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P06729 (CD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface antigen CD2
Alternative name(s):
Erythrocyte receptor
LFA-2
LFA-3 receptor
Rosette receptor
T-cell surface antigen T11/Leu-5
CD_antigen=CD2
Gene names
Name:CD2
Synonyms:SRBC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.

Subunit structure

Interacts with CD2AP By similarity. Interacts with PSTPIP1. Ref.11

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation

Traceable author statement PubMed 2471997. Source: UniProtKB

apoptotic process

Traceable author statement PubMed 10575274PubMed 9270771. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Traceable author statement PubMed 10575274. Source: UniProtKB

cell-cell adhesion

Non-traceable author statement Ref.14. Source: UniProtKB

heterotypic cell-cell adhesion

Inferred from direct assay PubMed 15345303. Source: UniProt

leukocyte migration

Traceable author statement. Source: Reactome

membrane raft polarization

Traceable author statement PubMed 11376005PubMed 11591762. Source: UniProtKB

natural killer cell activation

Non-traceable author statement PubMed 12714509. Source: UniProtKB

positive regulation of interleukin-8 secretion

Inferred from mutant phenotype PubMed 19109405. Source: UniProt

positive regulation of myeloid dendritic cell activation

Non-traceable author statement PubMed 12714509. Source: UniProtKB

positive regulation of tumor necrosis factor production

Inferred from direct assay PubMed 19109405. Source: UniProt

regulation of T cell differentiation

Non-traceable author statement PubMed 11544295. Source: UniProtKB

   Cellular_componentanchored component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 15345303. Source: UniProt

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from direct assay PubMed 21460847. Source: MGI

extracellular region

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Non-traceable author statement Ref.14. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionreceptor activity

Non-traceable author statement Ref.14. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 17344209. Source: UniProt

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 351327T-cell surface antigen CD2
PRO_0000014600

Regions

Topological domain25 – 209185Extracellular Potential
Transmembrane210 – 23526Helical; Potential
Topological domain236 – 351116Cytoplasmic Potential
Domain25 – 128104Ig-like V-type
Domain129 – 20981Ig-like C2-type
Region61 – 7515LFA-3 (CD58) binding region 1
Region106 – 12015LFA-3 (CD58) binding region 2
Compositional bias282 – 33857Pro-rich

Amino acid modifications

Glycosylation891N-linked (GlcNAc...)
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Disulfide bond139 ↔ 203 Ref.12
Disulfide bond146 ↔ 186 Ref.12

Natural variations

Natural variant2171C → Y in a breast cancer sample; somatic mutation. Ref.15
VAR_035504
Natural variant2661H → Q. Ref.2 Ref.6 Ref.8
Corresponds to variant rs699738 [ dbSNP | Ensembl ].
VAR_017104
Natural variant3391H → N.
Corresponds to variant rs35880225 [ dbSNP | Ensembl ].
VAR_033608

Experimental info

Mutagenesis671K → R: Loss of LFA-3 binding.
Mutagenesis701Q → K: Loss of LFA-3 binding.
Mutagenesis1101Y → D: Loss of LFA-3 and CD59 binding.
Mutagenesis1111D → H: Loss of LFA-3 and CD59 binding.
Sequence conflict2871G → A Ref.3
Sequence conflict339 – 35113HGAAE…SPSSN → MGQQKTHCPLPLIKKDRNCL FQ in AAA51946. Ref.3

Secondary structure

........................................ 351
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06729 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: A03D853C3B618917

FASTA35139,448
        10         20         30         40         50         60 
MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM SDDIDDIKWE 

        70         80         90        100        110        120 
KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD DQDIYKVSIY DTKGKNVLEK 

       130        140        150        160        170        180 
IFDLKIQERV SKPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHLKLSQR VITHKWTTSL 

       190        200        210        220        230        240 
SAKFKCTAGN KVSKESSVEP VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ 

       250        260        270        280        290        300 
RSRRNDEELE TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP 

       310        320        330        340        350 
GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS N 

