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BLNK (B-cell linker)

Written2012-08Saravanan Yuvaraj, Rudi W Hendriks
Department of Pulmonary Medicine, Erasmus MC, Rotterdam, The Netherlands

(Note : for Links provided by Atlas : click)


Alias (NCBI)AGM4
HGNC Alias symbSLP65
HGNC Alias nameB-cell adapter containing a SH2 domain protein
 B-cell activation
 Src homology [SH2] domain-containing leukocyte protein of 65 kD
 B cell adaptor containing SH2 domain
LocusID (NCBI) 29760
Atlas_Id 804
Location 10q24.1  [Link to chromosome band 10q24]
Location_base_pair Starts at 96189171 and ends at 96271569 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping BLNK.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
BLNK (10q24.1)::PIK3AP1 (10q24.1)BLNK (10q24.1)::ZNF536 (19q12)DNTT (10q24.1)::BLNK (10q24.1)
UBN1 (16p13.3)::BLNK (10q24.1)
Note BLNK is a cytoplasmic linker or adaptor protein that plays a critical role in B cell development in human and mice.


Description The gene spans over 79 kb in human and is encoded in 17 exons on the long arm of chromosome 10.
Transcription The transcript is about 1829 bps in human and about 2097 in mice and UTR regions are present in exons 1, 2 and 17.


Description BLNK is a 65 kDa protein of 456 amino acids. Translation of the BLNK begins at the ATG site located in exon 2 and ends at exon 17. The amino-terminal region of BLNK is rich in tyrosines and contains a highly conserved leucine zipper that is responsible for the recruitment of BLNK to the plasma membrane. The mid-portion of the molecule contains a proline-rich region that has efficient SH3-domain binding properties. Finally the C-terminus consists of an SH2-domain that allows interaction with other tyrosine phosphorylated proteins. Phosphorylated BLNK provides docking sites for several proteins that induces Ig L chain recombination and differentiation.
Expression BLNK is expressed exclusively in hematopoietic cells, mainly in B cells and myeloid cells.
Localisation It has been shown that the highly conserved N terminus of BLNK comprises a domain for constitutive membrane association, which is essential for its function. Membrane association depends on a leucine zipper motif in the N-terminal domain. The BLNK N-terminus can be functionally replaced by a heterologuous membrane localization signal and can be transferred to other proteins to confer membrane localization. To connect the pre-B cell receptor (pre-BCR) or the BCR with downstream signaling elements, BLNK must be localized at the plasma membrane where these receptors reside. A stimulation-independent and constant association of BLNK with the Cbl-interacting protein of 85 kDa (CIN85) is requisite for BLNK phosphorylation.
Function BLNK lacks intrinsic enzymatic function, but regulates the assembly and localization of signaling complexes. Such molecules are known as adapters or linkers and have the capacity to regulate the availability of a substrate to an enzyme and create a scaffold for bridging signaling cascades. Phosphorylated BLNK (by the spleen tyrosine kinase SYK) provides docking sites for several proteins including the BTK, GRB2, VAV, NCK and PLCγ2 (Figure 1). SYK and its substrate BLNK are proximal signal transducer elements of the BCR. When the in vivo interactome of BLNK in resting and stimulated B cells was determined by mass spectrometry, it was found that BLNK orchestrated a complex signal network of ~30 proteins that was predominantly based on dynamic interactions.
Pre-BCR signaling leads to activation of SYK, which then phosphorylates BLNK and thereby regulates pre-B cell differentiation (Figure 1). BLNK is required for the downregulation of the pre-BCR surrogate light chain component λ-like (λ5 in mice), thereby terminating pre-BCR expression. It has been shown in mice that Blnk-mediated signals induces activation of Ig κ light chain recombination by induction of the expression of the transcription factors Aiolos, Irf-4, Foxo3a and Foxo1. Deficiency of Blnk in mice results in an increased proliferative response of pre-B cells to IL-7 in vitro, indicating that Blnk is crucially involved in the termination of IL-7 driven proliferation. BLNK inhibits IL-7R signaling through direct binding to Jak3 in a Btk-independent manner and also by downregulating IL-7R expression (Figure 1). In the absence of Btk mainly Ig λ L chain germline transcription and recombination is impaired, whereas in Btk/BLNK double-deficient pre-B cells, both κ and λ L chain germline transcripts are severely reduced. These data suggests a dual role of BLNK in the downregulation of surrogate light chain expression and the activation of Igκ germline transcription.
  Figure 1. Function of Blnk in pre-BCR signaling in the mouse. A. Pre-BCR activation results in the activation of Syk tyrosine kinase, which together with the Src family kinase Lyn phosphorylates several downstream signaling molecules. This provides signals for proliferation and survival by PI3K-dependent activation of Pkb/Akt and by synergy with the MAP kinase pathway downstream of the IL-7R. In addition, pre-BCR signaling also leads to Blnk-Btk-PLCγ complex formation that is essential for downregulation of proliferative signals. Blnk acts as (1) a negative regulator of Jak3 and (2) through inhibition of Pkb/Akt activation. Activation of FoxO is associated with downregulation of surrogate light chain (SLC) and IL-7R expression and the activation of the Ig kappa locus for gene recombination. B. When in pre-B lymphoma cells Blnk expression is low or absent, proliferative signals are maintained because of (1) ongoing Jak/Stat signaling and (2) Pkb/Akt activation, leading to FoxO phosphorylation and degradation, thereby precluding proper maturation and downregulation of pre-BCR and IL-7R expression, resulting in Syk-dependent pre-B cell proliferation (3).
Homology The SLP76 family of adapters has three members namely SLP76, BLNK (SLP65) and Clnk/MIST.

Implicated in

Entity Pre-B cell tumors
Disease Deficiency of BLNK has been found in ~50% of childhood precursor-B cell acute lymphocytic leukemia (ALL) cases. The loss of BLNK protein was found to be due to defective splicing, leading to premature stop codons. Moreover, in precursor-B ALL that where positive for the BCR-ABL translocation the activity of the fusion protein, the BCR-ABL1 kinase, was linked to the expression of the same aberrant BLNK transcripts. Because other expression profiling studies with a large number of patients reported a low frequency it is not clear whether the loss of BLNK is a common leukemogenic event. Nevertheless, the reported findings indicate that loss of BLNK and the accompanying pre-B cell differentiation arrest may be one of the primary causes of precursor-B ALL. In a study of 28 pre-B ALL and 27 B cell lymphomas, BLNK expression was found to be defective in seven and five cases, respectively. BLNK deficiency correlated with RAG1/RAG2 expression and unremitting VH gene rearrangement activity BLNK deficiency resulted in perpetual V(D)J recombinase activity in pre-B-lymphoblastic leukemia and B-cell lymphoma cells.
Blnk-deficient mice spontaneously develop pre-B cell leukemia with a similar phenotype as found in humans. In contrast, mice deficient for Btk, do not develop pre-B cell leukemia. Nevertheless, Btk and Blnk cooperate as tumor suppressors whereby Btk exerts its tumor suppressor function independently of its kinase activity. Combined deficiency of Blnk and Btk result in a more complete arrest at the pre-B cell stage and a higher incidence of pre-B cell leukemia than compared with single deficient mice, suggesting that the developmental block is one of the tumor-promoting factors. In addition, expression of the pre-BCR is also essential for the development of leukemia, because mice which are Rag-deficient or which cannot express the Ig µ H chain on the surface (e.g. because of deficiency of the pre-BCR component λ5 or due to a disruption of the membrane exon of the Ig µ H chain constant region) are arrested at the pro-B cell stage, but do not develop leukemia. Furthermore, Blnk has a specific function that suppresses malignant transformation because in Btk/Plcγ2 and Irf-4/Irf-8 double-deficient mice with a nearly complete arrest at the large pre-B cell stage no leukemias have been reported. The absence of Blnk results in sustained expression of the pre-BCR and the IL-7R in large cycling pre-B cells (Figure 1). Since IL-7R signaling induces c-Myc this results in constitutively high levels of c-Myc. At this stage, Foxo transcription factors that normally suppress c-Myc-driven lymphomagenesis via direct activation of p19Arf are not properly activated because of the absence of BLNK. Furthermore, IL-7R signaling and aberrant pre-BCR signaling represses Bcl6 and thereby induces p19Arf expression. Subsequently, Blnk-deficient pre-B cells acquiring sporadic alterations in the p19Arf-Mdm2-p53 are selected to become malignant. Furthermore, expression of p19Arf in Blnk-deficient leukemias possibly promotes survival under metabolic stress. The Jak3/Stat5 signaling pathway is constitutively activated in pre-B leukemia cells derived from Blnk-deficient mice, mostly due to autocrine production of IL-7. In the leukemia cells, exogenously expressed Blnk inhibited autocrine Jak3/Stat5 signaling, resulting in induction, cell-cycle arrest, and apoptosis. Blnk-inhibition of Jak3 was dependent on the binding of Blnk to Jak3.
Btk/Slp65 double-deficient mice that carried a functional B cell receptor transgene (3-83µδ), developed B-cell leukemias expressing both the 3-83µδ BCR and the pre-BCR components λ5/VpreB. Interestingly, these leukemias were found at similar frequencies in mice concomitantly deficient for Rag1 or the non-homologous end-joining factor DNA-PKcs. It was therefore concluded that malignant transformation of Btk/Slp65 double-deficient pre-B cells is independent of deregulated V(D)J recombination activity in the mouse.
Entity Other disease
Note In human, mutations in SLP65 or BTK result in defective pre-B cell proliferation and an almost complete arrest of B cell development at the pro-B to pre-B cell transition, associated with the immunodeficiency disorder agammaglobulinemia. In contrast, mice deficient for Slp65 or Btk show only a partial arrest at the large cycling pre-B cell stage, while a nearly complete block is present in Btk/Slp65 double deficient mice.


