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P15813

- CD1D_HUMAN

UniProt

P15813 - CD1D_HUMAN

Protein

Antigen-presenting glycoprotein CD1d

Gene

CD1D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981Glycolipid
    Binding sitei169 – 1691Glycolipid
    Binding sitei172 – 1721Glycolipid

    GO - Molecular functioni

    1. beta-2-microglobulin binding Source: UniProtKB
    2. cell adhesion molecule binding Source: BHF-UCL
    3. exogenous lipid antigen binding Source: UniProtKB
    4. histone binding Source: UniProtKB
    5. lipid antigen binding Source: BHF-UCL
    6. receptor activity Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation, endogenous lipid antigen via MHC class Ib Source: UniProtKB
    2. detection of bacterium Source: UniProtKB
    3. heterotypic cell-cell adhesion Source: BHF-UCL
    4. innate immune response Source: UniProtKB-KW
    5. positive regulation of innate immune response Source: UniProtKB
    6. positive regulation of T cell proliferation Source: BHF-UCL
    7. T cell selection Source: UniProtKB
    8. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Immunity, Innate immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Antigen-presenting glycoprotein CD1d
    Alternative name(s):
    R3G1
    CD_antigen: CD1d
    Gene namesi
    Name:CD1D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1637. CD1D.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Endosome membrane. Lysosome membrane
    Note: Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes.

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: BHF-UCL
    3. endosome membrane Source: UniProtKB-SubCell
    4. integral component of plasma membrane Source: UniProtKB
    5. lysosomal membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi331 – 3311Y → A: Strongly reduced internalization. 1 Publication
    Mutagenesisi334 – 3341V → A: Strongly reduced internalization. 1 Publication

    Organism-specific databases

    PharmGKBiPA26196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 335316Antigen-presenting glycoprotein CD1dPRO_0000014581Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)1 Publication
    Glycosylationi60 – 601N-linked (GlcNAc...)2 Publications
    Disulfide bondi120 ↔ 1841 PublicationPROSITE-ProRule annotation
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi224 ↔ 2791 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP15813.
    PaxDbiP15813.
    PRIDEiP15813.

    PTM databases

    PhosphoSiteiP15813.

    Expressioni

    Tissue specificityi

    Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.

    Gene expression databases

    BgeeiP15813.
    CleanExiHS_CD1D.
    GenevestigatoriP15813.

    Organism-specific databases

    HPAiCAB016107.

    Interactioni

    Subunit structurei

    Heterodimer with B2M (beta-2-microglobulin). Interacts with MHC II.3 Publications

    Protein-protein interaction databases

    BioGridi107350. 5 interactions.
    DIPiDIP-60257N.
    STRINGi9606.ENSP00000357153.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 3811
    Beta strandi41 – 5010
    Beta strandi53 – 586
    Beta strandi63 – 675
    Turni70 – 756
    Helixi78 – 10528
    Beta strandi112 – 12211
    Beta strandi124 – 1263
    Beta strandi128 – 1369
    Beta strandi139 – 1457
    Beta strandi148 – 1514
    Helixi158 – 1669
    Helixi170 – 18112
    Helixi183 – 19412
    Helixi196 – 1994
    Beta strandi206 – 2116
    Beta strandi216 – 23217
    Beta strandi235 – 2406
    Beta strandi241 – 2433
    Beta strandi248 – 2503
    Turni257 – 2593
    Beta strandi261 – 27212
    Beta strandi278 – 2825
    Turni284 – 2874
    Beta strandi291 – 2944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZT4X-ray3.00A/C19-299[»]
    2PO6X-ray3.20A/E24-295[»]
    3HUJX-ray2.50A/C21-295[»]
    3SDXX-ray3.12A/C24-295[»]
    3TZVX-ray3.06C21-295[»]
    3U0PX-ray2.80A/C/E21-295[»]
    3VWJX-ray3.09A21-295[»]
    3VWKX-ray2.94A21-295[»]
    4EN3X-ray2.57C21-295[»]
    4LHUX-ray2.87A24-295[»]
    4MNGX-ray3.01A/C21-201[»]
    4MQ7X-ray2.60A21-202[»]
    ProteinModelPortaliP15813.
    SMRiP15813. Positions 23-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15813.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 301282ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini323 – 33513CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei302 – 32221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini185 – 292108Ig-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi331 – 3344Internalization signal

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG26626.
    HOGENOMiHOG000111666.
    HOVERGENiHBG004453.
    InParanoidiP15813.
    KOiK06448.
    OMAiLNDTCPQ.
    OrthoDBiEOG7DZ8K9.
    PhylomeDBiP15813.
    TreeFamiTF336723.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    [Graphical view]
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15813-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCLLFLLLW ALLQAWGSAE VPQRLFPLRC LQISSFANSS WTRTDGLAWL    50
    GELQTHSWSN DSDTVRSLKP WSQGTFSDQQ WETLQHIFRV YRSSFTRDVK 100
    EFAKMLRLSY PLELQVSAGC EVHPGNASNN FFHVAFQGKD ILSFQGTSWE 150
    PTQEAPLWVN LAIQVLNQDK WTRETVQWLL NGTCPQFVSG LLESGKSELK 200
    KQVKPKAWLS RGPSPGPGRL LLVCHVSGFY PKPVWVKWMR GEQEQQGTQP 250
    GDILPNADET WYLRATLDVV AGEAAGLSCR VKHSSLEGQD IVLYWGGSYT 300
    SMGLIALAVL ACLLFLLIVG FTSRFKRQTS YQGVL 335
    Length:335
    Mass (Da):37,717
    Last modified:April 1, 1990 - v1
    Checksum:iEA041C1C45A5777F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641T → S.1 Publication
    Corresponds to variant rs62621276 [ dbSNP | Ensembl ].
    VAR_010211

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38820
    , L38815, L38817, L38816, L38818, L38819 Genomic DNA. Translation: AAA59672.1.
    X14974 Genomic DNA. Translation: CAA33099.1.
    J04142 mRNA. Translation: AAA59673.1.
    AL138899 Genomic DNA. Translation: CAH73515.1.
    CH471121 Genomic DNA. Translation: EAW52847.1.
    CH471121 Genomic DNA. Translation: EAW52848.1.
    CH471121 Genomic DNA. Translation: EAW52849.1.
    BC027926 mRNA. Translation: AAH27926.1.
    AF142668 Genomic DNA. Translation: AAD37581.1.
    M14664 Genomic DNA. Translation: AAA51935.1.
    CCDSiCCDS1173.1.
    PIRiS07715. HLHUR3.
    RefSeqiNP_001757.1. NM_001766.3.
    UniGeneiHs.1799.
    Hs.731511.

    Genome annotation databases

    EnsembliENST00000368171; ENSP00000357153; ENSG00000158473.
    GeneIDi912.
    KEGGihsa:912.
    UCSCiuc001frr.3. human.

    Polymorphism databases

    DMDMi115964.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38820
    , L38815 , L38817 , L38816 , L38818 , L38819 Genomic DNA. Translation: AAA59672.1 .
    X14974 Genomic DNA. Translation: CAA33099.1 .
    J04142 mRNA. Translation: AAA59673.1 .
    AL138899 Genomic DNA. Translation: CAH73515.1 .
    CH471121 Genomic DNA. Translation: EAW52847.1 .
    CH471121 Genomic DNA. Translation: EAW52848.1 .
    CH471121 Genomic DNA. Translation: EAW52849.1 .
    BC027926 mRNA. Translation: AAH27926.1 .
    AF142668 Genomic DNA. Translation: AAD37581.1 .
    M14664 Genomic DNA. Translation: AAA51935.1 .
    CCDSi CCDS1173.1.
    PIRi S07715. HLHUR3.
    RefSeqi NP_001757.1. NM_001766.3.
    UniGenei Hs.1799.
    Hs.731511.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZT4 X-ray 3.00 A/C 19-299 [» ]
    2PO6 X-ray 3.20 A/E 24-295 [» ]
    3HUJ X-ray 2.50 A/C 21-295 [» ]
    3SDX X-ray 3.12 A/C 24-295 [» ]
    3TZV X-ray 3.06 C 21-295 [» ]
    3U0P X-ray 2.80 A/C/E 21-295 [» ]
    3VWJ X-ray 3.09 A 21-295 [» ]
    3VWK X-ray 2.94 A 21-295 [» ]
    4EN3 X-ray 2.57 C 21-295 [» ]
    4LHU X-ray 2.87 A 24-295 [» ]
    4MNG X-ray 3.01 A/C 21-201 [» ]
    4MQ7 X-ray 2.60 A 21-202 [» ]
    ProteinModelPortali P15813.
    SMRi P15813. Positions 23-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107350. 5 interactions.
    DIPi DIP-60257N.
    STRINGi 9606.ENSP00000357153.

