Skip Header

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

Q9NZW4

- DSPP_HUMAN

UniProt

Q9NZW4 - DSPP_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dentin sialophosphoprotein

Gene

DSPP

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. calcium ion binding Source: ProtInc
  2. collagen binding Source: ProtInc
  3. extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. cellular response to cell-matrix adhesion Source: Ensembl
  3. extracellular matrix organization Source: Reactome
  4. multicellular organismal development Source: ProtInc
  5. ossification Source: ProtInc
  6. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Keywords - Ligandi

Calcium, Sialic acid

Enzyme and pathway databases

ReactomeiREACT_163906. 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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3054. DSPP.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular region Source: Reactome
  3. 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) [MIM:605594]: A disorder characterized by the association of progressive sensorineural high-frequency hearing loss with dentinogenesis imperfecta.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. 1 Publication
Corresponds to variant rs121912986 [ dbSNP | Ensembl ].
VAR_012280
Natural varianti18 – 181V → F in DFNA39/DGI1 and DGI3. 2 Publications
Corresponds to variant rs121912987 [ dbSNP | Ensembl ].
VAR_012281
Dentinogenesis imperfecta, Shields type 2 (DGI2) [MIM:125490]: A 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.4 Publications
Note: 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).
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151A → V in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane. 1 Publication
Corresponds to variant rs121912989 [ dbSNP | Ensembl ].
VAR_036862
Natural varianti17 – 171P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
VAR_054443
Natural varianti18 – 181V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. 1 Publication
VAR_070253
Natural varianti68 – 681R → W in DGI2. 2 Publications
Corresponds to variant rs36094464 [ dbSNP | Ensembl ].
VAR_030661
Dentinogenesis imperfecta, Shields type 3 (DGI3) [MIM:125500]: A 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.3 Publications
Note: 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).
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171P → L in DGI3; the mutant protein is largely retained in the ER. 1 Publication
VAR_070252
Natural varianti17 – 171P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
VAR_054443
Natural varianti18 – 181V → F in DFNA39/DGI1 and DGI3. 2 Publications
Corresponds to variant rs121912987 [ dbSNP | Ensembl ].
VAR_012281
Dentin dysplasia 2 (DTDP2) [MIM:125420]: A 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.2 Publications
Note: 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
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61Y → D in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum. 1 Publication
Corresponds to variant rs121912988 [ dbSNP | Ensembl ].
VAR_036861

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 13011286Dentin sialophosphoproteinPRO_0000021120Add
BLAST
Chaini16 – 462447Dentin sialoproteinPRO_0000021121Add
BLAST
Chaini463 – 1301839Dentin phosphoproteinPRO_0000021122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi49 – 491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
Modified residuei259 – 2591Phosphoserine; by CK1Sequence Analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Modified residuei301 – 3011PhosphoserineBy similarity
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

DSP is glycosylated.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9NZW4.
PRIDEiQ9NZW4.

PTM databases

PhosphoSiteiQ9NZW4.

Miscellaneous databases

PMAP-CutDBA8MUI0.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NZW4.
CleanExiHS_DSPP.
ExpressionAtlasiQ9NZW4. baseline and differential.
GenevestigatoriQ9NZW4.

Organism-specific databases

HPAiHPA036230.

Interactioni

Subunit structurei

Interacts with FBLN7.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000382213.

Structurei

3D structure databases

ProteinModelPortaliQ9NZW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi488 – 4903Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi439 – 1301863Asp/Ser-richAdd
BLAST

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000111489.
HOVERGENiHBG098252.
InParanoidiQ9NZW4.
OMAiGMILGKG.
OrthoDBiEOG7D2FF4.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti673 – 6731D → DSSDSSS in AAF42472. (PubMed:10706475)Curated
Sequence conflicti734 – 7396Missing in AAF42472. (PubMed:10706475)Curated
Sequence conflicti799 – 7991N → D in AAD16120. (PubMed:9879917)Curated
Sequence conflicti836 – 8361S → C in AAD16120. (PubMed:9879917)Curated
Sequence conflicti850 – 8501G → S in AAF42472. (PubMed:10706475)Curated
Sequence conflicti875 – 8751N → NSSD in AAF42472. (PubMed:10706475)Curated
Sequence conflicti960 – 9601S → G in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1002 – 10021N → D in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1022 – 10221S → G in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1029 – 10291N → D in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1029 – 10291N → D in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1044 – 10441D → N in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1050 – 10501D → N in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1056 – 10561N → D in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1056 – 10561N → D in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1062 – 10621D → G in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1077 – 10771D → E in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1083 – 10831E → D in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1083 – 10831E → D in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1090 – 114051Missing in AAF42472. (PubMed:10706475)CuratedAdd
BLAST
Sequence conflicti1090 – 114051Missing in AAD16120. (PubMed:9879917)CuratedAdd
BLAST
Sequence conflicti1143 – 11431D → E in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1149 – 11491E → D in AAF42472. (PubMed:10706475)Curated
Sequence conflicti1152 – 11521D → N in AAD16120. (PubMed:9879917)Curated
Sequence conflicti1180 – 11801S → R in AAD16120. (PubMed:9879917)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61Y → D in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum. 1 Publication
Corresponds to variant rs121912988 [ dbSNP | Ensembl ].
VAR_036861
Natural varianti15 – 151A → V in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane. 1 Publication
Corresponds to variant rs121912989 [ dbSNP | Ensembl ].
VAR_036862
Natural varianti17 – 171P → L in DGI3; the mutant protein is largely retained in the ER. 1 Publication
VAR_070252
Natural varianti17 – 171P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
VAR_054443
Natural varianti17 – 171P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. 1 Publication
Corresponds to variant rs121912986 [ dbSNP | Ensembl ].
VAR_012280
Natural varianti18 – 181V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. 1 Publication
VAR_070253
Natural varianti18 – 181V → F in DFNA39/DGI1 and DGI3. 2 Publications
Corresponds to variant rs121912987 [ dbSNP | Ensembl ].
VAR_012281
Natural varianti68 – 681R → W in DGI2. 2 Publications
Corresponds to variant rs36094464 [ dbSNP | Ensembl ].
VAR_030661
Natural varianti243 – 2431D → N.
Corresponds to variant rs3750025 [ dbSNP | Ensembl ].
VAR_047551

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.

Polymorphism databases

DMDMi215273974.

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 .
CCDSi CCDS43248.1.
RefSeqi NP_055023.2. NM_014208.3.
UniGenei Hs.678914.

3D structure databases

ProteinModelPortali Q9NZW4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000382213.

PTM databases

PhosphoSitei Q9NZW4.

Polymorphism databases

DMDMi 215273974.

Proteomic databases

PaxDbi Q9NZW4.
PRIDEi Q9NZW4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282478 ; ENSP00000282478 ; ENSG00000152591 .
ENST00000399271 ; ENSP00000382213 ; ENSG00000152591 .
GeneIDi 1834.
KEGGi hsa:1834.
UCSCi uc003hqu.3. human.

Organism-specific databases

CTDi 1834.
GeneCardsi GC04P088529.
HGNCi HGNC:3054. DSPP.
HPAi HPA036230.
MIMi 125420. phenotype.
125485. gene.
125490. phenotype.
125500. phenotype.
605594. phenotype.
neXtProti NX_Q9NZW4.
Orphaneti 99789. Dentin dysplasia type I.
99791. Dentin dysplasia type II.
166260. Dentinogenesis imperfecta type 2.
166265. Dentinogenesis imperfecta type 3.
PharmGKBi PA27507.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000111489.
HOVERGENi HBG098252.
InParanoidi Q9NZW4.
OMAi GMILGKG.
OrthoDBi EOG7D2FF4.
PhylomeDBi Q9NZW4.
TreeFami TF318563.

Enzyme and pathway databases

Reactomei REACT_163906. ECM proteoglycans.

