Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15812 (CD1E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD1e, membrane-associated

Short name=hCD1e
Alternative name(s):
R2G1
CD_antigen=CD1e

Cleaved into the following chain:

  1. T-cell surface glycoprotein CD1e, soluble
    Short name=sCD1e
Gene names
Name:CD1E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

T-cell surface glycoprotein CD1e, soluble binds diacetylated lipids, including phosphatidyl inositides and diacylated sulfoglycolipids, and is required for the presentation of glycolipid antigens on the cell surface. The membrane-associated form is not active. Ref.2 Ref.10 Ref.14

Subunit structure

Heterodimer with B2M (beta-2-microglobulin). The association with B2M appears to be facilitated by the presence of the propeptide. Ref.14

Subcellular location

T-cell surface glycoprotein CD1e, membrane-associated: Golgi apparatus membrane; Single-pass type I membrane protein. Early endosome. Late endosome. Note: Predominantly localized in the trans-Golgi network in immature dendritic cells, and as a cleaved, soluble protein in the lysosome lumen of mature dendritic cells. Ref.2 Ref.11 Ref.12

T-cell surface glycoprotein CD1e, soluble: Lysosome lumen Ref.2 Ref.11 Ref.12.

Tissue specificity

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

Post-translational modification

Mono-ubiquitinated.

Proteolytically cleaved in late endosomes to yield a soluble form. Ref.2 Ref.11 Ref.12

Polymorphism

Six alleles of CD1E are known. CD1E*01 has His-102/Gln-106/Ser-149/Arg-164/Leu-194, CD1E*02 has His-102/Arg-106/Ser-149/Arg-164/Leu-194, CD1E*03 (9L) has His-102/Gln-106/Ser-149/Trp-164/Leu-194, CD1E*04 (15L) has His-102/Gln-106/Ser-149/Arg-164/Pro-194, CD1E*05 has Arg-102/Arg-106/Ser-149/Arg-164/Leu-194 and CD1E*06 has His-102/Arg-106/Asn-149/Arg-164/Leu-194. The sequence shown is that of allele CD1E*01.

Sequence similarities

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

Sequence caution

The sequence CAA33100.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15812-1)

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: P15812-2)

The sequence of this isoform differs from the canonical sequence as follows:
     334-345: Missing.
Isoform 3 (identifier: P15812-3)

The sequence of this isoform differs from the canonical sequence as follows:
     268-290: YLRATLDVAAGEAAGLSCRVKHS → WIFHLSHPDLFDCDSYPGHIGCS
     291-388: Missing.
Isoform 4 (identifier: P15812-4)

The sequence of this isoform differs from the canonical sequence as follows:
     248-302: Missing.
     334-345: Missing.
Isoform 5 (identifier: P15812-5)

The sequence of this isoform differs from the canonical sequence as follows:
     119-209: YPFEIQILAG...AGESELKRKV → L
Isoform 6 (identifier: P15812-6)

The sequence of this isoform differs from the canonical sequence as follows:
     119-209: YPFEIQILAG...AGESELKRKV → L
     334-345: Missing.
Isoform 7 (identifier: P15812-7)

The sequence of this isoform differs from the canonical sequence as follows:
     119-209: YPFEIQILAG...AGESELKRKV → L
     248-302: Missing.
     334-345: Missing.
Isoform 8 (identifier: P15812-8)

The sequence of this isoform differs from the canonical sequence as follows:
     20-208: Missing.
Isoform 9 (identifier: P15812-9)

The sequence of this isoform differs from the canonical sequence as follows:
     20-208: Missing.
     334-345: Missing.
Isoform 10 (identifier: P15812-10)

The sequence of this isoform differs from the canonical sequence as follows:
     20-208: Missing.
     268-290: YLRATLDVAAGEAAGLSCRVKHS → WIFHLSHPDLFDCDSYPGHIGCS
     291-388: Missing.
Isoform 11 (identifier: P15812-11)

The sequence of this isoform differs from the canonical sequence as follows:
     20-208: Missing.
     248-302: Missing.
Isoform 12 (identifier: P15812-12)

