Biology:C7orf50

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Short description: Mammalian protein found in Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

C7orf50 (Chromosome 7, Open Reading Frame 50) is a gene in humans (Homo sapiens) that encodes a protein known as C7orf50 (uncharacterized protein C7orf50). This gene is ubiquitously expressed in the kidneys, brain, fat, prostate, spleen, among 22 other tissues and demonstrates low tissue specificity.[1][2] C7orf50 is conserved in chimpanzees, Rhesus monkeys, dogs, cows, mice, rats, and chickens, along with 307 other organisms from mammals to fungi.[3] This protein is predicted to be involved with the import of ribosomal proteins into the nucleus to be assembled into ribosomal subunits as a part of rRNA processing.[4][5] Additionally, this gene is predicted to be a microRNA (miRNA) protein coding host gene, meaning that it may contain miRNA genes in its introns and/or exons.[6][7]

Gene

Background

C7orf50, also known as YCR016W, MGC11257, and LOC84310, is a protein coding gene of poor characterization in need of further research. This gene can be accessed on NCBI at the accession number NC_000007.14, on HGNC at the ID number 22421, on ENSEMBL at the ID ENSG00000146540, on GeneCards at GCID:GC07M000996, and on UniProtKB at the ID Q9BRJ6.

Location

C7orf50 is located on the short arm of chromosome 7 (7p22.3), starting at base pair (bp) 977,964 and ending at bp 1,138,325. This gene spans 160,361 bps on the minus (-) strand and contains a total of 13 exons.[1]

Gene Neighborhood

Genes within the neighborhood of C7orf50 are the following: LOC105375120, GPR146, LOC114004405, LOC107986755, ZFAND2A, LOC102723758, LOC106799841, COX19, ADAP1, CYP2W1, MIR339, GPER1, and LOC101927021. This neighborhood extends from bp 89700 to bp 1165958 on chromosome 7.[1]

mRNA

Alternative Splicing

C7orf50 has a total of 7 experimentally curated mRNA transcripts.[1] These transcripts are maintained independently of annotated genomes and were not generated computationally from a specific genome build such as the GRCh38.p13 primary assembly; therefore, they are typically more reliable. The longest and most complete of these transcripts (transcript 4) being 2138bp, producing a 194 amino acid-long (aa) protein, and consisting of 5 exons.[8] Of these transcripts, four of them encode for the same 194aa protein (isoform a),[9] only differing in their 5' and 3' untranslated regions (UTRs). The three other transcripts encode isoform b, c, and d, respectively. The table below is representative of these transcripts.

C7orf50 Experimentally Determined

NCBI Reference Sequences (RefSeq) mRNA Transcripts

Name NCBI Accession # Transcript Length # of Exons Protein Length Isoform
Transcript Variant 1 NM_032350.5 1311bp 5 194aa a
Transcript Variant 2 NM_001134395.1 1301bp 5 194aa a
Transcript Variant 3 NM_001134396.1 1282bp 5 194aa a
Transcript Variant 4 NM_001318252.2 2138bp 5 194aa a
Transcript Variant 7 NM_001350968.1 1081bp 6 193aa b
Transcript Variant 8 NM_001350969.1 1500bp 5 180aa c
Transcript Variant 9 NM_001350970.1 1448bp 3 60aa d

Alternatively, when the primary genomic assembly, GRCh38.p13, is used for annotation (NCBI: NC_000007.14), there are 10 computationally predicted mRNA transcripts.[1] The most complete and supported of these transcripts (transcript variant X6) is 1896bp, producing a 225aa-long protein.[10] In total, there are 6 different isoforms predicted for C7orf50. Of these transcripts, 5 of them encode for the same isoform (X3).[11] The remaining transcripts encode isoforms X2, X4, X5, X6, and X7 as represented below.

C7orf50 Computationally Determined

NCBI Reference Sequences (RefSeq) mRNA Transcripts

Name NCBI Accession # Transcript Length Protein Length Isoform
Transcript Variant X2 XM_017012719.1 1447bp 375aa X2
Transcript Variant X3 XM_011515582.3 1192bp 225aa X3
Transcript Variant X4 XM_024446977.1 1057bp 193aa X4
Transcript Variant X5 XM_011515581.3 1240bp 225aa X3
Transcript Variant X6 XM_011515584.2 1896bp 225aa X3
Transcript Variant X7 XM_017012720.2 1199bp 225aa X3
Transcript Variant X8 XM_011515583.2 1215bp 225aa X3
Transcript Variant X9 XM_017012721.2 2121bp 211aa X5
Transcript Variant X10 XM_024446978.1 2207bp 180aa X6
Transcript Variant X11 XM_024446979.1 933bp 93aa X7

5' and 3' UTR

Based on the experimentally determined C7orf50 mRNA transcript variant 4, the 5' UTR of C7orf50 is 934 nucleotides (nt) long, while the 3' UTR is 619nt. The coding sequence (CDS) of this transcript spans nt 935..1519 for a total length of 584nt and is encoded in reading frame 2.[8] Interestingly, the 5'UTR of C7orf50 contains a uORF in need of further study, ranging from nt 599 to nt 871 also in the second reading frame.[12]

Protein

General Properties

The C7orf50 Isoform a's 194aa protein sequence from NCBI [9] is as follows: 

>NP_001127867.1 uncharacterized protein C7orf50 isoform a [Homo sapiens]
MAKQKRKVPEVTEKKNKKLKKASAEGPLLGPEAAPSGEGAGSKGEAVLRPGLDAEPELSPEEQRVLERKL 70
KKERKKEERQRLREAGLVAQHPPARRSGAELALDYLCRWAQKHKNWRFQKTRQTWLLLHMYDSDKVPDEH 140
FSTLLAYLEGLQGRARELTVQKAEALMRELDEEGSDPPLPGRAQRIRQVLQLLS                 194

The underlined region within the sequence is indicative of a domain known as DUF2373 ("domain of unknown function 2373"), found in isoforms a, b, and c.

C7orf50 has a predicted molecular weight (Mw) of 22 kDa, making C7orf50 smaller than the average protein (52 kDa).[13] The isoelectric point (theoretical pI) for this isoform is 9.7, meaning that C7orf50 is slightly basic.[14][15] As for charge runs and patterns within isoform a, there is a significant mixed charge (*) run (-++0++-+++--+) from aa67 to aa79 and an acidic (-) run from aa171 – aa173. It is likely that this mixed charge run encodes the protein-protein interaction (PPI) site of C7orf50.[16][17]

Domains and Motifs

DUF2373 is a domain of unknown function found in the C7orf50 protein. This is a highly conserved c-terminal region found from fungi to humans.[18] As for motifs, a bipartite nuclear localization signal (NLS) was predicted from aa6 to aa21, meaning that C7orf50 is likely localized in the nucleus.[19] Interestingly, a nuclear export signal (NES) is also found within the C7orf50 protein at the following amino acids: 150, and 153 - 155, suggesting that C7orf50 has function both inside and outside the nucleus.[20][21]

Schematic Model of C7orf50 Protein. Green region is indicative of nuclear localization signal (NLS), blue of the mixed charge run, and orange of the DUF2373. Marked sites are indicative of post-translational modifications. Image made with Prosite MyDomains tool.

Structure

Secondary Structure

The majority of C7orf50 (isoform a) secondary structure is made up of alpha helices, with the remainder being small portions of random coils, beta turns, or extended strands.[22][23]

Tertiary Structure

The tertiary structure of C7orf50 consists primarily of alpha helices as determined I-TASSER.[5][24][25]

Quaternary Structure

The interaction network (quaternary structure) involving the C7orf50 protein has significantly more (p < 1.0e-16) interactions than a randomly selected set of proteins. This indicates that these proteins are partially connected biologically as a group; therefore, they intrinsically depend on each other within their biological pathway.[26] This means that although the function of C7orf50 is uncharacterized, it is most likely to be associated with the same processes and functions as the proteins within its network.

Functional Enrichments within the C7orf50 Network
Biological Processes rRNA processing maturation of 5.8S, LSU, and SSU rRNA
Molecular Functions catalytic activity, acting on RNA ATP-dependent RNA helicase activity
Cellular Components nucleolus preribosomes
Reactome Pathways major pathway of rRNA processing in the nucleolus and cytosol rRNA modification in the nucleus and cytosol
Protein Domains and Motifs helicase conserved C-terminal domain DEAD/DEAH box helicase

The closest predicted functional partners of C7orf50 are the following proteins: DDX24, DDX52, PES1, EBNA1BP2, RSLD1, NOP14, FTSJ3, KRR1, LYAR, and PWP1. These proteins are predicted to co-express rather than bind directly C7orf50 and each other.

