P32970 · CD70_HUMAN

  • Protein
    CD70 antigen
  • Gene
    CD70
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Expressed at the plasma membrane of B cells, it is the ligand of the CD27 receptor which is specifically expressed at the surface of T cells (PubMed:28011863, PubMed:28011864, PubMed:8387892).
The CD70-CD27 signaling pathway mediates antigen-specific T cell activation and expansion which in turn provides immune surveillance of B cells (PubMed:28011863, PubMed:28011864).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular exosome
Cellular Componentplasma membrane
Molecular Functionreceptor ligand activity
Molecular Functiontumor necrosis factor receptor binding
Biological Processadaptive immune memory response involving T cells and B cells
Biological ProcessB cell mediated immunity
Biological ProcessB cell proliferation
Biological ProcessCD27 signaling pathway
Biological Processcell surface receptor signaling pathway
Biological Processextrinsic apoptotic signaling pathway
Biological Processpositive regulation of T cell proliferation
Biological ProcessT cell activation
Biological ProcessT cell mediated immunity
Biological Processtumor necrosis factor-mediated signaling pathway

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CD70 antigen
  • Alternative names
    • CD27 ligand
      (CD27-L
      )
    • Tumor necrosis factor ligand superfamily member 7
  • CD Antigen Name
    • CD70

Gene names

    • Name
      CD70
    • Synonyms
      CD27L
      , CD27LG
      , TNFSF7

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P32970
  • Secondary accessions
    • B4DPR8
    • Q53XX4
    • Q96J57

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-17Cytoplasmic
Transmembrane18-38Helical; Signal-anchor for type II membrane protein
Topological domain39-193Extracellular

Keywords

Disease & Variants

Involvement in disease

Lymphoproliferative syndrome 3 (LPFS3)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal recessive, early-onset immunologic disorder characterized by increased susceptibility to Epstein-Barr virus infection in B cells, abnormal B-cell proliferation and increased susceptibility to B-cell malignancies, including Hodgkin lymphoma. Patients usually have lymphadenopathy and hypogammaglobulinemia, and may suffer from recurrent infections.
  • See also
    MIM:618261
Natural variants in LPFS3
Variant IDPosition(s)ChangeDescription
VAR_081988179-193missingin LPFS3; loss of protein expression
VAR_081989186-193missingin LPFS3; no effect on protein expression; loss of interaction with CD27

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis61Decreased CD27 binding.
Mutagenesis63Loss of protein expression.
Mutagenesis65Loss of protein expression.
Mutagenesis80Decreased CD27 binding.
Mutagenesis83Loss of CD27 binding.
Mutagenesis115No effect on protein expression but loss of CD27 binding; when associated with A-151.
Mutagenesis133Loss of protein expression; when associated with A-168.
Mutagenesis135Decreased protein expression.
Mutagenesis137No effect on CD27 binding.
Mutagenesis137Decreased CD27 binding.
Mutagenesis144Decreased CD27 binding.
Mutagenesis146No effect on CD27 binding.
Mutagenesis146Loss of CD27 binding.
Mutagenesis148Decreased CD27 binding.
Mutagenesis151No effect on protein expression but loss of CD27 binding; when associated with A-115.
Mutagenesis165Decreased protein expression.
Mutagenesis168Loss of protein expression; when associated with A-133.
Mutagenesis170Decreased expression and decreased binding to CD27.
Mutagenesis178Decreased CD27 binding.
Natural variantVAR_081988179-193in LPFS3; loss of protein expression
Mutagenesis180Decreased CD27 binding.
Natural variantVAR_081989186-193in LPFS3; no effect on protein expression; loss of interaction with CD27

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 282 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001854971-193CD70 antigen
Glycosylation63N-linked (GlcNAc...) asparagine
Disulfide bond115↔151
Disulfide bond133↔168
Glycosylation170N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homotrimer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P32970ELOVL4 Q9GZR53EBI-18539709, EBI-18535450

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain56-191THD

Sequence similarities

Belongs to the tumor necrosis factor family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P32970-1

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.

  • Length
    193
  • Mass (Da)
    21,118
  • Last updated
    2002-06-06 v2
  • Checksum
    9265856E33BE4D50
MPEEGSGCSVRRRPYGCVLRAALVPLVAGLVICLVVCIQRFAQAQQQLPLESLGWDVAELQLNHTGPQQDPRLYWQGGPALGRSFLHGPELDKGQLRIHRDGIYMVHIQVTLAICSSTTASRHHPTTLAVGICSPASRSISLLRLSFHQGCTIASQRLTPLARGDTLCTNLTGTLLPSRNTDETFFGVQWVRP

P32970-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 151-193: CTIASQRLTPLARGDTLCTNLTGTLLPSRNTDETFFGVQWVRP → LFGFWNWGLKVKCFLRHLIWTAHCFIPLTQLVFMQALQSWRNHHCSHFTDEENRGVNR

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M0QZW2M0QZW2_HUMANCD7065

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_056416151-193in isoform 2
Sequence conflict154in Ref. 1; AAA36175

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L08096
EMBL· GenBank· DDBJ
AAA36175.1
EMBL· GenBank· DDBJ
mRNA
S69339
EMBL· GenBank· DDBJ
AAB30121.1
EMBL· GenBank· DDBJ
mRNA
BT007211
EMBL· GenBank· DDBJ
AAP35875.1
EMBL· GenBank· DDBJ
mRNA
AK298467
EMBL· GenBank· DDBJ
BAG60680.1
EMBL· GenBank· DDBJ
mRNA
EF064709
EMBL· GenBank· DDBJ
ABK41892.1
EMBL· GenBank· DDBJ
Genomic DNA
AC008760
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471139
EMBL· GenBank· DDBJ
EAW69074.1
EMBL· GenBank· DDBJ
Genomic DNA
BC000725
EMBL· GenBank· DDBJ
AAH00725.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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