The sequence of this isoform differs from the canonical sequence as follows:
     20-208: Missing.
     248-302: Missing.
     334-345: Missing.
Isoform 13 (identifier: P15812-13)

The sequence of this isoform differs from the canonical sequence as follows:
     20-119: APQALQSYHL...ASAGQFQLEY → D

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 388369T-cell surface glycoprotein CD1e, membrane-associated
PRO_0000014582
Propeptide20 – 3112Removed in sCD1e
PRO_0000379780
Chain32 – 388357T-cell surface glycoprotein CD1e, soluble
PRO_0000379781

Regions

Transmembrane305 – 32521Helical; Potential
Domain191 – 301111Ig-like

Amino acid modifications

Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Disulfide bond230 ↔ 285 By similarity

Natural variations

Alternative sequence20 – 208189Missing in isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12.
VSP_037708
Alternative sequence20 – 119100APQAL…FQLEY → D in isoform 13.
VSP_046961
Alternative sequence119 – 20991YPFEI…LKRKV → L in isoform 5, isoform 6 and isoform 7.
VSP_037709
Alternative sequence248 – 30255Missing in isoform 4, isoform 7, isoform 11 and isoform 12.
VSP_037710
Alternative sequence268 – 29023YLRAT…RVKHS → WIFHLSHPDLFDCDSYPGHI GCS in isoform 3 and isoform 10.
VSP_037711
Alternative sequence291 – 38898Missing in isoform 3 and isoform 10.
VSP_037712
Alternative sequence334 – 34512Missing in isoform 2, isoform 4, isoform 6, isoform 7, isoform 9 and isoform 12.
VSP_037713
Natural variant151G → E.
Corresponds to variant rs3180089 [ dbSNP | Ensembl ].
VAR_056035
Natural variant1021H → R in allele CD1E*05. Ref.7
Corresponds to variant rs2873587 [ dbSNP | Ensembl ].
VAR_058324
Natural variant1061Q → R in allele CD1E*02, allele CD1E*05 and CD1E*06. Ref.2 Ref.6 Ref.7
Corresponds to variant rs1065457 [ dbSNP | Ensembl ].
VAR_010191
Natural variant1491S → N in allele CD1E*05. Ref.7
Corresponds to variant rs35116276 [ dbSNP | Ensembl ].
VAR_058325
Natural variant1641R → W in allele CD1E*03. Ref.7 Ref.8
VAR_010192
Natural variant1941L → P in allele CD1E*04; impairs localization to late endosomal compartments and lipid antigen presentation. Ref.8 Ref.13
Corresponds to variant rs200741122 [ dbSNP | Ensembl ].
VAR_010193

Experimental info

Sequence conflict2091V → A in BAG64215. Ref.3
Sequence conflict2481E → G in BAG64215. Ref.3

Secondary structure

..................................................... 388
Helix Strand Turn

Details...

Sequences

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

Last modified July 28, 2009. Version 2.
Checksum: F6503AE9608C6568

FASTA38843,626
        10         20         30         40         50         60 
MLLLFLLFEG LCCPGENTAA PQALQSYHLA AEEQLSFRML QTSSFANHSW AHSEGSGWLG 

        70         80         90        100        110        120 
DLQTHGWDTV LGTIRFLKPW SHGNFSKQEL KNLQSLFQLY FHSFIQIVQA SAGQFQLEYP 

       130        140        150        160        170        180 
FEIQILAGCR MNAPQIFLNM AYQGSDFLSF QGISWEPSPG AGIRAQNICK VLNRYLDIKE 

       190        200        210        220        230        240 
ILQSLLGHTC PRFLAGLMEA GESELKRKVK PEAWLSCGPS PGPGRLQLVC HVSGFYPKPV 

       250        260        270        280        290        300 
WVMWMRGEQE QRGTQRGDVL PNADETWYLR ATLDVAAGEA AGLSCRVKHS SLGGHDLIIH 

       310        320        330        340        350        360 
WGGYSIFLIL ICLTVIVTLV ILVVVDSRLK KQSSNKNILS PHTPSPVFLM GANTQDTKNS 

       370        380 
RHQFCLAQVS WIKNRVLKKW KTRLNQLW 

« Hide

Isoform 2 [UniParc].

