Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dentin matrix acidic phosphoprotein 1

Gene

DMP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite.1 Publication

GO - Molecular functioni

  • calcium ion binding Source: ProtInc
  • extracellular matrix binding Source: Ensembl
  • integrin binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Biomineralization

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.
SignaLinkiQ13316.

Names & Taxonomyi

Protein namesi
Recommended name:
Dentin matrix acidic phosphoprotein 1
Short name:
DMP-1
Short name:
Dentin matrix protein 1
Gene namesi
Name:DMP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:2932. DMP1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Secretedextracellular spaceextracellular matrix 1 Publication

  • Note: In proliferating preosteoblasts it is nuclear, during early maturation stage is cytoplasmic and in mature osteoblast localizes in the mineralized matrix. Export from the nucleus of differentiating osteoblast is triggered by the release of calcium from intracellular stores followed by a massive influx of this pool of calcium into the nucleus.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Extracellular matrix, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Hypophosphatemic rickets, autosomal recessive, 1 (ARHR1)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA hereditary form of hypophosphatemic rickets, a disorder of proximal renal tubule function that causes phosphate loss, hypophosphatemia and skeletal deformities, including rickets and osteomalacia unresponsive to vitamin D. Symptoms are bone pain, fractures and growth abnormalities.

See also OMIM:241520

Organism-specific databases

MIMi241520. phenotype.
Orphaneti289176. Autosomal recessive hypophosphatemic rickets.
PharmGKBiPA27379.

Polymorphism and mutation databases

BioMutaiDMP1.
DMDMi7673998.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 513497Dentin matrix acidic phosphoprotein 1PRO_0000021110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi467 – 4671N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated in the cytosol and extracellular matrix and unphosphorylated in the nucleus. Phosphorylation is necessary for nucleocytoplasmic transport and may be catalyzed by a nuclear isoform of CK2 and can be augmented by calcium. Phosphorylated (in vitro) by FAM20C in the extracellular medium at sites within the S-x-E/pS motif.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ13316.
PRIDEiQ13316.

PTM databases

PhosphoSiteiQ13316.

Expressioni

Tissue specificityi

Expressed in tooth particularly in odontoblast, ameloblast and cementoblast.

Gene expression databases

BgeeiQ13316.
CleanExiHS_DMP1.
GenevisibleiQ13316. HS.

Organism-specific databases

HPAiHPA037465.

Interactioni

Subunit structurei

Interacts with importin alpha.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000340935.

Structurei

3D structure databases

ProteinModelPortaliQ13316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi364 – 3663Cell attachment siteSequence Analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG86154.
GeneTreeiENSGT00730000111375.
HOGENOMiHOG000220909.
HOVERGENiHBG073257.
InParanoidiQ13316.
OMAiQEGLQSH.
OrthoDBiEOG7F24TN.
PhylomeDBiQ13316.
TreeFamiTF337029.

Family and domain databases

InterProiIPR009889. DMP1.
[Graphical view]
PANTHERiPTHR23400. PTHR23400. 1 hit.
PfamiPF07263. DMP1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13316-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKISILLMFL WGLSCALPVT RYQNNESEDS EEWKGHLAQA PTPPLESSES
60 70 80 90 100
SEGSKVSSEE QANEDPSDST QSEEGLGSDD HQYIYRLAGG FSRSTGKGGD
110 120 130 140 150
DKDDDEDDSG DDTFGDDDSG PGPKDRQEGG NSRLGSDEDS DDTIQASEES
160 170 180 190 200
APQGQDSAQD TTSESRELDN EDRVDSKPEG GDSTQESESE EHWVGGGSDG
210 220 230 240 250
ESSHGDGSEL DDEGMQSDDP ESIRSERGNS RMNSAGMKSK ESGENSEQAN
260 270 280 290 300
TQDSGGSQLL EHPSRKIFRK SRISEEDDRS ELDDNNTMEE VKSDSTENSN
310 320 330 340 350
SRDTGLSQPR RDSKGDSQED SKENLSQEES QNVDGPSSES SQEANLSSQE
360 370 380 390 400
NSSESQEEVV SESRGDNPDP TTSYVEDQED SDSSEEDSSH TLSHSKSESR
410 420 430 440 450
EEQADSESSE SLNFSEESPE SPEDENSSSQ EGLQSHSSSA ESQSEESHSE
460 470 480 490 500
EDDSDSQDSS RSKEDSNSTE SKSSSEEDGQ LKNIEIESRK LTVDAYHNKP
510
IGDQDDNDCQ DGY
Length:513
Mass (Da):55,782
Last modified:January 1, 1998 - v2
Checksum:i2C1FDE319A5D106F
GO
Isoform 2 (identifier: Q13316-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-61: Missing.

Show »
Length:497
Mass (Da):54,115
Checksum:i6E146232B6365507
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691S → C.2 Publications
Corresponds to variant rs10019009 [ dbSNP | Ensembl ].
VAR_030750
Natural varianti117 – 1171D → N in one individual with tumoral calcinosis. 1 Publication
VAR_030751
Natural varianti272 – 2721R → H.1 Publication
Corresponds to variant rs145237146 [ dbSNP | Ensembl ].
VAR_030752
Natural varianti463 – 4631K → R.
Corresponds to variant rs34661425 [ dbSNP | Ensembl ].
VAR_033848

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei46 – 6116Missing in isoform 2. 1 PublicationVSP_004191Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89012 mRNA. Translation: AAC51332.1.
U34037 Genomic DNA. Translation: AAA97602.1.
CH471057 Genomic DNA. Translation: EAX05996.1.
BC130581 mRNA. Translation: AAI30582.1.
BC132865 mRNA. Translation: AAI32866.1.
U65378 mRNA. Translation: AAB87728.1.
CCDSiCCDS3623.1. [Q13316-1]
CCDS43249.1. [Q13316-2]
RefSeqiNP_001073380.1. NM_001079911.2. [Q13316-2]
NP_004398.1. NM_004407.3. [Q13316-1]
UniGeneiHs.652366.

Genome annotation databases

EnsembliENST00000282479; ENSP00000282479; ENSG00000152592. [Q13316-2]
ENST00000339673; ENSP00000340935; ENSG00000152592.
GeneIDi1758.
KEGGihsa:1758.
UCSCiuc003hqv.3. human. [Q13316-1]
uc003hqw.3. human. [Q13316-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89012 mRNA. Translation: AAC51332.1.
U34037 Genomic DNA. Translation: AAA97602.1.
CH471057 Genomic DNA. Translation: EAX05996.1.
BC130581 mRNA. Translation: AAI30582.1.
BC132865 mRNA. Translation: AAI32866.1.
U65378 mRNA. Translation: AAB87728.1.
CCDSiCCDS3623.1. [Q13316-1]
CCDS43249.1. [Q13316-2]
RefSeqiNP_001073380.1. NM_001079911.2. [Q13316-2]
NP_004398.1. NM_004407.3. [Q13316-1]
UniGeneiHs.652366.

3D structure databases

ProteinModelPortaliQ13316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000340935.

PTM databases

PhosphoSiteiQ13316.

Polymorphism and mutation databases

BioMutaiDMP1.
DMDMi7673998.

Proteomic databases

PaxDbiQ13316.
PRIDEiQ13316.

Protocols and materials databases

DNASUi1758.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282479; ENSP00000282479; ENSG00000152592. [Q13316-2]
ENST00000339673; ENSP00000340935; ENSG00000152592.
GeneIDi1758.
KEGGihsa:1758.
UCSCiuc003hqv.3. human. [Q13316-1]
uc003hqw.3. human. [Q13316-2]

Organism-specific databases

CTDi1758.
GeneCardsiGC04P088571.
HGNCiHGNC:2932. DMP1.
HPAiHPA037465.
MIMi241520. phenotype.
600980. gene.
neXtProtiNX_Q13316.
Orphaneti289176. Autosomal recessive hypophosphatemic rickets.
PharmGKBiPA27379.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG86154.
GeneTreeiENSGT00730000111375.
HOGENOMiHOG000220909.
HOVERGENiHBG073257.
InParanoidiQ13316.
OMAiQEGLQSH.
OrthoDBiEOG7F24TN.
PhylomeDBiQ13316.
TreeFamiTF337029.

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.
SignaLinkiQ13316.

Miscellaneous databases

ChiTaRSiDMP1. human.
GeneWikiiDMP1_(gene).
GenomeRNAii1758.
NextBioi7157.
PROiQ13316.
SOURCEiSearch...

Gene expression databases

BgeeiQ13316.
CleanExiHS_DMP1.
GenevisibleiQ13316. HS.

Family and domain databases

InterProiIPR009889. DMP1.
[Graphical view]
PANTHERiPTHR23400. PTHR23400. 1 hit.
PfamiPF07263. DMP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Elucidation of the sequence and the genomic organization of the human dentin matrix acidic phosphoprotein 1 (DMP1) gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II."
    Hirst K.L., Simmons D., Feng J., Aplin H., Dixon M.J., McDougall M.
    Genomics 42:38-45(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Molar.
  2. McDougall M., Juan X., Simmons D., Feng J.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT CYS-69.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Mapping of the human dentin matrix acidic phosphoprotein gene (DMP1) to the dentinogenesis imperfecta type II critical region at chromosome 4q21."
    Aplin H.M., Hirst K.L., Crosby A.H., Dixon M.J.
    Genomics 30:347-349(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-513, GENE MAPPING.
  6. "Dual functional roles of dentin matrix protein 1. Implications in biomineralization and gene transcription by activation of intracellular Ca2+ store."
    Narayanan K., Ramachandran A., Hao J., He G., Park K.W., Cho M., George A.
    J. Biol. Chem. 278:17500-17508(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH IMPORTIN ALPHA.
  7. Cited for: INVOLVEMENT IN ARHR1, VARIANTS CYS-69; ASN-117 AND HIS-272.
  8. "Loss of DMP1 causes rickets and osteomalacia and identifies a role for osteocytes in mineral metabolism."
    Feng J.Q., Ward L.M., Liu S., Lu Y., Xie Y., Yuan B., Yu X., Rauch F., Davis S.I., Zhang S., Rios H., Drezner M.K., Quarles L.D., Bonewald L.F., White K.E.
    Nat. Genet. 38:1310-1315(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ARHR1.
  9. "Secreted kinase phosphorylates extracellular proteins that regulate biomineralization."
    Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A., Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.
    Science 336:1150-1153(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY FAM20C.

Entry informationi

Entry nameiDMP1_HUMAN
AccessioniPrimary (citable) accession number: Q13316
Secondary accession number(s): A1L4L3, O43265
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.