Wikipedia

ANKMY1

Ankyrin Repeat And MYND Domain Containing 1 (ANKMY1) is a protein that in humans is encoded by the ANKMY1 gene. Known aliases of ANKMY1 include Zinc Finger Myeloid, Nervy and DEAF-1 or ZMYND13.

ANKMY1
Identifiers
AliasesANKMY1, ZMYND13, ankyrin repeat and MYND domain containing 1
External IDsMGI: 3045261; HomoloGene: 9561; GeneCards: ANKMY1; OMA:ANKMY1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

51281

241158

Ensembl

ENSG00000144504

ENSMUSG00000034212

UniProt

Q9P2S6

Q8C0W1

RefSeq (mRNA)

NM_172850
NM_001347091

RefSeq (protein)

NP_001334020
NP_766438

Location (UCSC)Chr 2: 240.48 – 240.57 MbChr 1: 92.79 – 92.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gene

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The ANKMY1 gene is located on the minus strand of chromosome 2, at 2q37.3 .[5] The gene begins at base position 240,479,422 and ends at position 240,577,988. The coding sequence is 3424 nucleotides long and contains 17 exons.

mRNA Expression

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ANKMY1 is ubiquitously expressed in most tissue types in the body.[6]

Protein

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The ANKMY1 protein is 941 amino acids long and weighs approximately 105.5 kDa.[7] The pI is 6.3.

Domains and motifs

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ANKMY1 protein contains three MORN domains, seven ANK repeats and a single MYND zinc finger toward the end of the protein.[8]

Structure

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Figure 1. Secondary structure of ANKMY1 with beta sheets (green), alpha helixes (red) and turns (blue).[9]
 
Figure 2. iTasser tertiary structure of ANKMY1.[10]

The ANKMY1 protein contains both beta sheets and alpha helices. The MORN domains are exclusively beta sheets and the alpha helices appear only in the ANK domain.

Subcellular location

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Subcellular location of ANKMY1 protein was found to primarily be in the cytosol.[11] However, ANKMY1 contains nuclear export signals and evidence of nuclear transport indicating it is able to travel between both the nucleus and cytosol.[12]

Post-translational modifications

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ANKMY1 protein contains 3 sulfonated Tyrosines at positions 153, 155 and 162.[13] There is also a N-Glycosylation sites at 163.[14] ANKMY1 contains several (87) phosphorylation sites throughout.[15]

Homology

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Paralogs

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No paralogs were found for the ANKMY1 gene.

Orthologs

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ANKMY1 has numerous orthologs, strictly among vertebrates. The oldest known ortholog for ANKMY1 is the sea lamprey, an organism that diverged nearly 599 million years ago.

Genus and Species Common Name Taxonomic Group Median Date of Divergence (MYA) Accession # Sequence Length (aa) Sequence Identity to Human Protein (%) Sequence Similarity to Human Protein (%)
Homo Sapiens Human Primates 0 NP_057636.2 941 100 100
Mirounga angustirostris Northern Elephant Seal Pinnipedia 94 XP_054361851 688 31 37
Vombatus ursinus Common Wombat Diprotodontia 160 XP_027717300 1068 47 61
Ornithorhynchus anatinus Platypus Monotremata 180 XP_028935005 1054 48 61
Cygnus atratus Black Swan Anseriformes 318 XP_050570946 819 39 53
Pelecanus crispus Dalmatian Pelican Pelecaniformes 319 XP_009481272 741 42 56
Apteryx rowi Okarito Brown Kiwi Apterygiformes 319 XP_025939958 828 38 49
Gopherus evgoodei Goodes Thronscrub Tortoise Testudines 319 XP_030431806 1041 44 56
Alligator mississippiensis American Alligator Crocodylia 319 XP_014454066 1024 44 56
Dermochelys coriacea Leatherback Sea Turtle Testudines 319 XP_043347915 1054 43 56
Sphaerodactylus townsendi Townsend's Least Gecko Squamata 319 XP_048362796 1046 40 53
Notechis scutatus Mainland Tiger Snake Squamata 319 XP_026524636 990 36 50
Bombina bombina Fire-bellied Toad Salientia 352 XP_053567490 942 39 53
Hyla sarda Sardinian Tree Frog Anura 352 XP_056420535 952 35 49
Rhinatrema bivittatum Two-lined Caecilian Gymnophiona 352 XP_029472316 1260 32 45
Latimeria chalumnae West Indian Ocean Coelacanth Coelacanthiformes 413 XP_014354204 1223 35 48
Chiloscyllium plagiosum White-Spotted Bamboo Shark Orectolobiformes 462 XP_043557725 1055 37 51
Amblyraja radiata Thorny Skate Rajiformes 465 XP_032887417 1017 37 51
Petromyzon marinus Sea Lamprey Petromyzontiformes 599 XP_032831007 1265 28 38

Table 1. Orthologs of ANKMY1 in humans. Sorted first by estimated date of divergence, then by sequence identity to human protein. ANKMY1 is only found in vertebrates, not invertebrates.

