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P29016 (CD1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD1b
Alternative name(s):
CD_antigen=CD1b
Gene names
Name:CD1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8

Subunit structure

Heterodimer with B2M (beta-2-microglobulin). Interacts with saposin C. Ref.8

Subcellular location

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. Ref.6 Ref.7 Ref.8

Tissue specificity

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

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.

Sequence similarities

Contains 1 Ig-like (immunoglobulin-like) domain.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

B2MP617693EBI-1033762,EBI-714718

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29016-1)

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.
Isoform 2 (identifier: P29016-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 333316T-cell surface glycoprotein CD1b
PRO_0000014579

Regions

Topological domain18 – 303286Extracellular Potential
Transmembrane304 – 32421Helical; Potential
Topological domain325 – 3339Cytoplasmic Potential
Domain185 – 295111Ig-like
Motif329 – 3324Internalization signal

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Ref.13
Glycosylation751N-linked (GlcNAc...) Ref.10 Ref.13
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Disulfide bond120 ↔ 184 Ref.11 Ref.12 Ref.13
Disulfide bond149 ↔ 163 Ref.11 Ref.12 Ref.13
Disulfide bond224 ↔ 279 Ref.11 Ref.12 Ref.13

Natural variations

Alternative sequence242 – 29655Missing in isoform 2.
VSP_016911

Experimental info

Mutagenesis329 – 3302YQ → AA: Strongly reduced internalization and trafficking to endosomes. Ref.6

Secondary structure

................................................ 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 7D02B670D4DE8CC7

FASTA33336,939
        10         20         30         40         50         60 
MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL DDLQIHGWDS 

        70         80         90        100        110        120 
DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YIFGFAREVQ DFAGDFQMKY PFEIQGIAGC 

       130        140        150        160        170        180 
ELHSGGAIVS FLRGALGGLD FLSVKNASCV PSPEGGSRAQ KFCALIIQYQ GIMETVRILL 

       190        200        210        220        230        240 
YETCPRYLLG VLNAGKADLQ RQVKPEAWLS SGPSPGPGRL QLVCHVSGFY PKPVWVMWMR 

       250        260        270        280        290        300 
GEQEQQGTQL GDILPNANWT WYLRATLDVA DGEAAGLSCR VKHSSLEGQD IILYWRNPTS 

       310        320        330 
IGSIVLAIIV PSLLLLLCLA LWYMRRRSYQ NIP 

« Hide

Isoform 2 [UniParc].

Checksum: 087FD5FF65921339
Show »

FASTA27830,740

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Saposin C is required for lipid presentation by human CD1b."
Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., Modlin R.L., Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., Kaufmann S.H.E., Schaible U.E.
Nat. Immunol. 5:169-174(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SAPOSIN C, SUBCELLULAR LOCATION.
[9]Erratum
Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., Modlin R.L., Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., Kaufmann S.H.E., Schaible U.E.
Nat. Immunol. 5:344-344(2004)
[10]"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.
[11]"Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl chains."
Gadola S.D., Zaccai N.R., Harlos K., Shepherd D., Castro-Palomino J.C., Ritter G., Schmidt R.R., Jones E.Y., Cerundolo V.
Nat. Immunol. 3:721-726(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 18-295 IN COMPLEXES WITH B2M; GANGLIOSIDE GM2 AND PHOSPHATIDYLINOSITOL, DISULFIDE BONDS.
[12]"The crystal structure of human CD1b with a bound bacterial glycolipid."
Batuwangala T., Shepherd D., Gadola S.D., Gibson K.J.C., Zaccai N.R., Fersht A.R., Besra G.S., Cerundolo V., Jones E.Y.
J. Immunol. 172:2382-2388(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 18-295 IN COMPLEX WITH B2M AND GLUCOSE MONOMYCOLATE, DISULFIDE BONDS.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22173 expand/collapse EMBL AC list , 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.
PIRHLHUCB. B39957.
RefSeqNP_001755.1. NM_001764.2.
UniGeneHs.1310.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP29016.
SMRP29016. Positions 22-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107348. 1 interaction.
IntActP29016. 1 interaction.
MINTMINT-242013.
STRING9606.ENSP00000357150.

PTM databases

PhosphoSiteP29016.

Polymorphism databases

DMDM115962.

Proteomic databases

PaxDbP29016.
PRIDEP29016.

Protocols and materials databases

DNASU910.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368168; ENSP00000357150; ENSG00000158485. [P29016-1]
GeneID910.
KEGGhsa:910.
UCSCuc001frw.3. human. [P29016-2]
uc001frx.3. human. [P29016-1]

Organism-specific databases

CTD910.
GeneCardsGC01M158297.
HGNCHGNC:1635. CD1B.
HPAHPA021824.
MIM188360. gene.
neXtProtNX_P29016.
PharmGKBPA26194.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79438.
HOGENOMHOG000111666.
HOVERGENHBG004453.
InParanoidP29016.
KOK06448.
OMAWAQTQGS.
PhylomeDBP29016.
TreeFamTF336723.

Gene expression databases

ArrayExpressP29016.
BgeeP29016.
CleanExHS_CD1B.
GenevestigatorP29016.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProIPR007110. 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]
PfamPF07654. C1-set. 1 hit.
[Graphical view]
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMSSF54452. SSF54452. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29016.
GenomeRNAi910.
NextBio3754.
PROP29016.
SOURCESearch...

Entry information

Entry nameCD1B_HUMAN
AccessionPrimary (citable) accession number: P29016
Secondary accession number(s): Q5TDK9, Q5TDL0, Q9UMM2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 134 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries