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Protein

Dentin sialophosphoprotein

Gene

DSPP

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

Functioni

DSP may be an important factor in dentinogenesis. DPP may bind high amount of calcium and facilitate initial mineralization of dentin matrix collagen as well as regulate the size and shape of the crystals.

GO - Molecular functioni

  • calcium ion binding Source: ProtInc
  • collagen binding Source: ProtInc
  • extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

  • biomineral tissue development Source: UniProtKB-KW
  • extracellular matrix organization Source: Reactome
  • multicellular organism development Source: ProtInc
  • ossification Source: ProtInc
  • skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Keywords - Ligandi

Calcium, Sialic acid

Enzyme and pathway databases

BioCyciZFISH:ENSG00000152591-MONOMER.
ReactomeiR-HSA-3000178. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Dentin sialophosphoprotein
Cleaved into the following 2 chains:
Alternative name(s):
Dentin phosphophoryn
Short name:
DPP
Dentin sialoprotein
Short name:
DSP
Gene namesi
Name:DSPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3054. DSPP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: Reactome
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal dominant, 39, with dentinogenesis imperfecta 1 (DFNA39/DGI1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by the association of progressive sensorineural high-frequency hearing loss with dentinogenesis imperfecta.
See also OMIM:605594
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01228017P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. 2 PublicationsCorresponds to variant rs121912986dbSNPEnsembl.1
Natural variantiVAR_01228118V → F in DFNA39/DGI1 and DGI3. 2 PublicationsCorresponds to variant rs121912987dbSNPEnsembl.1
Dentinogenesis imperfecta, Shields type 2 (DGI2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry. DSPP defects causing dentin abnormalities act in a dominant negative manner and include missense, splice-site, frameshift mutations. 5' frameshift mutations cause dentin dysplasia while frameshift mutations at the 3' end cause the more severe dentinogenesis imperfecta phenotype (PubMed:18521831 and PubMed:22392858).
Disease descriptionA form of dentinogenesis imperfecta, an autosomal dominant dentin disorder characterized by amber-brown, opalescent teeth that fracture and shed their enamel during mastication, thereby exposing the dentin to rapid wear. Radiographically, the crown appears bulbous and pulpal obliteration is common. The pulp chambers are initially larger than normal prior and immediately after tooth eruption, and then progressively close down to become almost obliterated by abnormal dentin formation. Roots are short and thin. Both primary and permanent teeth are affected. DGI2 is not associated with osteogenesis imperfecta.
See also OMIM:125490
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03686215A → V in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane. 2 PublicationsCorresponds to variant rs121912989dbSNPEnsembl.1
Natural variantiVAR_05444317P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. 3 Publications1
Natural variantiVAR_07025318V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications1
Natural variantiVAR_03066168R → W in DGI2. 2 PublicationsCorresponds to variant rs36094464dbSNPEnsembl.1
Dentinogenesis imperfecta, Shields type 3 (DGI3)3 Publications
The disease is caused by mutations affecting the gene represented in this entry. DSPP defects causing dentin abnormalities act in a dominant negative manner and include missense, splice-site, frameshift mutations. 5' frameshift mutations cause dentin dysplasia while frameshift mutations at the 3' end cause the more severe dentinogenesis imperfecta phenotype (PubMed:18521831 and PubMed:22392858).
Disease descriptionA form of dentinogenesis imperfecta, an autosomal dominant dentin disorder characterized by amber-brown, opalescent teeth that fracture and shed their enamel during mastication, thereby exposing the dentin to rapid wear. Radiographically, the crown appears bulbous and pulpal obliteration is common. The pulp chambers are initially larger than normal prior and immediately after tooth eruption, and then progressively close down to become almost obliterated by abnormal dentin formation. Roots are short and thin. Both primary and permanent teeth are affected. DGI3 teeth typically manifest multiple periapical radiolucencies. DGI3 is not associated with osteogenesis imperfecta.
See also OMIM:125500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07025217P → L in DGI3; the mutant protein is largely retained in the ER. 1 Publication1
Natural variantiVAR_05444317P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. 3 Publications1
Natural variantiVAR_01228118V → F in DFNA39/DGI1 and DGI3. 2 PublicationsCorresponds to variant rs121912987dbSNPEnsembl.1
Dentin dysplasia 2 (DTDP2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. DSPP defects causing dentin abnormalities act in a dominant negative manner and include missense, splice-site, frameshift mutations. 5' frameshift mutations cause dentin dysplasia while frameshift mutations at the 3' end cause the more severe dentinogenesis imperfecta phenotype (PubMed:18521831, PubMed:22392858).2 Publications
Disease descriptionA dental defect in which the deciduous teeth are opalescent. The permanent teeth are of normal shape, form, and color in most cases. The root length is normal. On radiographs, the pulp chambers of permanent teeth are obliterated, have a thistle-tube deformity and contain pulp stones.
See also OMIM:125420
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0368616Y → D in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum. 1 PublicationCorresponds to variant rs121912988dbSNPEnsembl.1

