Overview of the Human **LYPD2** Gene and Protein
OpenAI
o3-deep-research-2025-06-26
68 citations
2025-11-03T21:38:32.395770
Overview of the Human LYPD2 Gene and Protein
LYPD2 (Ly6/PLAUR domain containing 2), also known by a previous symbol LYPDC2, is a human gene located on chromosome 8q24.3, within a cluster of Ly6/uPAR family genes (pmc.ncbi.nlm.nih.gov). It encodes a small protein (125 amino acids, ~13 kDa) that belongs to the Ly6 superfamily, characterized by the Ly6/uPAR (LU) domain (pmc.ncbi.nlm.nih.gov). Like other Ly6-family members, LYPD2 is produced with an N-terminal signal peptide and is attached to the cell surface via a glycosylphosphatidylinositol (GPI) anchor (www.genecards.org) (v16.proteinatlas.org). This means the mature protein is localized to the extracellular face of the plasma membrane, anchored to the lipid bilayer but lacking a transmembrane segment (www.genecards.org). Consistently, Gene Ontology annotations place LYPD2 in the extracellular region and as an anchored component of the membrane (www.genecards.org) (v16.proteinatlas.org). Some LYPD2 may also be released on membrane-derived vesicles (exosomes), in line with its GPI-anchored cell-surface localization (v16.proteinatlas.org).
Structurally, the LYPD2 protein contains a single LU domain with 10 conserved cysteine residues in a characteristic spacing (pmc.ncbi.nlm.nih.gov). These cysteines form multiple disulfide bonds, stabilizing a “three-finger” fold – a tertiary structure first observed in snake venom neurotoxins and shared by many Ly6 superfamily proteins (pmc.ncbi.nlm.nih.gov). This three-fingered LU domain is a hallmark of Ly6/PLAUR proteins and is thought to mediate protein–protein interactions on the cell surface (pmc.ncbi.nlm.nih.gov). Indeed, a common theme in this family is the ability to bind other molecules (such as receptors or ligands) through the LU domain’s surface loops, despite the protein’s small size and lack of enzymatic activity (pmc.ncbi.nlm.nih.gov).
Expression Profile and Localization in Tissues
LYPD2 is expressed in a tissue-selective manner, primarily in stratified squamous epithelia. RNA sequencing analyses indicate high expression in the esophagus, where LYPD2 transcripts exceed 250 TPM (transcripts per million) in normal tissue (pmc.ncbi.nlm.nih.gov). It is also expressed in keratinized epithelia of the skin and in the vaginal epithelium, though at more modest levels (on the order of a few tens of TPM) (pmc.ncbi.nlm.nih.gov). Data from the Human Protein Atlas classify LYPD2 as “tissue-enhanced” in esophagus (and also in tonsil, which contains oropharyngeal epithelium) (www.genecards.org). Consistent with the mRNA data, immunohistochemistry shows that LYPD2 protein is present in epidermal keratinocytes: in skin, keratinocytes show moderate LYPD2 staining, whereas adjacent cell types (e.g. melanocytes or Langerhans cells) do not express this protein (v19.proteinatlas.org). This points to a role for LYPD2 in epithelial cell function, especially in barrier tissues like the skin and mucosa.
Notably, the suprabasal layers of stratified epithelium (such as those in skin and esophagus) are likely sites of LYPD2 action, paralleling the expression pattern of related proteins. For example, the neighboring gene SLURP1 (another Ly6 family member) is also produced by suprabasal keratinocytes and is involved in epidermal differentiation (pmc.ncbi.nlm.nih.gov). LYPD2’s high expression in the esophagus and skin – tissues subject to constant environmental exposure – suggests it could play a part in surface defense, cell–cell signaling, or structural organization in these tissues. Its presence on the cell surface via a GPI anchor means it can readily interact with extracellular molecules or with receptors on adjacent cells.
Molecular Function and Biological Role
Despite clear information on its structure and where it’s expressed, the precise biological function of LYPD2 remains poorly characterized. As of recent reviews, “no known or proposed function” has been experimentally confirmed for LYPD2 (pmc.ncbi.nlm.nih.gov). It is not an enzyme (thus no catalytic reaction or substrate can be assigned), nor is it a transporter. Instead, LYPD2 is thought to act as an accessory or modulatory protein at the cell surface. This inference comes from its membership in the Ly6/PLAUR family, whose proteins often influence cell signaling or adhesion. Indeed, Ly6 family proteins generally fall into two functional categories: cell-adhesion molecules or signaling modulators (pmc.ncbi.nlm.nih.gov). Some murine Ly6 proteins (e.g. Ly6A/E) mediate cell–cell adhesion by binding partners on adjacent cells (pmc.ncbi.nlm.nih.gov), whereas others – including several human Ly6 orthologs – modulate neurotransmitter receptors (pmc.ncbi.nlm.nih.gov).
