MICA (MHC class I polypeptide-related sequence A)

2014-07-01   Zain Ahmed , Medhat Askar 

Cleveland Clinic\\\/, Cleveland, OH; askarm@ccf.org


Atlas Image
Figure 1: Chromosomal location of MICA genes shown on a map of the MHC on chromosome 6p21.3 (not to scale). Chromosome 6 [Drawing modified from the National Library of Medicine, the National Center for Biotechnology Information public website (2013)]


Human Major Histocompatibility Complex (MHC) Class I Chain-Related gene A (MICA) is located 46 Kb centromeric to the HLA-B locus on the short arm of human chromosome 6 and encodes for a 62-kda cell surface glycoprotein. It is expressed on endothelial cells, dendritic cells, fibroblasts, epithelial cells, and many tumours and serves as target for both cellular and humoral immune responses in transformed cells. MICA protein at normal states has a low level of expression in epithelial tissues but is upregulated in response to various stimuli of cellular stress. MICA also functions as a ligand recognized by the activating receptor NKG2D that is expressed on the surface of NK, NKT, CD8+ and TCRγδ+ T cells. Allelic variants of MICA due to a single amino acid substitution at position 129 in the α2 domain have been reported to result in large differences in NKG2D binding. These variable affinities have been suggested to affect thresholds of NK cell triggering and T cell modulation in autoimmune diseases and malignancies. MICA molecules exist also in soluble forms (sMICA) and altered serum levels of sMICA have been reported in multiple states of health and disease.


Atlas Image
Figure 2: The MICA gene spans a 11,720-bp stretch of DNA was located 46,445 bp centromeric of the HLA-B locus on the short arm of human chromosome 6 (Mizuki et al., 1997).


The MICA gene was described in 1994 among a group of genes within the MHC class I region (Bahram et al., 1994). It is a member of the MIC gene family, which consists of 7 members (MICA-MICG). MICA is classified as a non-classical MHC class I gene as opposed to classical MHC class I genes encoding the commonly known Human Leukocyte Antigen (HLA) proteins. Similar to the HLA genes, the MICA gene is highly polymorphic. One hundred alleles have been reported (according to IMGT Release 3.17.0, 2014-07-14), with new alleles being continuously described and added to the database. As such it is significantly less polymorphic than HLA loci A (2,884 alleles), B (3,589), C (2,375), DRB1 (1,540), DQB1 (664), and DPB1 (422). However, MICA is more polymorphic than HLA loci G (50), DRB3 (58), DRB4 (15), DRB5 (20), DRA (7), DQA1 (52), DPA1 (38), and its closely related MICB gene (40) (Robinson et al., 2013).
MICA gene is organized into 7 exons of which exon 5 encodes the transmembrane (TM) region of the MICA molecule. TM encodes the repeat polymorphism (GCT/Ala) and eight types of repeats have been described as A4, A5, A5.1, A6, A7, A8, A9, and A10 (Gambelunghe et al., 2006; Zou et al., 2006). The combinations of extracellular and TM types facilitates the identification of the MICA alleles and reduces the number of potential ambiguous typings in heterozygous individuals. This combination identifies MICA alleles based on polymorphisms in the TM region as well as elsewhere, e.g., MICA*007:01/A4, MICA*008:01/A5.1, etc.


MICA gene encodes 383 amino acids polypeptide. MICA is up-regulated on human endothelial cells by the pro-inflammatory cytokine TNFα. This up-regulation is controlled at the transcriptional level by a master regulatory control element positioned 130-base pair (bp) upstream of the MICA transcription start site integrating input from the NF-kB and heat shock pathways (Lin et al., 2012).


Of the MIC gene family, only MICA and MICB are true genes with protein products while the remaining (MICC-MICG) are pseudogenes.



Due to synonymous substitutions being the only differences among some of the MICA alleles, the 100 MICA alleles encode for only 79 distinct proteins. Two of the MICA alleles are null alleles with no expressed protein products. MICA molecules are considered non-classical MHC class I molecules rather than human leukocyte antigens (HLA) since they are not expressed on the surface of human leukocytes. Nevertheless they are expressed on endothelial cells, dendritic cells, fibroblasts, epithelial cells, and many tumors and serve as targets for both cellular and humoral immune responses (Bahram et al., 1994; Zou and Stastny, 2010). MICA protein at normal states has a low level of expression in epithelial tissues but is upregulated in many tumors and under various stimuli of cellular stress including heat shock proteins (Groh et al., 1996). Similar to MHC class I, MICA molecules have 3 extracellular immunoglobulin-like domains, a transmembrane domain and intracellular cytoplasmic tail. However, unlike class I, MICA is not covalently bound a monomorphic β2 microglobulin and its peptide binding groove is empty and does not present peptides (Figure 3).
Allelic variants of MICA based on a single amino acid substitution at position 129 in the α2 domain have been reported to result in large differences in the affinity of binding to the activating natural killer group 2, member D (NKG2D) (Steinle et al., 2001). MICA alleles with a methionine (M) or valine (V) have been classified as having strong or weak binding affinity for NKG2D, respectively. These variable affinities have been suggested to affect thresholds of NK cell triggering and T cell modulation and consequently influencing clinical phenotypes in autoimmune disorders and malignancies (Amroun et al., 2005; Douik et al., 2009).
MICA molecules exist also in soluble forms (sMICA) encompassing three extracellular domains (Salih et al., 2002). ADAM, a disintegrin and metalloproteinase, is reported to mediate sMICA generation by cleavage of the molecule in the α3 domain close to the papain cleavage site (Figure X), however the precise location of the cleavage site is still unknown (Waldhauer et al., 2008). sMICA are not normally detected in sera of healthy donors and tumor cells are the major source of sMICA generation (Holdenrieder et al., 2006). In addition to patients with malignancies, sMICA is detected in the sera of patients with autoimmune diseases, acute bacterial infections, renal insufficiency, and cholestasis (Holdenrieder et al., 2007). Unlike the surface-bound form of MICA that stimulates immune responses, the secreted soluble counterpart, sMICA abates immune responses primarily by down regulating NKG2D expression which impairs the cellular cytotoxicity of T cells and NK cells against tumor cells (Groh et al., 2002). This may partly explain why higher levels of sMICA were observed in the serum of chronically infected individuals compared to healthy controls and HIV-1 controllers (Nolting et al., 2010). Similarly CMV infection triggers shedding of sMICA (Andresen et al., 2009).
Atlas Image
Figure 3: Diagram of comparison among HLA-Class I, MICA and sMICA molecules


383 amino acids in length (including the 23 amino acids leader sequence that is lost from the 360 amino acid mature protein), 42,915 Da protein, undergoes N-glycoslation as post-translational modification, although not required to interact with NKG2D. MICA has three external (α1, α2, α3), a transmembrane and an intracytoplasmic domains (figure 4).
Atlas Image
Figure 4: The amino acid sequence of the full length MICA molecule. Source: IMGT/HLA online database (Robinson et al., 2013)


Co-dominantly and constitutively expressed on cell membranes of human epithelial, endothelial, fibroblasts cells, keratinocytes, monocytes, dendritic cells, thymic medulla, and gastrointestinal epithelial cells but not on the surface of other healthy cells (Zwirner et al., 1999). Activated CD4+ and CD8+ T cells are shown to express MICA. Nuclear factor (NF)-kB regulates MICA expression on activated T lymphocytes by binding to a specific sequence in the long intron 1 of the MICA gene (Molinero et al., 2004). MICA expression is also up-regulated on stressed cells, tumour cells, and pathogen-infected cells (Mistry and OCallaghan, 2007). Its noteworthy that in vitro CMV infection strongly induces expression of MICA (Groh et al., 2001). Similarly, respiratory syncytial virus (RSV) infection of epithelial cells up-regulated cell surface expression of MICA and levels of soluble MICA (Zdrenghea et al., 2012). It is also reported that CMV induced expression on the surface of fibroblasts is skewed towards a common form of MICA (A5.1), which has a nucleotide insertion in exon 5 corresponding to the transmembrane region and no cytoplasmic tail and less activation of the NKG2D pathway (Zou et al., 2005).
Atlas Image
Figure 5: A phylogram of the genetic distance between HLA class I consensus sequence, MICA and MICB reference alleles. This Phylogram considers only amino acid sequence of the Mature Protein excluding the 23 amino acids leader sequence in MICA and MICB reference sequences and 24 amino acids leader sequence in the Class I consensus sequence due to lack of consensus among leader sequences of loci HLA-A, B, and C