Checksum: 52F553915C2B64C6
Show »

FASTA37642,350
Isoform 3 [UniParc].

Checksum: 424FE9E60BE8A14C
Show »

FASTA29032,724
Isoform 4 [UniParc].

Checksum: 89D16362E367AF3F
Show »

FASTA32136,381
Isoform 5 [UniParc].

Checksum: 1F49C172E6EDCDE0
Show »

FASTA29833,553
Isoform 6 [UniParc].

Checksum: 87E830F20FD041B0
Show »

FASTA28632,276
Isoform 7 [UniParc].

Checksum: 453FEB8FE4A34853
Show »

FASTA23126,308
Isoform 8 [UniParc].

Checksum: 51D51CBAF23FA31E
Show »

FASTA19922,263
Isoform 9 [UniParc].

Checksum: DB1402070352AEF8
Show »

FASTA18720,987
Isoform 10 [UniParc].

Checksum: 41978EA9D317C67E
Show »

FASTA10111,361
Isoform 11 [UniParc].

Checksum: D433B9593AE045AB
Show »

FASTA14416,294
Isoform 12 [UniParc].

Checksum: 146E065421A1E709
Show »

FASTA13215,018
Isoform 13 [UniParc].

Checksum: 4377F02F388916F9
Show »

FASTA28932,303

References

« Hide 'large scale' references
[1]"Two classes of CD1 genes."
Calabi F., Jarvis J.M., Martin L., Milstein C.
Eur. J. Immunol. 19:285-292(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of CD1e, a third type of CD1 molecule expressed in dendritic cells."
Angenieux C., Salamero J., Fricker D., Cazenave J.-P., Goud B., Hanau D., de La Salle H.
J. Biol. Chem. 275:37757-37764(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12), VARIANT ARG-106, FUNCTION, INTERACTION WITH B2M, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[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. expand/collapse author list , 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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-386 (ISOFORM 13).
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. 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] (ALLELE CD1E*01).
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES CD1E*01).
[6]"Polymorphism of human CD1 genes."
Han M., Hannick L.I., DiBrino M., Robinson M.A.
Tissue Antigens 54:122-127(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-118, VARIANT ARG-106.
[7]"Two novel CD1 E alleles identified in black African individuals."
Tamouza R., Sghiri R., Ramasawmy R., Neonato M.G., Mombo L.E., Poirier J.C., Schaeffer V., Fortier C., Labie D., Girot R., Toubert A., Krishnamoorthy R., Charron D.
Tissue Antigens 59:417-420(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-208 (ALLELES CD1E*05 AND CD1E*06), VARIANTS ARG-102; ARG-106; ASN-149 AND TRP-164.
[8]"Identification of two novel human CD1E alleles."
Mirones I., Oteo M., Parra-Cuadrado J.F., Martinez-Naves E.
Tissue Antigens 56:159-161(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-208 (ALLELES CD1E*03 AND CD1E*04), VARIANTS TRP-164 AND PRO-194.
[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 209-301.
[10]"Assistance of microbial glycolipid antigen processing by CD1e."
de la Salle H., Mariotti S., Angenieux C., Gilleron M., Garcia-Alles L.-F., Malm D., Berg T., Paoletti S., Maitre B., Mourey L., Salamero J., Cazenave J.-P., Hanau D., Mori L., Puzo G., De Libero G.
Science 310:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Control of the intracellular pathway of CD1e."
Maitre B., Angenieux C., Salamero J., Hanau D., Fricker D., Signorino F., Proamer F., Cazenave J.-P., Goud B., Tourne S., de la Salle H.
Traffic 9:431-445(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, PROTEOLYTIC PROCESSING.
[12]"The assembly of CD1e is controlled by an N-terminal propeptide which is processed in endosomal compartments."
Maitre B., Angenieux C., Wurtz V., Layre E., Gilleron M., Collmann A., Mariotti S., Mori L., Fricker D., Cazenave J.P., van Dorsselaer A., Gachet C., de Libero G., Puzo G., Hanau D., de la Salle H.
