Full text data of BSG
BSG
[Confidence: high (a blood group or CD marker)]
Basigin (5F7; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; Leukocyte activation antigen M6; OK blood group antigen; Tumor cell-derived collagenase stimulatory factor; TCSF; CD147; Flags: Precursor)
Basigin (5F7; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; Leukocyte activation antigen M6; OK blood group antigen; Tumor cell-derived collagenase stimulatory factor; TCSF; CD147; Flags: Precursor)
hRBCD
IPI00019906
IPI00019906 Splice isoform 2 or 1 of P35613 Basigin precursor Splice isoform 2 or 1 of P35613 Basigin precursor membrane n/a n/a 5 3 5 n/a 4 n/a 8 n/a 3 3 n/a 3 n/a n/a 2 3 1 2 Type I membrane protein Basigin precurson and Long splice isoform found at its expected molecular weight found at molecular weight
IPI00019906 Splice isoform 2 or 1 of P35613 Basigin precursor Splice isoform 2 or 1 of P35613 Basigin precursor membrane n/a n/a 5 3 5 n/a 4 n/a 8 n/a 3 3 n/a 3 n/a n/a 2 3 1 2 Type I membrane protein Basigin precurson and Long splice isoform found at its expected molecular weight found at molecular weight
Comments
Isoform Q54A51 was detected.
Isoform Q54A51 was detected.
UniProt
P35613
ID BASI_HUMAN Reviewed; 385 AA.
AC P35613; A6NJW1; D3YLG5; Q7Z796; Q8IZL7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Basigin;
DE AltName: Full=5F7;
DE AltName: Full=Collagenase stimulatory factor;
DE AltName: Full=Extracellular matrix metalloproteinase inducer;
DE Short=EMMPRIN;
DE AltName: Full=Leukocyte activation antigen M6;
DE AltName: Full=OK blood group antigen;
DE AltName: Full=Tumor cell-derived collagenase stimulatory factor;
DE Short=TCSF;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor;
GN Name=BSG; ORFNames=UNQ6505/PRO21383;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1634773;
RA Kasinrerk W., Fiebiger E., Stefanova I., Baumruker T., Knapp W.,
RA Stockinger H.;
RT "Human leukocyte activation antigen M6, a member of the Ig
RT superfamily, is the species homologue of rat OX-47, mouse basigin, and
RT chicken HT7 molecule.";
RL J. Immunol. 149:847-854(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=1783610;
RA Miyauchi T., Masuzawa Y., Muramatsu T.;
RT "The basigin group of the immunoglobulin superfamily: complete
RT conservation of a segment in and around transmembrane domains of human
RT and mouse basigin and chicken HT7 antigen.";
RL J. Biochem. 110:770-774(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7812975;
RA Biswas C., Zhang Y., Decastro R., Guo H., Nakamura T., Kataoka H.,
RA Nabeshima K.;
RT "The human tumor cell-derived collagenase stimulatory factor (renamed
RT EMMPRIN) is a member of the immunoglobulin superfamily.";
RL Cancer Res. 55:434-439(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Wakasugi H., Scamps C., Yang G., Vancong N., Bernheim A., Tursz T.,
RA Harada N.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Decastro R., Zhang Y., Kataoka H., Coon J., Biswas C.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=9767135; DOI=10.1016/S0378-1119(98)00400-4;
RA Guo H., Majmudar G., Jensen T.C., Biswas C., Toole B.P., Gordon M.K.;
RT "Characterization of the gene for human EMMPRIN, a tumor cell surface
RT inducer of matrix metalloproteinases.";
RL Gene 220:99-108(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Sato T., Takita M., Noguchi Y., Hirata M., Sakai T., Ito A.;
RT "Regulation of EMMPRIN/CD147 expression and its function of
RT controlling matrix metalloproteinases production and cell-surface
RT localization in co-culture of human uterine cervical carcinoma SKG-II
RT cells and human uterine cervical fibroblasts.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y.,
RA Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=12939332; DOI=10.1167/iovs.02-0995;
RA Ochrietor J.D., Moroz T.P., van Ekeris L., Clamp M.F., Jefferson S.C.,
RA deCarvalho A.C., Fadool J.M., Wistow G., Muramatsu T., Linser P.J.;
RT "Retina-specific expression of 5A11/Basigin-2, a member of the
RT immunoglobulin gene superfamily.";
RL Invest. Ophthalmol. Vis. Sci. 44:4086-4096(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBUNIT, SUBCELLULAR
RP LOCATION, AND ALTERNATIVE PROMOTER USAGE.
RX PubMed=21536654; DOI=10.1128/MCB.05160-11;
RA Liao C.G., Kong L.M., Song F., Xing J.L., Wang L.X., Sun Z.J.,
RA Tang H., Yao H., Zhang Y., Wang L., Wang Y., Yang X.M., Li Y.,
RA Chen Z.N.;
RT "Characterization of basigin isoforms and the inhibitory function of
RT basigin-3 in human hepatocellular carcinoma proliferation and
RT invasion.";
RL Mol. Cell. Biol. 31:2591-2604(2011).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP PROTEIN SEQUENCE OF 22-36 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [17]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=1846736; DOI=10.1016/0003-9861(91)90332-D;
RA Nabeshima K., Lane W.S., Biswas C.;
RT "Partial sequencing and characterization of the tumor cell-derived
RT collagenase stimulatory factor.";
RL Arch. Biochem. Biophys. 285:90-96(1991).
