DMP1

Protein identityUniProt · HPA

UniProt accession

Q13316

Gene

DMP1

Ensembl

ENSG00000152592

Chromosome

4

Canonical length

513 aa

Protein class

Disease related genes, Human disease related genes, Predicted secreted proteins

Secretome location

Secreted to extracellular matrix

OverviewNCBI Gene

Dentin matrix acidic phosphoprotein is an extracellular matrix protein and a member of the small integrin binding ligand N-linked glycoprotein family. 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. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

513 residues, UniProt reviewed canonical sequence.

>Q13316|DMP1
     1  MKISILLMFL WGLSCALPVT RYQNNESEDS EEWKGHLAQA PTPPLESSES SEGSKVSSEE
    61  QANEDPSDST QSEEGLGSDD HQYIYRLAGG FSRSTGKGGD DKDDDEDDSG DDTFGDDDSG
   121  PGPKDRQEGG NSRLGSDEDS DDTIQASEES APQGQDSAQD TTSESRELDN EDRVDSKPEG
   181  GDSTQESESE EHWVGGGSDG ESSHGDGSEL DDEGMQSDDP ESIRSERGNS RMNSAGMKSK
   241  ESGENSEQAN TQDSGGSQLL EHPSRKIFRK SRISEEDDRS ELDDNNTMEE VKSDSTENSN
   301  SRDTGLSQPR RDSKGDSQED SKENLSQEES QNVDGPSSES SQEANLSSQE NSSESQEEVV
   361  SESRGDNPDP TTSYVEDQED SDSSEEDSSH TLSHSKSESR EEQADSESSE SLNFSEESPE
   421  SPEDENSSSQ EGLQSHSSSA ESQSEESHSE EDDSDSQDSS RSKEDSNSTE SKSSSEEDGQ
   481  LKNIEIESRK LTVDAYHNKP IGDQDDNDCQ DGY

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against DMP1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.7

Highest tissue expression

0.3 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about DMP1.

Disease | AllUniProt

Conditions DMP1 is implicated in, by any mechanism.

• Hypophosphatemic rickets, autosomal recessive, 1 (ARHR1) MIM:241520

Disease | GeneticClinVar

18 pathogenic / likely-pathogenic of 311 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Hypophosphatemic rickets, autosomal recessive, 1
• Hypophosphatemic rickets

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.14

gnomAD pLI

0

gnomAD missense Z

0.27

DepMap mean gene effect

-0.01

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• biomineral tissue development
• extracellular matrix organization
• ossification
• positive regulation of cell-substrate adhesion
• regulation of enamel mineralization

Molecular functions

• calcium ion binding
• extracellular matrix binding
• integrin binding

Cellular components

• endoplasmic reticulum lumen
• extracellular matrix
• extracellular region
• nucleus

Protein domainsUniProt · Pfam · InterPro

• Dentin matrix 1
• Dentin matrix protein 1 (DMP1)

KeywordsUniProt

• Biomineralization
• Cytoplasm
• Extracellular matrix
• Glycoprotein
• Nucleus
• Phosphoprotein
• Secreted
• Signal