Biochem. J. 419:661-668(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
[13]"A naturally occurring mutation in CD1e impairs lipid antigen presentation."
Tourne S., Maitre B., Collmann A., Layre E., Mariotti S., Signorino-Gelo F., Loch C., Salamero J., Gilleron M., Angenieux C., Cazenave J.P., Mori L., Hanau D., Puzo G., De Libero G., de la Salle H.
J. Immunol. 180:3642-3646(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, VARIANT PRO-194.
[14]"Crystal structure of human CD1e reveals a groove suited for lipid-exchange processes."
Garcia-Alles L.F., Giacometti G., Versluis C., Maveyraud L., de Paepe D., Guiard J., Tranier S., Gilleron M., Prandi J., Hanau D., Heck A.J., Mori L., De Libero G., Puzo G., Mourey L., de la Salle H.
Proc. Natl. Acad. Sci. U.S.A. 108:13230-13235(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-303 IN COMPLEX WITH B2M, FUNCTION, LIPID-BINDING, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14975 Genomic DNA. Translation: CAA33100.1. Sequence problems.
AJ289111 mRNA. Translation: CAB93150.1.
AJ289112 mRNA. Translation: CAB93151.1.
AJ289113 mRNA. Translation: CAB93152.1.
AJ289114 mRNA. Translation: CAB93153.1.
AJ289115 mRNA. Translation: CAB93154.1.
AJ289116 mRNA. Translation: CAB93155.1.
AJ289117 mRNA. Translation: CAB93156.1.
AJ289118 mRNA. Translation: CAB93157.1.
AJ289119 mRNA. Translation: CAB93158.1.
AJ289120 mRNA. Translation: CAB93159.1.
AJ289121 mRNA. Translation: CAB93160.1.
AJ289122 mRNA. Translation: CAB93161.1.
AK303108 mRNA. Translation: BAG64215.1.
AK311643 mRNA. No translation available.
AL121986 Genomic DNA. Translation: CAI10854.1.
AL121986 Genomic DNA. Translation: CAI10855.1.
AL121986 Genomic DNA. Translation: CAI10856.1.
AL121986 Genomic DNA. Translation: CAI10857.1.
AL121986 Genomic DNA. Translation: CAI10858.1.
AL121986 Genomic DNA. Translation: CAI10859.1.
AL121986 Genomic DNA. Translation: CAI10860.1.
AL121986 Genomic DNA. Translation: CAI10861.1.
AL121986 Genomic DNA. Translation: CAI10862.1.
AL121986 Genomic DNA. Translation: CAI10863.1.
AL121986 Genomic DNA. Translation: CAI10864.1.
AL121986 Genomic DNA. Translation: CAI10865.1.
CH471121 Genomic DNA. Translation: EAW52828.1.
CH471121 Genomic DNA. Translation: EAW52830.1.
CH471121 Genomic DNA. Translation: EAW52831.1.
CH471121 Genomic DNA. Translation: EAW52832.1.
CH471121 Genomic DNA. Translation: EAW52833.1.
CH471121 Genomic DNA. Translation: EAW52834.1.
CH471121 Genomic DNA. Translation: EAW52835.1.
CH471121 Genomic DNA. Translation: EAW52837.1.
CH471121 Genomic DNA. Translation: EAW52838.1.
CH471121 Genomic DNA. Translation: EAW52839.1.
CH471121 Genomic DNA. Translation: EAW52840.1.
AF142669 Genomic DNA. Translation: AAD37582.1.
AH010757 Genomic DNA. Translation: AAK52913.1.
AH010758 Genomic DNA. Translation: AAK52914.1.
AJ251334 Genomic DNA. Translation: CAB82829.1.
AJ251335 Genomic DNA. Translation: CAC07175.1.
M14666 Genomic DNA. Translation: AAA51937.1.
PIRHLHUR2. S07716.
RefSeqNP_001036048.1. NM_001042583.2.
NP_001036049.1. NM_001042584.2.
NP_001036050.1. NM_001042585.2.
NP_001036051.1. NM_001042586.2.
NP_001036052.1. NM_001042587.2.
NP_001172036.1. NM_001185107.1.
NP_001172037.1. NM_001185108.1.
NP_001172039.1. NM_001185110.1.
NP_001172041.1. NM_001185112.1.
NP_001172042.1. NM_001185113.1.
NP_001172043.1. NM_001185114.1.
NP_001172044.1. NM_001185115.1.
NP_112155.2. NM_030893.3.
UniGeneHs.249217.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S6CX-ray2.90A32-303[»]
ProteinModelPortalP15812.
SMRP15812. Positions 33-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107351. 1 interaction.
MINTMINT-4656055.

