CD79A
entrez
973
canonical
uniprot
P11912
canonical
ensembl
ENSG00000105369
resolver
ensp
ENSP00000221972
resolver
ensp
ENSP00000400605
resolver
genesymbol
CD79A
resolver
genesymbol_syn
IGA
resolver
genesymbol_syn
MB1
resolver
hgnc
HGNC:1698
resolver
uniprot
A0N775
resolver
uniprot
Q53FB8
resolver
uniprot_entry
CD79A_HUMAN
resolver
uniprot_sec
A0N775
resolver
uniprot_sec
Q53FB8
resolver
amino_acid_sequence
MPGGPGVLQALPATIFLLFLLSAVYLGPGCQALWMHKVPASLMVSLGEDAHFQCPHNSSNNANVTWWRVLHGNYTWPPEFLGPGEDPNGTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQPPPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKLGLDAGDEYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGSLNIGDVQLEKP
uniprot
proteins
disease_involvement
DISEASE: Agammaglobulinemia 3, autosomal recessive (AGM3) [MIM:613501]: A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. {ECO:0000269|PubMed:10525050, ECO:0000269|PubMed:11920841}. Note=The disease is caused by variants affecting the gene represented in this entry. Two different mutations, one at the splice donor site of intron 2 and the other at the splice acceptor site for exon 3, have been identified. Both mutations give rise to a truncated protein.
uniprot
proteins
function
FUNCTION: Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells. {ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}.
uniprot
proteins
mass_dalton
25038
uniprot
proteins
mutagenesis
MUTAGEN 152; /note="L->W: Blocks IgMBCR assembly."; /evidence="ECO:0000269|PubMed:35981043"; MUTAGEN 156; /note="A->W: Blocks IgMBCR assembly."; /evidence="ECO:0000269|PubMed:35981043"; MUTAGEN 197; /note="S->A: Increased phosphorylation of Y-188; when associated with A-203 and V-209."; /evidence="ECO:0000269|PubMed:10900006"; MUTAGEN 203; /note="S->A: Increased phosphorylation of Y-188; when associated with A-197 and V-209."; /evidence="ECO:0000269|PubMed:10900006"; MUTAGEN 209; /note="T->V: Increased phosphorylation of Y-188; when associated with A-197 and A-203."; /evidence="ECO:0000269|PubMed:10900006
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine, serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases, leading to their activation which in turn leads to phosphorylation of downstream targets. Phosphorylated by LYN. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation. {ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:10900006}.; PTM: Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex composed of at least CUL3, KLHL6 and RBX1; leading to proteasomal degradation. {ECO:0000269|PubMed:38630892}.
uniprot
proteins
pubmed
10525050
uniprot
proteins
pubmed
10748115
uniprot
proteins
pubmed
10900006
uniprot
proteins
pubmed
11920841
uniprot
proteins
pubmed
1395095
uniprot
proteins
pubmed
1534761
uniprot
proteins
pubmed
1538135
uniprot
proteins
pubmed
1639443
uniprot
proteins
pubmed
1729378
uniprot
proteins
pubmed
2463161
uniprot
proteins
pubmed
35981043
uniprot
proteins
pubmed
38630892
uniprot
proteins
pubmed
7514267
uniprot
proteins
pubmed
7643857
uniprot
proteins
pubmed
7916003
uniprot
proteins
pubmed
8207205
uniprot
proteins
pubmed
8617796
uniprot
proteins
pubmed
9057631
uniprot
proteins
sequence_length
226
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 144..165; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins