C1orf68

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Chromosome 1 open reading frame 68, or C1orf68, is a human gene which encodes for skin-specific protein 32. C1orf68 gene is expressed in the skin, [1] is a part of the epidermal differentiation complex, and potentially plays a role in epidermal cornification, and epidermal barrier function. [2] [3]

Contents

Gene

C1orf68 is mapped on the plus strand of chromosome 1 at 1q21.3, that spans 949 base pairs in the human genome. [4] [5] Other aliases include Late envelope protein 7 (LEP7), XP32, Skin-Specific Protein (Xp32). [4] This gene has only 1 exon, and no introns. It is a part of the epidermal differentiation complex (1q21).

Protein

Human C1orf68 conceptual translation of mRNA and protein sequence Human C1orf68 Conceptual Translation.png
Human C1orf68 conceptual translation of mRNA and protein sequence

Skin-specific protein 32 has only one isoform, and has a sequence length of 250 amino acids. [6] It has a molecular mass of 26 kDa, [7] [8] and a predicted pI value of 8.41. [8] It was noted that the amino acid sequence contained high levels of cysteine relative to other human protein sequences. [9]

Domains, repeats

Skin-specific protein 32 has one domain, PRK10264, which is a DNA translocase FtsK. [4] It also contains a cysteine rich region, which is shown to be conserved across most mammal orthologs, excluding Monotremes. [10]

The protein sequence also contains a repeat sequence, the three continuous repeat sequences are located from amino acid position Gln65 to Cys127. [11] The repeat sequences can be observed in the conceptual translation on the right. They are within the DNA translocase Ftsk domain and the cysteine rich region. The repeat sequences are conserved across mammal orthologs. The conservation of each individual amino acid can be observed in the LOGO below.

Diagram of human C1orf68 protein domains, which includes PRK10263 (DNA translocase Ftsk) and cysteine-rich region Human C1orf68 Protein Domains.png
Diagram of human C1orf68 protein domains, which includes PRK10263 (DNA translocase Ftsk) and cysteine-rich region
LOGO of repeat sequences in human C1orf68 conserved across select orthologs, Rhinopithecus roxellana (Golden snub-nosed monkey), Cavia porcellus (Guinea Pig), and Myotis brandtii (Brandt's bat) C1orf68 Repeat Sequence Conservation LOGO.png
LOGO of repeat sequences in human C1orf68 conserved across select orthologs, Rhinopithecus roxellana (Golden snub-nosed monkey), Cavia porcellus (Guinea Pig), and Myotis brandtii (Brandt's bat)

Gene level regulation

Promoter

One promoter was identified for C1orf68 using ElDorado Genomatics. [12] This promoter, GXP_1818199, spans 1,040 bases and overlaps C1orf68 by 40 bases. [12] Since C1orf68 does not contain a 5'-UTR, the promoter overlaps the start codon, which can be visualized in the diagram below.

Human C1orf68 (exon 1) with Promoter GXP_1818199 diagram. Start and stop codons represented as green and red arrows respectively. Human C1orf68 Promoter GXP 1818199 diagram.png
Human C1orf68 (exon 1) with Promoter GXP_1818199 diagram. Start and stop codons represented as green and red arrows respectively.

Expression pattern

C1orf68 is expressed in a select few tissues, specifically in the skin and in breast tissue. [13] In humans, C1orf68 protein abundance is moderate. [14] In terms of specific cell types within the skin, C1orf68 is expressed in suprabasal keratinocytes, which are a type of epithelial cell. [15] It has also been noted that C1orf68 is moderately expressed in stratum corneum and granular layer of skin. [16] This could be because the protein remains in the cell as it differentiates and matures.

Transcript level regulation

Predicted C1orf68 3'-UTR mRNA secondary structure with a Gibbs free energy of -41.19, created by mFold. 3'-UTR Secondary Structure of C1orf68.pdf
Predicted C1orf68 3’-UTR mRNA secondary structure with a Gibbs free energy of -41.19, created by mFold.

