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{{Infobox_gene}}
{{PBB_Controls
'''Basal cell adhesion molecule''' is a [[protein]] that in humans is encoded by the ''BCAM'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4059| accessdate = }}</ref> BCAM has also recently been designated '''CD239''' ([[cluster of differentiation]] 239).
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Basal cell adhesion molecule (Lutheran blood group)
| HGNCid = 6722
| Symbol = BCAM
| AltSymbols =; AU; CD239; LU; MSK19
| OMIM = 111200
| ECnumber = 
| Homologene = 21149
| MGIid = 1929940
| GeneAtlas_image1 = PBB_GE_BCAM_40093_at_tn.png
| GeneAtlas_image2 = PBB_GE_BCAM_203009_at_tn.png
| Function = {{GNF_GO|id=GO:0005055 |text = laminin receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4059
    | Hs_Ensembl = ENSG00000187244
    | Hs_RefseqProtein = NP_001013275
    | Hs_RefseqmRNA = NM_001013257
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 50004178
    | Hs_GenLoc_end = 50016517
    | Hs_Uniprot = P50895
    | Mm_EntrezGene = 57278
    | Mm_Ensembl = ENSMUSG00000002980
    | Mm_RefseqmRNA = NM_020486
    | Mm_RefseqProtein = NP_065232
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 18914905
    | Mm_GenLoc_end = 18929017
    | Mm_Uniprot = 
  }}
}}
'''Basal cell adhesion molecule (Lutheran blood group)''', also known as '''BCAM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4059| accessdate = }}</ref> BCAM has also recently been designated '''CD239''' ([[cluster of differentiation]] 239).


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Lutheran blood group glycoprotein is a member of the [[immunoglobulin superfamily]] and a receptor for the extracellular matrix protein, [[laminin]]. The protein contains five, [[N-terminus]], extracellular [[immunoglobulin domain]]s, a single transmembrane domain, and a short, [[C-terminal]] cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Lutheran blood group glycoprotein is a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five, N-terminus, extracellular immunoglobulin domains, a single transmembrane domain, and a short, C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4059| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}


==Further reading==
BCAM has been shown to [[Protein-protein interaction|interact]] with [[Laminin, alpha 5]].<ref name="pmid11133776">{{cite journal | vauthors = Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA | title = Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity | journal = Blood | volume = 97 | issue = 1 | pages = 312–20 | year = 2001 | pmid = 11133776 | doi = 10.1182/blood.v97.1.312}}</ref><ref name="pmid12244066">{{cite journal | vauthors = Kikkawa Y, Moulson CL, Virtanen I, Miner JH | title = Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo | journal = J. Biol. Chem. | volume = 277 | issue = 47 | pages = 44864–9 | year = 2002 | pmid = 12244066 | doi = 10.1074/jbc.M208731200 }}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== References ==
| citations =  
{{Reflist}}
*{{cite journal | author=Eyler CE, Telen MJ |title=The Lutheran glycoprotein: a multifunctional adhesion receptor. |journal=Transfusion |volume=46 |issue= 4 |pages= 668-77 |year= 2006 |pmid= 16584446 |doi= 10.1111/j.1537-2995.2006.00779.x }}
 
*{{cite journal | author=Lewis M, Kaita H, Coghlan G, ''et al.'' |title=The chromosome 19 linkage group LDLR, C3, LW, APOC2, LU, SE in man. |journal=Ann. Hum. Genet. |volume=52 |issue= Pt 2 |pages= 137-44 |year= 1989 |pmid= 2907851 |doi= }}
== Further reading ==
*{{cite journal  | author=Parsons SF, Mallinson G, Holmes CH, ''et al.'' |title=The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5496-500 |year= 1995 |pmid= 7777537 |doi= }}
{{Refbegin | 2}}
*{{cite journal  | author=Campbell IG, Foulkes WD, Senger G, ''et al.'' |title=Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily. |journal=Cancer Res. |volume=54 |issue= 22 |pages= 5761-5 |year= 1994 |pmid= 7954395 |doi= }}
*{{cite journal  | vauthors=Eyler CE, Telen MJ |title=The Lutheran glycoprotein: a multifunctional adhesion receptor. |journal=Transfusion |volume=46 |issue= 4 |pages= 668–77 |year= 2006 |pmid= 16584446 |doi= 10.1111/j.1537-2995.2006.00779.x }}
*{{cite journal  | author=Rahuel C, Le Van Kim C, Mattei MG, ''et al.'' |title=A unique gene encodes spliceoforms of the B-cell adhesion molecule cell surface glycoprotein of epithelial cancer and of the Lutheran blood group glycoprotein. |journal=Blood |volume=88 |issue= 5 |pages= 1865-72 |year= 1996 |pmid= 8781446 |doi= }}
*{{cite journal  | vauthors=Lewis M, Kaita H, Coghlan G |title=The chromosome 19 linkage group LDLR, C3, LW, APOC2, LU, SE in man. |journal=Ann. Hum. Genet. |volume=52 |issue= Pt 2 |pages= 137–44 |year= 1989 |pmid= 2907851 |doi=10.1111/j.1469-1809.1988.tb01089.x  |display-authors=etal}}
*{{cite journal  | author=Parsons SF, Mallinson G, Daniels GL, ''et al.'' |title=Use of domain-deletion mutants to locate Lutheran blood group antigens to each of the five immunoglobulin superfamily domains of the Lutheran glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the Au(a)/Au(b) polymorphisms. |journal=Blood |volume=89 |issue= 11 |pages= 4219-25 |year= 1997 |pmid= 9166867 |doi=  }}
*{{cite journal  | vauthors=Parsons SF, Mallinson G, Holmes CH |title=The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5496–500 |year= 1995 |pmid= 7777537 |doi=10.1073/pnas.92.12.5496  | pmc=41722  |display-authors=etal}}
*{{cite journal  | author=El Nemer W, Rahuel C, Colin Y, ''et al.'' |title=Organization of the human LU gene and molecular basis of the Lu(a)/Lu(b) blood group polymorphism. |journal=Blood |volume=89 |issue= 12 |pages= 4608-16 |year= 1997 |pmid= 9192786 |doi=  }}
*{{cite journal  | vauthors=Campbell IG, Foulkes WD, Senger G |title=Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily. |journal=Cancer Res. |volume=54 |issue= 22 |pages= 5761–5 |year= 1994 |pmid= 7954395 |doi=  |display-authors=etal}}
*{{cite journal  | author=Parsons SF, Lee G, Spring FA, ''et al.'' |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312-20 |year= 2001 |pmid= 11133776 |doi=  }}
*{{cite journal  | vauthors=Rahuel C, Le Van Kim C, Mattei MG |title=A unique gene encodes spliceoforms of the B-cell adhesion molecule cell surface glycoprotein of epithelial cancer and of the Lutheran blood group glycoprotein. |journal=Blood |volume=88 |issue= 5 |pages= 1865–72 |year= 1996 |pmid= 8781446 |doi=  |display-authors=etal}}
*{{cite journal  | author=El Nemer W, Gane P, Colin Y, ''et al.'' |title=Characterization of the laminin binding domains of the Lutheran blood group glycoprotein. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23757-62 |year= 2001 |pmid= 11319237 |doi= 10.1074/jbc.M102978200 }}
*{{cite journal  | vauthors=Parsons SF, Mallinson G, Daniels GL |title=Use of domain-deletion mutants to locate Lutheran blood group antigens to each of the five immunoglobulin superfamily domains of the Lutheran glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the Au(a)/Au(b) polymorphisms. |journal=Blood |volume=89 |issue= 11 |pages= 4219–25 |year= 1997 |pmid= 9166867 |doi=  |display-authors=etal}}
*{{cite journal  | author=Kikkawa Y, Moulson CL, Virtanen I, Miner JH |title=Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 44864-9 |year= 2003 |pmid= 12244066 |doi= 10.1074/jbc.M208731200 }}
*{{cite journal  | vauthors=El Nemer W, Rahuel C, Colin Y |title=Organization of the human LU gene and molecular basis of the Lu(a)/Lu(b) blood group polymorphism. |journal=Blood |volume=89 |issue= 12 |pages= 4608–16 |year= 1997 |pmid= 9192786 |doi= |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Parsons SF, Lee G, Spring FA |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312–20 |year= 2001 |pmid= 11133776 |doi=10.1182/blood.V97.1.312  |display-authors=etal}}
*{{cite journal  | author=Shin BK, Wang H, Yim AM, ''et al.'' |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607-16 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200 }}
*{{cite journal  | vauthors=El Nemer W, Gane P, Colin Y |title=Characterization of the laminin binding domains of the Lutheran blood group glycoprotein. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23757–62 |year= 2001 |pmid= 11319237 |doi= 10.1074/jbc.M102978200 |display-authors=etal}}
*{{cite journal  | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | vauthors=Kikkawa Y, Moulson CL, Virtanen I, Miner JH |title=Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 44864–9 |year= 2003 |pmid= 12244066 |doi= 10.1074/jbc.M208731200 }}
*{{cite journal  | author=Crew VK, Green C, Daniels G |title=Molecular bases of the antigens of the Lutheran blood group system. |journal=Transfusion |volume=43 |issue= 12 |pages= 1729-37 |year= 2004 |pmid= 14641871 |doi= }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Zen Q, Batchvarova M, Twyman CA, ''et al.'' |title=B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. |journal=Am. J. Hematol. |volume=75 |issue= 2 |pages= 63-72 |year= 2004 |pmid= 14755370 |doi= 10.1002/ajh.10442 }}
*{{cite journal  | vauthors=Shin BK, Wang H, Yim AM |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607–16 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200 |display-authors=etal}}
*{{cite journal  | author=Kroviarski Y, El Nemer W, Gane P, ''et al.'' |title=Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin. |journal=Br. J. Haematol. |volume=126 |issue= 2 |pages= 255-64 |year= 2004 |pmid= 15238148 |doi= 10.1111/j.1365-2141.2004.05010.x }}
*{{cite journal  | vauthors=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660–6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | author=Drewniok C, Wienrich BG, Schön M, ''et al.'' |title=Molecular interactions of B-CAM (basal-cell adhesion molecule) and laminin in epithelial skin cancer. |journal=Arch. Dermatol. Res. |volume=296 |issue= 2 |pages= 59-66 |year= 2005 |pmid= 15278364 |doi= 10.1007/s00403-004-0481-4 }}
*{{cite journal  | vauthors=Crew VK, Green C, Daniels G |title=Molecular bases of the antigens of the Lutheran blood group system. |journal=Transfusion |volume=43 |issue= 12 |pages= 1729–37 |year= 2004 |pmid= 14641871 |doi=10.1111/j.0041-1132.2003.00600.x }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Zen Q, Batchvarova M, Twyman CA |title=B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. |journal=Am. J. Hematol. |volume=75 |issue= 2 |pages= 63–72 |year= 2004 |pmid= 14755370 |doi= 10.1002/ajh.10442 |display-authors=etal}}
*{{cite journal  | author=Cheng J, Kapranov P, Drenkow J, ''et al.'' |title=Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution. |journal=Science |volume=308 |issue= 5725 |pages= 1149-54 |year= 2005 |pmid= 15790807 |doi= 10.1126/science.1108625 }}
*{{cite journal  | vauthors=Kroviarski Y, El Nemer W, Gane P |title=Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin. |journal=Br. J. Haematol. |volume=126 |issue= 2 |pages= 255–64 |year= 2004 |pmid= 15238148 |doi= 10.1111/j.1365-2141.2004.05010.x |display-authors=etal}}
*{{cite journal  | author=Vainionpää N, Kikkawa Y, Lounatmaa K, ''et al.'' |title=Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells. |journal=Am. J. Physiol., Cell Physiol. |volume=290 |issue= 3 |pages= C764-75 |year= 2006 |pmid= 16236823 |doi= 10.1152/ajpcell.00285.2005 }}
*{{cite journal  | vauthors=Drewniok C, Wienrich BG, Schön M |title=Molecular interactions of B-CAM (basal-cell adhesion molecule) and laminin in epithelial skin cancer. |journal=Arch. Dermatol. Res. |volume=296 |issue= 2 |pages= 59–66 |year= 2005 |pmid= 15278364 |doi= 10.1007/s00403-004-0481-4 |display-authors=etal}}
}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
{{refend}}
*{{cite journal  | vauthors=Cheng J, Kapranov P, Drenkow J |title=Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution. |journal=Science |volume=308 |issue= 5725 |pages= 1149–54 |year= 2005 |pmid= 15790807 |doi= 10.1126/science.1108625 |display-authors=etal}}
*{{cite journal  | vauthors=Vainionpää N, Kikkawa Y, Lounatmaa K |title=Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells. |journal=Am. J. Physiol., Cell Physiol. |volume=290 |issue= 3 |pages= C764–75 |year= 2006 |pmid= 16236823 |doi= 10.1152/ajpcell.00285.2005 |display-authors=etal}}
{{Refend}}


