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DCD (dermcidin)

Written2020-07Amanda Soares Hirata, Rodrigo dos Anjos Miguel, Paula Christine Jimenez, Leticia Veras Costa-Lotufo
Department of Pharmacology, Institute of Biomedical Sciences of University of Sâo Paulo, Sâo Paulo, Brazil, (ASH); (RAM); (LVC-L); Department of Marine Sciences, Federal University of Sâo Paulo, Santos, Brazil, (PCJ)

Abstract Dermcidin (DCD) is a 110-amino acid protein, which is cleaved in several other peptides with different functions. The best-known function of this protein is as antimicrobial host defense, acting majorly in the skin, where many DCD derivatives were identified to be constitutively secreted, mainly by sweat glands. Additionally, Y-P30, one of such derivatives, has been described as a survival factor predominantly in stressed neural cells. This function has also been investigated in cancer cells, portraying DCD as an oncogene, as well a novel biomarker for this disease. Furthermore, PIF, another DCD derivative, may be an important inducer of non-fat weight loss, which has been related with cachexia. The present review assesses data on DCD and derivatives observing DNA, RNA, encoded proteins and their various functions, highlighting their relevance in cancer and other clinical conditions.

Keywords DCD; Dermcidin; Antimicrobial Peptides; PIF; Proteolysis-Inducing Factor; Cachexia; Cancer; Y-P30; Survival Promoting Peptide

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Proteolysis Inducing Factor
Diffusible Survival/Evasion Peptide
Survival Promoting Peptide.
Cancer Cachectic Factor
HGNC Alias symbAIDD
HGNC Alias nameproteolysis inducing factor
 diffusible survival/evasion peptide
 survival promoting peptide
LocusID (NCBI) 117159
Atlas_Id 46314
Location 12q13.2  [Link to chromosome band 12q13]
Location_base_pair Starts at 54644589 and ends at 54648365 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping DCD.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


Description The entire DCD gene is approximately 3.9 Kb; starts at 54644589 and ends at 54648493 bp; orientation: reverse strand.
Transcription The DCD gene encodes 3 transcript variants (splice variants). There are two transcript variants deposited in the NCBI database ( and one additional transcript variant reported in Ensembl ( The transcript variant 1 is formed by 5 exons and 5 coding exons, resulting in a transcript length of 519 bps and a translation length of 110 amino acids (aa). The transcript variant 2 is the longest variant, with 6 exons and 6 coding exons (transcript length of 670 bps) and a translation length of 121 aa. The transcript variant 3 is formed by 6 exons and 3 coding exons (transcript length of 773 bps), which results in the shorter translation variant, with 77 aa.


  Figure 1. Gene and protein structure of full-length dermcidin (variant 1) and derived peptides. (A) Dermcidin gene (DCD) is formed by 5 exons and 4 introns, which codifies a protein of 110 amino acids (aa). (B) Dermcidin protein comprises a signal peptide (19 aa), followed by a prodomain (43 aa) and an antimicrobial peptide domain (48 aa). (C) The full protein can be processed into another 17 peptides, among which 3 peptides derive from the prodomain (represented in orange) and 14 peptides result from the antimicrobial peptide domain (represented in green). Each peptide is listed by name, known function and aa length and sequence.
Description The full-length dermcidin protein has 110 amino acids (aa) that consists of a 19-amino-acid signal peptide, a 43-amino-acid prodomain and a 48-amino-acid antimicrobial peptide domain (Schittek, 2012). This precursor is proteolytically processed into several derivatives. DCD-1 (47 aa), DCD-1L (48 aa), SSL-25 (25 aa) and SSL-23 (23 aa), the derivatives with the best described function, are secreted by eccrine sweat glands as antimicrobial peptides (Schittek et al., 2001; Steffen et al., 2006). The Y-P30 (30 aa) derivative has been described as a neuron survival-promoting peptide (Cunningham et al., 2000), while the PIF (20 aa) - Proteolysis-Inducing Factor, a proteolytic glycoprotein, is associated to a severe loss of skeletal muscles in cachectic cancer patients (Todorov et al., 1996; Lorite et al., 1997). The full primary structure of DCD is illustrated in Figure 1.
Expression Dermcidin is constitutively expressed by the dark mucous cells of the secretory coil of eccrine sweat glands, unlike the other antimicrobial peptides that are induced by injury and inflammation (Schittek et al., 2001; Rieg et al., 2004; Rieg et al., 2006). In these glands, the DCD mRNA is translated into a 110-amino acid peptide that can be processed and secreted into sweat or cleaved by several proteases in this fluid (Schittek et al., 2001; Schittek, 2012; Rieg et al., 2004; Flad et al., 2002). There are 14 DCD-derived peptides that occur in sweat. The C-terminal region of the protein contains the majority of the peptides with antimicrobial activity: DCD-1, DCD-1L, SSL-23, SSL-25, SSL-45 and SSL-46 (Schittek et al., 2001; Steffen et al., 2006; Mühlhäuser et al., 2017). Furthermore, there is one peptide derived from the prodomain YDP-42 (Schittek, 2012). Even DCD-1 or DCD-1L can be processed in sweat into smaller peptides like LEK-24 and SSL-25 by enzymes such as cathepsin D, 1,10-phenanthroline-sensitive carboxypeptidase and endoproteases (Baechle et al., 2006).
Dermcidin is also expressed by sebaceous glands and neutrophils in immunity-related circumstances (Dahlhoff et al., 2016; Lominadze et al., 2005) and, moreover, has been shown to be overexpressed in the context of HIV infection of monocytoid cells (Pathak et al., 2009). Additionally, oxidatively stressed neural cell lines express dermcidin in the form of the signal peptide Y-P30, described firstly as DSEP, the diffusible survival/evasion peptide, which can, indeed, be detected in culture media (Cunningham et al., 2002).
The human term placental tissue may express DCD as two splice variants under a restricted spatiotemporal pattern, which may be related to the involvement of dermcidin in the molecular mechanisms of pregnancy. Placental dermcidin can be processed into DCD-1 and defend the fetus against invading microorganisms (Motoyama et al., 2007), or into Y-P30 to exert neuritogenic activity during fetus brain development (Mikhaylova et al., 2014).
