CD274

Programmed cell death 1 ligand 1. UniProt annotates extracellular residues 19–238.

Predicted protein structure

A downloaded AlphaFold model connects the CD274 sequence to its predicted three-dimensional structure.

RNA expression in tumor samples

Median CD274 RNA expression by tumor type, measured in RSEM units. The study selected these samples using microsatellite-stability score thresholds.

Mucinous tumors37 samples14.5

Other tumor types438 samples13.5

Compare the sample groups · cBioPortal measurements (JSON)

Sequence & binding sites

Choose a protein region, search amino-acid letters, or inspect a recorded binding site.

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Sequence annotations and source records

Canonical sequence and topology

Target ID: T-ENSG00000120217
UniProt accession: Q9NZQ7
Sequence state: available
Canonical sequence: Yes
Length in amino acids: 290
Sequence SHA-256: b1b17c7fca3cbab15bc66b90bd4c07f73617cb5a03db105b0a38084fe7bca48b

View and select the full canonical sequence

Canonical amino-acid sequence

MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET

Sequence positions 1–290

Gray shows the full canonical sequence. Colored spans mark the listed intervals.

Signal peptide

1–18

Membrane-spanning segments

239–259 (Helical)

Source-annotated domains

19–238 (Extracellular); 260–290 (Cytoplasmic)

Source-annotated extracellular intervals

19–238

UniProt annotates the following extracellular intervals.

One-based positions include both interval endpoints.
Start	End	Length	Sequence and source
19	238	220	Sequence and source Basis reviewed-uniprot-topological-domain Evidence class source-annotated-topology Sequence SHA-256 b82ae0b447d54d331f0d78f47fcd2b88207d2417367b9de9d22dfcf911c88d73 Amino-acid sequence for this intervalFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNER

Sequence and topology sources

Source role: canonical-sequence
Source: alphafold-db-canonical-uniprot-field
Extracted field: uniprotSequence
Source row accession: Not recorded

Download source snapshot

Open sequence source

Source role: reviewed-topology
Source: UniProt reviewed human surface-field snapshot
Extracted field: Not recorded
Source row accession: Q9NZQ7

Download source snapshot (gzip)

subcellular_location: SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417, ECO:0000269|PubMed:36232715}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:28813417}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:28813417}; Single-pass type I membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:32929201}. Note=Associates with CMTM6 at recycling endosomes, where it is protected from being targeted for lysosomal degradation (PubMed:28813417). Translocates to the nucleus in response to hypoxia via its interaction with phosphorylated STAT3 (PubMed:32929201). {ECO:0000269|PubMed:28813417, ECO:0000269|PubMed:32929201}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15780196}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Endomembrane system {ECO:0000269|PubMed:15780196}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000269|PubMed:30564891}.
transmembrane: TRANSMEM 239..259; /note="Helical"; /evidence="ECO:0000255"
topological_domain: TOPO_DOM 19..238; /note="Extracellular"; /evidence="ECO:0000255"; TOPO_DOM 260..290; /note="Cytoplasmic"; /evidence="ECO:0000255"
signal_peptide: SIGNAL 1..18; /evidence="ECO:0000255"
lipidation: Not recorded

Download all canonical target sequences (FASTA)