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Q9NZW4

- DSPP_HUMAN

UniProt

Q9NZW4 - DSPP_HUMAN

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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. extracellular region Source: Reactome
  2. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
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.
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 (1 Publication and 1 Publication).6 Publications
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. 2 Publications
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. 3 Publications
VAR_054443
Natural varianti18 – 181V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
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.
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 (1 Publication and 1 Publication).3 Publications
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. 3 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.
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 (1 Publication, 1 Publication).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 – 1515 Reviewed predictionAdd
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...) Reviewed prediction
Glycosylationi49 – 491N-linked (GlcNAc...) Reviewed prediction
Glycosylationi81 – 811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi130 – 1301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi150 – 1501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi190 – 1901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi191 – 1911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi209 – 2091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi222 – 2221N-linked (GlcNAc...) Reviewed prediction
Modified residuei259 – 2591Phosphoserine; by CK1 Reviewed prediction
Glycosylationi275 – 2751N-linked (GlcNAc...) Reviewed prediction
Modified residuei301 – 3011Phosphoserine By similarity
Glycosylationi336 – 3361N-linked (GlcNAc...) Reviewed prediction
Glycosylationi387 – 3871N-linked (GlcNAc...) Reviewed prediction

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

ArrayExpressiQ9NZW4.
BgeeiQ9NZW4.
CleanExiHS_DSPP.
GenevestigatoriQ9NZW4.

Organism-specific databases

HPAiHPA036230.

Interactioni

Subunit structurei

Interacts with FBLN7 By similarity.

Protein-protein interaction databases

STRINGi9606.ENSP00000382213.

Structurei

3D structure databases

ProteinModelPortaliQ9NZW4.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi488 – 4903Cell attachment site Reviewed prediction

Compositional bias

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG098252.
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

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MKIITYFCIW AVAWAIPVPQ SKPLERHVEK SMNLHLLARS NVSVQDELNA     50
SGTIKESGVL VHEGDRGRQE NTQDGHKGEG NGSKWAEVGG KSFSTYSTLA 100
NEEGNIEGWN GDTGKAETYG HDGIHGKEEN ITANGIQGQV SIIDNAGATN 150
RSNTNGNTDK NTQNGDVGDA GHNEDVAVVQ EDGPQVAGSN NSTDNEDEII 200
ENSCRNEGNT SEITPQINSK RNGTKEAEVT PGTGEDAGLD NSDGSPSGNG 250
ADEDEDEGSG DDEDEEAGNG KDSSNNSKGQ EGQDHGKEDD HDSSIGQNSD 300
SKEYYDPEGK EDPHNEVDGD KTSKSEENSA GIPEDNGSQR IEDTQKLNHR 350
ESKRVENRIT KESETHAVGK SQDKGIEIKG PSSGNRNITK EVGKGNEGKE 400
DKGQHGMILG KGNVKTQGEV VNIEGPGQKS EPGNKVGHSN TGSDSNSDGY 450
DSYDFDDKSM QGDDPNSSDE SNGNDDANSE SDNNSSSRGD ASYNSDESKD 500
NGNGSDSKGA EDDDSDSTSD TNNSDSNGNG NNGNDDNDKS DSGKGKSDSS 550
DSDSSDSSNS SDSSDSSDSD SSDSNSSSDS DSSDSDSSDS SDSDSSDSSN 600
SSDSSDSSDS SDSSDSSDSS DSKSDSSKSE SDSSDSDSKS DSSDSNSSDS 650
SDNSDSSDSS NSSNSSDSSD SSDSSDSSSS SDSSNSSDSS DSSDSSNSSE 700
SSDSSDSSDS DSSDSSDSSN SNSSDSDSSN SSDSSDSSNS SDSSDSSDSS 750
NSSDSSDSSD SSNSSDSSDS SDSSDSSDSS NSSDSNDSSN SSDSSDSSNS 800
SDSSNSSDSS DSSDSSDSDS SNSSDSSNSS DSSDSSNSSD SSDSSDSSDG 850
SDSDSSNRSD SSNSSDSSDS SDSSNSSDSS DSSDSNESSN SSDSSDSSNS 900
SDSDSSDSSN SSDSSDSSNS SDSSESSNSS DNSNSSDSSN SSDSSDSSDS 950
SNSSDSSNSS DSSNSSDSSD SNSSDSSDSS NSSDSSDSSD SSDSSDSSDS 1000
SNSSDSSDSS DSSDSSNSSD SSNSSDSSNS SDSSDSSDSS DSSDSSDSSD 1050
SSDSSNSSDS SDSSDSSDSS DSSDSSDSSD SSESSDSSDS SNSSDSSDSS 1100
DSSDSSDSSD SSDSSDSSDS SNSSDSSDSS DSSDSSDSSN SSDSSDSSES 1150
SDSSDSSDSS DSSDSSDSSD SSDSSDSSNS SDSSDSSDSS DSSDSSDSSD 1200
SSDSSDSSDS SDSSDSSDSS DSSDSSDSSD SNESSDSSDS SDSSDSSNSS 1250
DSSDSSDSSD STSDSNDESD SQSKSGNGNN NGSDSDSDSE GSDSNHSTSD 1300
D 1301
Length:1,301
Mass (Da):131,151
Last modified:November 25, 2008 - v2
Checksum:iE0D86B52F5E53D05
GO

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. 2 Publications
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. 3 Publications
VAR_054443
Natural varianti17 – 171P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
Corresponds to variant rs121912986 [ dbSNP | Ensembl ].
VAR_012280
Natural varianti18 – 181V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. 2 Publications
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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti673 – 6731D → DSSDSSS in AAF42472. 1 Publication
Sequence conflicti734 – 7396Missing in AAF42472. 1 Publication
Sequence conflicti799 – 7991N → D in AAD16120. 1 Publication
Sequence conflicti836 – 8361S → C in AAD16120. 1 Publication
Sequence conflicti850 – 8501G → S in AAF42472. 1 Publication
Sequence conflicti875 – 8751N → NSSD in AAF42472. 1 Publication
Sequence conflicti960 – 9601S → G in AAF42472. 1 Publication
Sequence conflicti1002 – 10021N → D in AAD16120. 1 Publication
Sequence conflicti1022 – 10221S → G in AAD16120. 1 Publication
Sequence conflicti1029 – 10291N → D in AAF42472. 1 Publication
Sequence conflicti1029 – 10291N → D in AAD16120. 1 Publication
Sequence conflicti1044 – 10441D → N in AAF42472. 1 Publication
Sequence conflicti1050 – 10501D → N in AAD16120. 1 Publication
Sequence conflicti1056 – 10561N → D in AAF42472. 1 Publication
Sequence conflicti1056 – 10561N → D in AAD16120. 1 Publication
Sequence conflicti1062 – 10621D → G in AAF42472. 1 Publication
Sequence conflicti1077 – 10771D → E in AAD16120. 1 Publication
Sequence conflicti1083 – 10831E → D in AAF42472. 1 Publication
Sequence conflicti1083 – 10831E → D in AAD16120. 1 Publication
Sequence conflicti1090 – 114051Missing in AAF42472. 1 PublicationAdd
BLAST
Sequence conflicti1090 – 114051Missing in AAD16120. 1 PublicationAdd
BLAST
Sequence conflicti1143 – 11431D → E in AAF42472. 1 Publication
Sequence conflicti1149 – 11491E → D in AAF42472. 1 Publication
Sequence conflicti1152 – 11521D → N in AAD16120. 1 Publication
Sequence conflicti1180 – 11801S → R in AAD16120. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
HOVERGENi HBG098252.
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

ArrayExpressi Q9NZW4.
Bgeei Q9NZW4.
CleanExi HS_DSPP.
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: September 3, 2014
This is version 106 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

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