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P11912

- CD79A_HUMAN

UniProt

P11912 - CD79A_HUMAN

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Protein
B-cell antigen receptor complex-associated protein alpha chain
Gene
CD79A, IGA, MB1
Organism
Homo sapiens (Human)
Status
Reviewed - 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 BLNK By 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: Chromosome 19

Organism-specific databases

HGNCiHGNC:1698. CD79A.

Subcellular locationi

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 By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 143111Extracellular Reviewed prediction
Add
BLAST
Transmembranei144 – 16522Helical; Reviewed prediction
Add
BLAST
Topological domaini166 – 22661Cytoplasmic Reviewed prediction
Add
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) [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.
Note: 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.2 Publications

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 Publication
Add
BLAST
Chaini33 – 226194B-cell antigen receptor complex-associated protein alpha chain
PRO_0000014558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 106 Reviewed prediction
Glycosylationi57 – 571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi63 – 631N-linked (GlcNAc...) Reviewed prediction
Glycosylationi73 – 731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi88 – 881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi97 – 971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi112 – 1121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi119 – 119Interchain (with C-136 in beta chain) Reviewed prediction
Modified residuei188 – 1881Phosphotyrosine; by SRC-type Tyr-kinases By similarity
Modified residuei199 – 1991Phosphotyrosine; by SRC-type Tyr-kinases By similarity
Modified residuei204 – 2041Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residuei210 – 2101Phosphotyrosine; by Tyr-kinases By similarity

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP11912.
PaxDbiP11912.
PeptideAtlasiP11912.
PRIDEiP11912.

PTM databases

PhosphoSiteiP11912.

Expressioni

Tissue specificityi

B-cells.

Gene expression databases

ArrayExpressiP11912.
BgeeiP11912.
CleanExiHS_CD79A.
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.1 Publication

Protein-protein interaction databases

BioGridi107411. 11 interactions.
IntActiP11912. 1 interaction.
MINTiMINT-6491159.
STRINGi9606.ENSP00000221972.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CV9NMR-A184-195[»]
DisProtiDP00502.
ProteinModelPortaliP11912.

Miscellaneous databases

EvolutionaryTraceiP11912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 11684Ig-like C2-type
Add
BLAST
Domaini177 – 20529ITAM
Add
BLAST

Sequence similaritiesi

Contains 1 ITAM domain.

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41728.
HOGENOMiHOG000074307.
HOVERGENiHBG050854.
InParanoidiP11912.
KOiK06506.
OMAiRKRWQNE.
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. Align

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

MPGGPGVLQA LPATIFLLFL LSAVYLGPGC QALWMHKVPA SLMVSLGEDA    50
HFQCPHNSSN NANVTWWRVL HGNYTWPPEF LGPGEDPNGT LIIQNVNKSH 100
GGIYVCRVQE GNESYQQSCG TYLRVRQPPP RPFLDMGEGT KNRIITAEGI 150
ILLFCAVVPG TLLLFRKRWQ NEKLGLDAGD EYEDENLYEG LNLDDCSMYE 200
DISRGLQGTY QDVGSLNIGD VQLEKP 226
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei89 – 12739GTLII…LRVRQ → E in isoform 2.
VSP_002476Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471G → V in BAD97091. 1 Publication
Sequence conflicti69 – 691V → I in AAA60270. 1 Publication
Sequence conflicti189 – 1891E → G in BAD97091. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000608019; ENSP00000477348; ENSG00000272985. [P11912-1]
ENST00000609866; ENSP00000476512; ENSG00000272985. [P11912-2]
GeneIDi973.
KEGGihsa:973.
UCSCiuc002oru.3. human. [P11912-2]
uc002orv.3. human. [P11912-1]

Polymorphism databases

DMDMi547896.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

CD79Abase

CD79A mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS12589.1. [P11912-1 ]
CCDS46088.1. [P11912-2 ]
PIRi I54539. A46477.
S12504.
RefSeqi NP_001774.1. NM_001783.3. [P11912-1 ]
NP_067612.1. NM_021601.3. [P11912-2 ]
UniGenei Hs.631567.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CV9 NMR - A 184-195 [» ]
DisProti DP00502.
ProteinModelPortali P11912.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107411. 11 interactions.
IntActi P11912. 1 interaction.
MINTi MINT-6491159.
STRINGi 9606.ENSP00000221972.

PTM databases

PhosphoSitei P11912.

Polymorphism databases

DMDMi 547896.

Proteomic databases

MaxQBi P11912.
PaxDbi P11912.
PeptideAtlasi P11912.
PRIDEi P11912.

Protocols and materials databases

DNASUi 973.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000221972 ; ENSP00000221972 ; ENSG00000105369 . [P11912-1 ]
ENST00000444740 ; ENSP00000400605 ; ENSG00000105369 . [P11912-2 ]
ENST00000608019 ; ENSP00000477348 ; ENSG00000272985 . [P11912-1 ]
ENST00000609866 ; ENSP00000476512 ; ENSG00000272985 . [P11912-2 ]
GeneIDi 973.
KEGGi hsa:973.
UCSCi uc002oru.3. human. [P11912-2 ]
uc002orv.3. human. [P11912-1 ]

Organism-specific databases

CTDi 973.
GeneCardsi GC19P042381.
HGNCi HGNC:1698. CD79A.
HPAi CAB000019.
HPA017748.
MIMi 112205. gene.
613501. phenotype.
neXtProti NX_P11912.
Orphaneti 33110. Autosomal agammaglobulinemia.
PharmGKBi PA26237.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41728.
HOGENOMi HOG000074307.
HOVERGENi HBG050854.
InParanoidi P11912.
KOi K06506.
OMAi RKRWQNE.
OrthoDBi EOG7J70GM.
PhylomeDBi P11912.
TreeFami TF336032.

Enzyme and pathway databases

Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinki P11912.

Miscellaneous databases

EvolutionaryTracei P11912.
GeneWikii CD79A.
GenomeRNAii 973.
NextBioi 4076.
PROi P11912.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11912.
Bgeei P11912.
CleanExi HS_CD79A.
Genevestigatori P11912.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view ]
Pfami PF02189. ITAM. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00408. IGc2. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 145 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

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