RN [18]
RP REVIEW.
RX PubMed=12792908;
RA Muramatsu T., Miyauchi T.;
RT "Basigin (CD147): a multifunctional transmembrane protein involved in
RT reproduction, neural function, inflammation and tumor invasion.";
RL Histol. Histopathol. 18:981-987(2003).
RN [19]
RP GLYCOSYLATION AT ASN-160 AND ASN-268.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [22]
RP INTERACTION WITH AJAP1.
RX PubMed=17267690; DOI=10.1091/mbc.E06-07-0637;
RA Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
RA Starzinski-Powitz A.;
RT "junction protein shrew-1 influences cell invasion and interacts with
RT invasion-promoting protein CD147.";
RL Mol. Biol. Cell 18:1272-1281(2007).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-321, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=18430721; DOI=10.1074/jbc.M802694200;
RA Yu X.-L., Hu T., Du J.-M., Ding J.-P., Yang X.-M., Zhang J., Yang B.,
RA Shen X., Zhang Z., Zhong W.-D., Wen N., Jiang H., Zhu P., Chen Z.-N.;
RT "Crystal structure of HAb18G/CD147: implications for immunoglobulin
RT superfamily homophilic adhesion.";
RL J. Biol. Chem. 283:18056-18065(2008).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-219, MASS SPECTROMETRY,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=19768682; DOI=10.1002/prot.22577;
RA Luo J., Teplyakov A., Obmolova G., Malia T., Wu S.-J., Beil E.,
RA Baker A., Swencki-Underwood B., Zhao Y., Sprenkle J., Dixon K.,
RA Sweet R., Gilliland G.L.;
RT "Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-
RT strand swapping.";
RL Proteins 77:1009-1014(2009).
RN [31]
RP VARIANT LYS-208.
RX PubMed=9130641; DOI=10.1002/eji.1830270414;
RA Spring F.A., Holmes C.H., Simpson K.L., Mawby W.J., Mattes M.J.,
RA Okubo Y., Parsons S.F.;
RT "The Ok(a) blood group antigen is a marker for the M6 leukocyte
RT activation antigen, the human homolog of OX-47 antigen, basigin and
RT neurothelin, an immunoglobulin superfamily molecule that is widely
RT expressed in human cells and tissues.";
RL Eur. J. Immunol. 27:891-897(1997).
CC -!- FUNCTION: Plays pivotal roles in spermatogenesis, embryo
CC implantation, neural network formation and tumor progression.
CC Stimulates adjacent fibroblasts to produce matrix
CC metalloproteinases (MMPS). May target monocarboxylate transporters
CC SLC16A1, SLC16A3 and SLC16A8 to plasma membranes of retinal
CC pigment epithelium and neural retina. Seems to be a receptor for
CC oligomannosidic glycans. In vitro, promotes outgrowth of
CC astrocytic processes (By similarity).
CC -!- SUBUNIT: Forms homooligomers in a cis-dependent manner on the
CC plasma membrane. Forms heterooligomers of isoform 2 and isoform 3.
CC Forms a complex with MMP1 at the tumor cell surface. Interacts
CC with SLC16A1 and SLC1A3; probably a BSG dimer is associated with a
CC monocarboxylate transporter dimer. Interacts with ATP1B2, MAG and
CC L1CAM (By similarity). Interacts with AJAP1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Melanosome. Note=Colocalizes with SLC16A1 and SLC16A8 (By
CC similarity). Identified by mass spectrometry in melanosome
CC fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long, Basigin-2;
CC IsoId=P35613-1; Sequence=Displayed;
CC Name=2; Synonyms=Basigin-1;
CC IsoId=P35613-2; Sequence=VSP_011501;
CC Name=3; Synonyms=Basigin-3;
CC IsoId=P35613-3; Sequence=VSP_043225;
CC Note=Produced by alternative promoter usage. N-glycosylated;
CC Name=4; Synonyms=Basigin-4;
CC IsoId=P35613-4; Sequence=VSP_043226, VSP_043227;
CC Note=Produced by alternative promoter usage. N-glycosylated;
CC -!- TISSUE SPECIFICITY: Present only in vascular endothelium in non-
CC neoplastic regions of the brain, whereas it is present in tumor
CC cells but not in proliferating blood vessels in malignant gliomas.
CC -!- INDUCTION: Enriched on the surface of tumor cells. Up-regulated in
CC gliomas. Its expression levels correlate with malignant potential
CC of the tumor.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC mutation database;
CC URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system;=ok";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/bsg/";
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DR EMBL; X64364; CAA45716.1; -; mRNA.
DR EMBL; D45131; BAA08109.1; -; mRNA.
DR EMBL; L10240; AAA68936.1; -; mRNA.
DR EMBL; M87879; AAA91084.1; -; mRNA.
DR EMBL; L20471; AAB41120.1; -; mRNA.
DR EMBL; AF042854; AAD10704.1; -; Genomic_DNA.
