DMP1
Identifiers
Aliases	DMP1, ARHP, ARHR, DMP-1, dentin matrix acidic phosphoprotein 1
External IDs	OMIM: 600980 MGI: 94910 HomoloGene: 68396 GeneCards: DMP1
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q22.1 Start 87,650,280 bp[1] End 87,664,361 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 E5|5 50.61 cM Start 104,350,479 bp[2] End 104,361,968 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in periodontal fiber tibia spongy bone sperm upper respiratory tract sensory nervous system occipital lobe testicle thoracic aorta ascending aorta Top expressed in body of femur fossa molar cochlea calvaria ankle facial motor nucleus condyle otolith organ utricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding integrin binding extracellular matrix binding Cellular component cytoplasm extracellular region nucleus endoplasmic reticulum lumen extracellular matrix Biological process biomineral tissue development extracellular matrix organization ossification positive regulation of cell-substrate adhesion regulation of enamel mineralization post-translational protein modification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1758 13406 Ensembl ENSG00000152592 ENSMUSG00000029307 UniProt Q13316 O55188 RefSeq (mRNA) NM_001079911 NM_004407 NM_016779 NM_001359013 RefSeq (protein) NP_001073380 NP_004398 NP_058059 NP_001345942 Location (UCSC) Chr 4: 87.65 – 87.66 Mb Chr 5: 104.35 – 104.36 Mb PubMed search [3] [4]
Wikidata
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Dentin matrix acidic phosphoprotein 1 is a protein that in humans is encoded by the DMP1 gene.^[5][6][7]

Dentin matrix acidic phosphoprotein is an extracellular matrix protein and a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family (other members being DSPP, IBSP, MEPE, and SPP1). This protein, which is critical for proper mineralization of bone and dentin, is present in diverse cells of bone and tooth tissues. The protein contains a large number of acidic domains, multiple phosphorylation sites, a functional arg-gly-asp cell attachment sequence, and a DNA binding domain. In undifferentiated osteoblasts it is primarily a nuclear protein that regulates the expression of osteoblast-specific genes. During osteoblast maturation the protein becomes phosphorylated and is exported to the extracellular matrix, where it orchestrates mineralized matrix formation. Mutations in the gene are known to cause autosomal recessive hypophosphatemia, a disease that manifests as rickets and osteomalacia. The gene structure is conserved in mammals. Two transcript variants encoding different isoforms have been described for this gene.^[7]