Cholesin

CHLSN
Identifiers
AliasesCHLSN, YCR016W, chromosome 7 open reading frame 50, C7orf50, Cholesin, Uncharacterized Protein C7orf50
External IDsMGI: 1920462; GeneCards: CHLSN
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_028469

RefSeq (protein)

NP_082745

Location (UCSC)Chr 7: 1 – 1.14 MbChr 5: 139.35 – 139.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cholesin is a protein which in humans is encoded by the gene CHLSN.[5] It functions as a hormone that regulates the synthesis of cholesterol, and the way it does it is distinctive in that it can be involved in either increasing or decreasing synthesis, rather than a simple one-way effect.[5] This function appears to be occur through binding to its receptor GPR146.[5]

It is most highly produced in the upper digestive system and respiratory system, in addition to the (hormone producing) endocrine system.[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

Location

CHLSN is located on the short arm of chromosome 7 (7p22.3), and spans 160,361 bps on the minus (-) strand and contains a total of 13 exons.[8]

Gene Neighborhood

Genes within the neighborhood of CHLSN are the following: LOC105375120, GPR146, LOC114004405, LOC107986755, ZFAND2A, LOC102723758, LOC106799841, COX19, ADAP1, CYP2W1, MIR339, GPER1, and LOC101927021.[8]

Other animals

Cholesin is conserved in chimpanzees, Rhesus monkeys, dogs, cows, mice, rats, and chickens, along with 307 other organisms from mammals to fungi.[9]

mRNA

Alternative Splicing

CHLSN has a total of 7 experimentally curated mRNA transcripts.[8] 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.[10] Of these transcripts, four of them encode for the same 194aa protein (isoform a),[11] 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.

CHLSN 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.[8] The most complete and supported of these transcripts (transcript variant X6) is 1896bp, producing a 225aa-long protein.[12] In total, there are 6 different isoforms predicted for CHLSN. Of these transcripts, 5 of them encode for the same isoform (X3).[13] The remaining transcripts encode isoforms X2, X4, X5, X6, and X7 as represented below.

CHLSN 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 CHLSN mRNA transcript variant 4, the 5' UTR of CHLSN 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.[10]

Protein

General Properties

The CHLSN Isoform a's 194aa protein sequence from NCBI [11] is as follows:

>NP_001127867.1 cholesin 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.

Cholesin has a predicted molecular weight (Mw) of 22 kDa, making cholesin smaller than the average protein (52 kDa).[14] The isoelectric point (theoretical pI) for this isoform is 9.7, meaning that cholesin is slightly basic.[15][16] 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 cholesin.[17][18]

Characterization of the protein has shown binding to GPR146. Based on a proposed role in regulation of serum cholesterol levels in response to dietary cholesterol intake, the protein has been called cholesin.[19]

Domains and Motifs

DUF2373 is a domain of unknown function found in the cholesin. This is a highly conserved c-terminal region found from fungi to humans.[20] As for motifs, a bipartite nuclear localization signal (NLS) was predicted from aa6 to aa21, meaning that cholesin is likely localized in the nucleus.[21] Interestingly, a nuclear export signal (NES) is also found within cholesin at the following amino acids: 150, and 153 - 155, suggesting that cholesin has function both inside and outside the nucleus.[22][23]

Schematic Model of cholesin. 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 cholesin (isoform a) secondary structure is made up of alpha helices, with the remainder being small portions of random coils, beta turns, or extended strands.[24][25]

Tertiary Structure

The tertiary structure of cholesin consists primarily of alpha helices as determined I-TASSER.[26][27][28]

Quaternary Structure

The interaction network (quaternary structure) involving the cholesin has significantly more (p < 1.0e-16) interactions than a randomly selected set of proteins.[29]

Functional Enrichments within the CHLSN 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 cholesin 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 to cholesin 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

CHLSN 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.[30]

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.[31][32]

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 CHLSN in the promoter region.[30]

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

CHLSN shows ubiquitous expression in the kidneys, brain, fat, prostate, spleen and 22 other tissues and low tissue and immune cell specificity .[8][33] This expression is very high, 4 times above the average gene; therefore, there is a higher abundance of CHLSN mRNA than the average gene within a cell.[34] There does not appear to be a definitive cell type in which this gene is not expressed.[35]

Transcription Regulation

Splice Enhancers

The mRNA of CHLSN 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) [36][37]

miRNA Targeting

There are many poorly conserved miRNA binding sites predicted within the 3'UTR of CHLSN mRNA. The notable miRNA families that are predicted to bind to CHLSN 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.[38][39][40]

Protein Regulation

Subcellular Localization

Cholesin is predicted to localize intercellularly in both the nucleus and cytoplasm, but primarily within the nucleoplasm and nucleoli.[41][42][21][43]

Post-Translational Modification

Cholesin is predicted to be mucin-type GalNAc o-glycosylated at the following amino acid sites: 12, 23, 36, 42, 59, and 97.[44][45] Additionally, this protein is predicted to be SUMOylated at aa71 with the SUMO protein binding from aa189 through aa193.[46][47][48] Cholesin is also predicted to be kinase-specific phosphorylated at the following amino acids: 12, 23, 36, 42, 59, 97, 124, 133, 159, and 175.[49][50][51][52][53] 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.[54][55]

Homology

Paralogs

No paralogs of cholesin have been detected in the human genome; however, there is slight evidence (58% similarity) of a paralogous DUF2373 domain in the protein of KIDINS220.[56]

Orthologs

Below is a table of a variety of orthologs of the human CHLSN.[57][9] The table includes closely, moderately, and distantly related orthologs. CHLSN is highly evolutionary conserved from mammals to fungi. When these ortholog sequences are compared, the most conserved portions are those of DUF2373. CHLSN has evolved moderately and evenly over time with a divergence rate greater than Hemoglobin but less than Cytochrome C.

Selected Orthologs of CHLSN
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 CHLSN divergence compared to divergence rates of Hemoglobin and Cytochrome C.

Interacting Proteins

Proteins Predicted to Interact with cholesin [58][59]
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.[60] 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.[61] 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.[62] 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.[63] 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.[64][65] Q9NX58
Coiled-coil domain-containing protein 85B CCDC85B Functions as a transcriptional repressor.[66][67] 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.[68] 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.[69][70][71] 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.[72] P62753

Clinical Significance

CHLSN 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,[73] daytime sleepiness in African-Americans,[74] prenatal exposure to particulate matter,[75] heritable DNA methylation marks associated with breast cancer,[76] DNA methylation in relation to plasma carotenoids and lipid profile,[77] and has significant interactions with prion proteins.[78]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000146540Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000053553Ensembl, 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. ^ a b c d "CHLSN gene Cholesin". genecards.org. LifeMap Sciences Inc. Retrieved 2026-07-27.
  6. ^ Boivin V, Deschamps-Francoeur G, Scott MS (March 2018). "Protein coding genes as hosts for noncoding RNA expression". Seminars in Cell & Developmental Biology. 75: 3–12. doi:10.1016/j.semcdb.2017.08.016. PMID 28811264.
  7. ^ HUGO Gene Nomenclature Committee. "MicroRNA protein coding host genes". GeneNames. Archived from the original on 2018-11-21. Retrieved 2020-04-29.
  8. ^ a b c d e "C7orf50 chromosome 7 open reading frame 50 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2020-04-29.
  9. ^ a b "C7orf50 orthologs". NCBI. Retrieved 2020-05-02.
  10. ^ a b "Homo sapiens chromosome 7 open reading frame 50 (C7orf50), transcript variant 4, mRNA". 2020-04-25.
  11. ^ a b "uncharacterized protein C7orf50 isoform a [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2020-04-29.
  12. ^ "PREDICTED: Homo sapiens chromosome 7 open reading frame 50 (C7orf50), transcript variant X6, mRNA". 2020-03-02.
  13. ^ "uncharacterized protein C7orf50 isoform X3 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2020-04-29.
  14. ^ "Average protein size - Various - BNID 113349". bionumbers.hms.harvard.edu. Retrieved 2020-04-29.
  15. ^ Kozlowski LP. "Proteome-pI - Proteome Isoelectric Point Database statistics". isoelectricpointdb.org. Retrieved 2020-04-29.
  16. ^ "ExPASy - Compute pI/Mw tool". web.expasy.org. Retrieved 2020-04-29.
  17. ^ "SAPS < Sequence Statistics < EMBL-EBI". www.ebi.ac.uk. Retrieved 2020-04-29.
  18. ^ Zhu ZY, Karlin S (August 1996). "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. Bibcode:1996PNAS...93.8350Z. doi:10.1073/pnas.93.16.8350. PMC 38674. PMID 8710874.
  19. ^ Hu X, Chen F, Jia L, Long A, Peng Y, Li X, et al. (2024). "A gut-derived hormone regulates cholesterol metabolism". Cell. 187 (7): 1685-1700.e18. doi:10.1016/j.cell.2024.02.024. PMID 38503280.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  20. ^ "Pfam: Family: DUF2373 (PF10180)". pfam.xfam.org. Archived from the original on 2015-07-02. Retrieved 2020-04-29.
  21. ^ a b "Motif Scan". myhits.isb-sib.ch. Archived from the original on 2019-04-02. Retrieved 2020-04-29.
  22. ^ "NetNES 1.1 Server". www.cbs.dtu.dk. Retrieved 2020-05-02.
  23. ^ la Cour T, Kiemer L, Mølgaard A, Gupta R, Skriver K, Brunak S (June 2004). "Analysis and prediction of leucine-rich nuclear export signals". Protein Engineering, Design & Selection. 17 (6): 527–36. doi:10.1093/protein/gzh062. PMID 15314210.
  24. ^ "NPS@: CONSENSUS secondary structure prediction". npsa-prabi.ibcp.fr. Retrieved 2020-04-29.
  25. ^ "CFSSP: Chou & Fasman Secondary Structure Prediction Server". www.biogem.org. Retrieved 2020-04-29.
  26. ^ "I-TASSER server for protein structure and function prediction". zhanglab.ccmb.med.umich.edu. Retrieved 2020-04-29.
  27. ^ Zhang C, Freddolino PL, Zhang Y (July 2017). "COFACTOR: improved protein function prediction by combining structure, sequence and protein-protein interaction information". Nucleic Acids Research. 45 (W1): W291–W299. doi:10.1093/nar/gkx366. PMC 5793808. PMID 28472402.
  28. ^ Yang J, Zhang Y (July 2015). "I-TASSER server: new development for protein structure and function predictions". Nucleic Acids Research. 43 (W1): W174-81. doi:10.1093/nar/gkv342. PMC 4489253. PMID 25883148.
  29. ^ "C7orf50 protein (human) - STRING interaction network". string-db.org. Retrieved 2020-04-29.
  30. ^ a b "Genomatix - NGS Data Analysis & Personalized Medicine". www.genomatix.de. Retrieved 2020-04-29.[permanent dead link]
  31. ^ "CpG Island Info". genome.ucsc.edu. Retrieved 2020-05-03.