DR EMBL; AF042848; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042849; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042850; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042851; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042852; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042853; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AB072923; BAB88938.1; -; mRNA.
DR EMBL; AB085790; BAC76828.1; -; mRNA.
DR EMBL; AF548371; AAN40694.1; -; mRNA.
DR EMBL; GU557064; ADD31881.1; -; mRNA.
DR EMBL; GU557065; ADD31882.1; -; mRNA.
DR EMBL; AY358113; AAQ88480.1; -; mRNA.
DR EMBL; AY942196; AAX20110.1; -; Genomic_DNA.
DR EMBL; AC005559; AAC33279.1; -; Genomic_DNA.
DR EMBL; CH471242; EAW61181.1; -; Genomic_DNA.
DR EMBL; CH471242; EAW61185.1; -; Genomic_DNA.
DR EMBL; BC009040; AAH09040.1; -; mRNA.
DR PIR; A46506; A46506.
DR RefSeq; NP_001719.2; NM_001728.3.
DR RefSeq; NP_940991.1; NM_198589.2.
DR RefSeq; NP_940992.1; NM_198590.2.
DR RefSeq; NP_940993.1; NM_198591.2.
DR RefSeq; XP_005259676.1; XM_005259619.1.
DR UniGene; Hs.501293; -.
DR PDB; 3B5H; X-ray; 2.80 A; A/B/C/D=140-321.
DR PDB; 3I84; X-ray; 2.00 A; A/B=13-219.
DR PDB; 3I85; X-ray; 2.50 A; A/B=13-219.
DR PDB; 3QQN; X-ray; 2.31 A; A/B=23-138.
DR PDB; 3QR2; X-ray; 2.30 A; A/B=23-138.
DR PDBsum; 3B5H; -.
DR PDBsum; 3I84; -.
DR PDBsum; 3I85; -.
DR PDBsum; 3QQN; -.
DR PDBsum; 3QR2; -.
DR ProteinModelPortal; P35613; -.
DR SMR; P35613; 23-319.
DR IntAct; P35613; 13.
DR MINT; MINT-5004205; -.
DR STRING; 9606.ENSP00000333769; -.
DR TCDB; 8.A.23.1.1; the basigin (basigin) family.
DR PhosphoSite; P35613; -.
DR DMDM; 51704273; -.
DR PaxDb; P35613; -.
DR PRIDE; P35613; -.
DR DNASU; 682; -.
DR Ensembl; ENST00000333511; ENSP00000333769; ENSG00000172270.
DR Ensembl; ENST00000346916; ENSP00000344707; ENSG00000172270.
DR Ensembl; ENST00000353555; ENSP00000343809; ENSG00000172270.
DR Ensembl; ENST00000545507; ENSP00000473664; ENSG00000172270.
DR GeneID; 682; -.
DR KEGG; hsa:682; -.
DR UCSC; uc002loz.4; human.
DR CTD; 682; -.
DR GeneCards; GC19P000571; -.
DR HGNC; HGNC:1116; BSG.
DR HPA; CAB002427; -.
DR MIM; 109480; gene.
DR MIM; 111380; phenotype.
DR neXtProt; NX_P35613; -.
DR PharmGKB; PA25433; -.
DR eggNOG; NOG83713; -.
DR HOGENOM; HOG000263411; -.
DR HOVERGEN; HBG008120; -.
DR InParanoid; P35613; -.
DR KO; K06535; -.
DR OMA; DRNHLTR; -.
DR OrthoDB; EOG7V1FQN; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_118779; Extracellular matrix organization.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; BSG; human.
DR EvolutionaryTrace; P35613; -.
DR GeneWiki; Basigin; -.
DR GenomeRNAi; 682; -.
DR NextBio; 2802; -.
DR PMAP-CutDB; P35613; -.
DR PRO; PR:P35613; -.
DR ArrayExpress; P35613; -.
DR Bgee; P35613; -.
DR CleanEx; HS_BSG; -.
DR Genevestigator; P35613; -.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone stimulus; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR009151; Basigin.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075:SF6; PTHR10075:SF6; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Blood group antigen; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lectin; Mannose-binding; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 21
FT CHAIN 22 385 Basigin.
FT /FTId=PRO_0000014518.
FT TOPO_DOM 138 323 Extracellular (Potential).
FT TRANSMEM 324 344 Helical; (Potential).
FT TOPO_DOM 345 385 Cytoplasmic (Potential).
FT DOMAIN 138 219 Ig-like C2-type.
FT DOMAIN 221 315 Ig-like V-type.
FT COMPBIAS 356 359 Poly-Asp.
FT MOD_RES 362 362 Phosphoserine.
FT MOD_RES 368 368 Phosphoserine (By similarity).
FT CARBOHYD 160 160 N-linked (GlcNAc...).
FT CARBOHYD 268 268 N-linked (GlcNAc...).
FT CARBOHYD 302 302 N-linked (GlcNAc...) (Potential).
FT DISULFID 157 203
FT DISULFID 242 301
FT VAR_SEQ 1 209 Missing (in isoform 3).
FT /FTId=VSP_043225.
FT VAR_SEQ 1 11 MAAALFVLLGF -> MKQSDASPQER (in isoform
FT 4).