A well-known example is LYNX1, a GPI-anchored Ly6 protein in neurons that binds nicotinic acetylcholine receptors (nAChRs) to modulate their activity. Similarly, SLURP1 and SLURP2, two secreted Ly6-family proteins expressed in skin and immune cells, function as endogenous ligands for acetylcholine receptors (pmc.ncbi.nlm.nih.gov) (www.genecards.org). SLURP1 is a soluble modulator of alpha-7 nAChRs in the skin and has tumor suppressor effects in squamous cells (pmc.ncbi.nlm.nih.gov). SLURP2, the protein most closely related to LYPD2 by sequence, is also secreted by keratinocytes and has been shown in vitro to bind and influence both nicotinic and muscarinic acetylcholine receptors (www.genecards.org). Specifically, SLURP2 can inhibit acetylcholine-evoked currents through certain neuronal nAChR subtypes (α3β2, α4β2) and modulate α7-containing receptors, as well as alter signaling of muscarinic receptors like M1 and M3 (www.genecards.org). These paralogous proteins regulate keratinocyte proliferation, differentiation, and inflammation via cholinergic pathways (www.genecards.org).
By analogy, it is hypothesized that LYPD2 could partake in similar cholinergic or cell–signaling pathways in epithelial tissues, perhaps by interacting with a cell-surface receptor. However, it must be emphasized that no direct interaction or target of LYPD2 has been identified in experiments to date (pmc.ncbi.nlm.nih.gov). There is currently no biochemical evidence that LYPD2 binds to nicotinic acetylcholine receptors, integrins, growth factor receptors, or any other specific ligand. The lack of a known binding partner or activity means that LYPD2’s molecular function is still undefined in the literature (pmc.ncbi.nlm.nih.gov). Its role is essentially inferred from family characteristics: the LU domain and GPI anchoring suggest it could function as a ligand-like molecule that influences receptor signaling or as an adhesive scaffold on the cell surface (pmc.ncbi.nlm.nih.gov). For instance, one could speculate that LYPD2 helps organize epithelial cell junctions or modulates signaling in the skin’s nicotinic receptor network (since epidermal keratinocytes do express cholinergic receptors for autocrine signaling). Yet until targeted studies are done, these remain conjectures. In line with this, mouse knock-out studies have not reported any striking phenotype for the Lypd2 gene — in fact, a mouse homologous gene analysis noted no experimental evidence for its function (www.informatics.jax.org).
Pathways and Biological Processes
Given the unknown specific function, no dedicated signaling or metabolic pathway has been assigned to LYPD2. It is not part of any well-defined enzyme cascade or transporter system. Instead, LYPD2 is broadly associated with the “post-translational modification: synthesis of GPI-anchored proteins” pathway, simply because it undergoes GPI attachment in the endoplasmic reticulum and Golgi before reaching the cell surface (www.genecards.org). This indicates that, like other GPI-anchored proteins, LYPD2 traffics through the secretory pathway and is tethered to the membrane via a glycolipid, a process governed by the general GPI biosynthesis and attachment machinery (www.genecards.org).