C1orf68 does not contain a 5'-UTR, but does contain a 3'-UTR. The predicted secondary structure of C1orf68's 3'-UTR mRNA contains various stem loops. The stem loop containing PUM2 RNA protein binding site, which was shown in all of the predicted structures created by mFold. [17]

Protein level regulation

Subcellular localization

Skin-specific protein 32 is predicted to be localized in the cytoplasm. The protein has been shown to occupy the cytoplasm within skin cells, which can be observed in the immunofluorescence staining in Human Protein Atlas, Subcellular. [18]

Evolution

Paralogs

There are no known paralogs of C1orf68.

Orthologs

C1orf68 has a range of orthologs within mammals, and some amphibians, specifically shown in two frog species. The ortholog sequence similarity percentages range from 96 to 23%. There are no orthologs in birds, fish, and reptiles but there was a few in amphibians. Additionally, within the mammals, there was no orthologs in Cetacea (marine mammals). [19] The most highly conserved amino acids across mammals and amphibians with available sequences are Pro61, Pro73, Pro126, Pro182, which are all proline amino acids.

Genus SpeciesCommon NameTaxonomic GroupDivergence Data (MYA) Median Time [20] Accession NumberQuery CoverSequence Length (aa)Sequence Identity (%)Sequence Similarity (%)
Homo sapiens HumanPrimates0NP_001019850100%250100%100%
Rhinopithecus roxellana Golden snub-nosed monkeyPrimates29XP_03079211398%25094%96%
Callithrix jacchus Common marmosetPrimates43XP_03513577696%25683%85%
Cavia porcellus Guinea pigRotentia89XP_00500785896%24980%84%
Ochotona curzoniae Plateau pikaGlires89XP_040854203100%24177%80%
Sus scrofa Wild boarArtiodactyla94XP_00312580496%24879%82%
Myotis brandtii Brandt's batChiroptera94XP_00588069698%24875%79%
Sorex araneus Common shrewEulipotyphla94XP_00461816576%26170%73%
Orycteropus afer AardvarkAfrotheria102XP_00795647498%27073%76%
Echinops telfairi Lesser hedgehog tenrecAfrotheria102XP_00471774191%26273%75%
Dasypus novemcinctus Nine-banded armadilloXenarthra102XP_004469783100%25771%76%
Trichosurus vulpecula Common brushtail possumDiprotodontia160XP_036609710100%25462%67%
Phascolarctos cinereus KoalaDiprotodontia160XP_020847076100%26660%65%
Vombatus ursinus Common wombatDiprotodontia160XP_027726322100%29152%58%
Sarcophilus harrisii Tasmanian devilDasyuromorphia160XP_00377067099%26852%60%
Dromiciops gliroides Colocolo opossumMicrobiotheria160XP_043856143100%31751%57%
Monodelphis domestica Gray short-tailed opossumDidelphimorphia160XP_01628583996%29254%59%
Ornithorhynchus anatinus PlatypusMonotremata180XP_02891043998%24450%56%
Tachyglossus aculeatus Short-beaked echidnaMonotremata180XP_03862425498%26447%54%
Ranitomeya imitator Mimic poison frogAnura352CAF502599596%25126%33%
Xenopus tropicalis Western clawed frogAnura352KAE860639354%29623%33%

The figure below shows more information about the evolutionary rate of C1orf68 throughout its orthologs. The rate of evolution of C1orf68 was observed to be fast when comparing to cytochrome c and fibrinogen alpha. This observation is determined since C1orf68 appears to evolve at a similar rate to fibrinogen alpha, which serves as a standard for rapidly evolving genes.

Rate of evolution comparison between C1orf68, Cytochrome C, and Fibrinogen Alpha. C1orf68 appears to evolve at a similar rate to Fibrinogen alpha, which serves as a standard for rapidly evolving genes. Showing how the corrected % divergence (m) changes over time (Date of Divergence (MYA) Median Time). Skin-Specific Protein 32 Evolution Rate.png
Rate of evolution comparison between C1orf68, Cytochrome C, and Fibrinogen Alpha. C1orf68 appears to evolve at a similar rate to Fibrinogen alpha, which serves as a standard for rapidly evolving genes. Showing how the corrected % divergence (m) changes over time (Date of Divergence (MYA) Median Time).