Mimicry of a constitutively active pre-B cell receptor in acute lymphoblastic leukemia cells.
Feldhahn N, Klein F, Mooster JL, Hadweh P, Sprangers M, Wartenberg M, Bekhite MM, Hofmann WK, Herzog S, Jumaa H, Rowley JD, Muschen M.
J Exp Med. 2005 Jun 6;201(11):1837-52.
PMID 15939795
The adaptor protein SLP-65 acts as a tumor suppressor that limits pre-B cell expansion.
Flemming A, Brummer T, Reth M, Jumaa H.
Nat Immunol. 2003 Jan;4(1):38-43. Epub 2002 Nov 18.
PMID 12436112
Distinct signaling requirements for Dmu selection, IgH allelic exclusion, pre-B cell transition, and tumor suppression in B cell progenitors.
Hayashi K, Yamamoto M, Nojima T, Goitsuka R, Kitamura D.
Immunity. 2003 Jun;18(6):825-36.
PMID 12818163
SLP-65 regulates immunoglobulin light chain gene recombination through the PI(3)K-PKB-Foxo pathway.
Herzog S, Hug E, Meixlsperger S, Paik JH, DePinho RA, Reth M, Jumaa H.
Nat Immunol. 2008 Jun;9(6):623-31.
PMID 18488031
Regulation of B-cell proliferation and differentiation by pre-B-cell receptor signalling.
Herzog S, Reth M, Jumaa H.
Nat Rev Immunol. 2009 Mar;9(3):195-205.
PMID 19240758
Expression of the adaptor protein BLNK/SLP-65 in childhood acute lymphoblastic leukemia.
Imai C, Ross ME, Reid G, Coustan-Smith E, Schultz KR, Pui CH, Downing JR, Campana D.
Leukemia. 2004 May;18(5):922-5.
PMID 15029213
Regulation of immunoglobulin light-chain recombination by the transcription factor IRF-4 and the attenuation of interleukin-7 signaling.
Johnson K, Hashimshony T, Sawai CM, Pongubala JM, Skok JA, Aifantis I, Singh H.
Immunity. 2008 Mar;28(3):335-45. Epub 2008 Feb 14.
PMID 18280186
Deficiency of the adaptor SLP-65 in pre-B-cell acute lymphoblastic leukaemia.
Jumaa H, Bossaller L, Portugal K, Storch B, Lotz M, Flemming A, Schrappe M, Postila V, Riikonen P, Pelkonen J, Niemeyer CM, Reth M.
Nature. 2003 May 22;423(6938):452-6.
PMID 12761551
B cell signaling and tumorigenesis.
Jumaa H, Hendriks RW, Reth M.
Annu Rev Immunol. 2005;23:415-45.
PMID 15771577
The absence of SLP65 and Btk blocks B cell development at the preB cell receptor-positive stage.
Jumaa H, Mitterer M, Reth M, Nielsen PJ.
Eur J Immunol. 2001 Jul;31(7):2164-9.
PMID 11449370
Abnormal development and function of B lymphocytes in mice deficient for the signaling adaptor protein SLP-65.
Jumaa H, Wollscheid B, Mitterer M, Wienands J, Reth M, Nielsen PJ.
Immunity. 1999 Nov;11(5):547-54.
PMID 10591180
Bruton's tyrosine kinase and SLP-65 regulate pre-B cell differentiation and the induction of Ig light chain gene rearrangement.
Kersseboom R, Ta VB, Zijlstra AJ, Middendorp S, Jumaa H, van Loo PF, Hendriks RW.
J Immunol. 2006 Apr 15;176(8):4543-52.