In terms of biological processes, high-throughput gene expression analyses provide some clues. LYPD2’s elevated expression in differentiating keratinocytes and in epithelial layers hints at involvement in epidermal differentiation or barrier function. For example, SLURP1 (a paralog in the same cluster) is a known marker of late epidermal differentiation and contributes to skin barrier integrity (pmc.ncbi.nlm.nih.gov). Deficiency of SLURP1 in humans causes Mal de Meleda, a severe palmoplantar keratoderma with compromised skin barrier (pmc.ncbi.nlm.nih.gov). LYPD2 lies in the same genomic neighborhood as SLURP1 (and SLURP2), and these genes are co-expressed in the skin, raising the possibility that LYPD2 could also support normal keratinocyte function. Interestingly, in a mouse model where Slurp2 was knocked out, researchers noted that expression of Lypd2 in skin was modestly reduced (~35% lower than normal) (pmc.ncbi.nlm.nih.gov). This co-regulation (both Slurp1 and Lypd2 were down-regulated in Slurp2 knockout skin) suggests that these genes may share regulatory pathways or respond to similar signals in the tissue (pmc.ncbi.nlm.nih.gov). For instance, inflammatory cytokines or differentiation cues might coordinately control multiple Ly6-family genes in keratinocytes. Indeed, SLURP2 itself is known to be up-regulated by cytokines like IL-22 in psoriatic skin, as part of the response in inflammatory skin disease (www.genecards.org). It is plausible that LYPD2 may also be induced or repressed under certain conditions (such as inflammation or stress in epithelial tissues), although specific evidence for LYPD2 in skin disorders is lacking. To date, no direct link between LYPD2 and a human disease or a distinct physiological process has been published.
One area of interest is whether LYPD2 has any role in cancer or could serve as a biomarker. Ly6 family genes have been examined in oncology because several are differentially expressed in tumors. For example, PSCA (Prostate Stem Cell Antigen) and others in the Ly6 family are overexpressed in certain carcinomas (prostate, bladder, ovarian, some skin cancers) and have been studied as tumor-associated antigens (pmc.ncbi.nlm.nih.gov). A recent comprehensive analysis of the human Ly6 superfamily (2023) looked at expression patterns in uterine endometrial carcinoma and other cancers. In that study, most LY6 genes were found to have altered expression in tumors or prognostic value, but LYPD2 stood out as an outlier with no significant change in expression between normal and cancerous endometrial tissue (pmc.ncbi.nlm.nih.gov). LYPD2 mRNA levels were essentially similar in endometrial carcinoma versus normal endometrium, and no prognostic impact was noted (pmc.ncbi.nlm.nih.gov). Moreover, the authors highlighted that LYPD2 is one of the family members with no known functional annotation at present (pmc.ncbi.nlm.nih.gov). This suggests that unlike some Ly6 proteins (e.g., LY6E or LYPD3) that have been implicated in cancer cell signaling or metastasis, LYPD2 has not been linked to cancer-related processes, at least so far. It may simply be a tissue-specific molecule with a niche role that has not yet been discovered.
Expert Perspectives and Current Research
Expert reviews on the Ly6 superfamily underscore that proteins like LYPD2 likely participate in intercellular communication despite their small size and lack of enzymatic domains. Bamezai and colleagues (2023) note that all Ly6/PLAUR proteins share the LU domain and tend to function in one of a few ways: contributing to cell adhesion, signaling, or immune modulation (pmc.ncbi.nlm.nih.gov). They emphasize that in humans, Ly6 family members are found in diverse tissues (immune cells, epithelia, neurons) where they often regulate receptor signaling – for instance, regulation of nicotinic acetylcholine receptors is a recurrent theme for multiple Ly6 proteins (pmc.ncbi.nlm.nih.gov). This is an important contextual insight: it means that although LYPD2’s specific role is unconfirmed, scientists suspect it could modulate a receptor on the surface of keratinocytes or associated cells. Acetylcholine signaling is one plausible avenue, given that keratinocytes respond to cholinergic signals during differentiation and inflammation, and other Ly6 proteins (like SLURP-1 and -2) act in that pathway (www.genecards.org). Another possibility is that LYPD2 could interact with components of the extracellular matrix or with cell-surface adhesion molecules, thereby influencing how keratinocytes adhere and communicate. For example, the GPI-anchored Ly6 protein LYPD3 (also called C4.4A) binds to laminin in the extracellular matrix and has been shown to promote carcinoma cell migration and invasion (pmc.ncbi.nlm.nih.gov). If LYPD2 has a comparable function, it might bind a ligand on neighboring cells or in the matrix to stabilize cell–cell or cell–matrix contacts in epithelial layers. However, no such interaction for LYPD2 has been reported in the literature as of 2024.
From a research standpoint, LYPD2 was initially identified in genomic and proteomic surveys of secreted and membrane proteins. For instance, the Secreted Protein Discovery Initiative (SPDI) and the Mammalian Gene Collection projects in the early 2000s cloned LYPD2 cDNA as a novel putative secreted or membrane-tethered protein (sinoprot.com). These large-scale efforts provided the first sequences of LYPD2, but did not determine its function. Subsequent high-throughput studies (e.g. expression profiling) have catalogued LYPD2’s presence in certain tissues and cell types. Yet, targeted investigations are still needed. No knockout or overexpression functional studies specific to LYPD2 were found in the current literature, and there are no known ligands or inhibitors for this protein. Given its marked expression in esophagus and skin, one avenue of ongoing research is to explore LYPD2’s role in conditions affecting those tissues – for example, inflammatory skin diseases or esophageal disorders. It is notable that LYPD2’s gene neighbors SLURP1 and SLURP2 are involved in skin homeostasis (mutations in SLURP1 cause skin disease, and SLURP2 is up-regulated in psoriasis) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This raises the question of whether LYPD2 might also be induced in diseases like psoriasis or atopic dermatitis; in large transcriptomic studies of psoriasis, various keratinocyte genes including some Ly6 family members are dysregulated, but LYPD2 has not been prominently featured in published gene lists to date. Researchers may also consider LYPD2 as part of the mucosal immune interface, since tonsil (a lympho-epithelial organ) shows elevated LYPD2 expression. Its regulation by immune signaling is an open question.
In summary, LYPD2 is a cell-surface, GPI-anchored protein of the Ly6/uPAR family predominantly expressed in stratified epithelia (esophagus, skin, etc.). It has the structural capacity to mediate protein–protein interactions via its disulfide-bonded LU domain, but its biological function remains unelucidated in current scientific literature (pmc.ncbi.nlm.nih.gov). It does not catalyze reactions or transport molecules, but instead likely serves a modulatory role – possibly in intercellular signaling or adhesion – akin to other Ly6 family proteins. The protein localizes to the extracellular membrane surface (www.genecards.org), positioning it to influence signaling pathways at the cell-environment interface. While no specific pathway or target has been confirmed for LYPD2, experts speculate that it could modulate receptor signaling (such as nicotinic acetylcholine signaling in keratinocytes) or contribute to maintaining epithelial integrity, given its co-expression with other skin-related Ly6 proteins (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Current research has yet to provide direct evidence, and LYPD2 remains an intriguing protein with functional annotation largely inferred from homologs and bioinformatic predictions. As of 2023-2024, authoritative sources highlight the need for further studies to determine what LYPD2 “does,” since it is one of the few Ly6 family members with no assigned function despite clear tissue-specific expression (pmc.ncbi.nlm.nih.gov). Unlocking its role will likely involve biochemical binding assays to identify interaction partners, and genetic models (e.g. tissue-specific knockouts) to reveal any physiological phenotype. Until then, LYPD2 stands as a protein of unknown function (PUF) – a reminder of how even well-conserved protein families can harbor members whose roles in human biology are still enigmatic.
References:
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Rathbun LA et al. (2023). Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma. Oncotarget 14:426-437. PMID: 37141412 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).
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Human Protein Atlas (2022). LYPD2 protein expression and localization. Available from proteinatlas.org (www.genecards.org) (v19.proteinatlas.org).
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Alliance of Genome Resources (2025). Gene ontology report for LYPD2. (Accessed via GeneCards summary) (www.genecards.org) (v16.proteinatlas.org).
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Bamezai AK & Miwa JM (2023). Biology of Ly-6 supergene family (Editorial). Front. Immunol. 14:1182915. doi:10.3389/fimmu.2023.1182915 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).
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Tsuji H et al. (2003). SLURP-2, a novel member of the human Ly6 superfamily that is up-regulated in psoriasis vulgaris. Genomics 81(1):26-33. PMID: 12573258.
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Arredondo J et al. (2007). Immune system expression of SLURP-1 and SLURP-2, two endogenous nicotinic acetylcholine receptor ligands. Life Sci. 80(24-25):2365-2369. PMID: 17234279 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).
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Lyukmanova EN et al. (2016). Secreted Ly6/uPAR protein SLURP1 is an allosteric antagonist of nicotinic acetylcholine receptors. PLoS ONE 11(2):e0149733. PMID: 26905431.
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Chimienti F et al. (2003). Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda. Hum. Mol. Genet. 12(22):3017-3024. PMID: 145323 thirty-two. (Mutations in SLURP1 causing skin disease; context for Ly6 proteins in epidermis) (pmc.ncbi.nlm.nih.gov).
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Adeyo O et al. (2014). Palmoplantar keratoderma in Slurp1-deficient mice: a model for Mal de Meleda. J Invest Dermatol. 134(7):1988-1991. PMID: 24469795.
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Allan CM et al. (2016). Palmoplantar keratoderma in Slurp2-deficient mice. J Invest Dermatol. 136(2):436-443. PMID: 26967477 (pmc.ncbi.nlm.nih.gov).
(The above references provide context and evidence for LYPD2’s known properties and the general functions of related Ly6 family proteins. Key data points – such as expression levels, structural features, and the absence of a defined function – are drawn from recent high-quality sources including a 2023 review (pmc.ncbi.nlm.nih.gov) and protein databases (www.genecards.org). This comprehensive overview synthesizes current knowledge (up to 2024) about LYPD2 and highlights the gaps to be addressed by future research.)
Citations
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- AnnotationURLCitation(end_index=11161, start_index=11002, title='Lypd2 MGI Mouse Gene Detail - MGI:1915561 - Ly6/Plaur domain containing 2', type='url_citation', url='https://www.informatics.jax.org/marker/MGI%3A1915561#:~:text=No%20experimental%20evidence%20to%20support,templated%20transcription')
- AnnotationURLCitation(end_index=11758, start_index=11631, title='LYPD2 Gene - GeneCards | LYPD2 Protein | LYPD2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LYPD2#:~:text=LYPD2%20,of%20this%20gene%20is%20SLURP1')
- AnnotationURLCitation(end_index=12113, start_index=11986, title='LYPD2 Gene - GeneCards | LYPD2 Protein | LYPD2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LYPD2#:~:text=LYPD2%20,of%20this%20gene%20is%20SLURP1')
- AnnotationURLCitation(end_index=12662, start_index=12528, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=SLURP1%20%20,Late%20differentiation%20marker%20in')
- AnnotationURLCitation(end_index=12943, start_index=12785, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=SLURP1%2C%20a%20member%20of%20the,They%20also%20exhibited%20reduced%20body')
- AnnotationURLCitation(end_index=13459, start_index=13310, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=%28Adeyo%20et%20al,%E2%88%92%2F%E2%88%92%7D%20mice%20%28Fig.%203a')
- AnnotationURLCitation(end_index=13803, start_index=13654, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=%28Adeyo%20et%20al,%E2%88%92%2F%E2%88%92%7D%20mice%20%28Fig.%203a')
- AnnotationURLCitation(end_index=14213, start_index=14085, title='SLURP2 Gene - GeneCards | SLUR2 Protein | SLUR2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=SLURP2#:~:text=,provided%20by%20RefSeq%2C%20Sep%202017')
- AnnotationURLCitation(end_index=15130, start_index=14957, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=19%2C%20in%20addition%20to%20chromosome,domain%2C%20which%20consists%20of%206%E2%80%9310')
- AnnotationURLCitation(end_index=15686, start_index=15508, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=PLAUR%2C%20LY6E%2C%20SLURP1%2C%20LYPD6%2C%20and,LY6G6F%2C%20LYPD4%2C%20GPIHBP1%2C%20and%20GML')
- AnnotationURLCitation(end_index=15996, start_index=15818, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=PLAUR%2C%20LY6E%2C%20SLURP1%2C%20LYPD6%2C%20and,LY6G6F%2C%20LYPD4%2C%20GPIHBP1%2C%20and%20GML')
- AnnotationURLCitation(end_index=16262, start_index=16121, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=LYPD2%20%20,known%20or%20proposed%20function%20available')
- AnnotationURLCitation(end_index=17144, start_index=16986, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=expressed%20on%20immune%20and%20non,examining%20the%20function%20of%20LY6')
- AnnotationURLCitation(end_index=17578, start_index=17420, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=expressed%20on%20immune%20and%20non,examining%20the%20function%20of%20LY6')
- AnnotationURLCitation(end_index=18150, start_index=17994, title='SLURP2 Gene - GeneCards | SLUR2 Protein | SLUR2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=SLURP2#:~:text=Binds%20and%20may%20modulate%20the,CHRM1%20and%20CHRM3%2C%20in%20an')
- AnnotationURLCitation(end_index=18691, start_index=18533, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=expressed%20on%20immune%20and%20non,examining%20the%20function%20of%20LY6')
- AnnotationURLCitation(end_index=19406, start_index=19283, title='H484 | Ly6/PLAUR Domain Containing Protein 2 (LYPD2) | SinoProt', type='url_citation', url='https://sinoprot.com/items/H484#:~:text=,2270%282003%29%20%5BPubMed%5D%20%5BEurope%20PMC%5D%20%5BAbstract')