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

DisGeNETi1834.
MalaCardsiDSPP.
MIMi125420. phenotype.
125490. phenotype.
125500. phenotype.
605594. phenotype.
OpenTargetsiENSG00000152591.
Orphaneti99789. Dentin dysplasia type I.
99791. Dentin dysplasia type II.
166260. Dentinogenesis imperfecta type 2.
166265. Dentinogenesis imperfecta type 3.
PharmGKBiPA27507.

Polymorphism and mutation databases

BioMutaiDSPP.
DMDMi215273974.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Sequence analysisAdd BLAST15
ChainiPRO_000002112016 – 1301Dentin sialophosphoproteinAdd BLAST1286
ChainiPRO_000002112116 – 462Dentin sialoproteinAdd BLAST447
ChainiPRO_0000021122463 – 1301Dentin phosphoproteinAdd BLAST839

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...)Sequence analysis1
Glycosylationi49N-linked (GlcNAc...)Sequence analysis1
Glycosylationi81N-linked (GlcNAc...)Sequence analysis1
Glycosylationi130N-linked (GlcNAc...)Sequence analysis1
Glycosylationi150N-linked (GlcNAc...)Sequence analysis1
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1
Glycosylationi191N-linked (GlcNAc...)Sequence analysis1
Glycosylationi209N-linked (GlcNAc...)Sequence analysis1
Glycosylationi222N-linked (GlcNAc...)Sequence analysis1
Modified residuei259Phosphoserine; by CK1Sequence analysis1
Glycosylationi275N-linked (GlcNAc...)Sequence analysis1
Modified residuei301PhosphoserineBy similarity1
Glycosylationi336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi387N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

DSP is glycosylated.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9NZW4.
PRIDEiQ9NZW4.

PTM databases

iPTMnetiQ9NZW4.
PhosphoSitePlusiQ9NZW4.

Miscellaneous databases

PMAP-CutDBA8MUI0.

Expressioni

Tissue specificityi

Expressed in teeth. DPP is synthesized by odontoblast and transiently expressed by pre-ameloblasts.

Gene expression databases

BgeeiENSG00000152591.
CleanExiHS_DSPP.
GenevisibleiQ9NZW4. HS.

Organism-specific databases

HPAiHPA036230.

Interactioni

Subunit structurei

Interacts with FBLN7.By similarity

GO - Molecular functioni

  • collagen binding Source: ProtInc

Protein-protein interaction databases

STRINGi9606.ENSP00000282478.

Structurei

3D structure databases

ProteinModelPortaliQ9NZW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi488 – 490Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi439 – 1301Asp/Ser-richAdd BLAST863

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JAJ8. Eukaryota.
ENOG4111CIV. LUCA.
GeneTreeiENSGT00730000111489.
HOVERGENiHBG098252.
InParanoidiQ9NZW4.
OMAiGNEGNED.
OrthoDBiEOG091G0DJR.
PhylomeDBiQ9NZW4.
TreeFamiTF318563.

Sequencei

Sequence statusi: Complete.