STRING quaternary analysis of C7orf50. Shows protein-protein interactions (direct and indirect) associated with C7orf50. Network nodes (circles) represent proteins. Edges (lines) represent protein-protein associations.

Regulation

Gene Regulation

Promoter

C7orf50 has 6 predicted promoter regions. The promoter with the greatest number of transcripts and CAGE tags overall is promoter set 6 (GXP_6755694) on ElDorado by Genomatix. This promoter region is on the minus (-) strand and has a start position of 1,137,965 and an end position of 1,139,325, making this promoter 1,361bp long. It has 16 coding transcripts and the transcript with the greatest identity to C7orf50 transcript 4 is transcript GXT_27788039 with 98746 CAGE tags.[27]

Promoter ID Start Position End Position Length # of Coding Transcripts Greatest # of CAGE Tags in Transcripts
GXP_9000582 1013063 1013163 1101bp 0 N/A
GXP_6755691 1028239 1030070 1832bp 4 169233
GXP_6053282 1055206 1056306 1101bp 1 449
GXP_3207505 1127288 1128388 1101bp 1 545
GXP_9000584 1130541 1131641 1101bp 0 N/A
GXP_6755694 1137965 1139325 1361bp 16 100,070

The CpG island associated with this promoter has 75 CpGs (22% of island), and is 676bp long. The C count plus G count is 471, the percentage C or G is 70% within this island, and the ratio of observed to expected CpG is 0.91.[28][29]

C7orf50 with ElDorado suggested promoters with exons labeled. Gene is on the minus (-) strand, thus promoter (GXP_6755694) transcripts runs 5’ to 3’ on the bottom strand (R to L).

Transcription Factor Binding Sites

As determined by MatInspector at Genomatix, the following transcription factor (TFs) families are most highly predicted to bind to C7orf50 in the promoter region.[27]

Transcription Factor Detailed Family Information
NR2F Nuclear receptor subfamily 2 factors
PERO Peroxisome proliferator-activated receptor
HOMF Homeodomain transcription factors
PRDM PR (PRDI-BF1-RIZ1 homologous) domain transcription factor
VTBP Vertebrate TATA binding protein factor
HZIP Homeodomain-leucine zipper transcription factors
ZTRE Zinc transcriptional regulatory element
XBBF X-box binding factors
SP1F GC-Box factors SP1/GC
CAAT CCAAT binding factors
ZF57 KRAB domain zinc finger protein 57
CTCF CTCF and BORIS gene family, transcriptional regulators with highly conserved zinc finger domains
MYOD Myoblast determining factors
KLFS Krueppel like transcription factors

Expression Pattern

C7orf50 shows ubiquitous expression in the kidneys, brain, fat, prostrate, spleen and 22 other tissues and low tissue and immune cell specificity .[1][2] This expression is very high, 4 times above the average gene; therefore, there is a higher abundance of C7orf50 mRNA than the average gene within a cell.[30] There does not appear to be a definitive cell type in which this gene is not expressed.[31]

Transcription Regulation

Splice Enhancers

The mRNA of C7orf50 is predicted to have exonic splicing enhancers, in which SR proteins can bind, at bp positions 45 (SRSF1 (IgM-BRCA1)), 246 (SRSF6), 703 (SRSF5), 1301 (SRSF1), and 1308 (SRSF2) [32][33]

Stem Loop Prediction

Both the 5' and 3' UTRs of the mRNA of C7orf50 are predicted to fold into structures such as bulge loops, internal loops, multibranch loops, hairpin loops, and double helices. The 5'UTR has a predicted free energy of -416 kcal/mol with an ensemble diversity of 238. The 3' UTR has a predicted free energy of -279 kcal/mol with an ensemble diversity of 121.[34]

miRNA Targeting

There are many poorly conserved miRNA binding sites predicted within the 3’UTR of C7orf50 mRNA. The notable miRNA families that are predicted to bind to C7orf50 mRNA and regulate/repress transcription are the following: miR-138-5p, miR-18-5p, miR-129-3p, miR-124-3p.1, miR-10-5p, and miR-338-3p.[35][36][37]