Function

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The specific MYND finger of ANKMY1 is specialized for protein-protein interactions. MORN repeats are also associated with linking, more specifically linking parasites and their hosts together.[16] ANKMY1's fast evolution rate coupled with its binding capabilities make it a good candidate for cellular defense. ANKMY1 was found to interact with several proteins within the cell (Table 2).

Interacting proteins

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Name Function Subcellular Location
MKRN2 Opposite Strand N/A Golgi Apparatus
THAP Domain Containing 4 N/A Mostly cytoplasm, some nucleus
Zinc Finger Protein  227 May be involved in transcriptional regulation Nucleus
Zygote Arrest Protein 1 N/A Cytoplasm
FERM, ARHGEF and pleckstrin domain-containing protein 2 Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion Cytosol
Stress-associated endoplasmic reticulum protein 2 May protect unfolded target proteins against degradation and facilitate correct glycosylation Endoplasmic Reticulum
Thymidylate kinase Catalyzes the conversion of dTMP to dTDP Cytosol/Nucleus
Serine/threonine-protein Kinase 25 Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration. Golgi/Extracellular
Paired Box Protein Pax-9 Transcription factor required for normal development of thymus, parathyroid glands, ultimobranchial bodies, teeth, skeletal elements of skull and larynx as well as distal limbs Nucleus
Receptor Transporter Protein 5 N/A Cytosol

Table 2. Potential ANKMY1 protein-protein interactions drawn from the STRING database. [17] "N/A" indicates unknown function.

Clinical significance

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Figure 3. The lollipops represent recurrent and possibly oncogenic missense mutations. The blue heads indicate phosphorylation and the green indicates acetylation. Graph also illustrates the MORN Repeats, ANK repeats and Zinc finger.[18]

Missense mutations commonly resulting in oncogenic growths were identified at various sites within the coding region.[19] Via text-mining a link between increased expression of the ANKMY1 gene and longer time periods of metastasis-free survival in Osteosarcoma patients.[20][21][22] ANKMY1 also shows elevated expression in the omental adipose tissue of obese children.[23]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000144504 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034212 – 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.
  5. ^ "Homo sapiens ankyrin repeat and MYND domain containing 1 (ANKMY1), transcript variant 1, mRNA". April 18, 2022 – via NCBI Nucleotide.
  6. ^ "TMEM212 transmembrane protein 212 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov.
  7. ^ "ANKMY1 Gene - GeneCards | ANKY1 Protein | ANKY1 Antibody".
  8. ^ "InterPro". www.ebi.ac.uk. Retrieved 2023-12-06.
  9. ^ Kumar TA. "CFSSP: Chou & Fasman Secondary Structure Prediction Server". www.biogem.org. Retrieved 2023-12-15.
  10. ^ "I-TASSER results". zhanggroup.org. Retrieved 2023-12-15.
  11. ^ "Subcellular - ANKMY1 - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2023-12-15.
  12. ^ "PSORT II Prediction". psort.hgc.jp. Retrieved 2023-12-15.
  13. ^ "Expasy Sulfinator tool".
  14. ^ "NetNGlyc 1.0 - DTU Health Tech - Bioinformatic Services". services.healthtech.dtu.dk.
  15. ^ "NetPhos 3.1 - DTU Health Tech - Bioinformatic Services". services.healthtech.dtu.dk. Retrieved 2023-12-15.
  16. ^ Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, et al. (2020-12-09). "Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats". PLOS ONE. 15 (12): e0242677. Bibcode:2020PLoSO..1542677S. doi:10.1371/journal.pone.0242677. PMC 7725318. PMID 33296386.
  17. ^ "STRING: functional protein association networks". string-db.org. Retrieved 2023-12-06.
  18. ^ "PhosphoSitePlus". www.phosphosite.org. Retrieved 2023-12-15.
  19. ^ "PhosphoSitePlus". www.phosphosite.org. Retrieved 2023-12-06.
  20. ^ Wang F, Qin G, Liu J, Wang X, Ye B (2020). "Integrated Genome-Wide Methylation and Expression Analyses Reveal Key Regulators in Osteosarcoma". Computational and Mathematical Methods in Medicine. 2020: 7067649. doi:10.1155/2020/7067649. PMC 7443031. PMID 32855654.
  21. ^ Chen H, Xing K, He X (August 2015). "The dJ/dS Ratio Test Reveals Hundreds of Novel Putative Cancer Drivers". Molecular Biology and Evolution. 32 (8): 2181–2185. doi:10.1093/molbev/msv083. PMC 4833070. PMID 25873590.
  22. ^ Turi M, Anilkumar Sithara A, Hofmanová L, Žihala D, Radhakrishnan D, Vdovin A, et al. (March 2023). "Transcriptome Analysis of Diffuse Large B-Cell Lymphoma Cells Inducibly Expressing MyD88 L265P Mutation Identifies Upregulated CD44, LGALS3, NFKBIZ, and BATF as Downstream Targets of Oncogenic NF-κB Signaling". International Journal of Molecular Sciences. 24 (6): 5623. doi:10.3390/ijms24065623. PMC 10057398. PMID 36982699.
  23. ^ "GDS3688 / 220280_s_at". www.ncbi.nlm.nih.gov. Retrieved 2023-12-15.
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