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

Q9NZW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIITYFCIW AVAWAIPVPQ SKPLERHVEK SMNLHLLARS NVSVQDELNA
60 70 80 90 100
SGTIKESGVL VHEGDRGRQE NTQDGHKGEG NGSKWAEVGG KSFSTYSTLA
110 120 130 140 150
NEEGNIEGWN GDTGKAETYG HDGIHGKEEN ITANGIQGQV SIIDNAGATN
160 170 180 190 200
RSNTNGNTDK NTQNGDVGDA GHNEDVAVVQ EDGPQVAGSN NSTDNEDEII
210 220 230 240 250
ENSCRNEGNT SEITPQINSK RNGTKEAEVT PGTGEDAGLD NSDGSPSGNG
260 270 280 290 300
ADEDEDEGSG DDEDEEAGNG KDSSNNSKGQ EGQDHGKEDD HDSSIGQNSD
310 320 330 340 350
SKEYYDPEGK EDPHNEVDGD KTSKSEENSA GIPEDNGSQR IEDTQKLNHR
360 370 380 390 400
ESKRVENRIT KESETHAVGK SQDKGIEIKG PSSGNRNITK EVGKGNEGKE
410 420 430 440 450
DKGQHGMILG KGNVKTQGEV VNIEGPGQKS EPGNKVGHSN TGSDSNSDGY
460 470 480 490 500
DSYDFDDKSM QGDDPNSSDE SNGNDDANSE SDNNSSSRGD ASYNSDESKD
510 520 530 540 550
NGNGSDSKGA EDDDSDSTSD TNNSDSNGNG NNGNDDNDKS DSGKGKSDSS
560 570 580 590 600
DSDSSDSSNS SDSSDSSDSD SSDSNSSSDS DSSDSDSSDS SDSDSSDSSN
610 620 630 640 650
SSDSSDSSDS SDSSDSSDSS DSKSDSSKSE SDSSDSDSKS DSSDSNSSDS
660 670 680 690 700
SDNSDSSDSS NSSNSSDSSD SSDSSDSSSS SDSSNSSDSS DSSDSSNSSE
710 720 730 740 750
SSDSSDSSDS DSSDSSDSSN SNSSDSDSSN SSDSSDSSNS SDSSDSSDSS
760 770 780 790 800
NSSDSSDSSD SSNSSDSSDS SDSSDSSDSS NSSDSNDSSN SSDSSDSSNS
810 820 830 840 850
SDSSNSSDSS DSSDSSDSDS SNSSDSSNSS DSSDSSNSSD SSDSSDSSDG
860 870 880 890 900
SDSDSSNRSD SSNSSDSSDS SDSSNSSDSS DSSDSNESSN SSDSSDSSNS
910 920 930 940 950
SDSDSSDSSN SSDSSDSSNS SDSSESSNSS DNSNSSDSSN SSDSSDSSDS
960 970 980 990 1000
SNSSDSSNSS DSSNSSDSSD SNSSDSSDSS NSSDSSDSSD SSDSSDSSDS
1010 1020 1030 1040 1050
SNSSDSSDSS DSSDSSNSSD SSNSSDSSNS SDSSDSSDSS DSSDSSDSSD
1060 1070 1080 1090 1100
SSDSSNSSDS SDSSDSSDSS DSSDSSDSSD SSESSDSSDS SNSSDSSDSS
1110 1120 1130 1140 1150
DSSDSSDSSD SSDSSDSSDS SNSSDSSDSS DSSDSSDSSN SSDSSDSSES
1160 1170 1180 1190 1200
SDSSDSSDSS DSSDSSDSSD SSDSSDSSNS SDSSDSSDSS DSSDSSDSSD
1210 1220 1230 1240 1250
SSDSSDSSDS SDSSDSSDSS DSSDSSDSSD SNESSDSSDS SDSSDSSNSS
1260 1270 1280 1290 1300
DSSDSSDSSD STSDSNDESD SQSKSGNGNN NGSDSDSDSE GSDSNHSTSD

