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Q13291

- SLAF1_HUMAN

UniProt

Q13291 - SLAF1_HUMAN

Protein

Signaling lymphocytic activation molecule

Gene

SLAMF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    High-affinity self-ligand important in bidirectional T-cell to B-cell stimulation. SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAM signaling are likely to exist: one in which the inhibitor SH2D1A acts as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates.

    GO - Molecular functioni

    1. antigen binding Source: ProtInc
    2. protein binding Source: IntAct
    3. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. lymphocyte activation Source: InterPro
    2. positive regulation of cell proliferation Source: ProtInc
    3. signal transduction Source: GOC
    4. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Host-virus interaction

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signaling lymphocytic activation molecule
    Alternative name(s):
    CDw150
    IPO-3
    CD_antigen: CD150
    Gene namesi
    Name:SLAMF1
    Synonyms:SLAM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10903. SLAMF1.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein
    Note: Present on the surface of B-cells and T-cells.

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35803.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 335315Signaling lymphocytic activation moleculePRO_0000014959Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi158 ↔ 228PROSITE-ProRule annotation
    Disulfide bondi164 ↔ 209PROSITE-ProRule annotation
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated by FYN.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ13291.
    PRIDEiQ13291.

    PTM databases

    PhosphoSiteiQ13291.

    Expressioni

    Tissue specificityi

    Constitutively expressed on peripheral blood memory T-cells, T-cell clones, immature thymocytes and a proportion of B-cells, and is rapidly induced on naive T-cells after activation.

    Gene expression databases

    ArrayExpressiQ13291.
    BgeeiQ13291.
    CleanExiHS_SLAMF1.
    GenevestigatoriQ13291.

    Organism-specific databases

    HPAiCAB002438.

    Interactioni

    Subunit structurei

    Interacts (via cytoplasmic domain) with SH2D1A, SH2D1B and with PTPN11. Interacts with INPP5D/SHIP1. Binds to Measles virus H protein and acts as a receptor for this virus.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HQ786F22EBI-4315002,EBI-5323300From a different organism.
    SH2D1AO6088011EBI-4315002,EBI-6983382

    Protein-protein interaction databases

    BioGridi112395. 9 interactions.
    DIPiDIP-40767N.
    IntActiQ13291. 5 interactions.
    MINTiMINT-113752.
    STRINGi9606.ENSP00000306190.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi278 – 2814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D4TX-ray1.10B276-286[»]
    1D4WX-ray1.80C/D276-286[»]
    1I3ZX-ray2.15B273-286[»]
    1KA6NMR-B276-282[»]
    1KA7NMR-B275-286[»]
    1M27X-ray2.50B276-286[»]
    2DZFmodel-@1-335[»]
    2IE9model-@1-335[»]
    2IFLmodel-@3-335[»]
    2IG5model-@1-335[»]
    ProteinModelPortaliQ13291.
    SMRiQ13291. Positions 32-140.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13291.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 237217ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini259 – 33577CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei238 – 25821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini? – 152Ig-like V-type
    Domaini144 – 22380Ig-like C2-typeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi281 – 2866SH2-bindingSequence Analysis
    Motifi307 – 3126SH2-bindingSequence Analysis
    Motifi327 – 3326SH2-bindingSequence Analysis

    Domaini

    The most membrane-proximal SH2-binding motif interacts with SH2 domain of SH2D1A and does not need to be phosphorylated on tyrosine residues.

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG40451.
    HOGENOMiHOG000125310.
    HOVERGENiHBG054224.
    InParanoidiQ13291.
    KOiK06536.
    OMAiLYEQVST.
    OrthoDBiEOG7Q8CQJ.
    PhylomeDBiQ13291.
    TreeFamiTF334964.

    Family and domain databases

    InterProiIPR007110. Ig-like_dom.
    IPR010407. Sig_lymph_act_molc_N.
    IPR015631. SLAM_fam_rcpts.
    [Graphical view]
    PANTHERiPTHR12080. PTHR12080. 1 hit.
    PfamiPF06214. SLAM. 1 hit.
    [Graphical view]
    ProDomiPD090491. Sig_lymph_act_molc_N. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13291-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE    50
    RINKSMNKSI HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL 100
    ENLTLGIRES RKEDEGWYLM TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN 150
    KTQENGTCTL ILGCTVEKGD HVAYSWSEKA GTHPLNPANS SHLLSLTLGP 200
    QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSETKPWAV YAGLLGGVIM 250
    ILIMVVILQL RRRGKTNHYQ TTVEKKSLTI YAQVQKPGPL QKKLDSFPAQ 300
    DPCTTIYVAA TEPVPESVQE TNSITVYASV TLPES 335
    Length:335
    Mass (Da):37,231
    Last modified:November 1, 1996 - v1
    Checksum:iBFB0F27EA31D8C04
    GO
    Isoform 2 (identifier: Q13291-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         289-298: PLQKKLDSFP → DTHHQTSDLF
         299-335: Missing.

    Show »
    Length:298
    Mass (Da):33,365
    Checksum:iDCE97AC03ACDC045
    GO
    Isoform 3 (identifier: Q13291-3) [UniParc]FASTAAdd to Basket

    Also known as: Secreted

    The sequence of this isoform differs from the canonical sequence as follows:
         234-263: Missing.

    Show »
    Length:305
    Mass (Da):33,839
    Checksum:iF5CBDC25B2E19967
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111F → L.
    Corresponds to variant rs2295612 [ dbSNP | Ensembl ].
    VAR_021924
    Natural varianti81 – 811L → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035524
    Natural varianti333 – 3331P → T.
    Corresponds to variant rs3796504 [ dbSNP | Ensembl ].
    VAR_021925

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei234 – 26330Missing in isoform 3. 1 PublicationVSP_002567Add
    BLAST
    Alternative sequencei289 – 29810PLQKKLDSFP → DTHHQTSDLF in isoform 2. 1 PublicationVSP_002568
    Alternative sequencei299 – 33537Missing in isoform 2. 1 PublicationVSP_002569Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33017 mRNA. Translation: AAA75380.1.
    AL121985, AL138930 Genomic DNA. Translation: CAH73505.1.
    AL138930, AL121985 Genomic DNA. Translation: CAI15154.1.
    CH471121 Genomic DNA. Translation: EAW52706.1.
    BC132792 mRNA. Translation: AAI32793.1.
    AF252305 Genomic DNA. Translation: AAG10434.1.
    CCDSiCCDS1207.1. [Q13291-1]
    PIRiS58892.
    RefSeqiNP_003028.1. NM_003037.3. [Q13291-1]
    XP_005245513.1. XM_005245456.1. [Q13291-3]
    UniGeneiHs.523660.

    Genome annotation databases

    EnsembliENST00000235739; ENSP00000235739; ENSG00000117090. [Q13291-3]
    ENST00000302035; ENSP00000306190; ENSG00000117090. [Q13291-1]
    GeneIDi6504.
    KEGGihsa:6504.
    UCSCiuc001fwl.4. human. [Q13291-1]

    Polymorphism databases

    DMDMi9297047.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33017 mRNA. Translation: AAA75380.1 .
    AL121985 , AL138930 Genomic DNA. Translation: CAH73505.1 .
    AL138930 , AL121985 Genomic DNA. Translation: CAI15154.1 .
    CH471121 Genomic DNA. Translation: EAW52706.1 .
    BC132792 mRNA. Translation: AAI32793.1 .
    AF252305 Genomic DNA. Translation: AAG10434.1 .
    CCDSi CCDS1207.1. [Q13291-1 ]
    PIRi S58892.
    RefSeqi NP_003028.1. NM_003037.3. [Q13291-1 ]
    XP_005245513.1. XM_005245456.1. [Q13291-3 ]
    UniGenei Hs.523660.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D4T X-ray 1.10 B 276-286 [» ]
    1D4W X-ray 1.80 C/D 276-286 [» ]
    1I3Z X-ray 2.15 B 273-286 [» ]
    1KA6 NMR - B 276-282 [» ]
    1KA7 NMR - B 275-286 [» ]
    1M27 X-ray 2.50 B 276-286 [» ]
    2DZF model - @ 1-335 [» ]
    2IE9 model - @ 1-335 [» ]
    2IFL model - @ 3-335 [» ]
    2IG5 model - @ 1-335 [» ]
    ProteinModelPortali Q13291.
    SMRi Q13291. Positions 32-140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112395. 9 interactions.
    DIPi DIP-40767N.
    IntActi Q13291. 5 interactions.
    MINTi MINT-113752.
    STRINGi 9606.ENSP00000306190.