Cell surface as a single-pass type 1 membrane protein


Like other MHC Class I molecules, MICA is a highly polymorphic MHC Class I molecule expressed on the cell surface of cells mentioned above. However, unlike other classical MHC Class I molecules, MICA is not involved in antigen presentation because its peptide-binding groove is too narrow to present antigens and is not associated with β2-microglobulin (Groh et al., 1996). MICA is expressed under cellular stress and is a ligand for NKG2D receptor expressed on surface of NK, NKT, CD8+ and TCRγδ T cells (Bauer et al., 1999). NKG2D binding results in up-regulation of MICA and ultimately cytotoxicity and release of IFN? by NKG2D-expressing cells.
Atlas Image
Figure 6: Sequence alignment between MICA (MICA*001) and MICB (MICB*001) reference sequences. This alignment considers the Full Length Protein including the 23 amino acids leader sequence that is lost in the mature protein


Searching the non-redundant protein sequences (nr) database for the protein sequences similar to the MICA reference amino acid sequence (MICA*001) using Blastp (protein-protein BLAST) tool publicly available from the website of The National Center for Biotechnology Information (https://blast.ncbi.nlm.nih.gov/Blast) showed that the closest protein sequences are MICB followed by MHC class I (Wheeler and Bhagwat, 2007). The phylogenetic distance among these 3 sequences as determined by the online ClustalW2 (version CLUSTAL 2.1) Multiple Sequence Alignments tool publicly available at the website of the European Bioinformatics Institute of the European Molecular Biology Laboratory (EMBL-EBI) (http://www.ebi.ac.uk/Tools/msa/clustalw2/) is shown in figure (5) (McWilliam et al., 2013). Aligning MICA *001 and MICB reference amino acid sequence (MICB *001) using the same ClustalW2 tool yields scores of 83.03% sequence identity (Figure 6). Similarly alignment of MICA*001 and HLA class I consensus amino acid sequence yielded an identity score of 26.47% between (Figure 7).
Atlas Image
Figure 6: Sequence alignment between MICA reference sequence (MICA*001) and HLA Class I consensus sequence. This alignment considers only the Mature Protein excluding the 23 amino acids leader sequence in MICA reference sequence and 24 amino acids leader sequence in the Class I consensus sequence due to lack of consensus among leader sequences of loci HLA-A, B, and C



Similar to HLA genes, each allelic variant of MICA is given a distinct name that is officiated by the WHO Nomenclature Committee for Factors of the HLA System. The following are the 100 recognized MICA alleles (according to IMGT Release 3.17.0, 2014-07-14): MICA*001, MICA*002:01, MICA*002:02, MICA*002:03, MICA*002:04, MICA*004, MICA*005, MICA*006, MICA*007:01, MICA*007:02, MICA*007:03, MICA*007:04, MICA*007:05, MICA*007:06, MICA*008:01:01, MICA*008:01:02, MICA*008:02, MICA*008:03, MICA*008:04, MICA*008:05, MICA*009:01, MICA*009:02, MICA*010:01, MICA*010:02, MICA*011, MICA*012:01, MICA*012:02, MICA*012:03, MICA*012:04, MICA*013, MICA*014, MICA*015, MICA*016, MICA*017, MICA*018:01, MICA*018:02, MICA*019, MICA*020, MICA*022, MICA*023, MICA*024, MICA*025, MICA*026, MICA*027, MICA*028, MICA*029, MICA*030, MICA*031, MICA*032, MICA*033, MICA*034, MICA*035, MICA*036, MICA*037, MICA*038, MICA*039, MICA*040, MICA*041, MICA*042, MICA*043, MICA*044, MICA*045, MICA*046, MICA*047, MICA*048, MICA*049, MICA*050, MICA*051, MICA*052, MICA*053, MICA*054, MICA*055, MICA*056, MICA*057, MICA*058, MICA*059, MICA*060, MICA*061, MICA*062, MICA*063N, MICA*064N, MICA*065, MICA*066, MICA*067, MICA*068, MICA*069, MICA*070, MICA*072, MICA*073, MICA*074, MICA*075, MICA*076, MICA*077, MICA*078, MICA*079, MICA*080, MICA*081, MICA*082, MICA*083, MICA*084 (Robinson et al., 2013).