FT /FTId=VSP_043226.
FT VAR_SEQ 12 191 Missing (in isoform 4).
FT /FTId=VSP_043227.
FT VAR_SEQ 24 139 Missing (in isoform 2).
FT /FTId=VSP_011501.
FT VARIANT 208 208 E -> K (in Ok(A-)).
FT /FTId=VAR_013574.
FT VARIANT 269 269 G -> V (in dbSNP:rs1803203).
FT /FTId=VAR_011720.
FT CONFLICT 328 328 F -> L (in Ref. 2; BAC76828).
FT STRAND 24 27
FT STRAND 32 35
FT STRAND 40 47
FT STRAND 53 62
FT HELIX 74 77
FT STRAND 79 95
FT HELIX 100 102
FT STRAND 104 111
FT STRAND 116 118
FT STRAND 128 137
FT STRAND 142 149
FT STRAND 152 159
FT STRAND 166 173
FT STRAND 176 181
FT STRAND 186 192
FT HELIX 194 196
FT STRAND 199 207
FT STRAND 210 217
FT STRAND 224 226
FT STRAND 228 233
FT STRAND 238 243
FT STRAND 252 257
FT STRAND 260 262
FT HELIX 270 272
FT STRAND 274 279
FT STRAND 282 287
FT TURN 292 294
FT STRAND 295 305
FT STRAND 308 319
SQ SEQUENCE 385 AA; 42200 MW; D74C37455BF26685 CRC64;
MAAALFVLLG FALLGTHGAS GAAGFVQAPL SQQRWVGGSV ELHCEAVGSP VPEIQWWFEG
QGPNDTCSQL WDGARLDRVH IHATYHQHAA STISIDTLVE EDTGTYECRA SNDPDRNHLT
RAPRVKWVRA QAVVLVLEPG TVFTTVEDLG SKILLTCSLN DSATEVTGHR WLKGGVVLKE
DALPGQKTEF KVDSDDQWGE YSCVFLPEPM GTANIQLHGP PRVKAVKSSE HINEGETAML
VCKSESVPPV TDWAWYKITD SEDKALMNGS ESRFFVSSSQ GRSELHIENL NMEADPGQYR
CNGTSSKGSD QAIITLRVRS HLAALWPFLG IVAEVLVLVT IIFIYEKRRK PEDVLDDDDA
GSAPLKSSGQ HQNDKGKNVR QRNSS
//
ID BASI_HUMAN Reviewed; 385 AA.
AC P35613; A6NJW1; D3YLG5; Q7Z796; Q8IZL7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Basigin;
DE AltName: Full=5F7;
DE AltName: Full=Collagenase stimulatory factor;
DE AltName: Full=Extracellular matrix metalloproteinase inducer;
DE Short=EMMPRIN;
DE AltName: Full=Leukocyte activation antigen M6;
DE AltName: Full=OK blood group antigen;
DE AltName: Full=Tumor cell-derived collagenase stimulatory factor;
DE Short=TCSF;
DE AltName: CD_antigen=CD147;
DE Flags: Precursor;
GN Name=BSG; ORFNames=UNQ6505/PRO21383;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1634773;
RA Kasinrerk W., Fiebiger E., Stefanova I., Baumruker T., Knapp W.,
RA Stockinger H.;
RT "Human leukocyte activation antigen M6, a member of the Ig
RT superfamily, is the species homologue of rat OX-47, mouse basigin, and
RT chicken HT7 molecule.";
RL J. Immunol. 149:847-854(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=1783610;
RA Miyauchi T., Masuzawa Y., Muramatsu T.;
RT "The basigin group of the immunoglobulin superfamily: complete
RT conservation of a segment in and around transmembrane domains of human
RT and mouse basigin and chicken HT7 antigen.";
RL J. Biochem. 110:770-774(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7812975;
RA Biswas C., Zhang Y., Decastro R., Guo H., Nakamura T., Kataoka H.,
RA Nabeshima K.;
RT "The human tumor cell-derived collagenase stimulatory factor (renamed
RT EMMPRIN) is a member of the immunoglobulin superfamily.";
RL Cancer Res. 55:434-439(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Wakasugi H., Scamps C., Yang G., Vancong N., Bernheim A., Tursz T.,
RA Harada N.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Decastro R., Zhang Y., Kataoka H., Coon J., Biswas C.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=9767135; DOI=10.1016/S0378-1119(98)00400-4;
RA Guo H., Majmudar G., Jensen T.C., Biswas C., Toole B.P., Gordon M.K.;
RT "Characterization of the gene for human EMMPRIN, a tumor cell surface
RT inducer of matrix metalloproteinases.";
RL Gene 220:99-108(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Sato T., Takita M., Noguchi Y., Hirata M., Sakai T., Ito A.;
RT "Regulation of EMMPRIN/CD147 expression and its function of
RT controlling matrix metalloproteinases production and cell-surface
RT localization in co-culture of human uterine cervical carcinoma SKG-II
RT cells and human uterine cervical fibroblasts.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y.,
RA Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=12939332; DOI=10.1167/iovs.02-0995;
RA Ochrietor J.D., Moroz T.P., van Ekeris L., Clamp M.F., Jefferson S.C.,
RA deCarvalho A.C., Fadool J.M., Wistow G., Muramatsu T., Linser P.J.;
RT "Retina-specific expression of 5A11/Basigin-2, a member of the
RT immunoglobulin gene superfamily.";
RL Invest. Ophthalmol. Vis. Sci. 44:4086-4096(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBUNIT, SUBCELLULAR
RP LOCATION, AND ALTERNATIVE PROMOTER USAGE.
