CD33
entrez
945
canonical
uniprot
P20138
canonical
ensembl
ENSG00000105383
resolver
ensp
ENSP00000262262
resolver
ensp
ENSP00000375673
resolver
ensp
ENSP00000410126
resolver
genesymbol
CD33
resolver
genesymbol_syn
SIGLEC3
resolver
hgnc
HGNC:1659
resolver
uniprot
B4E3P8
resolver
uniprot
C9JEN7
resolver
uniprot
F8WAL2
resolver
uniprot
Q8TD24
resolver
uniprot_entry
CD33_HUMAN
resolver
uniprot_sec
B4E3P8
resolver
uniprot_sec
C9JEN7
resolver
uniprot_sec
F8WAL2
resolver
uniprot_sec
Q8TD24
resolver
amino_acid_sequence
MPLLLLLPLLWAGALAMDPNFWLQVQESVTVQEGLCVLVPCTFFHPIPYYDKNSPVHGYWFREGAIISRDSPVATNKLDQEVQEETQGRFRLLGDPSRNNCSLSIVDARRRDNGSYFFRMERGSTKYSYKSPQLSVHVTDLTHRPKILIPGTLEPGHSKNLTCSVSWACEQGTPPIFSWLSAAPTSLGPRTTHSSVLIITPRPQDHGTNLTCQVKFAGAGVTTERTIQLNVTYVPQNPTTGIFPGDGSGKQETRAGVVHGAIGGAGVTALLALCLCLIFFIVKTHRRKAARTAVGRNDTHPTTGSASPKHQKKSKLHGPTETSSCSGAAPTVEMDEELHYASLNFHGMNPSKDTSTEYSEVRTQ
uniprot
proteins
function
FUNCTION: Sialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state (PubMed:10611343, PubMed:11320212, PubMed:15597323). Preferentially recognizes and binds alpha-2,3- and more avidly alpha-2,6-linked sialic acid-bearing glycans (PubMed:7718872). Upon engagement of ligands such as C1q or syalylated glycoproteins, two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) located in CD33 cytoplasmic tail are phosphorylated by Src-like kinases such as LCK (PubMed:10887109, PubMed:28325905). These phosphorylations provide docking sites for the recruitment and activation of protein-tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10206955, PubMed:10556798, PubMed:10887109). In turn, these phosphatases regulate downstream pathways through dephosphorylation of signaling molecules (PubMed:10206955, PubMed:10887109). One of the repressive effect of CD33 on monocyte activation requires phosphoinositide 3-kinase/PI3K (PubMed:15597323). {ECO:0000269|PubMed:10206955, ECO:0000269|PubMed:10556798, ECO:0000269|PubMed:10611343, ECO:0000269|PubMed:10887109, ECO:0000269|PubMed:11320212, ECO:0000269|PubMed:15597323, ECO:0000269|PubMed:28325905, ECO:0000269|PubMed:7718872}.
uniprot
proteins
mass_dalton
39825
uniprot
proteins
mutagenesis
MUTAGEN 100; /note="N->A: Significant loss of binding to peripheral blood granulocytes."; /evidence="ECO:0000269|PubMed:8702538"; MUTAGEN 340; /note="Y->A: Abolishes binding to PTPN6 and PTPN11. Increases binding of red blood cells."; /evidence="ECO:0000269|PubMed:10206955"; MUTAGEN 340; /note="Y->F: Complete loss of phosphorylation by LCK."; /evidence="ECO:0000269|PubMed:10887109"; MUTAGEN 358; /note="Y->A,F: Reduces binding to PTPN6."; /evidence="ECO:0000269|PubMed:10556798"; MUTAGEN 358; /note="Y->F: More than 50% loss of phosphorylation by LCK."; /evidence="ECO:0000269|PubMed:10887109
uniprot
proteins
post_translational_modification
PTM: Glycosylated. Glycosylation at Asn-100 is critical for regulating ligand recognition. {ECO:0000269|PubMed:8702538}.; PTM: Phosphorylation of Tyr-340 is involved in binding to PTPN6 and PTPN11. Phosphorylation of Tyr-358 is involved in binding to PTPN6. LCK phosphorylates Tyr-340 efficiently and Tyr-358 to a lesser extent. {ECO:0000269|PubMed:10206955, ECO:0000269|PubMed:10556798, ECO:0000269|PubMed:10887109}.
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
protein_family
SIGLEC (sialic acid binding Ig-like lectin) family
uniprot
proteins
pubmed
10206955
uniprot
proteins
pubmed
10556798
uniprot
proteins
pubmed
10611343
uniprot
proteins
pubmed
10887109
uniprot
proteins
pubmed
11320212
uniprot
proteins
pubmed
11943481
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15597323
uniprot
proteins
pubmed
16380601
uniprot
proteins
pubmed
28325905
uniprot
proteins
pubmed
28747436
uniprot
proteins
pubmed
3139766
uniprot
proteins
pubmed
7718872
uniprot
proteins
pubmed
8702538
uniprot
proteins
sequence_length
364
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform CD33M]: Cell membrane {ECO:0000269|PubMed:10611343, ECO:0000269|PubMed:28747436}; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform CD33m]: Peroxisome {ECO:0000269|PubMed:28747436}. Note=CD33m isoform does not localize to cell surfaces but instead accumulates in peroxisomes. {ECO:0000269|PubMed:28747436}.
uniprot
proteins
transmembrane_region
TRANSMEM 260..282; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins