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Protein

B-cell antigen receptor complex-associated protein alpha chain

Gene

CD79A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei210 – 2101Required for binding to BLNKBy similarity

GO - Molecular functioni

  1. transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell differentiation Source: UniProtKB
  3. B cell proliferation Source: UniProtKB
  4. B cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP11912.

Names & Taxonomyi

Protein namesi
Recommended name:
B-cell antigen receptor complex-associated protein alpha chain
Alternative name(s):
Ig-alpha
MB-1 membrane glycoprotein
Membrane-bound immunoglobulin-associated protein
Surface IgM-associated protein
CD_antigen: CD79a
Gene namesi
Name:CD79A
Synonyms:IGA, MB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1698. CD79A.

Subcellular locationi

  1. Cell membrane; Single-pass type I membrane protein

  2. 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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 143111ExtracellularSequence AnalysisAdd
BLAST
Transmembranei144 – 16522HelicalSequence AnalysisAdd
BLAST
Topological domaini166 – 22661CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. B cell receptor complex Source: UniProtKB
  2. external side of plasma membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane raft Source: UniProtKB
  5. multivesicular body Source: UniProtKB
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Agammaglobulinemia 3, autosomal recessive (AGM3)2 Publications

The disease is caused by mutations 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.

Disease descriptionA 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.

See also OMIM:613501

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi197 – 1971S → A: Increased phosphorylation of Y-188; when associated with A-203 and V-209. 1 Publication
Mutagenesisi203 – 2031S → A: Increased phosphorylation of Y-188; when associated with A-197 and V-209. 1 Publication
Mutagenesisi209 – 2091T → V: Increased phosphorylation of Y-188; when associated with A-197 and A-203. 1 Publication

Organism-specific databases

MIMi613501. phenotype.
Orphaneti33110. Autosomal agammaglobulinemia.
PharmGKBiPA26237.

Polymorphism and mutation databases

BioMutaiCD79A.
DMDMi547896.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 226194B-cell antigen receptor complex-associated protein alpha chainPRO_0000014558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 106PROSITE-ProRule annotation
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi119 – 119Interchain (with C-136 in beta chain)PROSITE-ProRule annotation
Modified residuei188 – 1881Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation
Modified residuei199 – 1991Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation
Modified residuei204 – 2041Asymmetric dimethylarginine; by PRMT1By similarity
Modified residuei210 – 2101Phosphotyrosine; by Tyr-kinasesPROSITE-ProRule annotation

Post-translational modificationi

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.2 Publications
Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP11912.
PaxDbiP11912.
PeptideAtlasiP11912.
PRIDEiP11912.

PTM databases

PhosphoSiteiP11912.

Expressioni

Tissue specificityi

B-cells.

Gene expression databases

BgeeiP11912.
CleanExiHS_CD79A.
ExpressionAtlasiP11912. baseline and differential.
GenevestigatoriP11912.

Organism-specific databases

HPAiCAB000019.
HPA017748.

Interactioni

Subunit structurei

Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains. Interacts through its phosphorylated ITAM domain with the SH2 domains of SYK which stimulates SYK autophosphorylation and activation. Also interacts, when phosphorylated on Tyr-210, with the SH2 domain of BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK which is necessary for trafficking of the BCR to late endosomes. Interacts with Src-family tyrosine kinases including FYN and LYN, increasing their activity (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FATE1Q969F03EBI-7797864,EBI-743099

Protein-protein interaction databases

BioGridi107411. 55 interactions.
IntActiP11912. 2 interactions.
MINTiMINT-6491159.
STRINGi9606.ENSP00000221972.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CV9NMR-A184-195[»]
DisProtiDP00502.
ProteinModelPortaliP11912.
SMRiP11912. Positions 32-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 11684Ig-like C2-typeAdd
BLAST
Domaini177 – 20529ITAMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ITAM domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41728.
GeneTreeiENSGT00510000049127.
HOGENOMiHOG000074307.
HOVERGENiHBG050854.
InParanoidiP11912.
KOiK06506.
OMAiPFLDMGE.
OrthoDBiEOG7J70GM.
PhylomeDBiP11912.
TreeFamiTF336032.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamiPF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00408. IGc2. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11912-1) [UniParc]FASTAAdd to basket

Also known as: Long

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.

« Hide

        10         20         30         40         50
MPGGPGVLQA LPATIFLLFL LSAVYLGPGC QALWMHKVPA SLMVSLGEDA
60 70 80 90 100
HFQCPHNSSN NANVTWWRVL HGNYTWPPEF LGPGEDPNGT LIIQNVNKSH
110 120 130 140 150
GGIYVCRVQE GNESYQQSCG TYLRVRQPPP RPFLDMGEGT KNRIITAEGI
160 170 180 190 200
ILLFCAVVPG TLLLFRKRWQ NEKLGLDAGD EYEDENLYEG LNLDDCSMYE
210 220
DISRGLQGTY QDVGSLNIGD VQLEKP
Length:226
Mass (Da):25,038
Last modified:June 1, 1994 - v2
Checksum:i6E5B837409969292
GO
Isoform 2 (identifier: P11912-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     89-127: GTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQ → E

Show »
Length:188
Mass (Da):20,786
Checksum:i176B170B710E6EEB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471G → V in BAD97091 (Ref. 10) Curated
Sequence conflicti69 – 691V → I in AAA60270 (PubMed:1639443).Curated
Sequence conflicti189 – 1891E → G in BAD97091 (Ref. 10) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei89 – 12739GTLII…LRVRQ → E in isoform 2. 2 PublicationsVSP_002476Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S46706 mRNA. Translation: AAB23558.1.
M80462 mRNA. Translation: AAA59556.1.
M74721 mRNA. Translation: AAA60270.1.
S75217 mRNA. Translation: AAB20812.1.
M86921 mRNA. Translation: AAA59557.1.
U05259 Genomic DNA. Translation: AAA20495.1.
S79248 mRNA. Translation: AAC60653.1.
X83540 mRNA. Translation: CAA58523.1.
AK223371 mRNA. Translation: BAD97091.1.
X13451 mRNA. Translation: CAA31802.1. Sequence problems.
CCDSiCCDS12589.1. [P11912-1]
CCDS46088.1. [P11912-2]
PIRiI54539. A46477.
S12504.
RefSeqiNP_001774.1. NM_001783.3. [P11912-1]
NP_067612.1. NM_021601.3. [P11912-2]
UniGeneiHs.631567.

Genome annotation databases

EnsembliENST00000221972; ENSP00000221972; ENSG00000105369. [P11912-1]
ENST00000444740; ENSP00000400605; ENSG00000105369. [P11912-2]
GeneIDi973.
KEGGihsa:973.
UCSCiuc002oru.3. human. [P11912-2]
uc002orv.3. human. [P11912-1]

Polymorphism and mutation databases

BioMutaiCD79A.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

CD79Abase

CD79A mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S46706 mRNA. Translation: AAB23558.1.
M80462 mRNA. Translation: AAA59556.1.
M74721 mRNA. Translation: AAA60270.1.
S75217 mRNA. Translation: AAB20812.1.
M86921 mRNA. Translation: AAA59557.1.
U05259 Genomic DNA. Translation: AAA20495.1.
S79248 mRNA. Translation: AAC60653.1.
X83540 mRNA. Translation: CAA58523.1.
AK223371 mRNA. Translation: BAD97091.1.
X13451 mRNA. Translation: CAA31802.1. Sequence problems.
CCDSiCCDS12589.1. [P11912-1]
CCDS46088.1. [P11912-2]
PIRiI54539. A46477.
S12504.
RefSeqiNP_001774.1. NM_001783.3. [P11912-1]
NP_067612.1. NM_021601.3. [P11912-2]
UniGeneiHs.631567.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CV9NMR-A184-195[»]
DisProtiDP00502.
ProteinModelPortaliP11912.
SMRiP11912. Positions 32-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107411. 55 interactions.
IntActiP11912. 2 interactions.
MINTiMINT-6491159.
STRINGi9606.ENSP00000221972.

PTM databases

PhosphoSiteiP11912.

Polymorphism and mutation databases

BioMutaiCD79A.
DMDMi547896.

Proteomic databases

MaxQBiP11912.
PaxDbiP11912.
PeptideAtlasiP11912.
PRIDEiP11912.

Protocols and materials databases

DNASUi973.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221972; ENSP00000221972; ENSG00000105369. [P11912-1]
ENST00000444740; ENSP00000400605; ENSG00000105369. [P11912-2]
GeneIDi973.
KEGGihsa:973.
UCSCiuc002oru.3. human. [P11912-2]
uc002orv.3. human. [P11912-1]

Organism-specific databases

CTDi973.
GeneCardsiGC19P042381.
HGNCiHGNC:1698. CD79A.
HPAiCAB000019.
HPA017748.
MIMi112205. gene.
613501. phenotype.
neXtProtiNX_P11912.
Orphaneti33110. Autosomal agammaglobulinemia.
PharmGKBiPA26237.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41728.
GeneTreeiENSGT00510000049127.
HOGENOMiHOG000074307.
HOVERGENiHBG050854.
InParanoidiP11912.
KOiK06506.
OMAiPFLDMGE.
OrthoDBiEOG7J70GM.
PhylomeDBiP11912.
TreeFamiTF336032.

Enzyme and pathway databases

ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP11912.

Miscellaneous databases

EvolutionaryTraceiP11912.
GeneWikiiCD79A.
GenomeRNAii973.
NextBioi4076.
PROiP11912.
SOURCEiSearch...

Gene expression databases

BgeeiP11912.
CleanExiHS_CD79A.
ExpressionAtlasiP11912. baseline and differential.
GenevestigatoriP11912.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamiPF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00408. IGc2. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the mb-1 transcript in human lymphoid cells."
    Leduc I., Preud'Homme J.L., Cogne M.
    Clin. Exp. Immunol. 90:141-146(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin-associated protein B29."
    Mueller B.S., Cooper L., Terhorst C.
    Eur. J. Immunol. 22:1621-1625(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Tonsil.
  3. "Molecular cloning of the Ig-alpha subunit of the human B-cell antigen receptor complex."
    Flaswinkel H., Reth M.
    Immunogenetics 36:266-269(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Human mb-1 gene: complete cDNA sequence and its expression in B cells bearing membrane Ig of various isotypes."
    Yu L.M., Chang T.W.
    J. Immunol. 148:633-637(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Molecular cloning and expression pattern of a human gene homologous to the murine mb-1 gene."
    Ha H.J., Kubagawa H., Burrows P.D.
    J. Immunol. 148:1526-1531(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  6. "Chromosomal localization, genomic structure, and allelic polymorphism of the human CD79 alpha (Ig-alpha/mb-1) gene."
    Hashimoto S., Mohrenweiser H.W., Gregersen P.K., Chiorazzi N.
    Immunogenetics 40:287-295(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  7. "Structure, chromosomal localization, and methylation pattern of the human mb-1 gene."
    Ha H., Barnoski B.L., Sun L., Emanuel B.S., Burrows P.D.
    J. Immunol. 152:5749-5757(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Alternative splicing of CD79a (Ig-alpha/mb-1) and CD79b (Ig-beta/B29) RNA transcripts in human B cells."
    Hashimoto S., Chiorazzi N., Gregersen P.K.
    Mol. Immunol. 32:651-659(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  9. Koyama M., Nakamura T.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  10. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Small intestine.
  11. "Isolation and chemical characterization of the human B29 and mb-1 proteins of the B cell antigen receptor complex."
    Vasile S., Coligan J.E., Yoshida M., Seon B.K.
    Mol. Immunol. 31:419-427(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-52.
  12. "B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-like structural properties."
    Sakaguchi N., Kashiwamura S., Kimoto M., Thalmann P., Melchers F.
    EMBO J. 7:3457-3464(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 190-226 (ISOFORM 1).
  13. "Cooperativity and segregation of function within the Ig-alpha/beta heterodimer of the B cell antigen receptor complex."
    Luisiri P., Lee Y.J., Eisfelder B.J., Clark M.R.
    J. Biol. Chem. 271:5158-5163(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig beta."
    Tseng J., Eisfelder B.J., Clark M.R.
    Blood 89:1513-1520(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Mutations in Igalpha (CD79a) result in a complete block in B-cell development."
    Minegishi Y., Coustan-Smith E., Rapalus L., Ersoy F., Campana D., Conley M.E.
    J. Clin. Invest. 104:1115-1121(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AGM3.
  16. "The serine and threonine residues in the Ig-alpha cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction."
    Mueller R., Wienands J., Reth M.
    Proc. Natl. Acad. Sci. U.S.A. 97:8451-8454(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-197; SER-203 AND THR-209.
  17. "Novel Igalpha (CD79a) gene mutation in a Turkish patient with B cell-deficient agammaglobulinemia."
    Wang Y., Kanegane H., Sanal O., Tezcan I., Ersoy F., Futatani T., Miyawaki T.
    Am. J. Med. Genet. 108:333-336(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AGM3.
  18. "Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor."
    Gaul B.S., Harrison M.L., Geahlen R.L., Burton R.A., Post C.B.
    J. Biol. Chem. 275:16174-16182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 184-195, PHOSPHORYLATION, INTERACTION WITH LYN.

Entry informationi

Entry nameiCD79A_HUMAN
AccessioniPrimary (citable) accession number: P11912
Secondary accession number(s): A0N775, Q53FB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: June 1, 1994
Last modified: April 29, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.