In plasma, dermcidin may be found in different conditions: 1) in hepatocellular carcinoma patients (Qiu et al., 2018); 2) overexpressed in patients with arterial hypertension, as a player in modulation of NO levels and induction of platelet aggregation (Ghosh et al., 2011; Ghosh et al., 2012a); 3) in type I diabetes mellitus, inhibiting the synthesis of insulin in hepatocytes and pancreatic cells (Ghosh et al., 2011; Ghosh et al., 2012b). Dermcidin is also secreted by ischemic skeletal muscles, enhancing cardiomyocytes apoptosis under hypoxic conditions and infarct size after permanent coronary artery ligation (Esposito et al., 2015). Moreover, dermcidin is abundantly present in exhaled breath condensate of asthmatic and lung cancer patients, and it can be regarded as a biomarker in these diseases (Bloemen et al., 2001; Chang et al., 2010).
Also, dermcidin has revealed a relevant role in cancer; it offers a survival advantage in some tumors, as reported for breast cancers (Porter et al., 2003; Brauer et al., 2014); prostate cancer (Wang et al., 2003; Stewart et al., 2007); lung cancer, as a biomarker in exhaled breath condensate (Chang et al., 2010); hepatic cancer cells (Lowrie et al., 2006; Shen et al., 2011; Qiu et al., 2018; Lowrie et al., 2011); gastro-oesophageal cancer (Deans et al., 2006); pancreatic cancer cells (Stewart et al., 2008a); a myelogenous leukemia cell line (Stocki et al., 2011); and melanoma (Smith et al., 2005; Rieg et al., 2004; Trzoss et al., 2014). Additionally, tumor cells express PIF, which is resistant to proteolytic digestion by trypsin and the human cancer expression has been related to inhibition of muscle cell differentiation and a high weight loss (Majczak et al., 2007; Todorov et al., 1997; Wigmore et al., 2000; Jiang and Clemens, 2006; Wieland et al., 2007). In fact, PIF was discovered in 1996 in mice and later described as a potent catabolic factor that acts as a cachectic cancer factor (Tisdale et al., 2004; Schittek et al., 2012; Todorov et al., 1996). Although the role of murine PIF is well established, its biology remains speculative in humans (Stewart et al., 2008b).
Localisation Dermcidin is mainly found in the cytoplasm or extracellularly.
In the dark mucous cells of the secretory coil of eccrine sweat glands, dermcidin is detected in the Golgi complex and in the secretory granules, released in the cell surface and transported to epidermal surface by the sweat duct (Schittek et al., 2001; Rieg et al., 2006, Sakurada et al., 2010). There are differences in the levels of DCD-derived peptides in eccrine sweat of distinct anatomic sites; highest concentrations are found in palms, arms and forehead, where the density of eccrine sweat glands is higher and the body is more exposed to pathogens and minor trauma (Rieg et al., 2004).
Although less profusely, dermcidin is also found in basal tears, in cervicovaginal fluid and in breast milk, in which it also assumes a function associated to innate immunity (You et al., 2010; Shaw et al., 2007; Azkargorta et al., 2015; Chow et al., 2016). Furthermore, dermcidin-derived peptides can be found in lipid droplets secreted by the holocrine sebaceous glands and in the granules of neutrophils, suggesting that this protein has, likewise, an immunity related purpose in these cells (Dahlhoff et al., 2016; Lominadze et al., 2005).
Function DCD-1, DCD-1L, SSL-25, SSL-23, SSL-45 and SSL-46 peptides have a broad and overlapping spectrum regarding antimicrobial activity against, for example, Staphylococcus aureus, Enterococcus faecalis, Staphylococcus epidermidis, Escherichia coli, Pseudomonas aeruginosa and Candida albicans (Schittek et al., 2001; Steffen et al., 2006; Mühlhäuser et al., 2017). Anionic DCD-1L monomers can bind bacterial membrane and fold into an amphiphilic alpha-helix, interacting parallelly to the surface. Further studies indicate the proteins can self-assemble into high-order oligomers and form ion channels, which can lead to bacterial cell death by abrogation of the transmembrane potential (Paulmann et al., 2012; Song et al., 2013). Such conformation is indeed favored by transmembrane potential as well as by the presence of Zn2+ due to neutralization of protein charge. On the other hand, SSL-29, LEK-44, LEK-45 and YDP-42 peptides showed no antimicrobial activity against the same bacterial species: S. aureus, E. faecalis, S. epidermidis, E. coli and P. aeruginosa (Rieg et al., 2005; Steffen et al., 2006).
DCD-1L has been studied as a stimulant for production of pro-inflammatory cytokines and chemokines by human keratinocytes cells controlled by G-protein and mitogen-activated protein kinase (MAPK) signaling pathways, thus contributing to the cutaneous immunity (Niyonsaba et al., 2009).
High blood levels of dermcidin variant 2 was found in patients following acute ischemic heart disease. There have been further investigations on rather such variant may inhibit synthesis and release of insulin by the pancreas, an effect that was then shown to be reversed by aspirin or insulin administration (Bank et al., 2014; Ghosh et al., 2014). As a consequence of insulin resistance, there may be increase in blood pressure and atherosclerosis through inhibition of NO production and promotion of prothrombotic effects (Ghosh et al., 2011). The same role for dermcidin was observed in ischemic and hemorrhagic stroke patients (Bank et al., 2015).
Dermcidin has been shown to interact with few proteins within the cell. In this context, phosphorylation at Tyr20 enabled dermcidin to interact with the SH2 domain of NCK1, which, through effector proteins like the PAK1 /ARHGEF6 (also called PIX) complex, stimulates Rho GTPases RAC1 and CDC42 and reorganizes actin cytoskeleton, ultimately promoting cell migration in a hepatocellular carcinoma cell line (SK-HEP1) (Shen et al., 2011). Furthermore, in a gastric cancer cell line (BGC-823), dermcidin protein was one of the proteins bound to a long non-coding RNA (STCAT3), while overexpression of both dermcidin and STCAT3 were related to poor prognosis for patients (Zhang et al., 2018). Considering small molecules - natural products, in this case - dermcidin has been shown to bind paclitaxel and seriniquinone, a marine bacterium derived compound. In the first setting, dermcidin precursor was recovered, along with HSP90AA1 and actinin, from a paclitaxel-biotin probe fed to drug-sensitive breast cancer cell line (MCF7), but not from their paclitaxel-resistant analogue, suggesting a role of dermcidin in the cell resistance profile to this compound and cross-resistance to other anticancer drugs (Zuo et al., 2010). Regarding the later natural product , dermcidin protein was revealed to be a direct target of a seriniquinone probe, which was found to be further bound to other proteins, such as GAPDH and Hsp70, in a colorectal carcinoma cell line (HCT 116) model (Trzoss et al., 2014).
