research Articles

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References

1 2 3 GRCh38: Ensembl release 89: ENSG00000089847 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000054708 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "I-TASSER server for protein structure and function prediction". zhanglab.ccmb.med.umich.edu. Retrieved 2016-04-26.
↑ "ankyrin repeat domain-containing protein 24 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-02-07.
↑ "ANKRD24 - Ankyrin repeat domain-containing protein 24 - Homo sapiens (Human) - ANKRD24 gene & protein". www.uniprot.org. Retrieved 2016-02-07.
↑ "Gene Card entry for ANKRD24". Gene Card. Retrieved 2016-05-09.
1 2 "ANKRD24 ankyrin repeat domain 24 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-05-09.
↑ "Gene Card Entry on ANKRD24". www.genecards.org. Retrieved 2016-02-07.
↑ "Gene: ANKRD24 (ENSG00000089847) - Summary - Homo sapiens - Ensembl genome browser 84". useast.ensembl.org. Retrieved 2016-05-09.
↑ "Homo sapiens ankyrin repeat domain 24 (ANKRD24), mRNA - Nucleotide - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-26.
↑ "ANKRD24 ankyrin repeat domain 24 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-27.
↑ "EST Profile - Hs.197872". www.ncbi.nlm.nih.gov. Retrieved 2016-04-27.
↑ "ankyrin repeat domain-containing protein 24 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-24.
↑ "SDSC Biology Workbench". workbench.sdsc.edu. Retrieved 2016-05-09.
↑ "Phyre 2 Results for My_protein". www.sbg.bio.ic.ac.uk. Retrieved 2016-04-27.^{[ permanent dead link ]}
↑ "SAPS submission on ANKRD24". Biology WorkBench.
↑ "Gene Card Entry on ANKRD24". www.genecards.org. Retrieved 2016-04-24.
↑ Mosavi LK, Cammett TJ, Desrosiers DC, Peng ZY (June 2004). "The ankyrin repeat as molecular architecture for protein recognition". Protein Science. 13 (6): 1435–48. doi:10.1110/ps.03554604. PMC 2279977 . PMID 15152081.
↑ "ANKRD24 - Ankyrin repeat domain-containing protein 24 - Homo sapiens (Human) - ANKRD24 gene & protein". www.uniprot.org. Retrieved 2016-02-08.
↑ "NetCGlyc 1.0 Server". www.cbs.dtu.dk. Retrieved 2016-05-09.
↑ "8 binary interactions found for search term ANKRD24". IntAct Molecular Interaction Database. EMBL-EBI. Retrieved 2018-08-25.
↑ al., David Lynn et. "InnateDB: Systems Biology of the Innate Immune Response". www.innatedb.com. Retrieved 2016-04-24.
↑ "mentha: the interactome browser". mentha.uniroma2.it. Retrieved 2016-04-24.
↑ "mint database". mint.bio.uniroma2.it. Archived from the original on 2006-05-06. Retrieved 2016-04-24.
↑ "STRING: functional protein association networks". string-db.org. Retrieved 2016-02-08.
↑ "DRAWTREE". Biology WorkBench.
↑ "BLAST: Basic Local Alignment Search Tool". blast.ncbi.nlm.nih.gov. Retrieved 2016-05-09.
↑ "UCSC Genome Bioinformatics: FAQ". genome.ucsc.edu. Retrieved 2016-05-09.
↑ Hedges SB, Marin J, Suleski M, Paymer M, Kumar S (April 2015). "Tree of life reveals clock-like speciation and diversification". Molecular Biology and Evolution. 32 (4): 835–45. arXiv: 1412.4312 . doi:10.1093/molbev/msv037. PMC 4379413 . PMID 25739733.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000089847 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000054708 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[:1-5] 1 2 "I-TASSER server for protein structure and function prediction". zhanglab.ccmb.med.umich.edu. Retrieved 2016-04-26.

[6] "ankyrin repeat domain-containing protein 24 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-02-07.

[7] "ANKRD24 - Ankyrin repeat domain-containing protein 24 - Homo sapiens (Human) - ANKRD24 gene & protein". www.uniprot.org. Retrieved 2016-02-07.

[8] "Gene Card entry for ANKRD24". Gene Card. Retrieved 2016-05-09.

[ncbi.nlm.nih.gov-9] 1 2 "ANKRD24 ankyrin repeat domain 24 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-05-09.

[10] "Gene Card Entry on ANKRD24". www.genecards.org. Retrieved 2016-02-07.

[11] "Gene: ANKRD24 (ENSG00000089847) - Summary - Homo sapiens - Ensembl genome browser 84". useast.ensembl.org. Retrieved 2016-05-09.

[12] "Homo sapiens ankyrin repeat domain 24 (ANKRD24), mRNA - Nucleotide - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-26.

[13] "ANKRD24 ankyrin repeat domain 24 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-27.

[14] "EST Profile - Hs.197872". www.ncbi.nlm.nih.gov. Retrieved 2016-04-27.

[15] "ankyrin repeat domain-containing protein 24 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-24.

[16] "SDSC Biology Workbench". workbench.sdsc.edu. Retrieved 2016-05-09.

[17] "Phyre 2 Results for My_protein". www.sbg.bio.ic.ac.uk. Retrieved 2016-04-27.^{[ permanent dead link ]}

[18] "SAPS submission on ANKRD24". Biology WorkBench.

[19] "Gene Card Entry on ANKRD24". www.genecards.org. Retrieved 2016-04-24.

[20] Mosavi LK, Cammett TJ, Desrosiers DC, Peng ZY (June 2004). "The ankyrin repeat as molecular architecture for protein recognition". Protein Science. 13 (6): 1435–48. doi:10.1110/ps.03554604. PMC 2279977 . PMID 15152081.

[21] "ANKRD24 - Ankyrin repeat domain-containing protein 24 - Homo sapiens (Human) - ANKRD24 gene & protein". www.uniprot.org. Retrieved 2016-02-08.

[22] "NetCGlyc 1.0 Server". www.cbs.dtu.dk. Retrieved 2016-05-09.

[23] "8 binary interactions found for search term ANKRD24". IntAct Molecular Interaction Database. EMBL-EBI. Retrieved 2018-08-25.

[24] ., David Lynn et. "InnateDB: Systems Biology of the Innate Immune Response". www.innatedb.com. Retrieved 2016-04-24.

[25] "mentha: the interactome browser". mentha.uniroma2.it. Retrieved 2016-04-24.

[26] "mint database". mint.bio.uniroma2.it. Archived from the original on 2006-05-06. Retrieved 2016-04-24.

[27] "STRING: functional protein association networks". string-db.org. Retrieved 2016-02-08.

[28] "DRAWTREE". Biology WorkBench.

[29] "BLAST: Basic Local Alignment Search Tool". blast.ncbi.nlm.nih.gov. Retrieved 2016-05-09.

[30] "UCSC Genome Bioinformatics: FAQ". genome.ucsc.edu. Retrieved 2016-05-09.

[31] Hedges SB, Marin J, Suleski M, Paymer M, Kumar S (April 2015). "Tree of life reveals clock-like speciation and diversification". Molecular Biology and Evolution. 32 (4): 835–45. arXiv: 1412.4312 . doi:10.1093/molbev/msv037. PMC 4379413 . PMID 25739733.