    PTM databases

    PhosphoSitei Q13291.

    Polymorphism databases

    DMDMi 9297047.

    Proteomic databases

    PaxDbi Q13291.
    PRIDEi Q13291.

    Protocols and materials databases

    DNASUi 6504.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000235739 ; ENSP00000235739 ; ENSG00000117090 . [Q13291-3 ]
    ENST00000302035 ; ENSP00000306190 ; ENSG00000117090 . [Q13291-1 ]
    GeneIDi 6504.
    KEGGi hsa:6504.
    UCSCi uc001fwl.4. human. [Q13291-1 ]

    Organism-specific databases

    CTDi 6504.
    GeneCardsi GC01M160577.
    HGNCi HGNC:10903. SLAMF1.
    HPAi CAB002438.
    MIMi 603492. gene.
    neXtProti NX_Q13291.
    PharmGKBi PA35803.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40451.
    HOGENOMi HOG000125310.
    HOVERGENi HBG054224.
    InParanoidi Q13291.
    KOi K06536.
    OMAi LYEQVST.
    OrthoDBi EOG7Q8CQJ.
    PhylomeDBi Q13291.
    TreeFami TF334964.

    Miscellaneous databases

    EvolutionaryTracei Q13291.
    GeneWikii SLAMF1.
    GenomeRNAii 6504.
    NextBioi 25289.
    PROi Q13291.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13291.
    Bgeei Q13291.
    CleanExi HS_SLAMF1.
    Genevestigatori Q13291.

    Family and domain databases

    InterProi IPR007110. Ig-like_dom.
    IPR010407. Sig_lymph_act_molc_N.
    IPR015631. SLAM_fam_rcpts.
    [Graphical view ]
    PANTHERi PTHR12080. PTHR12080. 1 hit.
    Pfami PF06214. SLAM. 1 hit.
    [Graphical view ]
    ProDomi PD090491. Sig_lymph_act_molc_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: T-cell.
    2. "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].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Testis.
    5. "Absence of SLAM mutations in EBV-associated lymphoproliferative disease patients."
      Ferrand V., Li C., Romeo G., Yin L.
      J. Med. Virol. 70:131-136(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 265-288.
    6. "CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis."
      Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A., Sidorenko S.P.
      J. Immunol. 162:5719-5727(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    7. "SLAM (CDw150) is a cellular receptor for measles virus."
      Tatsuo H., Ono N., Tanaka K., Yanagi Y.
      Nature 406:893-897(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEASLES VIRUS HN PROTEIN.
    8. "The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM."
      Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S., Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E., Aversa G., Terhorst C.
      Nature 395:462-469(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A.
    9. "Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells."
      Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C., Howie D., Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B., Engel P., Eck M.J., Terhorst C.
      EMBO J. 20:5840-5852(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 273-286 IN COMPLEX WITH SH2D1B, INTERACTION WITH SH2D1B.
    10. "A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome."
      Hwang P.M., Li C., Morra M., Lillywhite J., Muhandiram D.R., Gertler F., Terhorst C., Kay L.E., Pawson T., Forman-Kay J.D., Li S.-C.
      EMBO J. 21:314-323(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 276-282 IN COMPLEX WITH SH2D1A.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A AND FYN.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-81.

    Entry informationi

    Entry nameiSLAF1_HUMAN
    AccessioniPrimary (citable) accession number: Q13291
    Secondary accession number(s): Q5W172, Q9HBE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 137 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

    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