« Hide

References

« Hide 'large scale' references
[1]"Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes."
Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L.
Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure."
Seed B., Aruffo A.
Proc. Natl. Acad. Sci. U.S.A. 84:3365-3369(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-266.
[3]"Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen."
Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.
Proc. Natl. Acad. Sci. U.S.A. 83:8718-8722(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Erratum
Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.
Proc. Natl. Acad. Sci. U.S.A. 84:7256-7256(1987)
Cited for: SEQUENCE REVISION.
[5]"Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes."
Sayre P.H., Chang H.-C., Hussey R.E., Brown N.R., Richardson N.E., Spagnoli G., Clayton L.K., Reinherz E.L.
Proc. Natl. Acad. Sci. U.S.A. 84:2941-2945(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"The structure of the human CD2 gene and its expression in transgenic mice."
Lang G., Wotton D., Owen M.J., Sewell W.A., Brown M.H., Mason D.Y., Crumpton M.J., Kioussis D.
EMBO J. 7:1675-1682(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-266.
[7]"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].
[8]"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], VARIANT GLN-266.
Tissue: Pancreas and Spleen.
[9]"Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)."
Peterson A., Seed B.
Nature 329:842-846(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[10]"Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59."
Hahn W.C., Menu E., Bothwell A.L.M., Sims P.J., Bierer B.E.
Science 256:1805-1807(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CD59-BINDING DATA.
[11]"A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion."
Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L.
EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSTPIP1.
[12]"Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5-A resolution."
Bodian D.L., Jones E.Y., Harlos K., Stuart D.I., Davis S.J.
Structure 2:755-766(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-206, DISULFIDE BONDS.
[13]"Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2."
Withka J.M., Wyss D.F., Wagner G., Arulanandam A.R.N., Reinherz E.L., Recny M.A.
Structure 1:69-81(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 25-129.
[14]"Conformation and function of the N-linked glycan in the adhesion domain of human CD2."
Wyss D.F., Choi J.S., Li J., Knoppers M.H., Willis K.J., Arulanandam A.R., Smolyar A., Reinherz E.L., Wagner G.
Science 269:1273-1278(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 25-129.
[15]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-217.
+Additional computationally mapped references.

Web resources

Wikipedia

CD2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19806 expand/collapse EMBL AC list , M19798, M19800, M19802, M19804 Genomic DNA. Translation: AAA53095.1.
M16445 mRNA. Translation: AAA51738.1.
M14362 mRNA. Translation: AAA35571.1.
M16336 mRNA. Translation: AAA51946.1.
X07871 expand/collapse EMBL AC list , X07872, X07873, X07874 Genomic DNA. Translation: CAA30721.1.
AL135798 Genomic DNA. Translation: CAC14840.1.
BC033583 mRNA. Translation: AAH33583.1.
PIRRWHUC2. A28967.
RefSeqNP_001758.2. NM_001767.3.
UniGeneHs.523500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDBNMR-A25-129[»]
1GYANMR-A25-129[»]
1HNFX-ray2.50A25-206[»]
1L2ZNMR-B294-304[»]
1QA9X-ray3.20A/C28-129[»]
2J6OX-ray2.22C324-333[»]
2J7IX-ray2.90C/D324-333[»]
ProteinModelPortalP06729.
SMRP06729. Positions 28-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107352. 16 interactions.
IntActP06729. 7 interactions.
MINTMINT-99488.
STRING9606.ENSP00000358490.

Chemistry

ChEMBLCHEMBL2040.
DrugBankDB00092. Alefacept.
GuidetoPHARMACOLOGY2600.

PTM databases

PhosphoSiteP06729.
UniCarbKBP06729.

Polymorphism databases

DMDM160370002.

Proteomic databases

PaxDbP06729.
PRIDEP06729.

Protocols and materials databases

DNASU914.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369478; ENSP00000358490; ENSG00000116824.
GeneID914.
KEGGhsa:914.
UCSCuc001egu.4. human.

Organism-specific databases

CTD914.
GeneCardsGC01P117297.
H-InvDBHIX0000931.
HGNCHGNC:1639. CD2.
HPACAB002430.
HPA003883.
MIM186990. gene.
neXtProtNX_P06729.
PharmGKBPA26198.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47564.
HOGENOMHOG000276890.
HOVERGENHBG000262.
InParanoidP06729.
KOK06449.
OMAGTQVHQQ.
OrthoDBEOG7KSX9X.
PhylomeDBP06729.
TreeFamTF335971.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SignaLinkP06729.

Gene expression databases

ArrayExpressP06729.
BgeeP06729.
CleanExHS_CD2.
GenevestigatorP06729.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR015632. CD2.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013106. Ig_V-set.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERPTHR12080. PTHR12080. 1 hit.
PTHR12080:SF10. PTHR12080:SF10. 1 hit.
PfamPF05790. C2-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR01870. CD2ANTIGEN.
ProtoNetSearch...

Other

EvolutionaryTraceP06729.
GeneWikiCD2.
GenomeRNAi914.
NextBio3780.
PROP06729.
SOURCESearch...

Entry information

Entry nameCD2_HUMAN
AccessionPrimary (citable) accession number: P06729
Secondary accession number(s): Q96TE5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 165 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