Polymorphism databases

DMDM254763260.

Proteomic databases

PaxDbP15812.
PRIDEP15812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368154; ENSP00000357136; ENSG00000158488. [P15812-11]
ENST00000368155; ENSP00000357137; ENSG00000158488. [P15812-7]
ENST00000368156; ENSP00000357138; ENSG00000158488. [P15812-6]
ENST00000368157; ENSP00000357139; ENSG00000158488. [P15812-12]
ENST00000368160; ENSP00000357142; ENSG00000158488. [P15812-2]
ENST00000368161; ENSP00000357143; ENSG00000158488. [P15812-3]
ENST00000368163; ENSP00000357145; ENSG00000158488. [P15812-4]
ENST00000368164; ENSP00000357146; ENSG00000158488. [P15812-10]
ENST00000368165; ENSP00000357147; ENSG00000158488. [P15812-5]
ENST00000368166; ENSP00000357148; ENSG00000158488. [P15812-9]
ENST00000368167; ENSP00000357149; ENSG00000158488. [P15812-1]
ENST00000444681; ENSP00000402906; ENSG00000158488. [P15812-13]
ENST00000452291; ENSP00000416228; ENSG00000158488. [P15812-8]
GeneID913.
KEGGhsa:913.
UCSCuc001fry.3. human. [P15812-4]
uc001frz.3. human. [P15812-6]
uc001fsa.3. human. [P15812-11]
uc001fsc.3. human. [P15812-8]
uc001fsd.3. human. [P15812-3]
uc001fse.3. human. [P15812-1]
uc001fsf.3. human. [P15812-2]
uc001fsg.3. human. [P15812-10]
uc001fsh.3. human. [P15812-9]
uc001fsj.3. human. [P15812-7]
uc001fsk.3. human. [P15812-5]
uc010pig.2. human. [P15812-12]

Organism-specific databases

CTD913.
GeneCardsGC01P158323.
HGNCHGNC:1638. CD1E.
HPAHPA057769.
MIM188411. gene.
neXtProtNX_P15812.
PharmGKBPA26197.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26626.
HOVERGENHBG004453.
InParanoidP15812.
KOK06448.
OrthoDBEOG7DZ8K9.
PhylomeDBP15812.
TreeFamTF336723.

Gene expression databases

ArrayExpressP15812.
BgeeP15812.
CleanExHS_CD1E.
GenevestigatorP15812.

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

GeneWikiCD1E.
GenomeRNAi913.
NextBio3766.
PROP15812.
SOURCESearch...

Entry information

Entry nameCD1E_HUMAN
AccessionPrimary (citable) accession number: P15812
Secondary accession number(s): B4DZV3 expand/collapse secondary AC list , E7EP01, Q5TDJ9, Q5TDK3, Q5TDK4, Q5TDK5, Q5TDK6, Q5TDK8, Q5TDL1, Q712E4, Q712E5, Q712E6, Q712E7, Q712E8, Q712E9, Q712F0, Q712F1, Q712F2, Q712F3, Q712F4, Q712F5, Q96TD0, Q96TD1, Q9UMM1, Q9Y5M3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 131 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

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