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Protein

T-cell surface glycoprotein CD1a

Gene

CD1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711Glycolipid

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface glycoprotein CD1a
Alternative name(s):
T-cell surface antigen T6/Leu-6
Short name:
hTa1 thymocyte antigen
CD_antigen: CD1a
Gene namesi
Name:CD1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1634. CD1A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 300284ExtracellularSequence AnalysisAdd
BLAST
Transmembranei301 – 32121HelicalSequence AnalysisAdd
BLAST
Topological domaini322 – 3276CytoplasmicSequence Analysis

GO - Cellular componenti

  • endosome membrane Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26193.

Chemistry

DrugBankiDB00098. Antithymocyte globulin.

Polymorphism and mutation databases

BioMutaiCD1A.
DMDMi288558852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Chaini17 – 327311T-cell surface glycoprotein CD1aPRO_0000014578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)2 Publications
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi74 – 741N-linked (GlcNAc...)2 Publications
Disulfide bondi119 ↔ 183PROSITE-ProRule annotation
Glycosylationi145 – 1451N-linked (GlcNAc...)2 Publications
Disulfide bondi223 ↔ 278PROSITE-ProRule annotation2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP06126.
PaxDbiP06126.
PRIDEiP06126.

Expressioni

Tissue specificityi

Expressed on cortical thymocytes, epidermal Langerhans cells, dendritic cells, on certain T-cell leukemias, and in various other tissues.2 Publications

Gene expression databases

BgeeiP06126.
CleanExiHS_CD1A.
GenevisibleiP06126. HS.

Organism-specific databases

HPAiCAB000009.
HPA010734.

Interactioni

Subunit structurei

Heterodimer with B2M (beta-2-microglobulin). Interacts with CD74.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B2MP617692EBI-1036766,EBI-714718

Protein-protein interaction databases

BioGridi107347. 4 interactions.
IntActiP06126. 4 interactions.
MINTiMINT-4655994.
STRINGi9606.ENSP00000289429.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 359Combined sources
Beta strandi37 – 393Combined sources
Beta strandi42 – 498Combined sources
Beta strandi52 – 587Combined sources
Turni59 – 624Combined sources
Beta strandi63 – 686Combined sources
Helixi69 – 724Combined sources
Helixi77 – 10529Combined sources
Beta strandi109 – 11911Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi138 – 1447Combined sources
Beta strandi147 – 1504Combined sources
Helixi152 – 1543Combined sources
Helixi155 – 16511Combined sources
Helixi169 – 18012Combined sources
Helixi182 – 19817Combined sources
Beta strandi205 – 2106Combined sources
Beta strandi218 – 23114Combined sources
Beta strandi234 – 2396Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi260 – 26910Combined sources
Helixi270 – 2723Combined sources
Beta strandi276 – 2816Combined sources
Helixi283 – 2853Combined sources
Beta strandi290 – 2945Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONQX-ray2.15A/C18-294[»]
1XZ0X-ray2.80A/C18-294[»]
4X6CX-ray2.80A/C21-295[»]
4X6DX-ray2.98A/C21-295[»]
4X6EX-ray2.10A21-295[»]
4X6FX-ray1.91A21-295[»]
ProteinModelPortaliP06126.
SMRiP06126. Positions 24-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06126.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini184 – 291108Ig-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 945Glycolipid binding

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG26626.
GeneTreeiENSGT00480000042665.
HOGENOMiHOG000111666.
HOVERGENiHBG004453.
InParanoidiP06126.
KOiK06448.
OMAiNDITHNL.
OrthoDBiEOG7DZ8K9.
PhylomeDBiP06126.
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.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 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.

P06126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFLLLPLLA VLPGDGNADG LKEPLSFHVT WIASFYNHSW KQNLVSGWLS
60 70 80 90 100
DLQTHTWDSN SSTIVFLCPW SRGNFSNEEW KELETLFRIR TIRSFEGIRR
110 120 130 140 150
YAHELQFEYP FEIQVTGGCE LHSGKVSGSF LQLAYQGSDF VSFQNNSWLP
160 170 180 190 200
YPVAGNMAKH FCKVLNQNQH ENDITHNLLS DTCPRFILGL LDAGKAHLQR
210 220 230 240 250
QVKPEAWLSH GPSPGPGHLQ LVCHVSGFYP KPVWVMWMRG EQEQQGTQRG
260 270 280 290 300
DILPSADGTW YLRATLEVAA GEAADLSCRV KHSSLEGQDI VLYWEHHSSV
310 320
GFIILAVIVP LLLLIGLALW FRKRCFC
Length:327
Mass (Da):37,077
Last modified:February 9, 2010 - v4
Checksum:iC575C3C538F0AA29
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 712WS → V in AAA51933 (PubMed:2784820).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221K → N.
Corresponds to variant rs3087217 [ dbSNP | Ensembl ].
VAR_062522
Natural varianti30 – 301T → I.2 Publications
Corresponds to variant rs2269714 [ dbSNP | Ensembl ].
VAR_010209
Natural varianti68 – 681C → W.2 Publications
Corresponds to variant rs2269715 [ dbSNP | Ensembl ].
VAR_010210

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28825 mRNA. Translation: AAA51931.1.
M22167
, M22080, M22163, M22164, M22165, M22166 Genomic DNA. Translation: AAA51932.1.
AK312945 mRNA. Translation: BAG35786.1.
AL121986 Genomic DNA. Translation: CAI10848.1.
CH471121 Genomic DNA. Translation: EAW52843.1.
CH471121 Genomic DNA. Translation: EAW52844.1.
AF142665 Genomic DNA. Translation: AAD37578.1.
M27735 mRNA. Translation: AAA51933.1.
X04450 mRNA. Translation: CAA28049.1.
M14663 Genomic DNA. Translation: AAA51934.1.
CCDSiCCDS1174.1.
PIRiA39957. HLHUCD.
RefSeqiNP_001754.2. NM_001763.2.
UniGeneiHs.1309.

Genome annotation databases

EnsembliENST00000289429; ENSP00000289429; ENSG00000158477.
GeneIDi909.
KEGGihsa:909.
UCSCiuc001frt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28825 mRNA. Translation: AAA51931.1.
M22167
, M22080, M22163, M22164, M22165, M22166 Genomic DNA. Translation: AAA51932.1.
AK312945 mRNA. Translation: BAG35786.1.
AL121986 Genomic DNA. Translation: CAI10848.1.
CH471121 Genomic DNA. Translation: EAW52843.1.
CH471121 Genomic DNA. Translation: EAW52844.1.
AF142665 Genomic DNA. Translation: AAD37578.1.
M27735 mRNA. Translation: AAA51933.1.
X04450 mRNA. Translation: CAA28049.1.
M14663 Genomic DNA. Translation: AAA51934.1.
CCDSiCCDS1174.1.
PIRiA39957. HLHUCD.
RefSeqiNP_001754.2. NM_001763.2.
UniGeneiHs.1309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONQX-ray2.15A/C18-294[»]
1XZ0X-ray2.80A/C18-294[»]
4X6CX-ray2.80A/C21-295[»]
4X6DX-ray2.98A/C21-295[»]
4X6EX-ray2.10A21-295[»]
4X6FX-ray1.91A21-295[»]
ProteinModelPortaliP06126.
SMRiP06126. Positions 24-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107347. 4 interactions.
IntActiP06126. 4 interactions.
MINTiMINT-4655994.
STRINGi9606.ENSP00000289429.

Chemistry

DrugBankiDB00098. Antithymocyte globulin.

Polymorphism and mutation databases

BioMutaiCD1A.
DMDMi288558852.

Proteomic databases

MaxQBiP06126.
PaxDbiP06126.
PRIDEiP06126.

Protocols and materials databases

DNASUi909.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000289429; ENSP00000289429; ENSG00000158477.
GeneIDi909.
KEGGihsa:909.
UCSCiuc001frt.3. human.

Organism-specific databases

CTDi909.
GeneCardsiGC01P158224.
H-InvDBHIX0001190.
HGNCiHGNC:1634. CD1A.
HPAiCAB000009.
HPA010734.
MIMi188370. gene.
neXtProtiNX_P06126.
PharmGKBiPA26193.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG26626.
GeneTreeiENSGT00480000042665.
HOGENOMiHOG000111666.
HOVERGENiHBG004453.
InParanoidiP06126.
KOiK06448.
OMAiNDITHNL.
OrthoDBiEOG7DZ8K9.
PhylomeDBiP06126.
TreeFamiTF336723.

Miscellaneous databases

EvolutionaryTraceiP06126.
GeneWikiiCD1A.
GenomeRNAii909.
NextBioi3750.
PROiP06126.
SOURCEiSearch...

Gene expression databases

BgeeiP06126.
CleanExiHS_CD1A.
GenevisibleiP06126. HS.

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.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANTS ILE-30 AND TRP-68.
  2. "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].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-108.
  7. "Molecular cloning of CD1a (T6), a human epidermal dendritic cell marker related to class I MHC molecules."
    Longley J., Kraus J., Alonso M., Edelson R.
    J. Invest. Dermatol. 92:628-631(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-327.
  8. "A novel family of human major histocompatibility complex-related genes not mapping to chromosome 6."
    Calabi F., Milstein C.
    Nature 323:540-543(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-327.
    Tissue: T-cell.
  9. "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 202-294.
  10. "CD1a molecules traffic through the early recycling endosomal pathway in human Langerhans cells."
    Salamero J., Bausinger H., Mommaas A.M., Lipsker D., Proamer F., Cazenave J.-P., Goud B., de la Salle H., Hanau D.
    J. Invest. Dermatol. 116:401-408(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "CD1a-, b-, and c-restricted TCRs recognize both self and foreign antigens."
    Vincent M.S., Xiong X., Grant E.P., Peng W., Brenner M.B.
    J. Immunol. 175:6344-6351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Regulation of CD1a surface expression and antigen presentation by invariant chain and lipid rafts."
    Sloma I., Zilber M.-T., Vasselon T., Setterblad N., Cavallari M., Mori L., De Libero G., Charron D., Mooney N., Gelin C.
    J. Immunol. 180:980-987(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD47, TISSUE SPECIFICITY.
  13. "Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A."
    Zajonc D.M., Elsliger M.-A., Teyton L., Wilson I.A.
    Nat. Immunol. 4:808-815(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 18-300 IN COMPLEX WITH B2M AND SULFATIDE SELF-ANTIGEN, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, DISULFIDE BOND.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-294 IN COMPLEX WITH B2M AND LIPOPEPTIDE, GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, DISULFIDE BOND.
  15. Cited for: VARIANTS ILE-30 AND TRP-68, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCD1A_HUMAN
AccessioniPrimary (citable) accession number: P06126
Secondary accession number(s): D3DVD7
, Q13962, Q5TDJ8, Q9UMM4, Q9Y5M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 9, 2010
Last modified: July 22, 2015
This is version 152 of the entry and version 4 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.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.