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P29016

- CD1B_HUMAN

UniProt

P29016 - CD1B_HUMAN

Protein

T-cell surface glycoprotein CD1b

Gene

CD1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. antigen processing and presentation Source: InterPro
    2. immune response Source: InterPro

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T-cell surface glycoprotein CD1b
    Alternative name(s):
    CD_antigen: CD1b
    Gene namesi
    Name:CD1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1635. CD1B.

    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. Localizes to cell surface lipid rafts.

    GO - Cellular componenti

    1. endosome membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: ProtInc
    3. lysosomal membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi329 – 3302YQ → AA: Strongly reduced internalization and trafficking to endosomes. 1 Publication

    Organism-specific databases

    PharmGKBiPA26194.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 333316T-cell surface glycoprotein CD1bPRO_0000014579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)1 Publication
    Glycosylationi75 – 751N-linked (GlcNAc...)2 Publications
    Disulfide bondi120 ↔ 184
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi149 ↔ 163
    Disulfide bondi224 ↔ 279
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP29016.
    PaxDbiP29016.
    PRIDEiP29016.

    PTM databases

    PhosphoSiteiP29016.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP29016.
    BgeeiP29016.
    CleanExiHS_CD1B.
    GenevestigatoriP29016.

    Organism-specific databases

    HPAiHPA021824.

    Interactioni

    Subunit structurei

    Heterodimer with B2M (beta-2-microglobulin). Interacts with saposin C.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    B2MP617693EBI-1033762,EBI-714718

    Protein-protein interaction databases

    BioGridi107348. 1 interaction.
    IntActiP29016. 1 interaction.
    MINTiMINT-242013.
    STRINGi9606.ENSP00000357150.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 3812
    Beta strandi41 – 5010
    Beta strandi53 – 597
    Turni60 – 634
    Beta strandi64 – 674
    Turni70 – 756
    Helixi78 – 10225
    Turni103 – 1075
    Beta strandi110 – 12213
    Beta strandi128 – 1369
    Beta strandi139 – 1457
    Beta strandi148 – 1514
    Helixi153 – 1553
    Helixi156 – 16611
    Helixi170 – 18112
    Helixi183 – 19412
    Helixi196 – 1994
    Beta strandi206 – 2138
    Beta strandi219 – 23214
    Beta strandi234 – 2407
    Beta strandi254 – 2563
    Turni257 – 2593
    Beta strandi261 – 27010
    Helixi271 – 2733
    Beta strandi277 – 2837
    Helixi284 – 2863
    Beta strandi291 – 2966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GZPX-ray2.80A18-295[»]
    1GZQX-ray2.26A18-295[»]
    1UQSX-ray3.10A18-295[»]
    2H26X-ray1.80A19-298[»]
    3OV6X-ray2.50A27-295[»]
    3T8XX-ray1.90A/C19-298[»]
    ProteinModelPortaliP29016.
    SMRiP29016. Positions 22-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29016.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 303286ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini325 – 3339CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei304 – 32421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini185 – 295111Ig-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi329 – 3324Internalization signal

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG79438.
    HOGENOMiHOG000111666.
    HOVERGENiHBG004453.
    InParanoidiP29016.
    KOiK06448.
    OMAiWAQTQGS.
    PhylomeDBiP29016.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P29016-1) [UniParc]FASTAAdd to Basket

    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

    MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL    50
    DDLQIHGWDS DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YIFGFAREVQ 100
    DFAGDFQMKY PFEIQGIAGC ELHSGGAIVS FLRGALGGLD FLSVKNASCV 150
    PSPEGGSRAQ KFCALIIQYQ GIMETVRILL YETCPRYLLG VLNAGKADLQ 200
    RQVKPEAWLS SGPSPGPGRL QLVCHVSGFY PKPVWVMWMR GEQEQQGTQL 250
    GDILPNANWT WYLRATLDVA DGEAAGLSCR VKHSSLEGQD IILYWRNPTS 300
    IGSIVLAIIV PSLLLLLCLA LWYMRRRSYQ NIP 333
    Length:333
    Mass (Da):36,939
    Last modified:December 1, 1992 - v1
    Checksum:i7D02B670D4DE8CC7
    GO
    Isoform 2 (identifier: P29016-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         242-296: Missing.

    Show »
    Length:278
    Mass (Da):30,740
    Checksum:i087FD5FF65921339
    GO

    Sequence cautioni

    The sequence CAI10852.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei242 – 29655Missing in isoform 2. CuratedVSP_016911Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22173
    , M22168, M22169, M22170, M22171, M22172 Genomic DNA. Translation: AAA51940.1.
    M28826 mRNA. Translation: AAA51939.1.
    AL121986 Genomic DNA. Translation: CAI10852.1. Sequence problems.
    AL121986 Genomic DNA. Translation: CAI10853.1.
    BC069481 mRNA. Translation: AAH69481.1.
    BC074747 mRNA. Translation: AAH74747.1.
    BC104216 mRNA. Translation: AAI04217.1.
    BC104217 mRNA. Translation: AAI04218.1.
    M14665 Genomic DNA. Translation: AAA51936.1.
    CCDSiCCDS1176.1. [P29016-1]
    PIRiB39957. HLHUCB.
    RefSeqiNP_001755.1. NM_001764.2. [P29016-1]
    UniGeneiHs.1310.

    Genome annotation databases

    EnsembliENST00000368168; ENSP00000357150; ENSG00000158485. [P29016-1]
    GeneIDi910.
    KEGGihsa:910.
    UCSCiuc001frw.3. human. [P29016-2]
    uc001frx.3. human. [P29016-1]

    Polymorphism databases

    DMDMi115962.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22173
    , M22168 , M22169 , M22170 , M22171 , M22172 Genomic DNA. Translation: AAA51940.1 .
    M28826 mRNA. Translation: AAA51939.1 .
    AL121986 Genomic DNA. Translation: CAI10852.1 . Sequence problems.
    AL121986 Genomic DNA. Translation: CAI10853.1 .
    BC069481 mRNA. Translation: AAH69481.1 .
    BC074747 mRNA. Translation: AAH74747.1 .
    BC104216 mRNA. Translation: AAI04217.1 .
    BC104217 mRNA. Translation: AAI04218.1 .
    M14665 Genomic DNA. Translation: AAA51936.1 .
    CCDSi CCDS1176.1. [P29016-1 ]
    PIRi B39957. HLHUCB.
    RefSeqi NP_001755.1. NM_001764.2. [P29016-1 ]
    UniGenei Hs.1310.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GZP X-ray 2.80 A 18-295 [» ]
    1GZQ X-ray 2.26 A 18-295 [» ]
    1UQS X-ray 3.10 A 18-295 [» ]
    2H26 X-ray 1.80 A 19-298 [» ]
    3OV6 X-ray 2.50 A 27-295 [» ]
    3T8X X-ray 1.90 A/C 19-298 [» ]
    ProteinModelPortali P29016.
    SMRi P29016. Positions 22-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107348. 1 interaction.
    IntActi P29016. 1 interaction.
    MINTi MINT-242013.
    STRINGi 9606.ENSP00000357150.

    PTM databases

    PhosphoSitei P29016.

    Polymorphism databases

    DMDMi 115962.

    Proteomic databases

    MaxQBi P29016.
    PaxDbi P29016.
    PRIDEi P29016.

    Protocols and materials databases

    DNASUi 910.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368168 ; ENSP00000357150 ; ENSG00000158485 . [P29016-1 ]
    GeneIDi 910.
    KEGGi hsa:910.
    UCSCi uc001frw.3. human. [P29016-2 ]
    uc001frx.3. human. [P29016-1 ]

    Organism-specific databases

    CTDi 910.
    GeneCardsi GC01M158297.
    HGNCi HGNC:1635. CD1B.
    HPAi HPA021824.
    MIMi 188360. gene.
    neXtProti NX_P29016.
    PharmGKBi PA26194.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG79438.
    HOGENOMi HOG000111666.
    HOVERGENi HBG004453.
    InParanoidi P29016.
    KOi K06448.
    OMAi WAQTQGS.
    PhylomeDBi P29016.
    TreeFami TF336723.

    Miscellaneous databases

    EvolutionaryTracei P29016.
    GenomeRNAii 910.
    NextBioi 3754.
    PROi P29016.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29016.
    Bgeei P29016.
    CleanExi HS_CD1B.
    Genevestigatori P29016.

    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. "Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c."
      Martin L.H., Calabi F., Lefebvre F.-A., Bilsland C.A.G., Milstein C.
      Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts."
      Aruffo A., Seed B.
      J. Immunol. 143:1723-1730(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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. "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: Lung.
    5. "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.
    6. "The alphabeta T cell response to self-glycolipids shows a novel mechanism of CD1b loading and a requirement for complex oligosaccharides."
      Shamshiev A., Donda A., Prigozy T.I., Mori L., Chigorno V., Benedict C.A., Kappos L., Sonnino S., Kronenberg M., De Libero G.
      Immunity 13:255-264(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 329-TYR-GLN-330, SUBCELLULAR LOCATION.
    7. "Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens."
      Briken V., Jackman R.M., Watts G.F.M., Rogers R.A., Porcelli S.A.
      J. Exp. Med. 192:281-288(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. Cited for: FUNCTION, INTERACTION WITH SAPOSIN C, SUBCELLULAR LOCATION.
    9. "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-75.
      Tissue: Leukemic T-cell.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 18-295 IN COMPLEXES WITH B2M; GANGLIOSIDE GM2 AND PHOSPHATIDYLINOSITOL, DISULFIDE BONDS.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 18-295 IN COMPLEX WITH B2M AND GLUCOSE MONOMYCOLATE, DISULFIDE BONDS.
    12. "Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b."
      Garcia-Alles L.F., Versluis K., Maveyraud L., Vallina A.T., Sansano S., Bello N.F., Gober H.-J., Guillet V., de la Salle H., Puzo G., Mori L., Heck A.J.R., De Libero G., Mourey L.
      EMBO J. 25:3684-3692(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-298 IN COMPLEX WITH B2M; PHOSPHATIDYLCHOLINE AND SPACER LIGAND, GLYCOSYLATION AT ASN-38 AND ASN-75, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCD1B_HUMAN
    AccessioniPrimary (citable) accession number: P29016
    Secondary accession number(s): Q5TDK9, Q5TDL0, Q9UMM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 138 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 or lysosomes, before trafficking back to the cell surface. Interaction with saposin C is required for the loading of bacterial lipid antigens onto CD1B in the lysosome.

    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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3