Interacting proteins

Transcription factor binding sites

Three different transcription factors for C1orf68 were predicted and obtained from MatInspector Genomatics. [12]

GRHL2

Grainyhead-like 2 has been shown to impair keratinocyte differentiation through transcriptional inhibition of the gene in the epidermal differentiation complex. [21] Also showed enhanced protein and mRNA levels in chronic skin lesions, such as in psoriasis. [21]

ZEB1

Zinc finger E-box-binding homeobox 1 has been shown to regulate corneal epithelial terminal phenotype. [22]

GATA3

GATA-binding factor 3 has been shown localized in the cytoplasm and nucleus of proliferating keratinocytes but only in the nucleus in differentiated keratinocytes. [23] It has also been shown that GATA3 induces differentiation of primary keratinocytes, and suggested that it may regulate human interfollicular epidermal renewal. [23]

Protein-protein interactions

Other potential proteins that interact with C1orf68 are located in the table below. These proteins were selected from the results from prediction tools [4] [24] [25] because of their participation in the epidermal cornified envelope, the location of their gene within the epidermal differentiation complex, and the localization to the cytoplasm.

Abbreviated NameFull NameBasis of IdentificationProtein Description
KPRPKeratinocyte proline-rich proteinAffinity Capture-MS [26] This protein's gene is located on the epidermal differentiation complex on chromosome 1q21. Protein has a potential role in keratinocyte differentiation. [27]
TGM3 Transglutaminase 3Affinity Capture-MS [26] An epidermal cross-linking enzyme, it's involved with the formation of the cornfield envelope. [28]
CYLD CYLD Lysine 63 DeubiquitinaseAffinity chromatography technology [29] This protein functions as a deubiquitinating enzyme, and is localized in the cytoplasm. [30]

Clinical significance

Psoriasis

C1orf68 is expressed differently when we look at samples of healthy skin, skin with psoriasis without lesions and skin with psoriasis with lesions. [31] In one study, it was suggested that proteins with significant differences in expression in skin with psoriasis without lesions and skin with psoriasis with lesions, could contribute to maintaining the non-lesional state and may add to our understanding of lesion formation. [32]

Related Research Articles

<span class="mw-page-title-main">Keratinocyte</span> Primary type of cell found in the epidermis

Keratinocytes are the primary type of cell found in the epidermis, the outermost layer of the skin. In humans, they constitute 90% of epidermal skin cells. Basal cells in the basal layer of the skin are sometimes referred to as basal keratinocytes. Keratinocytes form a barrier against environmental damage by heat, UV radiation, water loss, pathogenic bacteria, fungi, parasites, and viruses. A number of structural proteins, enzymes, lipids, and antimicrobial peptides contribute to maintain the important barrier function of the skin. Keratinocytes differentiate from epidermal stem cells in the lower part of the epidermis and migrate towards the surface, finally becoming corneocytes and eventually be shed off, which happens every 40 to 56 days in humans.

<span class="mw-page-title-main">Interleukin 17</span> Group of proteins

Interleukin 17 family is a family of pro-inflammatory cystine knot cytokines. They are produced by a group of T helper cell known as T helper 17 cell in response to their stimulation with IL-23. Originally, Th17 was identified in 1993 by Rouvier et al. who isolated IL17A transcript from a rodent T-cell hybridoma. The protein encoded by IL17A is a founding member of IL-17 family. IL17A protein exhibits a high homology with a viral IL-17-like protein encoded in the genome of T-lymphotropic rhadinovirus Herpesvirus saimiri. In rodents, IL-17A is often referred to as CTLA8.

<span class="mw-page-title-main">Keratinocyte transglutaminase</span> Protein-coding gene in humans

Protein-glutamine gamma-glutamyltransferase K is a transglutaminase enzyme that in humans is encoded by the TGM1 gene.

<span class="mw-page-title-main">S100A7</span>

S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.

Keratohyalin is a protein structure found in cytoplasmic granules of the keratinocytes in the stratum granulosum of the epidermis. Keratohyalin granules (KHG) mainly consist of keratin, profilaggrin, loricrin and trichohyalin proteins which contribute to cornification or keratinization, the process of the formation of epidermal cornified cell envelope. During the keratinocyte differentiation, these granules maturate and expand in size, which leads to the conversion of keratin tonofilaments into a homogenous keratin matrix, an important step in cornification.

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

Involucrin is a protein component of human skin and in humans is encoded by the IVL gene. In binding the protein loricrin, involucrin contributes to the formation of a cell envelope that protects corneocytes in the skin.

<span class="mw-page-title-main">FABP5</span> Protein-coding gene in the species Homo sapiens

Fatty acid-binding protein, epidermal is a protein that in humans is encoded by the FABP5 gene.

<span class="mw-page-title-main">Caspase 14</span> Protein-coding gene in the species Homo sapiens

Caspase 14 is an enzyme that in humans is encoded by the CASP14 gene.

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

Corneodesmosin is a protein that in humans is encoded by the CDSN gene.

miR-203

In molecular biology miR-203 is a short non-coding RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms, such as translational repression and Argonaute-catalyzed messenger RNA cleavage. miR-203 has been identified as a skin-specific microRNA, and it forms an expression gradient that defines the boundary between proliferative epidermal basal progenitors and terminally differentiating suprabasal cells. It has also been found upregulated in psoriasis and differentially expressed in some types of cancer.

<span class="mw-page-title-main">S100A7A</span> Protein-coding gene in the species Homo sapiens

Protein S100-A7A (S100A7A), also known as koebnerisin, is a protein that in humans is encoded by the S100A7A gene.

<span class="mw-page-title-main">Trichohyalin</span>

Trichohyalin is a protein that in mammals is encoded by the TCHH gene.

The S100 calcium-binding protein mS100a7a15 is the murine ortholog of human S100A7 (Psoriasin) and human S100A15 (Koebnerisin). mS100a7a15 is also known as S100a15, mS100a7 and mS100a7a and is encoded by the mS100a7a gene

The epidermal differentiation complex (EDC) is a gene complex comprising over fifty genes encoding proteins involved in the terminal differentiation and cornification of keratinocytes, the primary cell type of the epidermis. In humans, the complex is located on a 1.9 Mbp stretch within chromosome 1q21. The proteins encoded by EDC genes are closely related in terms of function, and evolutionarily they belong to three distinct gene families: the cornified envelope precursor family, the S100 protein family and the S100 fused type protein (SFTP) family.

UPF0575 protein C19orf67 is a protein which in humans is encoded by the C19orf67 gene. Orthologs of C19orf67 are found in many mammals, some reptiles, and most jawed fish. The protein is expressed at low levels throughout the body with the exception of the testis and breast tissue. Where it is expressed, the protein is predicted to be localized in the nucleus to carry out a function. The highly conserved and slowly evolving DUFF3314 region is predicted to form numerous alpha helices and may be vital to the function of the protein.

<span class="mw-page-title-main">C17orf98</span> Protein-coding gene in the species Homo sapiens

C17orf98 is a protein which in humans is coded by the gene c17orf98. The protein is derived from Homo sapiens chromosome 17. The C17orf98 gene consists of a 6,302 base sequence. Its mRNA has three exons and no alternative splice sites. The protein has 154 amino acids, with no abnormal amino acid levels. C17orf98 has a domain of unknown function (DUF4542) and is 17.6kDa in weight. C17orf98 does not belong to any other families nor does it have any isoforms. The protein has orthologs with high percent similarity in mammals and reptiles. The protein has additional distantly related orthologs across the metazoan kingdom, culminating with the sponge family.

<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.

<span class="mw-page-title-main">TMEM212</span> Protein-coding gene in the species Homo sapiens

Transmembrane protein 212 is a protein that in humans is encoded by the TMEM212 gene. The protein consists of 5 transmembrane domains and localizes in the plasma membrane and endoplasmic reticulum. TMEM212 has orthologs in vertebrates but not invertebrates. TMEM212 has been associated with sporadic Parkinson's disease, facial processing, and adiposity in African Americans.

<span class="mw-page-title-main">KIAA2013</span> Protein-coding gene in the species Homo sapiens

KIAA2013, also known as Q8IYS2 or MGC33867, is a single-pass transmembrane protein encoded by the KIAA2013 gene in humans. The complete function of KIAA2013 has not yet been fully elucidated.

<span class="mw-page-title-main">C4orf36</span> Draft for page on C4orf36 gene/protein

C4orf36 is a protein that in humans is encoded by the c4orf36 gene.

References

  1. ↑ Edqvist, Per-Henrik D.; Fagerberg, Linn; Hallström, Björn M.; Danielsson, Angelika; Edlund, Karolina; Uhlén, Mathias; Pontén, Fredrik (2014-11-19). "Expression of Human Skin-Specific Genes Defined by Transcriptomics and Antibody-Based Profiling". Journal of Histochemistry & Cytochemistry. 63 (2): 129–141. doi:10.1369/0022155414562646. ISSN   0022-1554. PMC   4305515 . PMID   25411189.
  2. ↑ Marshall, D.; Hardman, M. J.; Nield, K. M.; Byrne, C. (2001-11-06). "Differentially expressed late constituents of the epidermal cornified envelope". Proceedings of the National Academy of Sciences. 98 (23): 13031–13036. Bibcode:2001PNAS...9813031M. doi: 10.1073/pnas.231489198 . ISSN   0027-8424. PMC   60819 . PMID   11698679.
  3. ↑ Toulza, Eve; Mattiuzzo, Nicolas R; Galliano, Marie-Florence; Jonca, Nathalie; Dossat, Carole; Jacob, Daniel; de Daruvar, Antoine; Wincker, Patrick; Serre, Guy; Guerrin, Marina (2007). "Large-scale identification of human genes implicated in epidermal barrier function". Genome Biology. 8 (6): R107. doi: 10.1186/gb-2007-8-6-r107 . ISSN   1465-6906. PMC   2394760 . PMID   17562024.
  4. 1 2 3 4 "Homo Sapiens C1orf68". NCBI Nucleotide.
  5. ↑ "BLAT Results". UCSC Genome Browser.
  6. ↑ "skin-specific protein 32 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2021-12-18.
  7. ↑ "Anti-C1ORF68 Rabbit Polyclonal Antibody". VWR. Retrieved 2021-12-18.
  8. 1 2 "ExPASy - Compute pI/Mw tool". web.expasy.org. Retrieved 2021-12-18.
  9. ↑ "SAPS < Sequence Statistics < EMBL-EBI". www.ebi.ac.uk. Retrieved 2021-12-16.
  10. ↑ "Motif Scan". myhits.sib.swiss. Retrieved 2021-12-18.
  11. ↑ "Dotlet JS". dotlet.vital-it.ch. Retrieved 2021-12-18.
  12. 1 2 3 "Genomatix: Login Page". www.genomatix.de. Retrieved 2021-12-15.
  13. ↑ "Tissue expression of C1orf68 - Summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2021-12-16.
  14. ↑ "PAXdb: Protein Abundance Database". pax-db.org. Retrieved 2021-12-16.
  15. ↑ "Single cell type - C1orf68 - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2021-12-16.
  16. ↑ "Anti-C1orf68 Antibody (HPA040836) - Atlas Antibodies". www.atlasantibodies.com. Retrieved 2021-12-18.
  17. 1 2 "RNA Folding Form". www.unafold.org. Retrieved 2021-12-18.
  18. ↑ "Subcellular - C1orf68 - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2021-12-16.
  19. ↑ Holthaus, K (Jun 2021). "Gene duplications and gene loss in the epidermal differentiation complex during the evolutionary land-to-water transition of Cetaceans". Scientific Reports. 11 (1): 12334. doi:10.1038/s41598-021-91863-3. PMC   8192740 . PMID   34112911.
  20. 1 2 "TimeTree :: The Timescale of Life". www.timetree.org. Retrieved 2021-12-16.
  21. 1 2 Chen, W; Xiao Liu, Z; Oh, J-E; Shin, K-H; Kim, R H; Jiang, M; Park, N-H; Kang, M K (2012). "Grainyhead-like 2 (GRHL2) inhibits keratinocyte differentiation through epigenetic mechanism". Cell Death & Disease. 3 (12): e450. doi:10.1038/cddis.2012.190. ISSN   2041-4889. PMC   3542624 . PMID   23254293.
  22. ↑ Ortiz-Melo, María Teresa; Garcia-Murillo, Maria Jimena; Salazar-Rojas, Víctor Manuel; Campos, Jorge E.; Castro-Muñozledo, Federico (2021). "Transcriptional profiles along cell programming into corneal epithelial differentiation". Experimental Eye Research. 202: 108302. doi:10.1016/j.exer.2020.108302. ISSN   0014-4835. PMID   33098888. S2CID   225063977.