Protein Regulation

Subcellular Localization

The C7orf50 protein is predicted to localize intercellularly in both the nucleus and cytoplasm, but primarily within the nucleoplasm and nucleoli.[38][39][19][40]

Post-Translational Modification

The C7orf50 protein is predicted to be mucin-type GalNAc o-glycosylated at the following amino acid sites: 12, 23, 36, 42, 59, and 97.[41][42] Additionally, this protein is predicted to be SUMOylated at aa71 with the SUMO protein binding from aa189 through aa193.[43][44][45] C7orf50 is also predicted to be kinase-specific phosphorylated at the following amino acids: 12, 23, 36, 42, 59, 97, 124, 133, 159, and 175.[46][47][48][49][50] Interestingly, many of these sites overlap with the o-glycosylation sites. Of these phosphorylation sites, the majority are serines (53%) with the remainder being either tyrosines or threonines. The most associated kinases with these sites are the following kinase groups: AGC, CAMK, TKL, and STE. Finally, this protein is predicted to have 8 glycations of the ε amino groups of lysines at the following sites: aa3, 5, 14, 15, 17, 21, 76, and 120.[51][52]

Homology

Paralogs

No paralogs of C7orf50 have been detected in the human genome; however, there is slight evidence (58% similarity) of a paralogous DUF2373 domain in the protein of KIDINS220.[53]

Orthologs

Below is a table of a variety of orthologs of the human C7orf50 gene.[54][3] The table includes closely, moderately, and distantly related orthologs. C7orf50 is highly evolutionary conserved from mammals to fungi. When these ortholog sequences are compared, the most conserved portions are those of DUF2373, highlighting this domain's importance in the functioning of C7orf50. C7orf50 has evolved moderately and evenly over time with a divergence rate greater than Hemoglobin but less than Cytochrome C.

Selected Orthologs of C7orf50
Genus and Species Common Name Taxon Class Date of Divergence (MYA) Accession # Length (AA) % identity w/ human
Homo sapiens Human Mammalia N/A NM_001318252.2 194aa 100%
Tupaia chinensis Chinese Tree Shrew Mammalia 82 XP_006167949.1 194aa 76%
Dasypus novemcinctus Nine-banded Armadillo Mammalia 105 XP_004483895.1 198aa 70%
Miniopterus natalens Natal Long-fingered Bat Mammalia 96 XP_016068464.1 199aa 69%
Protobothrops mucrosquamatus Brown-spotted Pit Viper Reptilia 312 XP_015673296.1 196aa 64%
Balearica regulorum gibbericeps Grey-crowned Crane Aves 312 XP_010302837.1 194aa 61%
Falco peregrinus Peregrine Falcon Aves 312 XP_027635198.1 193aa 59%
Xenopus laevis African Clawed Frog Amphibia 352 XP_018094637.1 198aa 50%
Electrophorus electricus Electric Eel Actinopterygii 435 XP_026880604.1 195aa 53%
Rhincodon typus Whale Shark Chondrichthyes 465 XP_020372968.1 195aa 52%
Ciona intestinalis Sea Vase Ascidiacea 676 XP_026696561.1 282aa 37%
Octopus bimaculoides California Two-spot Octopus Cephalopoda 797 XP_014772175.1 221aa 40%
Priapulus caudatus Priapulus Priapulida 797 XP_014663190.1 333aa 39%
Bombus terrestris Buff-tailed Bumblebee Insecta 797 XP_012171653.1 260aa 32%
Actinia tenebrosa Australian Red Waratah Sea Anemone Anthozoa 824 XP_031575029.1 330aa 43%
Trichoplax adhaerens Trichoplax Trichoplacidae 948 XP_002110193.1 137aa 44%
Spizellomyces punctatus Branching Chytrid Fungi Fungi 1105 XP_016610491.1 412aa 29%
Eremothecium cymbalariae Fungi Fungi 1105 XP_003644395.1 266aa 25%
Quercus suber Cork Oak Tree Plantae 1496 XP_023896156.1 508aa 30%
Plasmopara halstedii Downy Mildew of Sunflower Oomycetes 1768 XP_024580369.1 179aa 26%
Rate of C7orf50 divergence compared to divergence rates of Hemoglobin and Cytochrome C.

Function

The consensus prediction of C7orf50 function (GO terms), as determined by I-TASSER,[55][24][25] predicts the molecular function to be protein binding, the biological process to be protein import (specifically into the nucleus), and the associated cellular component to be a pore complex (specifically of the nuclear envelope). It can be predicted that the function of C7orf50 is one in which C7orf50 imports ribosomal proteins into the nucleus in order to be made into ribosomes, but further research is needed to solidify this function.

Interacting Proteins

Proteins Predicted to Interact with C7orf50 [56][57]
Name of Protein Name of Gene Function UniProt Accession #
THAP1 domain-containing protein 1 THAP1 DNA-binding transcription regulator that regulates endothelial cell proliferation and G1/S cell-cycle progression.[58] Q9NVV9
Protein Tax-2 tax Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways.[59] P03410
Major Prion Protein PRNP Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis.[60] P04156
Aldehyde dehydrogenase X, mitochondrial ALDH1B1 Pay a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation.[61] P30837
Cell growth-regulating nucleolar protein LYAR Plays a role in the maintenance of the appropriate processing of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent processing to produce 18S and 28S rRNAs.[62][63] Q9NX58
Coiled-coil domain-containing protein 85B CCDC85B Functions as a transcriptional repressor.[64][65] Q15834
Nucleolar protein 56 NOP56 Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs.[66] O00567
rRNA 2'-O-methyltransferase fibrillarin FBL Has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA.[67][68][69] P22087
40S ribosomal protein S6 RPS6 May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.[70] P62753

Clinical Significance

C7orf50 has been noted in a variety of genome-wide association studies (GWAS) and has been shown to be associated with type 2 diabetes among sub-Saharan Africans,[71] daytime sleepiness in African-Americans,[72] prenatal exposure to particulate matter,[73] heritable DNA methylation marks associated with breast cancer,[74] DNA methylation in relation to plasma carotenoids and lipid profile,[75] and has significant interactions with prion proteins.[76]

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 "C7orf50 chromosome 7 open reading frame 50 [Homo sapiens (human) - Gene - NCBI"]. https://www.ncbi.nlm.nih.gov/gene?cmd=retrieve&list_uids=84310. 
  2. ↑ 2.0 2.1 "C7orf50 protein expression summary - The Human Protein Atlas". https://www.proteinatlas.org/ENSG00000146540-C7orf50. 
  3. ↑ 3.0 3.1 "C7orf50 orthologs" (in en). https://www.ncbi.nlm.nih.gov/gene/84310/ortholog/. 
  4. ↑ Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter (2002). "The Transport of Molecules between the Nucleus and the Cytosol". Molecular Biology of the Cell. (4th ed.). https://www.ncbi.nlm.nih.gov/books/NBK26932/. 
  5. ↑ 5.0 5.1 "I-TASSER server for protein structure and function prediction". https://zhanglab.ccmb.med.umich.edu/I-TASSER/. 
  6. ↑ "Protein coding genes as hosts for noncoding RNA expression". Seminars in Cell & Developmental Biology 75: 3–12. March 2018. doi:10.1016/j.semcdb.2017.08.016. PMID 28811264. 
  7. ↑ HUGO Gene Nomenclature Committee. "MicroRNA protein coding host genes". https://www.genenames.org/data/genegroup/#!/group/1691. 
  8. ↑ 8.0 8.1 (in en-US) Homo sapiens chromosome 7 open reading frame 50 (C7orf50), transcript variant 4, mRNA. 2020-04-25. http://www.ncbi.nlm.nih.gov/nuccore/NM_001318252.2. 
  9. ↑ 9.0 9.1 "uncharacterized protein C7orf50 isoform a [Homo sapiens - Protein - NCBI"]. https://www.ncbi.nlm.nih.gov/protein/970919379. 
  10. ↑ (in en-US) PREDICTED: Homo sapiens chromosome 7 open reading frame 50 (C7orf50), transcript variant X6, mRNA. 2020-03-02. http://www.ncbi.nlm.nih.gov/nuccore/XM_011515584.2. 
  11. ↑ "uncharacterized protein C7orf50 isoform X3 [Homo sapiens - Protein - NCBI"]. https://www.ncbi.nlm.nih.gov/protein/767945960. 
  12. ↑ "ORF Finder". https://www.bioinformatics.org/sms2/orf_find.html. 
  13. ↑ "Average protein size - Various - BNID 113349" (in en). https://bionumbers.hms.harvard.edu/bionumber.aspx?s=n&v=0&id=113349. 
  14. ↑ Kozlowski, Lukasz P.. "Proteome-pI - Proteome Isoelectric Point Database statistics" (in en). http://isoelectricpointdb.org/statistics.html. 
  15. ↑ "ExPASy - Compute pI/Mw tool". https://web.expasy.org/compute_pi/. 
  16. ↑ "SAPS < Sequence Statistics < EMBL-EBI". https://www.ebi.ac.uk/Tools/seqstats/saps/. 
  17. ↑ "Clusters of charged residues in protein three-dimensional structures". Proceedings of the National Academy of Sciences of the United States of America 93 (16): 8350–5. August 1996. doi:10.1073/pnas.93.16.8350. PMID 8710874. Bibcode: 1996PNAS...93.8350Z. 
  18. ↑ "Pfam: Family: DUF2373 (PF10180)". http://pfam.xfam.org/family/PF10180. 
  19. ↑ 19.0 19.1 "Motif Scan" (in en). https://myhits.isb-sib.ch/cgi-bin/motif_scan. 
  20. ↑ "NetNES 1.1 Server". http://www.cbs.dtu.dk/services/NetNES/. 
  21. ↑ "Analysis and prediction of leucine-rich nuclear export signals". Protein Engineering, Design & Selection 17 (6): 527–36. June 2004. doi:10.1093/protein/gzh062. PMID 15314210. 
  22. ↑ "NPS@ : CONSENSUS secondary structure prediction". https://npsa-prabi.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_seccons.html. 
  23. ↑ "CFSSP: Chou & Fasman Secondary Structure Prediction Server". https://www.biogem.org/tool/chou-fasman/index.php. 
  24. ↑ 24.0 24.1 "COFACTOR: improved protein function prediction by combining structure, sequence and protein-protein interaction information". Nucleic Acids Research 45 (W1): W291–W299. July 2017. doi:10.1093/nar/gkx366. PMID 28472402. 
  25. ↑ 25.0 25.1 "I-TASSER server: new development for protein structure and function predictions". Nucleic Acids Research 43 (W1): W174-81. July 2015. doi:10.1093/nar/gkv342. PMID 25883148. 
  26. ↑ "C7orf50 protein (human) - STRING interaction network". https://string-db.org/cgi/network.pl?taskId=hbSXbSZovONr. 
  27. ↑ 27.0 27.1 "Genomatix - NGS Data Analysis & Personalized Medicine". https://www.genomatix.de/?s=435a27c29323011e3aef6e3522bf640d. 
  28. ↑ "CpG Island Info". https://genome.ucsc.edu/cgi-bin/hgc?hgsid=831382483_oz24NTGzgAG5H4k6gGBN0YDsSK42&c=chr7&l=1064094&r=1205336&o=1137943&t=1138619&g=cpgIslandExt&i=CpG:+75. 
  29. ↑ "CpG islands in vertebrate genomes". Journal of Molecular Biology 196 (2): 261–82. July 1987. doi:10.1016/0022-2836(87)90689-9. PMID 3656447. 
  30. ↑ "AceView: Gene:C7orf50, a comprehensive annotation of human, mouse and worm genes with mRNAs or ESTsAceView.". https://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=C7orf50&submit=Go. 
  31. ↑ "2895856 - GEO Profiles - NCBI". https://www.ncbi.nlm.nih.gov/geoprofiles/2895856. 
  32. ↑ "An increased specificity score matrix for the prediction of SF2/ASF-specific exonic splicing enhancers". Human Molecular Genetics 15 (16): 2490–508. August 2006. doi:10.1093/hmg/ddl171. PMID 16825284. 
  33. ↑ "ESEfinder: A web resource to identify exonic splicing enhancers". Nucleic Acids Research 31 (13): 3568–71. July 2003. doi:10.1093/nar/gkg616. PMID 12824367. 
  34. ↑ "RNAfold web server". http://rna.tbi.univie.ac.at//cgi-bin/RNAWebSuite/RNAfold.cgi. 
  35. ↑ "TargetScanHuman 7.2". http://www.targetscan.org/vert_72/. 
  36. ↑ "miRNA Targeting: Growing beyond the Seed" (in English). Trends in Genetics 35 (3): 215–222. March 2019. doi:10.1016/j.tig.2018.12.005. PMID 30638669. 
  37. ↑ "Most mammalian mRNAs are conserved targets of microRNAs". Genome Research 19 (1): 92–105. January 2009. doi:10.1101/gr.082701.108. PMID 18955434. 
  38. ↑ "C7orf50 protein expression summary - The Human Protein Atlas". https://www.proteinatlas.org/ENSG00000146540-C7orf50. 
  39. ↑ "PSORT II Prediction". https://psort.hgc.jp/form2.html. 
  40. ↑ "Better prediction of protein cellular localization sites with the k nearest neighbors classifier". Proceedings. International Conference on Intelligent Systems for Molecular Biology 5: 147–52. 1997. PMID 9322029. 
  41. ↑ "NetOGlyc 4.0 Server" (in en). http://www.cbs.dtu.dk/services/NetOGlyc/. 
  42. ↑ "Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology". The EMBO Journal 32 (10): 1478–88. May 2013. doi:10.1038/emboj.2013.79. PMID 23584533. 
  43. ↑ "GPS-SUMO: a tool for the prediction of sumoylation sites and SUMO-interaction motifs". Nucleic Acids Research 42 (Web Server issue): W325-30. July 2014. doi:10.1093/nar/gku383. PMID 24880689. 
  44. ↑ "Systematic study of protein sumoylation: Development of a site-specific predictor of SUMOsp 2.0". Proteomics 9 (12): 3409–3412. June 2009. doi:10.1002/pmic.200800646. PMID 29658196. 
  45. ↑ "GPS-SUMO: Prediction of SUMOylation Sites & SUMO-interaction Motifs". http://sumosp.biocuckoo.org/. 
  46. ↑ "GPS 5.0 - Kinase-specific Phosphorylation Site Prediction". http://gps.biocuckoo.cn/online.php. 
  47. ↑ "NetPhos 3.1 Server". http://www.cbs.dtu.dk/services/NetPhos/. 
  48. ↑ "Sequence and structure-based prediction of eukaryotic protein phosphorylation sites". Journal of Molecular Biology 294 (5): 1351–62. December 1999. doi:10.1006/jmbi.1999.3310. PMID 10600390. 
  49. ↑ "Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence". Proteomics 4 (6): 1633–49. June 2004. doi:10.1002/pmic.200300771. PMID 15174133. 
  50. ↑ "GPS 5.0: An Update on the Prediction of Kinase-specific Phosphorylation Sites in Proteins". Genomics, Proteomics & Bioinformatics 18 (1): 72–80. March 2020. doi:10.1016/j.gpb.2020.01.001. PMID 32200042. 
  51. ↑ "NetGlycate 1.0 Server" (in en). http://www.cbs.dtu.dk/services/NetGlycate/. 
  52. ↑ "Analysis and prediction of mammalian protein glycation". Glycobiology 16 (9): 844–53. September 2006. doi:10.1093/glycob/cwl009. PMID 16762979. 
  53. ↑ "Protein BLAST: search protein databases using a protein query". https://blast.ncbi.nlm.nih.gov/Blast.cgi?PAGE=Proteins. 
  54. ↑ "BLAST: Basic Local Alignment Search Tool". https://blast.ncbi.nlm.nih.gov/Blast.cgi. 
  55. ↑ "I-TASSER results". https://zhanglab.ccmb.med.umich.edu/I-TASSER/output/S533933/. 
  56. ↑ "IntAct Portal". https://www.ebi.ac.uk/intact/. 
  57. ↑ "CCSB Interactome Database". http://interactome.dfci.harvard.edu/index.php?page=home. 
  58. ↑ "THAP1 - THAP domain-containing protein 1 - Homo sapiens (Human) - THAP1 gene & protein". https://www.uniprot.org/uniprot/Q9NVV9. 
  59. ↑ "tax - Protein Tax-2 - Human T-cell leukemia virus 2 (HTLV-2) - tax gene & protein". https://www.uniprot.org/uniprot/P03410. 
  60. ↑ "PRNP - Major prion protein precursor - Homo sapiens (Human) - PRNP gene & protein". https://www.uniprot.org/uniprot/P04156. 
  61. ↑ "ALDH1B1 - Aldehyde dehydrogenase X, mitochondrial precursor - Homo sapiens (Human) - ALDH1B1 gene & protein". https://www.uniprot.org/uniprot/P30837. 
  62. ↑ "LYAR - Cell growth-regulating nucleolar protein - Homo sapiens (Human) - LYAR gene & protein". https://www.uniprot.org/uniprot/Q9NX58. 
  63. ↑ "Human cell growth regulator Ly-1 antibody reactive homologue accelerates processing of preribosomal RNA". Genes to Cells 19 (4): 273–86. April 2014. doi:10.1111/gtc.12129. PMID 24495227. 
  64. ↑ "DIPA, which can localize to the centrosome, associates with p78/MCRS1/MSP58 and acts as a repressor of gene transcription". Experimental and Molecular Pathology 81 (3): 184–90. December 2006. doi:10.1016/j.yexmp.2006.07.008. PMID 17014843. 
  65. ↑ "CCDC85B - Coiled-coil domain-containing protein 85B - Homo sapiens (Human) - CCDC85B gene & protein". https://www.uniprot.org/uniprot/Q15834. 
  66. ↑ "NOP56 - Nucleolar protein 56 - Homo sapiens (Human) - NOP56 gene & protein". https://www.uniprot.org/uniprot/O00567. 
  67. ↑ "FBL - rRNA 2'-O-methyltransferase fibrillarin - Homo sapiens (Human) - FBL gene & protein". https://www.uniprot.org/uniprot/P22087. 
  68. ↑ "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification". Nature 505 (7484): 564–8. January 2014. doi:10.1038/nature12819. PMID 24352239. Bibcode: 2014Natur.505..564T. 
  69. ↑ "SIRT7-Dependent Deacetylation of Fibrillarin Controls Histone H2A Methylation and rRNA Synthesis during the Cell Cycle". Cell Reports 25 (11): 2946–2954.e5. December 2018. doi:10.1016/j.celrep.2018.11.051. PMID 30540930. 
  70. ↑ "RPS6 - 40S ribosomal protein S6 - Homo sapiens (Human) - RPS6 gene & protein". https://www.uniprot.org/uniprot/P62753. 
  71. ↑ "Epigenome-wide association study in whole blood on type 2 diabetes among sub-Saharan African individuals: findings from the RODAM study". International Journal of Epidemiology 48 (1): 58–70. February 2019. doi:10.1093/ije/dyy171. PMID 30107520. 
  72. ↑ "Epigenome-wide association analysis of daytime sleepiness in the Multi-Ethnic Study of Atherosclerosis reveals African-American-specific associations". Sleep 42 (8): zsz101. August 2019. doi:10.1093/sleep/zsz101. PMID 31139831. 
  73. ↑ "Prenatal Particulate Air Pollution and DNA Methylation in Newborns: An Epigenome-Wide Meta-Analysis". Environmental Health Perspectives 127 (5): 57012. May 2019. doi:10.1289/EHP4522. PMID 31148503. 
  74. ↑ "Heritable DNA methylation marks associated with susceptibility to breast cancer". Nature Communications 9 (1): 867. February 2018. doi:10.1038/s41467-018-03058-6. PMID 29491469. Bibcode: 2018NatCo...9..867J. 
  75. ↑ "Network Analysis of the Potential Role of DNA Methylation in the Relationship between Plasma Carotenoids and Lipid Profile". Nutrients 11 (6): 1265. June 2019. doi:10.3390/nu11061265. PMID 31167428. 
  76. ↑ "Protein microarray analysis identifies human cellular prion protein interactors". Neuropathology and Applied Neurobiology 35 (1): 16–35. February 2009. doi:10.1111/j.1365-2990.2008.00947.x. PMID 18482256. 



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