Y-P30 was first seen overexpressed as a neuron survival-promoting peptide in response to oxidative stress (Cunningham et al., 1998), promoting survival of cortical neurons after cerebral lesions by retaining calreticulin in the cytosol and reducing calcium signaling to a degree in which it is protective, regardless of any immune cell inhibition (Cunningham et al., 2000). During hypoxia and hypoglycemia, Y-P30 expression is associated with reduced neural cell death in vitro (Schneeberg et al., 2009). This protein is also related to induction of neurite outgrowth in cortical neurons during early brain development, a role that is suggested by the effect of binding of Y-P30 to PTN (pleiotrophin) in the extracellular axonal membrane, thus increasing syndecan local concentrations and promoting neurite growth (Landgraf et al., 2008). Furthermore, this mechanism can be related to calcium/calmodulin-dependent serine kinase ( CASK) migration to the nucleus, where Y-P30 interacts differently with syndecan-2 ( SDC2) or -3 ( SDC3) in immature or mature neurons, contributing with migration and axonal outgrowth (Landgraf et al., 2014; Neumann et al., 2019).
PIF has been investigated as a catalytic protein, which can induce proteasome expression through NF-kB activation (Wyke and Tisdale, 2005). Consequently, this process results in decreased protein synthesis and severe degradation of skeletal muscle, thus correlating with the weight loss in cachectic cancer patients, an effect typically attributed to PIF (Todorov et al., 1996; Lorite et al., 1997; Todorov et al., 2007). PIF was also associated with the release of Ca2+ from intracellular stocks, suggesting PIF receptor (a zinc-sensing receptor) is coupled to a G-protein to cause calcium release from endoplasmic reticulum (Mirza and Tisdale, 2012). Reinforcing these data, direct and indirect inhibitors of NF-kB were able to attenuate the development of muscle loss (Wyke et al., 2004; Russell et al., 2007).
Homology The DCD gene is highly homologous among different non-human primate species, as shown in Table 1, which compares DCD isoform 1 among species.
Table 1. Comparative identity of human DCD with other species.
% Identity for: Homo sapiens CDCSymbolProteinDNA
vs. P. paniscus DCD 100 100
vs. P. abelii DCD 96.9 98.2
vs. N. leucogenys DCD 93.8 98.4
vs. H. moloch DCD 92.8 91.7
vs. T. francoisi DCD 91.7 95.3
vs. R. roxellana DCD 91.7 94.2
vs. C. angolensis palliatus DCD 91.7 94
vs. C. jacchus DCD 91 96
vs. P. tephrosceles DCD 90.7 92.7
vs. M. mulatta DCD 89.7 95.2
vs. T. gelada DCD 89.7 91.1
vs. M. leucophaeus DCD 89.7 95.9
vs. M. nemestrina DCD 89.7 89.9
vs. C. sabaeus DCD 84.8 93.7
vs. A. nancymaae DCD 82.3 96.8
vs. S. boliviensis boliviensis DCD 80.4 95.0
vs. S. apella DCD 77.3 94.3
vs. C. capucinus imitator DCD 76.5 95.2



Somatic From 37420 unique samples reported in COSMIC (Catalogue of Somatic Mutations in Cancer;, a total of 145 unique samples presented DCD mutations, of which 67 different mutations are distributed among 47 missense substitutions, 16 synonymous substitutions, 2 frameshift insertion and 2 frameshift deletions. Somatic mutation frequency of 0.3% is similar to that reported in cBioPortal ( From 10967 samples, 31 mutations are classified as 25 missense substitutions and 6 truncated mutations.

Implicated in

Entity Breast cancer
Note DCD is overexpressed in approximately 10% of breast carcinomas; in some cases, it is associated with a focal copy number gain of its locus at 12q13.2, or with advanced clinical staging and poor prognosis. In animal models, dermcidin was found in high concentrations in serum of early breast cancer rats, whereas women displayed increased levels of dermcidin just prior to diagnosis. Moreover, such high dermcidin levels were related to disease progression and more aggressive types of this neoplasm (Brauer et al., 2014). Besides its function in cell growth and survival, overexpression of dermcidin results in a reduction of serum dependency by the tumor (Porter et al., 2003). Furthermore, cell survival and growth-promoting functions of dermcidin were described as a consequence of modulation of ERBB receptor by dermcidin (Bancovik et al., 2015). Dermcidin also coordinates the expression of genes involved in oxidative stress as well as amino acid and glucose metabolism, while it may be likewise associated to drug resistance in breast cancer cells (Moreira et al., 2008).
Dermcidin was found among intracellular proteins bound to paclitaxel in a naïve breast cancer cell line (MCF7), however it was not analogously recovered in the paclitaxel resistant counterpart, suggesting involvement of dermcidin in the drug-resistance phenotype (Zuo et al., 2010).
Entity Cervical cancer
Note Studies with human uterine cervical cancer (Yumoto) transplanted mice revealed the expression of PIF in tumor, serum and urine of cachexia-induced murine models. Furthermore, PIF expression and cachexia development were reversed by administration of a fluorinated pyrimidine (5'-deoxy-5-fluorouridine) (Hussey et al., 2000).
Entity Colon cancer
Note Studies with murine colon adenocarcinoma cell line (MAC 16) transplanted mice demonstrated expression of PIF in tumor, serum and urine in cachexia-induced animals, while this peptide was absent in non-cachexic models. PIF expression and cachexia development were also completely reversed by administration of a fluorinated pyrimidine (5'-deoxy-5-fluorouridine) (Hussey et al., 2000).
Entity Gastro-oesophageal cancer
Note DCD mRNA expression was analyzed in primary tissues of gastric cancers (n=20) and 25% of the samples had detectable levels of mRNA; in turn, 14% of oesophageal cancers samples (n=28) displayed detectable DCD mRNA expression (Stewart et al., 2008).
Patients with PIF expression from gastric cancer tissues also presented detectable PIF in urine samples and higher percentages of weight loss (Cabal-Manzano et al., 2001). PIF expression in gastro-oesophageal tumors were found to be elevated in 59% of the cancer samples analyzed and in 67% of adjacent benign tissues. Although this study revealed a high correlation between PIF expression and cancer, upregulation of PIF did not show correlation with cachexia or prognosis (Deans et al., 2006).