Miscellaneous databases

GeneWikii Dentin_sialophosphoprotein_(gene).
GenomeRNAii 1834.
NextBioi 7491.
PMAP-CutDB A8MUI0.
PROi Q9NZW4.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZW4.
CleanExi HS_DSPP.
ExpressionAtlasi Q9NZW4. baseline and differential.
Genevestigatori Q9NZW4.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a human dentin sialophosphoprotein gene."
    Gu K., Chang S.R., Ritchie H.H., Clarkson B.H., Rutherford R.B.
    Eur. J. Oral Sci. 108:35-42(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 463-1301.
    Tissue: Tooth.
  4. "DSPP mutation in dentinogenesis imperfecta Shields type II."
    Zhang X., Zhao J., Li C., Gao S., Qiu C., Liu P., Wu G., Qiang B., Lo W.H.Y., Shen Y.
    Nat. Genet. 27:151-152(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DGI2.
  5. "A comprehensive analysis of normal variation and disease-causing mutations in the human DSPP gene."
    McKnight D.A., Suzanne Hart P., Hart T.C., Hartsfield J.K., Wilson A., Wright J.T., Fisher L.W.
    Hum. Mutat. 29:1392-1404(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DGI2; DGI3 AND DTDP2, VARIANT DGI3 SER-17.
  6. "Dentinogenesis imperfecta 1 with or without progressive hearing loss is associated with distinct mutations in DSPP."
    Xiao S., Yu C., Chou X., Yuan W., Wang Y., Bu L., Fu G., Qian M., Yang J., Shi Y., Hu L., Han B., Wang Z., Huang W., Liu J., Chen Z., Zhao G., Kong X.
    Nat. Genet. 27:201-204(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DFNA39/DGI1 THR-17 AND PHE-18.
  7. "Mutation of the signal peptide region of the bicistronic gene DSPP affects translocation to the endoplasmic reticulum and results in defective dentine biomineralization."
    Rajpar M.H., Koch M.J., Davies R.M., Mellody K.T., Kielty C.M., Dixon M.J.
    Hum. Mol. Genet. 11:2559-2565(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DTDP2 ASP-6, CHARACTERIZATION OF VARIANT DTDP2 ASP-6.
  8. "Clinical, histopathologic, and genetic investigation in two large families with dentinogenesis imperfecta type II."
    Malmgren B., Lindskog S., Elgadi A., Norgren S.
    Hum. Genet. 114:491-498(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DGI2 VAL-15 AND TRP-68.
  9. "Mutational hot spot in the DSPP gene causing dentinogenesis imperfecta type II."
    Kim J.-W., Hu J.C.-C., Lee J.-I., Moon S.-K., Kim Y.-J., Jang K.-T., Lee S.-H., Kim C.-C., Hahn S.-H., Simmer J.P.
    Hum. Genet. 116:186-191(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DGI3 PHE-18.
  10. Cited for: VARIANT TRP-68.
  11. Cited for: VARIANT DGI2 SER-17.
  12. "Identification of the DSPP mutation in a new kindred and phenotype-genotype correlation."
    Lee S.K., Lee K.E., Hwang Y.H., Kida M., Tsutsumi T., Ariga T., Park J.C., Kim J.W.
    Oral Dis. 17:314-319(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DGI2 ASP-18.
  13. "Rough endoplasmic reticulum trafficking errors by different classes of mutant dentin sialophosphoprotein (DSPP) cause dominant negative effects in both dentinogenesis imperfecta and dentin dysplasia by entrapping normal DSPP."
    von Marschall Z., Mok S., Phillips M.D., McKnight D.A., Fisher L.W.
    J. Bone Miner. Res. 27:1309-1321(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT DFNA39/DGI1 THR-17, CHARACTERIZATION OF VARIANTS DGI2 VAL-15; SER-17 AND ASP-18.
  14. "A DSPP mutation causing dentinogenesis imperfecta and characterization of the mutational effect."
    Lee S.K., Lee K.E., Song S.J., Hyun H.K., Lee S.H., Kim J.W.
    Biomed. Res. Int. 2013:948181-948181(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DGI3 LEU-17, CHARACTERIZATION OF VARIANT DGI3 LEU-17.

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: October 29, 2014
This is version 108 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