Implicated in

Entity name
MICA genotypes MICA5.0/5.1 were associated with autoimmune type 1 diabetes with onset during pregnancy (Torn et al., 2004). On the other hand sMIC molecules released from the placenta is considered as a possible immune escape mechanism important for fetal survival (Mincheva-Nilsson et al., 2006). sMIC was also reported as a novel blood biomarker of the chances of a viable baby in infertile women undergoing in vitro fertilization (Porcu-Buisson et al., 2007). Consistent with these reports is the finding of reduced production of sMICA by the aged placenta playing a role in parturition (Huang et al., 2011).
Entity name
MICA 129 M/V dimorphism with variable NKG2D binding affinities has been reported to affect thresholds of NK cell triggering and T cell modulation in malignancies (Douik et al., 2009). In cancer patients, elevated sMICA levels are significantly correlated with cancer stage, differentiation, and metastasis (Holdenrieder et al., 2006). MICA is also expressed in abundance in large granular lymphocyte leukemia cells. Neutrophil counts were inversely correlated with MICA expression and MICA*00801/A5.1 was reported in higher frequency in patients with large granular lymphocyte leukemia (Viny et al., 2010).
Entity name
Graft versus host disease (GVHD)
GVHD is an immunological disorder that affects many organ systems, including the gastrointestinal tract, liver, skin, and lungs and results from donor-host disparities in major and minor histocompatibility antigens following solid organs and hematopoietic stem cell transplantation (Ferrara et al., 2009; Sharma et al., 2012).
GVHD remains a significant hurdle in overcoming the morbidity and mortality associated with hematopoietic stem cell transplantation (Dhir et al., 2014).
Because of its genomic location between MHC Class I and Class II genes, there is strong linkage disequilibrium between many MICA and HLA-B alleles. MICA could also serve as a genetic marker of recombination between MHC classes I and II in otherwise MHC matched individuals where MICA mismatched individuals would be predicted to have mismatched haplotypes whereas the MICA matched pairs may or may not be haplotype matched. This distinction is biologically relevant since MHC haplotype mismatching in otherwise HLA matched donor/recipient pairs was reported in association with a statistically significantly increased risk of severe acute GvHD (Petersdorf et al., 2007). Donor/recipient MICA mismatches were associated with increased risk of severe acute GVHD and were also reported to have a synergistic effect with HLA-DPB1 mismatches on the risk of severe acute GVHD (Askar et al., 2012). MICA-129 genotype, sMICA, and anti-MICA antibodies were reported as biomarkers of chronic GVHD (Boukouaci et al., 2009).
Entity name
Allograft rejection
MICA mismatch is associated with presence of MICA antibodies in serum of solid organ transplant recipient, which in turn is associated with acute rejection. Anti-MICA sera can bind to endothelial cells from MICA A5.1 donors. Thus, MICA A5.1 can potentially serve as an alloantigen and possibly mediate an alloimmune response. Transplant recipients can also develop donor-specific antibodies to MICA. MICA DSA were associated with decreased graft function.
Presensitization of kidney-transplant recipients to MICA antigens was reported in association with an increased frequency of graft loss and was suggested to contribute to allograft loss among recipients who are otherwise well matched for HLA (Zou et al., 2007).
Donor MICA A5.1 mismatch is associated with anti-MICA antibody formation and increased proteinuria in kidney recipients. MICA*001,*004, *007, *009, *012, and *018 are more prevalent in patients with impaired renal function than normal function.
Entity name
Psoriasis is a disease of the skin characterized by chronic inflammation leading to scaly plaques.
MICA transmembrane (MICA-TM) A9 allele is associated with increased susceptibility to psoriasis in Asian populations (Song et al., 2014).
Entity name
Psoriatic arthritis
Psoriastic arthritis is a seronegative inflammatory arthritis that develops in a more than 10% of patients with psoriasis. Like other seronegative spondyloarthropathies, psoriastic arthritis is associated with HLA-B27 allele.
Psoriastic arthritis tends not to be as serve as rheumatoid arthritis in joint destruction.
MICA-TM A9 allele is associated with a PsA susceptibility in European populations (Amroun H et. al, 2005).
Since MICA is located 46 kb centromeric to the HLA-B gene cluster, its location may explain its association.
Entity name
Ankylosing spondylitis (AS)
Ankylosing spondylitis is a seronegative spondyloarthropathies associated with HLA-B27 allele. AS is characterized by chronic inflammation of joints typically in the axial skeleton, such as spine and sacroiliac joints, leading to destruction of cartilage and ultimately bony ankylosis causing severe joint immobility. AS is also characterized by extraarticular manifestations including uveitis, aortitis, and amyloidosis.
MICA alleles are associated with AS in both HLA-B27-positive and B27-negative AS patients. The MICA*007:01 allele is associated with increased susceptibility to AS in Caucasian and Han Chinese populations. The MICA*019 allele increases the risk for AS in Chinese patients. In a small cohort study of of Algerian patients with AS, MICA-129 allele was associated with an early onset of AS (Tong, 2013).
Entity name
Systemic lupus erythematosus (SLE)
Poor (Susceptibility)
Polymorphisms of MICA TM region have been reported in association with susceptibility to SLE (Yoshida et al., 2011).
Entity name
Hepatitis B and C
There is an association of MICA rs2596542G/A promoter variant and substitutions MICA-129Met/Val, MICA-251Gln/Arg, MICA-175Gly/Ser with HBV-induced hepatocellular carcinoma and HBV persistence (Kumar V, 2012).
Hepatitis B and C are viral infections that can chronically predispose to hepatocellular carcinoma. MICA genetic variations and soluble MICA levels may serve as predictive biomarker for HBV- and HCV-induced HCC. Expression of MICA may be induced by the stress of viral infection and play a role in tumor immune surveillance (Kumar V, 2012).
Poor. HBV-induced HCC patients with the high serum level of sMICA have shown to have worse prognosis than those with low serum level of sMICA (?5 pg/ml).5
A single nucleotide polymorphism of MICA rs2596542 located in MICA promotor region is associated with hepatitis C-induced HCC in a Japanese patients and serum levels of soluble MICA (sMICA).