Prognosis STCAT3, a long non-coding RNA (lncRNA), is highly expressed in gastric cancer tissues and is has been associated with specific cancer features, such as proliferation, migration and invasion. Furthermore, upregulation of this lncRNA is related to poor prognosis. Dermcidin protein was shown to bind STCAT3 in a gastric cancer cell line (BGC-823); as expression of both markers are positively correlated, dermcidin overexpression was also identified in cancer tissues and associated to poor prognosis in patients (Zhang et al., 2018).
Entity Liver cancer
Note Dermcidin, when compared with non-tumoral hepatic tissues, is overexpressed in hepatocellular carcinoma, mainly in SK-HEP1 cell line, a high invasive endothelial cell line. The role of dermcidin in metastasis was described using such cell line: this protein is phosphorylated at Tyr20 allowing its interaction with the SH2 domain of Nck1, which, in turn, binds to proline-rich sequences of several effector proteins. One example of these proteins is the PAK1/ARHGEF6 complex that stimulates Rho GTPases RAC1 and CDC42 and regulates cell adhesion, migration and gene transcription, mainly by reorganizing actin cytoskeleton (Shen et al., 2011).
Additionally, dermcidin has, likewise, been associated to cell survival in this cancer type (Lowrie et al., 2006), while Y-P30/PIF-core was accounted for cell proliferation in HuH7 hepatic cancer cell lines through different pathways (Lowrie et al., 2011). Dermcidin has been studied as a hepatocellular cancer biomarker, as it is significantly increased in patients enduring this disease (Qiu et al., 2018).
Entity Lung cancer
Note Dermcidin was identified in the peptidome of exhaled breath condensate (EBC) from lung cancer patients. In this context, dermcidin expression was confirmed in two out of six squamous cell carcinoma and in three out of six adenocarcinoma tissues assessed (Chang et al., 2010). The expression was also present in lung cancer cell lines (H520, squamous cell carcinoma; and PC13, adenocarcinoma), which underwent growth reduction upon DCD knockdown (Chang et al., 2010). Similarly, another study found higher levels of dermcidin in EBCs of lung cancer patients and have suggested this protein as a novel biomarker for diagnosis (López-Sánchez et al., 2017; Núñez-Naveira et al., 2019).
Analogously, PIF displayed elevated expression levels in non-small-cell lung cancer (NSCLC) tissues, which was higher in patients supporting greater weight losses. Although there was no correlation between PIF and tumor clinical staging, a significant correlation between weight loss and survival in the PIF-positive patients was identified (Wang et al., 2010).
Entity Melanoma
Note DCD mRNA expression was detected following pro-inflammatory stimuli (exposure to 12-O-tetradeca-noyl-phorbol-13-acetate, TNF (tumor necrosis factor-alpha), lipopolysaccharide or H2O2) in SK-MEL-28 and MeWo melanoma cell lines (Rieg et al., 2004).
Production of PIF was also identified in human melanoma cell line G361. Within this study, the protein was further purified and administered to mice, and those who received treatment experienced weight loss specifically by non-fat mass (Todorov et al., 1999). Moreover, expression of PIF by the melanoma cell line Mel impaired muscle cell differentiation; a feature that could be then counteracted by treatment with a caspase-8-like inhibitory protein (Jiang and Clemens, 2006).
Prognosis Serum levels of dermcidin have displayed prognostic potential in melanoma patients, once early staged patients (stages I and II) who developed metastasis showed lower concentration of the protein, thus presenting this as an important biomarker to predict such event. In turn, dermcidin was elevated in III-IV staged patients, which displayed poor survival rates (Ortega-Martínez et al., 2016). A new cohort of patients then confirmed this observation, further enabling the establishment of an algorithm to predict the risk of tumor metastasis where dermcidin levels is actually one of the variables (Mancuso et al., 2020).
Entity Pancreatic cancer
Note Tissue samples of pancreatic cancer demonstrated that 3 of the 5 tumors subjected to analysis displayed moderate to high DCD mRNA expression. The pancreatic cell line MIA-Pa-Ca-2 also revealed increased levels of DCD mRNA (Stewart et al., 2008).
First evidences of the part taken by PIF in pancreatic cancer revealed the protein was only present in urine samples of cancer patients with high proportions of weight loss per month, while it was absent in patients with low to normal weight loss rates (Todorov et al., 1996). Furthermore, PIF was detected in 80% of urine samples from patients with pancreatic cancer (n=55), which also revealed to be the same group that supported a high rate of weight loss (Wigmore et al., 2000). Nevertheless, the occurrence of PIF in urine does not appear to correlate with malignancy of the pancreatic tumor (Teich et al., 2005). Interestingly, cachectic pancreatic cancer patients consuming a nutritional fish oil-enriched supplement decreased their urinary excretion of PIF and actually presented weight gain, suggesting important metabolic modulations between cancer and cachexia (Barber et al., 2001).
Entity Prostate cancer
Note Insulin resistance has been described as a risk factor for cardiovascular diseases in patients with prostate cancer, where high expression levels of dermcidin isoform-2 were related with a low production or function impairment of insulin through NO inhibition, further contributing to cardiovascular disease in these patients (Ray et al., 2019).
DCD demonstrated to be proliferative and survival factors for DCD-transfected PC-3M prostate cell line under oxidative stress or hypoxia conditions, besides PIF portion was attributed to these effects (Stewart et al., 2007). Same authors did not detect DCD mRNA expression in primary prostate cancer tissues (Stewart et al., 2008).
Human cachexia-associated protein (HCAP), a homolog to the PIF protein, is expressed in prostate cancer: cell lines, primary tumors, metastases and present in the urine of cachectic patients, but not in healthy prostate (Wang et al., 2003). Additionally, PIF expression was detected in a prostate cancer cell line (PC-3) causing inhibition of muscle cell differentiation, what could be reversed by cellular caspase-8-like inhibitory protein treatment in vitro (Jiang and Clemens, 2006).
Entity Retinoblastoma
Note Y-P30 is expressed after the induction of oxidative stress with H2O2 in human retinoblastoma Y79 cell line, acting as a survival-promoting peptide (Cunningham et al., 1998).