  32. ^ Gardiner-Garden M, Frommer M (July 1987). "CpG islands in vertebrate genomes". Journal of Molecular Biology. 196 (2): 261–82. doi:10.1016/0022-2836(87)90689-9. PMID 3656447.
  33. ^ "C7orf50 protein expression summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2020-04-29.
  34. ^ "AceView: Gene:C7orf50, a comprehensive annotation of human, mouse and worm genes with mRNAs or ESTsAceView". www.ncbi.nlm.nih.gov. Retrieved 2020-04-29.
  35. ^ "2895856 - GEO Profiles - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2020-04-29.
  36. ^ Smith PJ, Zhang C, Wang J, Chew SL, Zhang MQ, Krainer AR (August 2006). "An increased specificity score matrix for the prediction of SF2/ASF-specific exonic splicing enhancers". Human Molecular Genetics. 15 (16): 2490–508. doi:10.1093/hmg/ddl171. PMID 16825284.
  37. ^ Cartegni L, Wang J, Zhu Z, Zhang MQ, Krainer AR (July 2003). "ESEfinder: A web resource to identify exonic splicing enhancers". Nucleic Acids Research. 31 (13): 3568–71. doi:10.1093/nar/gkg616. PMC 169022. PMID 12824367.
  38. ^ "TargetScanHuman 7.2". www.targetscan.org. Retrieved 2020-04-30.
  39. ^ Chipman LB, Pasquinelli AE (March 2019). "miRNA Targeting: Growing beyond the Seed". Trends in Genetics. 35 (3): 215–222. doi:10.1016/j.tig.2018.12.005. PMC 7083087. PMID 30638669.
  40. ^ Friedman RC, Farh KK, Burge CB, Bartel DP (January 2009). "Most mammalian mRNAs are conserved targets of microRNAs". Genome Research. 19 (1): 92–105. doi:10.1101/gr.082701.108. PMC 2612969. PMID 18955434.
  41. ^ "C7orf50 protein expression summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2020-05-02.
  42. ^ "PSORT II Prediction". psort.hgc.jp. Retrieved 2020-05-02.
  43. ^ Horton P, Nakai K (1997). "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. PMID 9322029.
  44. ^ "NetOGlyc 4.0 Server". www.cbs.dtu.dk. Retrieved 2020-05-02.
  45. ^ Steentoft C, Vakhrushev SY, Joshi HJ, Kong Y, Vester-Christensen MB, Schjoldager KT, et al. (May 2013). "Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology". The EMBO Journal. 32 (10): 1478–88. doi:10.1038/emboj.2013.79. PMC 3655468. PMID 23584533.
  46. ^ Zhao Q, Xie Y, Zheng Y, Jiang S, Liu W, Mu W, et al. (July 2014). "GPS-SUMO: a tool for the prediction of sumoylation sites and SUMO-interaction motifs". Nucleic Acids Research. 42 (Web Server issue): W325-30. doi:10.1093/nar/gku383. PMC 4086084. PMID 24880689.
  47. ^ Ren J, Gao X, Jin C, Zhu M, Wang X, Shaw A, et al. (June 2009). "Systematic study of protein sumoylation: Development of a site-specific predictor of SUMOsp 2.0". Proteomics. 9 (12): 3409–3412. doi:10.1002/pmic.200800646. PMID 29658196. S2CID 4900031.
  48. ^ "GPS-SUMO: Prediction of SUMOylation Sites & SUMO-interaction Motifs". sumosp.biocuckoo.org. Archived from the original on 2013-05-10. Retrieved 2020-05-02.
  49. ^ "GPS 5.0 - Kinase-specific Phosphorylation Site Prediction". gps.biocuckoo.cn. Retrieved 2020-05-02.
  50. ^ "NetPhos 3.1 Server". www.cbs.dtu.dk. Retrieved 2020-05-02.
  51. ^ Blom N, Gammeltoft S, Brunak S (December 1999). "Sequence and structure-based prediction of eukaryotic protein phosphorylation sites". Journal of Molecular Biology. 294 (5): 1351–62. doi:10.1006/jmbi.1999.3310. PMID 10600390.
  52. ^ Blom N, Sicheritz-Pontén T, Gupta R, Gammeltoft S, Brunak S (June 2004). "Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence". Proteomics. 4 (6): 1633–49. doi:10.1002/pmic.200300771. PMID 15174133. S2CID 18810164.
  53. ^ Wang C, Xu H, Lin S, Deng W, Zhou J, Zhang Y, et al. (March 2020). "GPS 5.0: An Update on the Prediction of Kinase-specific Phosphorylation Sites in Proteins". Genomics, Proteomics & Bioinformatics. 18 (1): 72–80. doi:10.1016/j.gpb.2020.01.001. PMC 7393560. PMID 32200042.
  54. ^ "NetGlycate 1.0 Server". www.cbs.dtu.dk. Retrieved 2020-05-02.
  55. ^ Johansen MB, Kiemer L, Brunak S (September 2006). "Analysis and prediction of mammalian protein glycation". Glycobiology. 16 (9): 844–53. doi:10.1093/glycob/cwl009. PMID 16762979.
  56. ^ "Protein BLAST: search protein databases using a protein query". blast.ncbi.nlm.nih.gov. Retrieved 2020-05-02.
  57. ^ "BLAST: Basic Local Alignment Search Tool". blast.ncbi.nlm.nih.gov. Retrieved 2020-05-02.