RX PubMed=21536654; DOI=10.1128/MCB.05160-11;
RA Liao C.G., Kong L.M., Song F., Xing J.L., Wang L.X., Sun Z.J.,
RA Tang H., Yao H., Zhang Y., Wang L., Wang Y., Yang X.M., Li Y.,
RA Chen Z.N.;
RT "Characterization of basigin isoforms and the inhibitory function of
RT basigin-3 in human hepatocellular carcinoma proliferation and
RT invasion.";
RL Mol. Cell. Biol. 31:2591-2604(2011).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP PROTEIN SEQUENCE OF 22-36 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [17]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=1846736; DOI=10.1016/0003-9861(91)90332-D;
RA Nabeshima K., Lane W.S., Biswas C.;
RT "Partial sequencing and characterization of the tumor cell-derived
RT collagenase stimulatory factor.";
RL Arch. Biochem. Biophys. 285:90-96(1991).
RN [18]
RP REVIEW.
RX PubMed=12792908;
RA Muramatsu T., Miyauchi T.;
RT "Basigin (CD147): a multifunctional transmembrane protein involved in
RT reproduction, neural function, inflammation and tumor invasion.";
RL Histol. Histopathol. 18:981-987(2003).
RN [19]
RP GLYCOSYLATION AT ASN-160 AND ASN-268.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [21]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [22]
RP INTERACTION WITH AJAP1.
RX PubMed=17267690; DOI=10.1091/mbc.E06-07-0637;
RA Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
RA Starzinski-Powitz A.;
RT "junction protein shrew-1 influences cell invasion and interacts with
RT invasion-promoting protein CD147.";
RL Mol. Biol. Cell 18:1272-1281(2007).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-321, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=18430721; DOI=10.1074/jbc.M802694200;
RA Yu X.-L., Hu T., Du J.-M., Ding J.-P., Yang X.-M., Zhang J., Yang B.,
RA Shen X., Zhang Z., Zhong W.-D., Wen N., Jiang H., Zhu P., Chen Z.-N.;
RT "Crystal structure of HAb18G/CD147: implications for immunoglobulin
RT superfamily homophilic adhesion.";
RL J. Biol. Chem. 283:18056-18065(2008).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-219, MASS SPECTROMETRY,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=19768682; DOI=10.1002/prot.22577;
RA Luo J., Teplyakov A., Obmolova G., Malia T., Wu S.-J., Beil E.,
RA Baker A., Swencki-Underwood B., Zhao Y., Sprenkle J., Dixon K.,
RA Sweet R., Gilliland G.L.;
RT "Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-
RT strand swapping.";
RL Proteins 77:1009-1014(2009).
RN [31]
RP VARIANT LYS-208.
RX PubMed=9130641; DOI=10.1002/eji.1830270414;
RA Spring F.A., Holmes C.H., Simpson K.L., Mawby W.J., Mattes M.J.,
RA Okubo Y., Parsons S.F.;
RT "The Ok(a) blood group antigen is a marker for the M6 leukocyte
RT activation antigen, the human homolog of OX-47 antigen, basigin and
RT neurothelin, an immunoglobulin superfamily molecule that is widely
RT expressed in human cells and tissues.";
RL Eur. J. Immunol. 27:891-897(1997).
CC -!- FUNCTION: Plays pivotal roles in spermatogenesis, embryo
CC implantation, neural network formation and tumor progression.
CC Stimulates adjacent fibroblasts to produce matrix
CC metalloproteinases (MMPS). May target monocarboxylate transporters
CC SLC16A1, SLC16A3 and SLC16A8 to plasma membranes of retinal
CC pigment epithelium and neural retina. Seems to be a receptor for
CC oligomannosidic glycans. In vitro, promotes outgrowth of
CC astrocytic processes (By similarity).
CC -!- SUBUNIT: Forms homooligomers in a cis-dependent manner on the
CC plasma membrane. Forms heterooligomers of isoform 2 and isoform 3.
CC Forms a complex with MMP1 at the tumor cell surface. Interacts
CC with SLC16A1 and SLC1A3; probably a BSG dimer is associated with a
CC monocarboxylate transporter dimer. Interacts with ATP1B2, MAG and
CC L1CAM (By similarity). Interacts with AJAP1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Melanosome. Note=Colocalizes with SLC16A1 and SLC16A8 (By
CC similarity). Identified by mass spectrometry in melanosome
CC fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long, Basigin-2;
CC IsoId=P35613-1; Sequence=Displayed;
CC Name=2; Synonyms=Basigin-1;
CC IsoId=P35613-2; Sequence=VSP_011501;
CC Name=3; Synonyms=Basigin-3;
CC IsoId=P35613-3; Sequence=VSP_043225;
CC Note=Produced by alternative promoter usage. N-glycosylated;
CC Name=4; Synonyms=Basigin-4;
CC IsoId=P35613-4; Sequence=VSP_043226, VSP_043227;
CC Note=Produced by alternative promoter usage. N-glycosylated;
CC -!- TISSUE SPECIFICITY: Present only in vascular endothelium in non-
CC neoplastic regions of the brain, whereas it is present in tumor
CC cells but not in proliferating blood vessels in malignant gliomas.