To be noted

Pharmacological Applications
Antimicrobial peptides (AMPs) are produced innately by the healthy human body to act as antimicrobial host defense and are considered to own a superior mode of action than typical small-molecule antibiotics, however dragging lower antimicrobial efficacy (Fjell et al., 2011). There is still a knowledge shortage regarding the mechanisms by which AMPs target microbial membranes and, moreover, on biochemical features of such essential microbial systems (Zeth, 2013). Nevertheless, these peptides have been approached as models for rational antibiotic drug design. In this context, DCD-1/DCD-1L, which have been shown to form a hexameric channel-like complex prior to microbial membrane fusion, are still one of the best studied AMPs (Zasloff, 2002; Song et al., 2013; Zeth & Sanch-Vaello, 2017). Indeed, peptide mixtures of dermcidin-derived peptides and other AMPs were shown to counteract Staphylococcus and Streptococcus infections in injured epidermal surface at comparable concentrations (5 - 30 μg/mL) to IC90 values previously determined for DCD-1L (45 μg/mL against S. aureus; 8 μg/mL against MRSA) (Steffen et al., 2006).
Natural products that modulate AMPs have shown interesting pharmacological potential. In this sense, lugdunin, a cyclic peptide antibiotic produced by the nasal and skin commensal S. lugdunensis in human nostril, presented potent antimicrobial activities, acting against colonization of its co-habitant S. aureus as well as towards a wide range of other Gram-positive bacteria (Zipperer et al, 2016). It was later revealed that lugdunin, in addition to owning a direct effect against S. aureus, including MRSA strains, operates in synergy with DCD-1 and DCD-1L, thus enhancing the inherent host defense response elicited by the AMPs (Bitschar et al., 2019). Furthermore, a second compound, seriniquinone, a natural product from a rare marine bacteria of the genus Serinicoccus sp., was found to induce cancer cell death through direct targeting DCD. The molecule displayed high cytotoxicity, with particular selectivity towards cell lines originated from melanoma tumors. Moreover, seriniquinone triggers autophagy early on, as shown by assessment to biochemical markers and also through co-localization studies, as it localizes into the ER then is transported to the arising autophagosomes (Trzoss et al., 2014). Although there is not yet a clear correlation between seriniquinone interaction with DCD and induction of autophagy, it has been further shown that cells exposed to this natural compound and also to synthetic analogues thereof increased DCD expression, an effect that is, once again, more prominent in melanoma cells (Hammons et al., 2019).
Funding: Fundaçâo de Amparo à Pesquisa do Estado de Sâo Paulo - FAPESP (number processes: 2018/07661-6, 2015/17177-6) and Conselho Nacional de Desenvolvimento Cientèfico e Tecnológico - CNPq (number processes: 165935/2019-7, 306913/2017-8).


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PMID 10833321
Expression of dermcidin in sebocytes supports a role for sebum in the constitutive innate defense of human skin
Dahlhoff M, Zouboulis CC, Schneider MR
J Dermatol Sci 2016 Feb;81(2):124-6.
PMID 26718508
Expression of the proteolysis-inducing factor core peptide mRNA is upregulated in both tumour and adjacent normal tissue in gastro-oesophageal malignancy
Deans DA, Wigmore SJ, Gilmour H, Tisdale MJ, Fearon KC, Ross JA
Br J Cancer 2006 Mar 13;94(5):731-6.
PMID 16495932
Dermcidin: a skeletal muscle myokine modulating cardiomyocyte survival and infarct size after coronary artery ligation
Esposito G, Schiattarella GG, Perrino C, Cattaneo F, Pironti G, Franzone A, Gargiulo G, Magliulo F, Serino F, Carotenuto G, Sannino A, Ilardi F, Scudiero F, Brevetti L, Oliveti M, Giugliano G, Del Giudice C, Ciccarelli M, Renzone G, Scaloni A, Zambrano N, Trimarco B
Cardiovasc Res 2015 Sep 1;107(4):431-41.
PMID 26101262
Designing antimicrobial peptides: form follows function
Fjell CD, Hiss JA, Hancock RE, Schneider G
Nat Rev Drug Discov 2011 Dec 16;11(1):37-51.
PMID 22173434
Detection of dermcidin-derived peptides in sweat by ProteinChip technology
Flad T, Bogumil R, Tolson J, Schittek B, Garbe C, Deeg M, Mueller CA, Kalbacher H
J Immunol Methods 2002 Dec 1;270(1):53-62.
PMID 12379338
Neutralization by insulin of the hypertensive effect of dermcidin isoform 2: an environmentally induced diabetogenic and hypertensive protein
Ghosh R, Bank S, Bhattacharya R, Khan NN, Sinha AK
Cardiol Res Pract 2014;2014:412815.
PMID 24649391
The control of hyperglycemia in alloxan treated diabetic mice through the stimulation of hepatic insulin synthesis due to the production of nitric oxide
Ghosh R, Jana P, Sinha AK
Exp Clin Endocrinol Diabetes 2012 Mar;120(3):145-51.
PMID 22231923
The appearance of dermcidin isoform 2, a novel platelet aggregating agent in the circulation in acute myocardial infarction that inhibits insulin synthesis and the restoration by acetyl salicylic acid of its effects
Ghosh R, Karmohapatra SK, Bhattacharyya M, Bhattacharya R, Bhattacharya G, Sinha AK
J Thromb Thrombolysis 2011 Jan;31(1):13-21.
PMID 20809104
The role of dermcidin isoform 2: a two-faceted atherosclerotic risk factor for coronary artery disease and the effect of acetyl salicylic Acid on it
Ghosh R, Maji UK, Bhattacharya R, Sinha AK
Thrombosis 2012;2012:987932.
PMID 22448321
Advance of Seriniquinone Analogues as Melanoma Agents
Hammons JC, Trzoss L, Jimenez PC, Hirata AS, Costa-Lotufo LV, La Clair JJ, Fenical W
ACS Med Chem Lett 2019 Feb 6;10(2):186-190.
PMID 30783501
Effect of a fluorinated pyrimidine on cachexia and tumour growth in murine cachexia models: relationship with a proteolysis inducing factor
Hussey HJ, Todorov PT, Field WN, Inagaki N, Tanaka Y, Ishitsuka H, Tisdale MJ
Br J Cancer 2000 Jul;83(1):56-62.
PMID 10883668
Cellular caspase-8-like inhibitory protein (cFLIP) prevents inhibition of muscle cell differentiation induced by cancer cells
Jiang Z, Clemens PR
FASEB J 2006 Dec;20(14):2570-2.
PMID 17060399
Exhaled breath condensate biomarkers for the early diagnosis of lung cancer using proteomics
López-Sánchez LM, Jurado-Gámez B, Feu-Collado N, Valverde A, Cañas A, Fernández-Rueda JL, Aranda E, Rodríguez-Ariza A
Am J Physiol Lung Cell Mol Physiol 2017 Oct 1;313(4):L664-L676.
PMID 28619761
The survival-promoting peptide Y-P30 enhances binding of pleiotrophin to syndecan-2 and -3 and supports its neuritogenic activity
Landgraf P, Wahle P, Pape HC, Gundelfinger ED, Kreutz MR
J Biol Chem 2008 Sep 5;283(36):25036-45.
PMID 18599487
Identification of dermcidin in human gestational tissue and characterization of its proteolytic activity
Lee Motoyama JP, Kim-Motoyama H, Kim P, Nakagama H, Miyagawa K, Suzuki K
Biochem Biophys Res Commun 2007 Jun 15;357(4):828-33.
PMID 17448443
Proteomic analysis of human neutrophil granules
Lominadze G, Powell DW, Luerman GC, Link AJ, Ward RA, McLeish KR
Mol Cell Proteomics 2005 Oct;4(10):1503-21.
PMID 15985654
Induction of muscle protein degradation by a tumour factor
Lorite MJ, Cariuk P, Tisdale MJ
Br J Cancer 1997;76(8):1035-40.
PMID 9376263
Proteolysis-inducing factor core peptide mediates dermcidin-induced proliferation of hepatic cells through multiple signalling networks
Lowrie AG, Dickinson P, Wheelhouse N, Stewart GD, Ross AJ, Forster T, Ross JA
Int J Oncol 2011 Sep;39(3):709-18.
PMID 21643625
Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues
Lowrie AG, Wigmore SJ, Wright DJ, Waddell ID, Ross JA
Br J Cancer 2006 Jun 5;94(11):1663-71.
PMID 16685272
Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat
Mühlhäuser P, Wadhwani P, Strandberg E, Bürck J, Ulrich AS
Biochim Biophys Acta Biomembr 2017 Dec;1859(12):2308-2318.
PMID 28888369
Prediction and biochemical characterization of intrinsic disorder in the structure of proteolysis-inducing factor/dermcidin
Majczak G, Lilla S, Garay-Malpartida M, Markovic J, Medrano FJ, de Nucci G, Belizário JE
Genet Mol Res 2007 Oct 5;6(4):1000-11.
PMID 18058718
Serum markers improve current prediction of metastasis development in early-stage melanoma patients: a machine learning-based study
Mancuso F, Lage S, Rasero J, Díaz-Ramón JL, Apraiz A, Pérez-Yarza G, Ezkurra PA, Penas C, Sánchez-Diez A, García-Vazquez MD, Gardeazabal J, Izu R, Mujika K, Cortés J, Asumendi A, Boyano MD
Mol Oncol 2020 Aug;14(8):1705-1718.
PMID 32485045
Analysis of Y-P30/Dermcidin expression and properties of the Y-P30 peptide
Mikhaylova M, Schumacher A, Borutzki C, Neumann JR, Macharadze T, El-Mousleh T, Wahle P, Zenclussen AC, Kreutz MR
BMC Res Notes 2014 Jun 26;7:400.
PMID 24969620
Role of Ca2+ in proteolysis-inducing factor (PIF)-induced atrophy of skeletal muscle
Mirza KA, Tisdale MJ
Cell Signal 2012 Nov;24(11):2118-22.
PMID 22820507
Genes up- and down-regulated by dermcidin in breast cancer: a microarray analysis
Moreira DF, Strauss BE, Vannier E, Belizário JE
Genet Mol Res 2008 Sep 30;7(3):925-32.
PMID 18949710
Mass Spectrometry Analysis of the Exhaled Breath Condensate and Proposal of Dermcidin and S100A9 as Possible Markers for Lung Cancer Prognosis
Núñez-Naveira L, Mariñas-Pardo LA, Montero-Martínez C
Lung 2019 Aug;197(4):523-531.
PMID 31115649
The primate-specific peptide Y-P30 regulates morphological maturation of neocortical dendritic spines
Neumann JR, Dash-Wagh S, Jack A, Räk A, Jüngling K, Hamad MIK, Pape HC, Kreutz MR, Puskarjov M, Wahle P
PLoS One 2019 Feb 13;14(2):e0211151.
PMID 30759095
The human antimicrobial peptide dermcidin activates normal human keratinocytes
Niyonsaba F, Suzuki A, Ushio H, Nagaoka I, Ogawa H, Okumura K
Br J Dermatol 2009 Feb;160(2):243-9.
PMID 19014393
Vitronectin and dermcidin serum levels predict the metastatic progression of AJCC I-II early-stage melanoma
Ortega-Martínez I, Gardeazabal J, Erramuzpe A, Sanchez-Diez A, Cortés J, García-Vázquez MD, Pérez-Yarza G, Izu R, Luís Díaz-Ramón J, de la Fuente IM, Asumendi A, Boyano MD
Int J Cancer 2016 Oct 1;139(7):1598-607.
PMID 27216146
HIV induces both a down-regulation of IRAK-4 that impairs TLR signalling and an up-regulation of the antibiotic peptide dermcidin in monocytic cells
Pathak S, De Souza GA, Salte T, Wiker HG, Asjö B
Scand J Immunol 2009 Sep;70(3):264-76.
PMID 19703016
Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat
Paulmann M, Arnold T, Linke D, Özdirekcan S, Kopp A, Gutsmann T, Kalbacher H, Wanke I, Schuenemann VJ, Habeck M, Bürck J, Ulrich AS, Schittek B
J Biol Chem 2012 Mar 9;287(11):8434-43.
PMID 22262861
A neural survival factor is a candidate oncogene in breast cancer
Porter D, Weremowicz S, Chin K, Seth P, Keshaviah A, Lahti-Domenici J, Bae YK, Monitto CL, Merlos-Suarez A, Chan J, Hulette CM, Richardson A, Morton CC, Marks J, Duyao M, Hruban R, Gabrielson E, Gelman R, Polyak K
Proc Natl Acad Sci U S A 2003 Sep 16;100(19):10931-6.
PMID 12953101
The Role of Dermcidin in the Diagnosis and Staging of Hepatocellular Carcinoma
Qiu F, Qiu F, Liu L, Liu J, Xu J, Huang X
Genet Test Mol Biomarkers 2018 Apr;22(4):218-223.
PMID 29641283
Insulin resistance in prostate cancer patients and predisposing them to acute ischemic heart disease
Ray U, Bank S, Jayawardana MW, Bhowmik J, Redwig F, Jana P, Bhattacharya S, Manna E, Kumar De S, Maiti S, Roberts-Thomson P, Parameswaran V, Sinha AK
Biosci Rep 2019 Jul 29;39(7):BSR20182313.
PMID 31300527
Dermcidin is constitutively produced by eccrine sweat glands and is not induced in epidermal cells under inflammatory skin conditions
Rieg S, Garbe C, Sauer B, Kalbacher H, Schittek B
Br J Dermatol 2004 Sep;151(3):534-9.
PMID 15377337
Generation of multiple stable dermcidin-derived antimicrobial peptides in sweat of different body sites
Rieg S, Seeber S, Steffen H, Humeny A, Kalbacher H, Stevanovic S, Kimura A, Garbe C, Schittek B
J Invest Dermatol 2006 Feb;126(2):354-65.
PMID 16374474
Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo
Rieg S, Steffen H, Seeber S, Humeny A, Kalbacher H, Dietz K, Garbe C, Schittek B
J Immunol 2005 Jun 15;174(12):8003-10.
PMID 15944307
Role of reactive oxygen species in protein degradation in murine myotubes induced by proteolysis-inducing factor and angiotensin II
Russell ST, Eley H, Tisdale MJ
Cell Signal 2007 Aug;19(8):1797-806.
PMID 17532611
Detection of dermcidin for sweat identification by real-time RT-PCR and ELISA
Sakurada K, Akutsu T, Fukushima H, Watanabe K, Yoshino M
Forensic Sci Int 2010 Jan 30;194(1-3):80-4.
PMID 19914015
The multiple facets of dermcidin in cell survival and host defense
Schittek B
J Innate Immun 2012;4(4):349-60.
PMID 22455996
Dermcidin: a novel human antibiotic peptide secreted by sweat glands
Schittek B, Hipfel R, Sauer B, Bauer J, Kalbacher H, Stevanovic S, Schirle M, Schroeder K, Blin N, Meier F, Rassner G, Garbe C
Nat Immunol 2001 Dec;2(12):1133-7.
PMID 11694882
Neuroprotective effects of the survival promoting peptide Y-P30
Schneeberg J, Riek-Burchardt M, Braun H, Landgraf P, Kreutz MR, Reymann KG
Eur J Pharmacol 2009 Aug 15;616(1-3):81-5.
PMID 19490911
Proteomic analysis of human cervico-vaginal fluid
Shaw JL, Smith CR, Diamandis EP
J Proteome Res 2007 Jul;6(7):2859-65.
PMID 17567164
Identification of Dermcidin as a novel binding protein of Nck1 and characterization of its role in promoting cell migration
Shen SL, Qiu FH, Dayarathna TK, Wu J, Kuang M, Li SS, Peng BG, Nie J
Biochim Biophys Acta 2011 Jun;1812(6):703-10.
PMID 21397687
Whole-genome expression profiling of the melanoma progression pathway reveals marked molecular differences between nevi/melanoma in situ and advanced-stage melanomas
Smith AP, Hoek K, Becker D
Cancer Biol Ther 2005 Sep;4(9):1018-29.
PMID 16251803
Crystal structure and functional mechanism of a human antimicrobial membrane channel
Song C, Weichbrodt C, Salnikov ES, Dynowski M, Forsberg BO, Bechinger B, Steinem C, de Groot BL, Zachariae U, Zeth K
Proc Natl Acad Sci U S A 2013 Mar 19;110(12):4586-91.
PMID 23426625
Naturally processed dermcidin-derived peptides do not permeabilize bacterial membranes and kill microorganisms irrespective of their charge
Steffen H, Rieg S, Wiedemann I, Kalbacher H, Deeg M, Sahl HG, Peschel A, Götz F, Garbe C, Schittek B
Antimicrob Agents Chemother 2006 Aug;50(8):2608-20.
PMID 16870749
The dermcidin gene in cancer: role in cachexia, carcinogenesis and tumour cell survival
Stewart GD, Skipworth RJ, Ross JA, Fearon KCh, Baracos VE
Curr Opin Clin Nutr Metab Care 2008 May;11(3):208-13.
PMID 18403914
The presence of the proteolysis-inducing factor in urine does not predict the malignancy of a pancreatic tumour
Teich N, Kleeff J, Lochs H, Mössner J, Keim V, Friess H, Ockenga J
BMC Gastroenterol 2005 Jun 21;5:20.
PMID 15969757
Characterization of a cancer cachectic factor
Todorov P, Cariuk P, McDevitt T, Coles B, Fearon K, Tisdale M
Nature 1996 Feb 22;379(6567):739-42.
PMID 8602222
Identification and characterization of a membrane receptor for proteolysis-inducing factor on skeletal muscle
Todorov PT, Wyke SM, Tisdale MJ
Cancer Res 2007 Dec 1;67(23):11419-27.
PMID 18056470
Seriniquinone, a selective anticancer agent, induces cell death by autophagocytosis, targeting the cancer-protective protein dermcidin
Trzoss L, Fukuda T, Costa-Lotufo LV, Jimenez P, La Clair JJ, Fenical W
Proc Natl Acad Sci U S A 2014 Oct 14;111(41):14687-92.
PMID 25271322
Expression and clinicopathologic significance of proteolysis-inducing factor in non-small-cell lung cancer: an immunohistochemical analysis
Wang Q, Lu JB, Wu B, Hao LY
Clin Lung Cancer 2010 Sep 1;11(5):346-51.
PMID 20837461
Expression of the human cachexia-associated protein (HCAP) in prostate cancer and in a prostate cancer animal model of cachexia
Wang Z, Corey E, Hass GM, Higano CS, True LD, Wallace D, Tisdale MJ, Vessella RL
Int J Cancer 2003 May 20;105(1):123-9.
PMID 12672042
Is there a human homologue to the murine proteolysis-inducing factor?
Wieland BM, Stewart GD, Skipworth RJ, Sangster K, Fearon KC, Ross JA, Reiman TJ, Easaw J, Mourtzakis M, Kumar V, Pak BJ, Calder K, Filippatos G, Kremastinos DT, Palcic M, Baracos VE
Clin Cancer Res 2007 Sep 1;13(17):4984-92.