  58. ^ "IntAct Portal". www.ebi.ac.uk. Retrieved 2020-05-03.
  59. ^ "CCSB Interactome Database". interactome.dfci.harvard.edu. Retrieved 2020-05-03.
  60. ^ "THAP1 - THAP domain-containing protein 1 - Homo sapiens (Human) - THAP1 gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  61. ^ "tax - Protein Tax-2 - Human T-cell leukemia virus 2 (HTLV-2) - tax gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  62. ^ "PRNP - Major prion protein precursor - Homo sapiens (Human) - PRNP gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  63. ^ "ALDH1B1 - Aldehyde dehydrogenase X, mitochondrial precursor - Homo sapiens (Human) - ALDH1B1 gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  64. ^ "LYAR - Cell growth-regulating nucleolar protein - Homo sapiens (Human) - LYAR gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  65. ^ Miyazawa N, Yoshikawa H, Magae S, Ishikawa H, Izumikawa K, Terukina G, et al. (April 2014). "Human cell growth regulator Ly-1 antibody reactive homologue accelerates processing of preribosomal RNA". Genes to Cells. 19 (4): 273–86. doi:10.1111/gtc.12129. PMID 24495227. S2CID 6143550.
  66. ^ Du X, Wang Q, Hirohashi Y, Greene MI (December 2006). "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. doi:10.1016/j.yexmp.2006.07.008. PMID 17014843.
  67. ^ "CCDC85B - Coiled-coil domain-containing protein 85B - Homo sapiens (Human) - CCDC85B gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  68. ^ "NOP56 - Nucleolar protein 56 - Homo sapiens (Human) - NOP56 gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  69. ^ "FBL - rRNA 2'-O-methyltransferase fibrillarin - Homo sapiens (Human) - FBL gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  70. ^ Tessarz P, Santos-Rosa H, Robson SC, Sylvestersen KB, Nelson CJ, Nielsen ML, et al. (January 2014). "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification". Nature. 505 (7484): 564–8. Bibcode:2014Natur.505..564T. doi:10.1038/nature12819. PMC 3901671. PMID 24352239.
  71. ^ Iyer-Bierhoff A, Krogh N, Tessarz P, Ruppert T, Nielsen H, Grummt I (December 2018). "SIRT7-Dependent Deacetylation of Fibrillarin Controls Histone H2A Methylation and rRNA Synthesis during the Cell Cycle". Cell Reports. 25 (11): 2946–2954.e5. doi:10.1016/j.celrep.2018.11.051. PMID 30540930.
  72. ^ "RPS6 - 40S ribosomal protein S6 - Homo sapiens (Human) - RPS6 gene & protein". www.uniprot.org. Retrieved 2020-05-03.
  73. ^ Meeks KA, Henneman P, Venema A, Addo J, Bahendeka S, Burr T, et al. (February 2019). "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. doi:10.1093/ije/dyy171. PMC 6380309. PMID 30107520.
  74. ^ Barfield R, Wang H, Liu Y, Brody JA, Swenson B, Li R, et al. (August 2019). "Epigenome-wide association analysis of daytime sleepiness in the Multi-Ethnic Study of Atherosclerosis reveals African-American-specific associations". Sleep. 42 (8) zsz101. doi:10.1093/sleep/zsz101. PMC 6685317. PMID 31139831.
  75. ^ Gruzieva O, Xu CJ, Yousefi P, Relton C, Merid SK, Breton CV, et al. (May 2019). "Prenatal Particulate Air Pollution and DNA Methylation in Newborns: An Epigenome-Wide Meta-Analysis". Environmental Health Perspectives. 127 (5): 57012. doi:10.1289/EHP4522. PMC 6792178. PMID 31148503.
  76. ^ Joo JE, Dowty JG, Milne RL, Wong EM, Dugué PA, English D, et al. (February 2018). "Heritable DNA methylation marks associated with susceptibility to breast cancer". Nature Communications. 9 (1): 867. Bibcode:2018NatCo...9..867J. doi:10.1038/s41467-018-03058-6. PMC 5830448. PMID 29491469.
  77. ^ Tremblay BL, Guénard F, Lamarche B, Pérusse L, Vohl MC (June 2019). "Network Analysis of the Potential Role of DNA Methylation in the Relationship between Plasma Carotenoids and Lipid Profile". Nutrients. 11 (6): 1265. doi:10.3390/nu11061265. PMC 6628241. PMID 31167428.
  78. ^ Satoh J, Obayashi S, Misawa T, Sumiyoshi K, Oosumi K, Tabunoki H (February 2009). "Protein microarray analysis identifies human cellular prion protein interactors". Neuropathology and Applied Neurobiology. 35 (1): 16–35. doi:10.1111/j.1365-2990.2008.00947.x. PMID 18482256. S2CID 32299311.

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