==External links==
==External links==
* {{MeshName|BCAM+protein,+human}}
* {{MeshName|BCAM+protein,+human}}
* {{UCSC gene info|BCAM}}
{{Clusters of differentiation}}


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{{NLM content}}
{{NLM content}}
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[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
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{{Membrane-protein-stub}}

Revision as of 02:30, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

Basal cell adhesion molecule is a protein that in humans is encoded by the BCAM gene.[1] BCAM has also recently been designated CD239 (cluster of differentiation 239).

Function

Lutheran blood group glycoprotein is a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five, N-terminus, extracellular immunoglobulin domains, a single transmembrane domain, and a short, C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Two transcript variants encoding different isoforms have been found for this gene.[1]

Interactions

BCAM has been shown to interact with Laminin, alpha 5.[2][3]

References

  1. ↑ 1.0 1.1 "Entrez Gene: BCAM basal cell adhesion molecule (Lutheran blood group)".
  2. ↑ Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA (2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity". Blood. 97 (1): 312–20. doi:10.1182/blood.v97.1.312. PMID 11133776.
  3. ↑ Kikkawa Y, Moulson CL, Virtanen I, Miner JH (2002). "Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo". J. Biol. Chem. 277 (47): 44864–9. doi:10.1074/jbc.M208731200. PMID 12244066.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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