CC -!- INDUCTION: Enriched on the surface of tumor cells. Up-regulated in
CC gliomas. Its expression levels correlate with malignant potential
CC of the tumor.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC domain.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC mutation database;
CC URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system;=ok";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/bsg/";
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DR EMBL; X64364; CAA45716.1; -; mRNA.
DR EMBL; D45131; BAA08109.1; -; mRNA.
DR EMBL; L10240; AAA68936.1; -; mRNA.
DR EMBL; M87879; AAA91084.1; -; mRNA.
DR EMBL; L20471; AAB41120.1; -; mRNA.
DR EMBL; AF042854; AAD10704.1; -; Genomic_DNA.
DR EMBL; AF042848; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042849; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042850; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042851; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042852; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AF042853; AAD10704.1; JOINED; Genomic_DNA.
DR EMBL; AB072923; BAB88938.1; -; mRNA.
DR EMBL; AB085790; BAC76828.1; -; mRNA.
DR EMBL; AF548371; AAN40694.1; -; mRNA.
DR EMBL; GU557064; ADD31881.1; -; mRNA.
DR EMBL; GU557065; ADD31882.1; -; mRNA.
DR EMBL; AY358113; AAQ88480.1; -; mRNA.
DR EMBL; AY942196; AAX20110.1; -; Genomic_DNA.
DR EMBL; AC005559; AAC33279.1; -; Genomic_DNA.
DR EMBL; CH471242; EAW61181.1; -; Genomic_DNA.
DR EMBL; CH471242; EAW61185.1; -; Genomic_DNA.
DR EMBL; BC009040; AAH09040.1; -; mRNA.
DR PIR; A46506; A46506.
DR RefSeq; NP_001719.2; NM_001728.3.
DR RefSeq; NP_940991.1; NM_198589.2.
DR RefSeq; NP_940992.1; NM_198590.2.
DR RefSeq; NP_940993.1; NM_198591.2.
DR RefSeq; XP_005259676.1; XM_005259619.1.
DR UniGene; Hs.501293; -.
DR PDB; 3B5H; X-ray; 2.80 A; A/B/C/D=140-321.
DR PDB; 3I84; X-ray; 2.00 A; A/B=13-219.
DR PDB; 3I85; X-ray; 2.50 A; A/B=13-219.
DR PDB; 3QQN; X-ray; 2.31 A; A/B=23-138.
DR PDB; 3QR2; X-ray; 2.30 A; A/B=23-138.
DR PDBsum; 3B5H; -.
DR PDBsum; 3I84; -.
DR PDBsum; 3I85; -.
DR PDBsum; 3QQN; -.
DR PDBsum; 3QR2; -.
DR ProteinModelPortal; P35613; -.
DR SMR; P35613; 23-319.
DR IntAct; P35613; 13.
DR MINT; MINT-5004205; -.
DR STRING; 9606.ENSP00000333769; -.
DR TCDB; 8.A.23.1.1; the basigin (basigin) family.
DR PhosphoSite; P35613; -.
DR DMDM; 51704273; -.
DR PaxDb; P35613; -.
DR PRIDE; P35613; -.
DR DNASU; 682; -.
DR Ensembl; ENST00000333511; ENSP00000333769; ENSG00000172270.
DR Ensembl; ENST00000346916; ENSP00000344707; ENSG00000172270.
DR Ensembl; ENST00000353555; ENSP00000343809; ENSG00000172270.
DR Ensembl; ENST00000545507; ENSP00000473664; ENSG00000172270.
DR GeneID; 682; -.
DR KEGG; hsa:682; -.
DR UCSC; uc002loz.4; human.
DR CTD; 682; -.
DR GeneCards; GC19P000571; -.
DR HGNC; HGNC:1116; BSG.
DR HPA; CAB002427; -.
DR MIM; 109480; gene.
DR MIM; 111380; phenotype.
DR neXtProt; NX_P35613; -.
DR PharmGKB; PA25433; -.
DR eggNOG; NOG83713; -.
DR HOGENOM; HOG000263411; -.
DR HOVERGEN; HBG008120; -.
DR InParanoid; P35613; -.
DR KO; K06535; -.
DR OMA; DRNHLTR; -.
DR OrthoDB; EOG7V1FQN; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_118779; Extracellular matrix organization.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; BSG; human.
DR EvolutionaryTrace; P35613; -.
DR GeneWiki; Basigin; -.
DR GenomeRNAi; 682; -.
DR NextBio; 2802; -.
DR PMAP-CutDB; P35613; -.
DR PRO; PR:P35613; -.
DR ArrayExpress; P35613; -.
DR Bgee; P35613; -.
DR CleanEx; HS_BSG; -.
DR Genevestigator; P35613; -.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone stimulus; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR009151; Basigin.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075:SF6; PTHR10075:SF6; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Blood group antigen; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lectin; Mannose-binding; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 21
FT CHAIN 22 385 Basigin.
FT /FTId=PRO_0000014518.
FT TOPO_DOM 138 323 Extracellular (Potential).
FT TRANSMEM 324 344 Helical; (Potential).
FT TOPO_DOM 345 385 Cytoplasmic (Potential).
FT DOMAIN 138 219 Ig-like C2-type.
FT DOMAIN 221 315 Ig-like V-type.
FT COMPBIAS 356 359 Poly-Asp.
FT MOD_RES 362 362 Phosphoserine.
FT MOD_RES 368 368 Phosphoserine (By similarity).
FT CARBOHYD 160 160 N-linked (GlcNAc...).
FT CARBOHYD 268 268 N-linked (GlcNAc...).
FT CARBOHYD 302 302 N-linked (GlcNAc...) (Potential).
FT DISULFID 157 203
FT DISULFID 242 301
FT VAR_SEQ 1 209 Missing (in isoform 3).
FT /FTId=VSP_043225.
FT VAR_SEQ 1 11 MAAALFVLLGF -> MKQSDASPQER (in isoform
FT 4).
FT /FTId=VSP_043226.
FT VAR_SEQ 12 191 Missing (in isoform 4).
FT /FTId=VSP_043227.
FT VAR_SEQ 24 139 Missing (in isoform 2).
FT /FTId=VSP_011501.
FT VARIANT 208 208 E -> K (in Ok(A-)).
FT /FTId=VAR_013574.
FT VARIANT 269 269 G -> V (in dbSNP:rs1803203).
FT /FTId=VAR_011720.
FT CONFLICT 328 328 F -> L (in Ref. 2; BAC76828).
FT STRAND 24 27
FT STRAND 32 35
FT STRAND 40 47
FT STRAND 53 62
FT HELIX 74 77
FT STRAND 79 95
FT HELIX 100 102
FT STRAND 104 111
FT STRAND 116 118
FT STRAND 128 137
FT STRAND 142 149
FT STRAND 152 159
FT STRAND 166 173
FT STRAND 176 181
FT STRAND 186 192
FT HELIX 194 196
FT STRAND 199 207
FT STRAND 210 217
FT STRAND 224 226
FT STRAND 228 233
FT STRAND 238 243
FT STRAND 252 257
FT STRAND 260 262
FT HELIX 270 272
FT STRAND 274 279
FT STRAND 282 287
FT TURN 292 294
FT STRAND 295 305
FT STRAND 308 319
SQ SEQUENCE 385 AA; 42200 MW; D74C37455BF26685 CRC64;
MAAALFVLLG FALLGTHGAS GAAGFVQAPL SQQRWVGGSV ELHCEAVGSP VPEIQWWFEG
QGPNDTCSQL WDGARLDRVH IHATYHQHAA STISIDTLVE EDTGTYECRA SNDPDRNHLT
RAPRVKWVRA QAVVLVLEPG TVFTTVEDLG SKILLTCSLN DSATEVTGHR WLKGGVVLKE
DALPGQKTEF KVDSDDQWGE YSCVFLPEPM GTANIQLHGP PRVKAVKSSE HINEGETAML
VCKSESVPPV TDWAWYKITD SEDKALMNGS ESRFFVSSSQ GRSELHIENL NMEADPGQYR
CNGTSSKGSD QAIITLRVRS HLAALWPFLG IVAEVLVLVT IIFIYEKRRK PEDVLDDDDA
GSAPLKSSGQ HQNDKGKNVR QRNSS
//
MIM
109480
*RECORD*
*FIELD* NO
109480
*FIELD* TI
*109480 BASIGIN; BSG
;;TCSF;;
EXTRACELLULAR MATRIX METALLOPROTEINASE INDUCER; EMMPRIN;;
read moreM6 LEUKOCYTE ACTIVATION ANTIGEN; M6;;
CD147 ANTIGEN; CD147
*FIELD* TX
DESCRIPTION
Basigin is a member of the immunoglobulin superfamily, with a structure
related to the putative primordial form of the family. As members of the
immunoglobulin superfamily play fundamental roles in intercellular
recognition involved in various immunologic phenomena, differentiation,
and development, basigin is thought also to play a role in intercellular
recognition (Miyauchi et al., 1991; Kanekura et al., 1991).
CLONING
Basigin was cloned as a carrier of an oncodevelopmental carbohydrate
marker expressed in teratocarcinoma stem cells. It is expressed broadly
in both embryos and adults. (Miyauchi et al., 1990, 1991; Kanekura et
al., 1991).
By biochemical, immunochemical, and micropeptide sequencing analyses,
Spring et al. (1997) determined that the OK blood group antigen (see
111380) is identical to the M6 leukocyte activation antigen and BSG.
Flow cytometric analysis demonstrated ubiquitous expression in
leukocytes. Immunohistochemistry indicated that OK antigen is expressed
in a number of normal human tissues as well as in malignant cells.
Immunoblot analysis showed expression of a 34-kD protein and a 50- to
70-kD protein of similar size to that seen in erythrocyte membranes.
