Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NZW4 (DSPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dentin sialophosphoprotein

Cleaved into the following 2 chains:

  1. Dentin phosphoprotein
    Alternative name(s):
    Dentin phosphophoryn
    Short name=DPP
  2. Dentin sialoprotein
    Short name=DSP
Gene names
Name:DSPP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1301 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with FBLN7 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

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

Post-translational modification

DSP is glycosylated.

Involvement in disease

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. Ref.6 Ref.13

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 (Ref.5 and Ref.13). Ref.4 Ref.5 Ref.8 Ref.11 Ref.12 Ref.13

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 (Ref.5 and Ref.13). Ref.5 Ref.9 Ref.14

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 (Ref.5, Ref.13). Ref.5 Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 13011286Dentin sialophosphoprotein
PRO_0000021120
Chain16 – 462447Dentin sialoprotein
PRO_0000021121
Chain463 – 1301839Dentin phosphoprotein
PRO_0000021122

Regions

Motif488 – 4903Cell attachment site Potential
Compositional bias439 – 1301863Asp/Ser-rich

Amino acid modifications

Modified residue2591Phosphoserine; by CK1 Potential
Modified residue3011Phosphoserine By similarity
Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential

Natural variations

Natural variant61Y → D in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum. Ref.7
Corresponds to variant rs121912988 [ dbSNP | Ensembl ].
VAR_036861
Natural variant151A → V in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane. Ref.8 Ref.13
Corresponds to variant rs121912989 [ dbSNP | Ensembl ].
VAR_036862
Natural variant171P → L in DGI3; the mutant protein is largely retained in the ER. Ref.14
VAR_070252
Natural variant171P → S in DGI2 AND DGI3; dominant negative mutation; the mutant protein is retained intracellularly. Ref.5 Ref.11 Ref.13
VAR_054443
Natural variant171P → T in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly. Ref.6 Ref.13
Corresponds to variant rs121912986 [ dbSNP | Ensembl ].
VAR_012280
Natural variant181V → D in DGI2; dominant negative mutation; the mutant protein is retained intracellularly. Ref.12 Ref.13
VAR_070253
Natural variant181V → F in DFNA39/DGI1 and DGI3. Ref.6 Ref.9
Corresponds to variant rs121912987 [ dbSNP | Ensembl ].
VAR_012281
Natural variant681R → W in DGI2. Ref.8 Ref.10
Corresponds to variant rs36094464 [ dbSNP | Ensembl ].
VAR_030661
Natural variant2431D → N.
Corresponds to variant rs3750025 [ dbSNP | Ensembl ].
VAR_047551

Experimental info

Sequence conflict6731D → DSSDSSS in AAF42472. Ref.1
Sequence conflict734 – 7396Missing in AAF42472. Ref.1
Sequence conflict7991N → D in AAD16120. Ref.3
Sequence conflict8361S → C in AAD16120. Ref.3
Sequence conflict8501G → S in AAF42472. Ref.1
Sequence conflict8751N → NSSD in AAF42472. Ref.1
Sequence conflict9601S → G in AAF42472. Ref.1
Sequence conflict10021N → D in AAD16120. Ref.3
Sequence conflict10221S → G in AAD16120. Ref.3
Sequence conflict10291N → D in AAF42472. Ref.1
Sequence conflict10291N → D in AAD16120. Ref.3
Sequence conflict10441D → N in AAF42472. Ref.1
Sequence conflict10501D → N in AAD16120. Ref.3
Sequence conflict10561N → D in AAF42472. Ref.1
Sequence conflict10561N → D in AAD16120. Ref.3
Sequence conflict10621D → G in AAF42472. Ref.1
Sequence conflict10771D → E in AAD16120. Ref.3
Sequence conflict10831E → D in AAF42472. Ref.1
Sequence conflict10831E → D in AAD16120. Ref.3
Sequence conflict1090 – 114051Missing in AAF42472. Ref.1
Sequence conflict1090 – 114051Missing in AAD16120. Ref.3
Sequence conflict11431D → E in AAF42472. Ref.1
Sequence conflict11491E → D in AAF42472. Ref.1
Sequence conflict11521D → N in AAD16120. Ref.3
Sequence conflict11801S → R in AAD16120. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9NZW4 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: E0D86B52F5E53D05

FASTA1,301131,151
        10         20         30         40         50         60 
MKIITYFCIW AVAWAIPVPQ SKPLERHVEK SMNLHLLARS NVSVQDELNA SGTIKESGVL 

        70         80         90        100        110        120 
VHEGDRGRQE NTQDGHKGEG NGSKWAEVGG KSFSTYSTLA NEEGNIEGWN GDTGKAETYG 

       130        140        150        160        170        180 
HDGIHGKEEN ITANGIQGQV SIIDNAGATN RSNTNGNTDK NTQNGDVGDA GHNEDVAVVQ 

       190        200        210        220        230        240 
EDGPQVAGSN NSTDNEDEII ENSCRNEGNT SEITPQINSK RNGTKEAEVT PGTGEDAGLD 

       250        260        270        280        290        300 
NSDGSPSGNG ADEDEDEGSG DDEDEEAGNG KDSSNNSKGQ EGQDHGKEDD HDSSIGQNSD 

       310        320        330        340        350        360 
SKEYYDPEGK EDPHNEVDGD KTSKSEENSA GIPEDNGSQR IEDTQKLNHR ESKRVENRIT 

       370        380        390        400        410        420 
KESETHAVGK SQDKGIEIKG PSSGNRNITK EVGKGNEGKE DKGQHGMILG KGNVKTQGEV 

       430        440        450        460        470        480 
VNIEGPGQKS EPGNKVGHSN TGSDSNSDGY DSYDFDDKSM QGDDPNSSDE SNGNDDANSE 

       490        500        510        520        530        540 
SDNNSSSRGD ASYNSDESKD NGNGSDSKGA EDDDSDSTSD TNNSDSNGNG NNGNDDNDKS 

       550        560        570        580        590        600 
DSGKGKSDSS DSDSSDSSNS SDSSDSSDSD SSDSNSSSDS DSSDSDSSDS SDSDSSDSSN 

       610        620        630        640        650        660 
SSDSSDSSDS SDSSDSSDSS DSKSDSSKSE SDSSDSDSKS DSSDSNSSDS SDNSDSSDSS 

       670        680        690        700        710        720 
NSSNSSDSSD SSDSSDSSSS SDSSNSSDSS DSSDSSNSSE SSDSSDSSDS DSSDSSDSSN 

       730        740        750        760        770        780 
SNSSDSDSSN SSDSSDSSNS SDSSDSSDSS NSSDSSDSSD SSNSSDSSDS SDSSDSSDSS 

       790        800        810        820        830        840 
NSSDSNDSSN SSDSSDSSNS SDSSNSSDSS DSSDSSDSDS SNSSDSSNSS DSSDSSNSSD 

       850        860        870        880        890        900 
SSDSSDSSDG SDSDSSNRSD SSNSSDSSDS SDSSNSSDSS DSSDSNESSN SSDSSDSSNS 

       910        920        930        940        950        960 
SDSDSSDSSN SSDSSDSSNS SDSSESSNSS DNSNSSDSSN SSDSSDSSDS SNSSDSSNSS 

       970        980        990       1000       1010       1020 
DSSNSSDSSD SNSSDSSDSS NSSDSSDSSD SSDSSDSSDS SNSSDSSDSS DSSDSSNSSD 

      1030       1040       1050       1060       1070       1080 
SSNSSDSSNS SDSSDSSDSS DSSDSSDSSD SSDSSNSSDS SDSSDSSDSS DSSDSSDSSD 

      1090       1100       1110       1120       1130       1140 
SSESSDSSDS SNSSDSSDSS DSSDSSDSSD SSDSSDSSDS SNSSDSSDSS DSSDSSDSSN 

      1150       1160       1170       1180       1190       1200 
SSDSSDSSES SDSSDSSDSS DSSDSSDSSD SSDSSDSSNS SDSSDSSDSS DSSDSSDSSD 

      1210       1220       1230       1240       1250       1260 
SSDSSDSSDS SDSSDSSDSS DSSDSSDSSD SNESSDSSDS SDSSDSSNSS DSSDSSDSSD 

      1270       1280       1290       1300 
STSDSNDESD SQSKSGNGNN NGSDSDSDSE GSDSNHSTSD D 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Human dentin phosphophoryn nucleotide and amino acid sequence."
Gu K., Chang S.R., Slaven M.S., Clarkson B.H., Rutherford R.B., Ritchie H.H.
Eur. J. Oral Sci. 106:1043-1047(1998) [PubMed] [Europe PMC] [Abstract]
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]"DMP1 mutations in autosomal recessive hypophosphatemia implicate a bone matrix protein in the regulation of phosphate homeostasis."
Lorenz-Depiereux B., Bastepe M., Benet-Pages A., Amyere M., Wagenstaller J., Mueller-Barth U., Badenhoop K., Kaiser S.M., Rittmaster R.S., Shlossberg A.H., Olivares J.L., Loris C., Ramos F.J., Glorieux F., Vikkula M., Jueppner H., Strom T.M.
Nat. Genet. 38:1248-1250(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRP-68.
[11]"Disorders of human dentin."
Hart P.S., Hart T.C.
Cells Tissues Organs 186:70-77(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF163151 Genomic DNA. Translation: AAF42472.1.
AC093895 Genomic DNA. No translation available.
AF094508 mRNA. Translation: AAD16120.1.
CCDSCCDS43248.1.
RefSeqNP_055023.2. NM_014208.3.
UniGeneHs.678914.

3D structure databases

ProteinModelPortalQ9NZW4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000382213.

PTM databases

PhosphoSiteQ9NZW4.

Polymorphism databases

DMDM215273974.

Proteomic databases

PaxDbQ9NZW4.
PRIDEQ9NZW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282478; ENSP00000282478; ENSG00000152591.
ENST00000399271; ENSP00000382213; ENSG00000152591.
GeneID1834.
KEGGhsa:1834.
UCSCuc003hqu.3. human.

Organism-specific databases

CTD1834.
GeneCardsGC04P088529.
HGNCHGNC:3054. DSPP.
HPAHPA036230.
MIM125420. phenotype.
125485. gene.
125490. phenotype.
125500. phenotype.
605594. phenotype.
neXtProtNX_Q9NZW4.
Orphanet99789. Dentin dysplasia type I.
99791. Dentin dysplasia type II.
166260. Dentinogenesis imperfecta type 2.
166265. Dentinogenesis imperfecta type 3.
PharmGKBPA27507.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG098252.
OMAGMILGKG.
OrthoDBEOG7D2FF4.
PhylomeDBQ9NZW4.
TreeFamTF318563.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9NZW4.
BgeeQ9NZW4.
CleanExHS_DSPP.
GenevestigatorQ9NZW4.

Family and domain databases

ProtoNetSearch...

Other

GeneWikiDentin_sialophosphoprotein_(gene).
GenomeRNAi1834.
NextBio7491.
PMAP-CutDBA8MUI0.
PROQ9NZW4.
SOURCESearch...

Entry information

Entry nameDSPP_HUMAN
AccessionPrimary (citable) accession number: Q9NZW4
Secondary accession number(s): A8MUI0, O95815
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM