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Q9NZW4

- DSPP_HUMAN

UniProt

Q9NZW4 - DSPP_HUMAN

Protein

Dentin sialophosphoprotein

Gene

DSPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    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

    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

    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

    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.
    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.
    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

    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:
    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

    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 1, 2014
    This is version 107 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