- AnnotationURLCitation(end_index=20378, start_index=20254, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=In%20mammals%2C%20SLURP1%20is%20not,2006')
- AnnotationURLCitation(end_index=20551, start_index=20379, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=SLURP2%20was%20initially%20identified%20as,Ly6%20protein%20that%20shuttles%20lipoprotein')
- AnnotationURLCitation(end_index=21572, start_index=21431, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=LYPD2%20%20,known%20or%20proposed%20function%20available')
- AnnotationURLCitation(end_index=21948, start_index=21820, title='LYPD2 Gene - GeneCards | LYPD2 Protein | LYPD2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LYPD2#:~:text=,of%20Genome%20Resources%2C%20Jun%202025')
- AnnotationURLCitation(end_index=22493, start_index=22335, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=expressed%20on%20immune%20and%20non,examining%20the%20function%20of%20LY6')
- AnnotationURLCitation(end_index=22643, start_index=22494, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=%28Adeyo%20et%20al,%E2%88%92%2F%E2%88%92%7D%20mice%20%28Fig.%203a')
- AnnotationURLCitation(end_index=23203, start_index=23062, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=LYPD2%20%20,known%20or%20proposed%20function%20available')
- AnnotationURLCitation(end_index=23956, start_index=23815, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=LYPD2%20%20,known%20or%20proposed%20function%20available')
- AnnotationURLCitation(end_index=24115, start_index=23957, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=expressed%20on%20immune%20and%20non,examining%20the%20function%20of%20LY6')
- AnnotationURLCitation(end_index=24355, start_index=24227, title='LYPD2 Gene - GeneCards | LYPD2 Protein | LYPD2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LYPD2#:~:text=,of%20Genome%20Resources%2C%20Jun%202025')
- AnnotationURLCitation(end_index=24513, start_index=24356, title='Tissue expression of LYPD2 - Staining in skin - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000197353-LYPD2/tissue/skin#:~:text=Keratinocytes%3A%20Medium%20Langerhans%3A%20Not%20detected,i')
- AnnotationURLCitation(end_index=24751, start_index=24623, title='LYPD2 Gene - GeneCards | LYPD2 Protein | LYPD2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LYPD2#:~:text=,of%20Genome%20Resources%2C%20Jun%202025')
- AnnotationURLCitation(end_index=24883, start_index=24752, title='Tissue expression of LYPD2 - Summary - The Human Protein Atlas', type='url_citation', url='https://v16.proteinatlas.org/ENSG00000197353/tissue#:~:text=Protein%20evidence%20,extracellular%20exosome')
- AnnotationURLCitation(end_index=25205, start_index=25030, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=chromosomal%20location%2C%20the%20LY6%20proteins,reported%20to%20possess%20cell%20adhesion')
- AnnotationURLCitation(end_index=25364, start_index=25206, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=expressed%20on%20immune%20and%20non,examining%20the%20function%20of%20LY6')
- AnnotationURLCitation(end_index=25852, start_index=25728, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=In%20mammals%2C%20SLURP1%20is%20not,2006')
- AnnotationURLCitation(end_index=26025, start_index=25853, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=SLURP2%20was%20initially%20identified%20as,Ly6%20protein%20that%20shuttles%20lipoprotein')
- AnnotationURLCitation(end_index=26654, start_index=26496, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=SLURP1%2C%20a%20member%20of%20the,They%20also%20exhibited%20reduced%20body')
- AnnotationURLCitation(end_index=27110, start_index=26961, title='Palmoplantar keratoderma in Slurp2-deficient mice - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4789766/#:~:text=%28Adeyo%20et%20al,%E2%88%92%2F%E2%88%92%7D%20mice%20%28Fig.%203a')
- AnnotationURLCitation(end_index=27566, start_index=27425, title='Human LY6 gene family: potential tumor-associated antigens and biomarkers of prognosis in uterine corpus endometrial carcinoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10159366/#:~:text=LYPD2%20%20,known%20or%20proposed%20function%20available')
- AnnotationURLCitation(end_index=27717, start_index=27589, title='LYPD2 Gene - GeneCards | LYPD2 Protein | LYPD2 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=LYPD2#:~:text=,of%20Genome%20Resources%2C%20Jun%202025')