PMID 16585544
The BCR-ABL1 kinase bypasses selection for the expression of a pre-B cell receptor in pre-B acute lymphoblastic leukemia cells.
Klein F, Feldhahn N, Harder L, Wang H, Wartenberg M, Hofmann WK, Wernet P, Siebert R, Muschen M.
J Exp Med. 2004 Mar 1;199(5):673-85.
PMID 14993251
A leucine zipper in the N terminus confers membrane association to SLP-65.
Kohler F, Storch B, Kulathu Y, Herzog S, Kuppig S, Reth M, Jumaa H.
Nat Immunol. 2005 Feb;6(2):204-10. Epub 2005 Jan 16.
PMID 15654340
IRF-4,8 orchestrate the pre-B-to-B transition in lymphocyte development.
Lu R, Medina KL, Lancki DW, Singh H.
Genes Dev. 2003 Jul 15;17(14):1703-8. Epub 2003 Jun 27.
PMID 12832394
An essential role for BLNK in human B cell development.
Minegishi Y, Rohrer J, Coustan-Smith E, Lederman HM, Pappu R, Campana D, Chan AC, Conley ME.
Science. 1999 Dec 3;286(5446):1954-7.
PMID 10583958
BLNK suppresses pre-B-cell leukemogenesis through inhibition of JAK3.
Nakayama J, Yamamoto M, Hayashi K, Satoh H, Bundo K, Kubo M, Goitsuka R, Farrar MA, Kitamura D.
Blood. 2009 Feb 12;113(7):1483-92. Epub 2008 Dec 1.
PMID 19047679
The B-cell antigen receptor signals through a preformed transducer module of SLP65 and CIN85.
Oellerich T, Bremes V, Neumann K, Bohnenberger H, Dittmann K, Hsiao HH, Engelke M, Schnyder T, Batista FD, Urlaub H, Wienands J.
EMBO J. 2011 Aug 5;30(17):3620-34. doi: 10.1038/emboj.2011.251.
PMID 21822214
Malignant transformation of Slp65-deficient pre-B cells involves disruption of the Arf-Mdm2-p53 tumor suppressor pathway.
Ta VB, de Bruijn MJ, ter Brugge PJ, van Hamburg JP, Diepstraten HJ, van Loo PF, Kersseboom R, Hendriks RW.
Blood. 2010 Feb 18;115(7):1385-93. Epub 2009 Dec 14.
PMID 20008789
Pre-B-cell leukemias in Btk/Slp65-deficient mice arise independently of ongoing V(D)J recombination activity.
Ta VB, de Haan AB, de Bruijn MJ, Dingjan GM, Hendriks RW.
Leukemia. 2011 Jan;25(1):48-56. Epub 2010 Oct 29.
PMID 21030983
Ikaros DNA-binding proteins as integral components of B cell developmental-stage-specific regulatory circuits.
Thompson EC, Cobb BS, Sabbattini P, Meixlsperger S, Parelho V, Liberg D, Taylor B, Dillon N, Georgopoulos K, Jumaa H, Smale ST, Fisher AG, Merkenschlager M.
Immunity. 2007 Mar;26(3):335-44.
PMID 17363301
SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation.
Wienands J, Schweikert J, Wollscheid B, Jumaa H, Nielsen PJ, Reth M.
J Exp Med. 1998 Aug 17;188(4):791-5.
PMID 9705962
Combined deficiencies in Bruton tyrosine kinase and phospholipase Cgamma2 arrest B-cell development at a pre-BCR+ stage.
Xu S, Lee KG, Huo J, Kurosaki T, Lam KP.
Blood. 2007 Apr 15;109(8):3377-84. Epub 2006 Dec 12.
PMID 17164342