D
Length:1,301
Mass (Da):131,151
Last modified:November 25, 2008 - v2
Checksum:iE0D86B52F5E53D05
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti673D → DSSDSSS in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti734 – 739Missing in AAF42472 (PubMed:10706475).Curated6
Sequence conflicti799N → D in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti836S → C in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti850G → S in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti875N → NSSD in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti960S → G in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1002N → D in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1022S → G in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1029N → D in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1029N → D in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1044D → N in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1050D → N in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1056N → D in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1056N → D in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1062D → G in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1077D → E in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1083E → D in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1083E → D in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1090 – 1140Missing in AAF42472 (PubMed:10706475).CuratedAdd BLAST51
Sequence conflicti1090 – 1140Missing in AAD16120 (PubMed:9879917).CuratedAdd BLAST51
Sequence conflicti1143D → E in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1149E → D in AAF42472 (PubMed:10706475).Curated1
Sequence conflicti1152D → N in AAD16120 (PubMed:9879917).Curated1
Sequence conflicti1180S → R in AAD16120 (PubMed:9879917).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0368616Y → D in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum. 1 PublicationCorresponds to variant rs121912988dbSNPEnsembl.1
Natural variantiVAR_03686215A → V in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane. 2 PublicationsCorresponds to variant rs121912989dbSNPEnsembl.1
Natural variantiVAR_07025217P → L in DGI3; the mutant protein is largely retained in the ER. 1 Publication1
Natural variantiVAR_05444317P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. 3 Publications1
Natural variantiVAR_01228017P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. 2 PublicationsCorresponds to variant rs121912986dbSNPEnsembl.1
Natural variantiVAR_07025318V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications1
Natural variantiVAR_01228118V → F in DFNA39/DGI1 and DGI3. 2 PublicationsCorresponds to variant rs121912987dbSNPEnsembl.1
Natural variantiVAR_03066168R → W in DGI2. 2 PublicationsCorresponds to variant rs36094464dbSNPEnsembl.1
Natural variantiVAR_047551243D → N.Corresponds to variant rs3750025dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF163151 Genomic DNA. Translation: AAF42472.1.
AC093895 Genomic DNA. No translation available.
AF094508 mRNA. Translation: AAD16120.1.
CCDSiCCDS43248.1.
RefSeqiNP_055023.2. NM_014208.3.
UniGeneiHs.678914.

Genome annotation databases

EnsembliENST00000282478; ENSP00000282478; ENSG00000152591.
ENST00000399271; ENSP00000382213; ENSG00000152591.
GeneIDi1834.
KEGGihsa:1834.
UCSCiuc003hqu.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF163151 Genomic DNA. Translation: AAF42472.1.
AC093895 Genomic DNA. No translation available.
AF094508 mRNA. Translation: AAD16120.1.
CCDSiCCDS43248.1.
RefSeqiNP_055023.2. NM_014208.3.
UniGeneiHs.678914.

3D structure databases

ProteinModelPortaliQ9NZW4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000282478.

PTM databases

iPTMnetiQ9NZW4.
PhosphoSitePlusiQ9NZW4.

Polymorphism and mutation databases

BioMutaiDSPP.
DMDMi215273974.

Proteomic databases

PaxDbiQ9NZW4.
PRIDEiQ9NZW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282478; ENSP00000282478; ENSG00000152591.
ENST00000399271; ENSP00000382213; ENSG00000152591.
GeneIDi1834.
KEGGihsa:1834.
UCSCiuc003hqu.3. human.

Organism-specific databases

CTDi1834.
DisGeNETi1834.
GeneCardsiDSPP.
HGNCiHGNC:3054. DSPP.
HPAiHPA036230.
MalaCardsiDSPP.
MIMi125420. phenotype.
125485. gene.
125490. phenotype.
125500. phenotype.
605594. phenotype.
neXtProtiNX_Q9NZW4.
OpenTargetsiENSG00000152591.
Orphaneti99789. Dentin dysplasia type I.
99791. Dentin dysplasia type II.
166260. Dentinogenesis imperfecta type 2.
166265. Dentinogenesis imperfecta type 3.
PharmGKBiPA27507.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JAJ8. Eukaryota.
ENOG4111CIV. LUCA.
GeneTreeiENSGT00730000111489.
HOVERGENiHBG098252.
InParanoidiQ9NZW4.
OMAiGNEGNED.
OrthoDBiEOG091G0DJR.
PhylomeDBiQ9NZW4.
TreeFamiTF318563.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000152591-MONOMER.
ReactomeiR-HSA-3000178. ECM proteoglycans.

Miscellaneous databases

GeneWikiiDentin_sialophosphoprotein_(gene).
GenomeRNAii1834.
PMAP-CutDBA8MUI0.
PROiQ9NZW4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000152591.
CleanExiHS_DSPP.
GenevisibleiQ9NZW4. HS.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiDSPP_HUMAN
AccessioniPrimary (citable) accession number: Q9NZW4
Secondary accession number(s): A8MUI0, O95815
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 124 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

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 one 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.