    Chemistry

    ChEMBLi CHEMBL1649053.

    PTM databases

    PhosphoSitei P15813.

    Polymorphism databases

    DMDMi 115964.

    Proteomic databases

    MaxQBi P15813.
    PaxDbi P15813.
    PRIDEi P15813.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368171 ; ENSP00000357153 ; ENSG00000158473 .
    GeneIDi 912.
    KEGGi hsa:912.
    UCSCi uc001frr.3. human.

    Organism-specific databases

    CTDi 912.
    GeneCardsi GC01P158149.
    HGNCi HGNC:1637. CD1D.
    HPAi CAB016107.
    MIMi 188410. gene.
    neXtProti NX_P15813.
    PharmGKBi PA26196.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26626.
    HOGENOMi HOG000111666.
    HOVERGENi HBG004453.
    InParanoidi P15813.
    KOi K06448.
    OMAi LNDTCPQ.
    OrthoDBi EOG7DZ8K9.
    PhylomeDBi P15813.
    TreeFami TF336723.

    Miscellaneous databases

    EvolutionaryTracei P15813.
    GeneWikii CD1D.
    GenomeRNAii 912.
    NextBioi 3762.
    PROi P15813.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15813.
    CleanExi HS_CD1D.
    Genevestigatori P15813.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    [Graphical view ]
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation and characterization of a cDNA and gene coding for a fourth CD1 molecule."
      Balk S.P., Bleicher P.A., Terhorst C.
      Proc. Natl. Acad. Sci. U.S.A. 86:252-256(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-109, VARIANT SER-64.
    7. "Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens."
      Martin L.H., Calabi F., Milstein C.
      Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-295.
    8. "A critical tyrosine residue in the cytoplasmic tail is important for CD1d internalization but not for its basolateral sorting in MDCK cells."
      Rodionov D.G., Nordeng T.W., Pedersen K., Balk S.P., Bakke O.
      J. Immunol. 162:1488-1495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-331 AND VAL-334.
    9. "Regulation of intracellular trafficking of human CD1d by association with MHC class II molecules."
      Kang S.-J., Cresswell P.
      EMBO J. 21:1650-1660(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH B2M AND MHC II.
    10. "CD1d ligands: the good, the bad, and the ugly."
      Brutkiewicz R.R.
      J. Immunol. 177:769-775(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "Distinct endosomal trafficking requirements for presentation of autoantigens and exogenous lipids by human CD1d molecules."
      Chen X., Wang X., Keaton J.M., Reddington F., Illarionov P.A., Besra G.S., Gumperz J.E.
      J. Immunol. 178:6181-6190(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60.
      Tissue: Leukemic T-cell.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-299 IN COMPLEX WITH B2M AND GALACTOSYLCERAMIDE, DISULFIDE BONDS.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 24-295 IN COMPLEX WITH B2M AND T-CELL RECEPTOR, GLYCOSYLATION AT ASN-38 AND ASN-60.

    Entry informationi

    Entry nameiCD1D_HUMAN
    AccessioniPrimary (citable) accession number: P15813
    Secondary accession number(s): D3DVD5
    , Q5W0J3, Q9UMM3, Q9Y5M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 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

    Miscellaneous

    During protein synthesis and maturation, CD1 family members bind endogenous lipids that are replaced by lipid or glycolipid antigens when the proteins are internalized and pass through endosomes, before trafficking back to the cell surface.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3