This paper should be referenced as such :
Yuvaraj, S ; Hendriks, RW
BLNK (B-cell linker)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(2):106-109.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(10;10)(q24;q24) DNTT::BLNK

External links


HGNC (Hugo)BLNK   14211
LRG (Locus Reference Genomic)LRG_21
Atlas Explorer : (Salamanque)BLNK
Entrez_Gene (NCBI)BLNK    B cell linker
AliasesAGM4; BASH; BLNK-S; LY57; 
SLP-65; SLP65; bca
GeneCards (Weizmann)BLNK
Ensembl hg19 (Hinxton)ENSG00000095585 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000095585 [Gene_View]  ENSG00000095585 [Sequence]  chr10:96189171-96271569 [Contig_View]  BLNK [Vega]
ICGC DataPortalENSG00000095585
Genatlas (Paris)BLNK
SOURCE (Princeton)BLNK
Genetics Home Reference (NIH)BLNK
Genomic and cartography
GoldenPath hg38 (UCSC)BLNK  -     chr10:96189171-96271569 -  10q24.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)BLNK  -     10q24.1   [Description]    (hg19-Feb_2009)
GoldenPathBLNK - 10q24.1 [CytoView hg19]  BLNK - 10q24.1 [CytoView hg38]
Genome Data Viewer NCBIBLNK [Mapview hg19]  
OMIM604515   613502   
Gene and transcription
Genbank (Entrez)AF068180 AF068181 AI307343 AK027779 AK225546
RefSeq transcript (Entrez)NM_001114094 NM_001258440 NM_001258441 NM_001258442 NM_013314
Consensus coding sequences : CCDS (NCBI)BLNK
Gene ExpressionBLNK [ NCBI-GEO ]   BLNK [ EBI - ARRAY_EXPRESS ]   BLNK [ SEEK ]   BLNK [ MEM ]
Gene Expression Viewer (FireBrowse)BLNK [ Firebrowse - Broad ]
GenevisibleExpression of BLNK in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)29760
GTEX Portal (Tissue expression)BLNK
Human Protein AtlasENSG00000095585-BLNK [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ8WV28   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ8WV28  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ8WV28
Domaine pattern : Prosite (Expaxy)SH2 (PS50001)   
Domains : Interpro (EBI)SH2    SH2_dom_sf   
Domain families : Pfam (Sanger)SH2 (PF00017)   
Domain families : Pfam (NCBI)pfam00017   
Domain families : Smart (EMBL)SH2 (SM00252)  
Conserved Domain (NCBI)BLNK
AlphaFold pdb e-kbQ8WV28   
Human Protein Atlas [tissue]ENSG00000095585-BLNK [tissue]
Protein Interaction databases
IntAct (EBI)Q8WV28
Ontologies - Pathways
Ontology : AmiGOtransmembrane receptor protein tyrosine kinase adaptor activity  protein binding  cytoplasm  cytosol  cytosol  plasma membrane  plasma membrane  inflammatory response  humoral immune response  transmembrane receptor protein tyrosine kinase signaling pathway  positive regulation of gene expression  membrane  enzyme binding  protein kinase binding  B cell differentiation  intracellular signal transduction  intracellular signal transduction  signaling adaptor activity  cytoplasmic ribonucleoprotein granule  SH2 domain binding  phospholipase binding  B cell receptor signaling pathway  B cell receptor signaling pathway  protein tyrosine kinase binding  
Ontology : EGO-EBItransmembrane receptor protein tyrosine kinase adaptor activity  protein binding  cytoplasm  cytosol  cytosol  plasma membrane  plasma membrane  inflammatory response  humoral immune response  transmembrane receptor protein tyrosine kinase signaling pathway  positive regulation of gene expression  membrane  enzyme binding  protein kinase binding  B cell differentiation  intracellular signal transduction  intracellular signal transduction  signaling adaptor activity  cytoplasmic ribonucleoprotein granule  SH2 domain binding  phospholipase binding  B cell receptor signaling pathway  B cell receptor signaling pathway  protein tyrosine kinase binding  
REACTOMEQ8WV28 [protein]
REACTOME PathwaysR-HSA-983695 [pathway]   
NDEx NetworkBLNK
Atlas of Cancer Signalling NetworkBLNK
Wikipedia pathwaysBLNK
Orthology - Evolution
GeneTree (enSembl)ENSG00000095585
Phylogenetic Trees/Animal Genes : TreeFamBLNK
Homologs : HomoloGeneBLNK
Homology/Alignments : Family Browser (UCSC)BLNK
Gene fusions - Rearrangements
Fusion : MitelmanBLNK::PIK3AP1 [10q24.1/10q24.1]  
Fusion : MitelmanBLNK::ZNF536 [10q24.1/19q12]  
Fusion : MitelmanUBN1::BLNK [16p13.3/10q24.1]  
Fusion : FusionHubBLNK--CD74    BLNK--CDK17    BLNK--DNTT    BLNK--PDLIM1    BLNK--PIK3AP1    BLNK--TM9SF3    BLNK--ZNF536    GNB4--BLNK    LIPF--BLNK    RCC1--BLNK   
Fusion : QuiverBLNK
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerBLNK [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)BLNK
Exome Variant ServerBLNK
GNOMAD BrowserENSG00000095585
Varsome BrowserBLNK
ACMGBLNK variants
Genomic Variants (DGV)BLNK [DGVbeta]
DECIPHERBLNK [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisBLNK 
ICGC Data PortalBLNK 
TCGA Data PortalBLNK 
Broad Tumor PortalBLNK
OASIS PortalBLNK [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICBLNK  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DBLNK
Mutations and Diseases : HGMDBLNK
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)BLNK
DoCM (Curated mutations)BLNK
CIViC (Clinical Interpretations of Variants in Cancer)BLNK
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM604515    613502   
Genetic Testing Registry BLNK
NextProtQ8WV28 [Medical]
Target ValidationBLNK
Huge Navigator BLNK [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDBLNK
Pharm GKB GenePA25371
Clinical trialBLNK
DataMed IndexBLNK
PubMed69 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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