PMID 17785548
Characteristics of patients with pancreatic cancer expressing a novel cancer cachectic factor
Wigmore SJ, Todorov PT, Barber MD, Ross JA, Tisdale MJ, Fearon KC
Br J Surg 2000 Jan;87(1):53-8.
PMID 10606911
Induction of proteasome expression in skeletal muscle is attenuated by inhibitors of NF-kappaB activation
Wyke SM, Russell ST, Tisdale MJ
Br J Cancer 2004 Nov 1;91(9):1742-50.
PMID 15477867
NF-kappaB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle
Wyke SM, Tisdale MJ
Br J Cancer 2005 Feb 28;92(4):711-21.
PMID 15714207
Post-translation modification of proteins in tears
You J, Fitzgerald A, Cozzi PJ, Zhao Z, Graham P, Russell PJ, Walsh BJ, Willcox M, Zhong L, Wasinger V, Li Y
Electrophoresis 2010 Jun;31(11):1853-61.
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Dermcidin: what is its antibiotic potential?
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Future Microbiol 2013 Jul;8(7):817-9.
PMID 23841626
The Human Antimicrobial Peptides Dermcidin and LL-37 Show Novel Distinct Pathways in Membrane Interactions
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Front Chem 2017 Nov 7;5:86.
PMID 29164103
Dermcidin as a novel binding protein of lncRNA STCAT3 and its effect on prognosis in gastric cancer
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This paper should be referenced as such :
Hirata AS, Miguel RA, Jimenez PC, Costa-Lotufo LV
DCD (dermcidin)
Atlas Genet Cytogenet Oncol Haematol. 2021;25(2)73-82.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)DCD   14669
Entrez_Gene (NCBI)DCD    dermcidin
AliasesAIDD; DCD-1; DSEP; HCAP; 
GeneCards (Weizmann)DCD
Ensembl hg19 (Hinxton)ENSG00000161634 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000161634 [Gene_View]  ENSG00000161634 [Sequence]  chr12:54644589-54648365 [Contig_View]  DCD [Vega]
ICGC DataPortalENSG00000161634
TCGA cBioPortalDCD
Genatlas (Paris)DCD
SOURCE (Princeton)DCD
Genetics Home Reference (NIH)DCD
Genomic and cartography
GoldenPath hg38 (UCSC)DCD  -     chr12:54644589-54648365 -  12q13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)DCD  -     12q13.2   [Description]    (hg19-Feb_2009)
GoldenPathDCD - 12q13.2 [CytoView hg19]  DCD - 12q13.2 [CytoView hg38]
Genome Data Viewer NCBIDCD [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF144011 AY590150 BC062682 BC069108 BP313072
RefSeq transcript (Entrez)NM_001300854 NM_053283
Consensus coding sequences : CCDS (NCBI)DCD
Gene ExpressionDCD [ NCBI-GEO ]   DCD [ EBI - ARRAY_EXPRESS ]   DCD [ SEEK ]   DCD [ MEM ]
Gene Expression Viewer (FireBrowse)DCD [ Firebrowse - Broad ]
GenevisibleExpression of DCD in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)117159
GTEX Portal (Tissue expression)DCD
Human Protein AtlasENSG00000161634-DCD [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP81605   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP81605  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP81605
Catalytic activity : Enzyme3.4.-.- [ Enzyme-Expasy ]   3.4.-.-3.4.-.- [ IntEnz-EBI ]   3.4.-.- [ BRENDA ]   3.4.-.- [ KEGG ]   [ MEROPS ]
Domains : Interpro (EBI)Dermcidin    Dermcidin/Lacritin   
Domain families : Pfam (Sanger)Dermcidin (PF15291)   
Domain families : Pfam (NCBI)pfam15291   
Conserved Domain (NCBI)DCD
PDB (RSDB)2KSG    2NDK    2YMK    6SHK   
PDB Europe2KSG    2NDK    2YMK    6SHK   
PDB (PDBSum)2KSG    2NDK    2YMK    6SHK   
PDB (IMB)2KSG    2NDK    2YMK    6SHK   
Structural Biology KnowledgeBase2KSG    2NDK    2YMK    6SHK   
SCOP (Structural Classification of Proteins)2KSG    2NDK    2YMK    6SHK   
CATH (Classification of proteins structures)2KSG    2NDK    2YMK    6SHK   
AlphaFold pdb e-kbP81605   
Human Protein Atlas [tissue]ENSG00000161634-DCD [tissue]
Protein Interaction databases
IntAct (EBI)P81605
Ontologies - Pathways
Ontology : AmiGORNA binding  protein binding  extracellular region  extracellular region  extracellular region  proteolysis  peptidase activity  antimicrobial humoral response  defense response to bacterium  defense response to fungus  killing by host of symbiont cells  extracellular exosome  
Ontology : EGO-EBIRNA binding  protein binding  extracellular region  extracellular region  extracellular region  proteolysis  peptidase activity  antimicrobial humoral response  defense response to bacterium  defense response to fungus  killing by host of symbiont cells  extracellular exosome  
REACTOMEP81605 [protein]
REACTOME PathwaysR-HSA-6803157 [pathway]   
NDEx NetworkDCD
Atlas of Cancer Signalling NetworkDCD
Wikipedia pathwaysDCD
Orthology - Evolution
GeneTree (enSembl)ENSG00000161634
Phylogenetic Trees/Animal Genes : TreeFamDCD
Homologs : HomoloGeneDCD
Homology/Alignments : Family Browser (UCSC)DCD
Gene fusions - Rearrangements
Fusion : QuiverDCD
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDCD [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DCD
Exome Variant ServerDCD
GNOMAD BrowserENSG00000161634
Varsome BrowserDCD
ACMGDCD variants
Genomic Variants (DGV)DCD [DGVbeta]
DECIPHERDCD [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisDCD 
ICGC Data PortalDCD 
TCGA Data PortalDCD 
Broad Tumor PortalDCD
OASIS PortalDCD [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDCD  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DDCD
Mutations and Diseases : HGMDDCD
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)DCD
DoCM (Curated mutations)DCD
CIViC (Clinical Interpretations of Variants in Cancer)DCD
NCG (London)DCD
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry DCD
NextProtP81605 [Medical]
Target ValidationDCD
Huge Navigator DCD [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDDCD
Pharm GKB GenePA27171
Clinical trialDCD
DataMed IndexDCD
PubMed138 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Oct 8 21:15:58 CEST 2021

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