Pubmed IDLast YearTitleAuthors
163866472005Early-onset ankylosing spondylitis is associated with a functional MICA polymorphism.Amroun H et al
195535472009Propionic acid secreted from propionibacteria induces NKG2D ligand expression on human-activated T lymphocytes and cancer cells.Andresen L et al
80227711994A second lineage of mammalian major histocompatibility complex class I genes.Bahram S et al
104269931999Activation of NK cells and T cells by NKG2D, a receptor for stress-inducible MICA.Bauer S et al
197866162009MICA-129 genotype, soluble MICA, and anti-MICA antibodies as biomarkers of chronic graft-versus-host disease.Boukouaci W et al
250166132014Recent advances in the management of graft-versus-host disease.Dhir S et al
190007292009Association of MICA-129 polymorphism with nasopharyngeal cancer risk in a Tunisian population.Douik H et al
192820262009Graft-versus-host disease.Ferrara JL et al
171747502006MICA A8: a new allele within MHC class I chain-related A transmembrane region with eight GCT repeats.Gambelunghe G et al
89016011996Cell stress-regulated human major histocompatibility complex class I gene expressed in gastrointestinal epithelium.Groh V et al
112245262001Costimulation of CD8alphabeta T cells by NKG2D via engagement by MIC induced on virus-infected cells.Groh V et al
123847022002Tumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation.Groh V et al
160946212006Soluble MICA in malignant diseases.Holdenrieder S et al
214263092011The alteration of placental-derived soluble MHC class I chain-related protein A and B during pregnancy.Huang SY et al
230247572012Soluble MICA and a MICA variation as possible prognostic biomarkers for HBV-induced hepatocellular carcinoma.Kumar V et al
221700632012NF-κB regulates MICA gene transcription in endothelial cell through a genetically inhibitable control site.Lin D et al
236713382013Analysis Tool Web Services from the EMBL-EBI.McWilliam H et al
165177272006Placenta-derived soluble MHC class I chain-related molecules down-regulate NKG2D receptor on peripheral blood mononuclear cells during human pregnancy: a possible novel immune escape mechanism for fetal survival.Mincheva-Nilsson L et al
176148772007Regulation of ligands for the activating receptor NKG2D.Mistry AR et al
91777761997Nucleotide sequence analysis of the HLA class I region spanning the 237-kb segment around the HLA-B and -C genes.Mizuki N et al
154945082004NF-kappa B regulates expression of the MHC class I-related chain A gene in activated T lymphocytes.Molinero LL et al
206675782010MHC class I chain-related protein A shedding in chronic HIV-1 infection is associated with profound NK cell dysfunction.Nolting A et al
173786972007MHC haplotype matching for unrelated hematopoietic cell transplantation.Petersdorf EW et al
175868362007Soluble MHC Class I chain-related molecule serum levels are predictive markers of implantation failure and successful term pregnancies following IVF.Porcu-Buisson G et al
230801222013The IMGT/HLA database.Robinson J et al
123703362002Cutting edge: down-regulation of MICA on human tumors by proteolytic shedding.Salih HR et al
232743342012Graft-versus-host disease after solid organ transplantation: a single center experience and review of literature.Sharma A et al
239744322014Associations between the major histocompatibility complex class I chain-related gene A transmembrane (MICA-TM) polymorphism and susceptibility to psoriasis and psoriatic arthritis: a meta-analysis.Song GG et al
114915312001Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family.Steinle A et al
156038712004Different HLA-DR-DQ and MHC class I chain-related gene A (MICA) genotypes in autoimmune and nonautoimmune gestational diabetes in a Swedish population.Törn C et al
204606362010MICA polymorphism identified by whole genome array associated with NKG2D-mediated cytotoxicity in T-cell large granular lymphocyte leukemia.Viny AD et al
186768622008Tumor-associated MICA is shed by ADAM proteases.Waldhauer I et al
179936722007BLAST QuickStart: example-driven web-based BLAST tutorial.Wheeler D et al
217020102011Role of the MICA polymorphism in systemic lupus erythematosus.Yoshida K et al
218523312012RSV infection modulates IL-15 production and MICA levels in respiratory epithelial cells.Zdrenghea MT et al
157285252005Effect of human cytomegalovirus on expression of MHC class I-related chains A.Zou Y et al
166984362006MICA allele-level typing by sequence-based typing with computerized assignment of polymorphic sites and short tandem repeats within the transmembrane region.Zou Y et al
178980982007Antibodies against MICA antigens and kidney-transplant rejection.Zou Y et al
103637231999Differential surface expression of MICA by endothelial cells, fibroblasts, keratinocytes, and monocytes.Zwirner NW et al

Other Information

Locus ID:

NCBI: 100507436
MIM: 600169
HGNC: 7090
Ensembl: ENSG00000204520


dbSNP: 100507436
ClinVar: 100507436
TCGA: ENSG00000204520


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
Natural killer cell mediated cytotoxicityKEGGko04650
Natural killer cell mediated cytotoxicityKEGGhsa04650
Immune SystemREACTOMER-HSA-168256
Adaptive Immune SystemREACTOMER-HSA-1280218
Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cellREACTOMER-HSA-198933


Pubmed IDYearTitleCitations
123847022002Tumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation.436
127144932003Functional expression and release of ligands for the activating immunoreceptor NKG2D in leukemia.133
174959322007Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands.109
186768622008Tumor-associated MICA is shed by ADAM proteases.105
146628962003Evasion from NK cell immunity by MHC class I chain-related molecules expressing colon adenocarcinoma.87
182021752008MHC class I chain-related protein A antibodies and shedding are associated with the progression of multiple myeloma.86
199131212009Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.85
172023582007Promoter region architecture and transcriptional regulation of the genes for the MHC class I-related chain A and B ligands of NKG2D.74
125695592003Expression and role of MICA and MICB in human hepatocellular carcinomas and their regulation by retinoic acid.69
175702102007CD4+NKG2D+ T cells in Crohn's disease mediate inflammatory and cytotoxic responses through MICA interactions.69


Zain Ahmed ; Medhat Askar

MICA (MHC class I polypeptide-related sequence A)

Atlas Genet Cytogenet Oncol Haematol. 2014-07-01

Online version: http://atlasgeneticsoncology.org/gene/41364/mica