  23. 1 2 Masse, Ingrid; Barbollat-Boutrand, Laetitia; Kharbili, Manale El; Berthier-Vergnes, Odile; Aubert, Damien; Lamartine, Jérôme (2013-12-18). "GATA3 inhibits proliferation and induces expression of both early and late differentiation markers in keratinocytes of the human epidermis". Archives of Dermatological Research. 306 (2): 201–208. doi:10.1007/s00403-013-1435-5. ISSN   0340-3696. PMID   24346062. S2CID   24204542.
  24. ↑ "BioGRID | Database of Protein, Chemical, and Genetic Interactions". thebiogrid.org. Retrieved 2021-12-18.
  25. ↑ "GeneMANIA". genemania.org. Retrieved 2021-12-18.
  26. 1 2 Marcon, Edyta; Ni, Zuyao; Pu, Shuye; Turinsky, Andrei L; Trimble, Sandra Smiley; Olsen, Jonathan B; Silverman-Gavrila, Rosalind; Silverman-Gavrila, Lorelei; Phanse, Sadhna; Guo, Hongbo; Zhong, Guoqing (2014). "Human Chromatin Related Protein Interactions Identify a Demethylase Complex Required for Chromosome Segregation". Cell Reports. 8 (1): 297–310. doi: 10.1016/j.celrep.2014.05.050 . ISSN   2211-1247. PMID   24981860.
  27. ↑ Lee, Woong-Hee; Jang, Sunhyae; Lee, Jung-Suk; Lee, Young; Seo, Eun-Young; You, Kwan-Hee; Lee, Seung-Chul; Nam, Kwang-Il; Kim, Jin-Man; Kee, Sun-Ho; Yang, Jun-Mo (2005). "Molecular Cloning and Expression of Human Keratinocyte Proline-Rich Protein (hKPRP), an Epidermal Marker Isolated from Calcium-Induced Differentiating Keratinocytes". Journal of Investigative Dermatology. 125 (5): 995–1000. doi: 10.1111/j.0022-202x.2005.23887.x . ISSN   0022-202X. PMID   16297201.
  28. ↑ de Koning, H.D.; van den Bogaard, E.H.; Bergboer, J.G.M.; Kamsteeg, M.; van Vlijmen-Willems, I.M.J.J.; Hitomi, K.; Henry, J.; Simon, M.; Takashita, N.; Ishida-Yamamoto, A.; Schalkwijk, J. (2012-05-25). "Expression profile of cornified envelope structural proteins and keratinocyte differentiation-regulating proteins during skin barrier repair". British Journal of Dermatology. 166 (6): 1245–1254. doi:10.1111/j.1365-2133.2012.10885.x. ISSN   0007-0963. PMID   22329734. S2CID   274172.
  29. ↑ Elliott, Paul R.; Leske, Derek; Hrdinka, Matous; Bagola, Katrin; Fiil, Berthe K.; McLaughlin, Stephen H.; Wagstaff, Jane; Volkmar, Norbert; Christianson, John C.; Kessler, Benedikt M.; Freund, Stefan M.V. (2016). "SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling". Molecular Cell. 63 (6): 990–1005. doi:10.1016/j.molcel.2016.08.001. ISSN   1097-2765. PMC   5031558 . PMID   27591049.
  30. ↑ "GeneCard-CYLD". www.genecards.org. Retrieved 2021-12-18.
  31. ↑ "Psoriasis lesional and non-lesional skin - - GEO DataSets - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2021-12-18.
  32. ↑ Szél, Edit; Bozó, Renáta; Hunyadi-Gulyás, Éva; Manczinger, Máté; Szabó, Kornélia; Kemény, Lajos; Bata-Csörgő, Zsuzsanna; Groma, Gergely (2019-08-06). "Comprehensive Proteomic Analysis Reveals Intermediate Stage of Non-Lesional Psoriatic Skin and Points out the Importance of Proteins Outside this Trend". Scientific Reports. 9 (1): 11382. Bibcode:2019NatSR...911382S. doi:10.1038/s41598-019-47774-5. ISSN   2045-2322. PMC   6684579 . PMID   31388062.
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