By PCR using primers designed from purified peptide fragments, followed
by RACE, Biswas et al. (1995) cloned EMMPRIN. The deduced 269-amino acid
protein encodes a 21-amino acid N-terminal signal peptide, followed by a
185-amino acid extracellular domain, a putative transmembrane region,
and a short C-terminal domain. The extracellular domain contains 2
immunoglobulin-like subdomains, and the putative transmembrane region
has features of a leucine zipper motif. Northern blot analysis detected
a 1.7-kb EMMPRIN transcript in a human hepatic stellate cell line.
Wu et al. (2011) stated that there are 4 splice variants of BSG. RT-PCR
showed that only variant-2 was expressed in peripheral blood mononuclear
cells. Variant-2 lacks exon 3 and encodes a protein with a deletion in
its N-terminal region compared with the full-length protein.
GENE STRUCTURE
Guo et al. (1998) determined that the BSG gene contains 8 exons and
spans 10.8 kb. Exon 1 contains the 5-prime UTR and the translation start
site, which falls within a CpG island. The 5-prime flanking sequence
contains 3 consensus binding sites for SP1 (189906) and 2 sites for AP2
(107580), but no TATA or CAAT boxes.
Wu et al. (2011) reported that the BSG gene contains 10 exons. The first
4 exons, including 2 alternative first exons, are subject to alternative
splicing.
MAPPING
Kaname et al. (1993) mapped the human BSG gene to 19p13.3 by
fluorescence in situ hybridization. Using an interspecific backcross
panel and microsatellite polymorphisms as markers, Simon-Chazottes et
al. (1992) mapped the gene for basigin (Bsg) to mouse chromosome 10.
GENE FUNCTION
Pushkarsky et al. (2001) identified CD147 as a receptor for
extracellular cyclophilin A (CYPA; 123840). They found that CD147
enhanced human immunodeficiency virus (HIV)-1 infection through
interaction with CYPA incorporated into virions. Virus-associated CYPA
coimmunoprecipitated with CD147 from infected cells, and antibody to
CD147 inhibited HIV-1 entry. Viruses whose replication did not require
CYPA were resistant to the inhibitory effect of anti-CD147 antibody.
Pushkarsky et al. (2001) concluded that HIV-1 entry depends on an
interaction between virus-associated CYPA and CD147 on a target cell.
Yurchenko et al. (2001) determined that CD147 also serves as a receptor
for cyclophilin B (CYPB; 123841). CYPB induced Ca(2+) flux, ERK (see
MAPK3; 601795) phosphorylation, and chemotaxis in CD147-transfected
Chinese hamster ovary cells, but not in control cells. The chemotactic
response of primary human neutrophils to CYPB was blocked by antibodies
to CD147.
Using expression cloning, Renno et al. (2002) identified CD147 as a
molecule expressed on the surface of cycling thymocytes. CD147
expression correlated with immature thymocyte cycling, and ligation of
the molecule on these cells inhibited their development into mature T
cells.
Zhou et al. (2005) identified CD147 as a subunit of native
gamma-secretase complexes (see PSEN1; 104311) purified from HeLa cell
membranes. Coimmunoprecipitation studies confirmed the presence of CD147
in HeLa cell complexes and in soluble complexes from a human neural cell
line and embryonic kidney cells. Depletion of CD147 by RNA interference
increased production of amyloid-beta (see APP; 104760) peptides without
changing the expression of other gamma-secretase components or APP
substrates. Zhou et al. (2005) concluded that the presence of CD147
within the gamma-secretase complex downmodulates production of
amyloid-beta peptides.
Schreiner et al. (2007) found that SHREW1 (AJAP1; 610972), a protein
associated with cellular invasion, interacted with CD147 in epithelial
cells. Downregulation of SHREW1 or CD147 using small interfering RNA in
HeLa cells decreased invasiveness without affecting proliferation.
Schreiner et al. (2007) concluded that SHREW1-CD147 interaction is
associated with regulation of cellular invasion.
By systematic screening of a library of erythrocyte proteins, Crosnier
et al. (2011) identified basigin as a receptor for PfRh5, a Plasmodium
falciparum ligand essential for blood stage growth of the parasite, the
causative agent of malaria (see 611162). Soluble basigin or basigin
knockdown inhibited erythrocyte invasion by all P. falciparum strains,
and complete blocking was achieved by anti-basigin antibodies. OK(a-)
red blood cells, which express the glu92-to-lys (E92K; 109480.0001)
variant of basigin, had reduced binding to PfRh5 due to slower
association and faster dissociation rates. Another basigin variant,
leu90 to pro (L90P), did not interact with PfRh5 at all. Crosnier et al.
(2011) concluded that the dependence on a single receptor-ligand pair
across many P. falciparum strains may provide novel possibilities for
therapeutic intervention.
MOLECULAR GENETICS
Wu et al. (2011) noted that a psoriasis susceptibility locus, PSORS6
(605364), is located on chromosome 19p13, where the BSG gene maps. They
genotyped a T-to-A SNP, dbSNP rs8259, in the 3-prime UTR of the BSG gene
in 668 psoriasis patients and 1,143 healthy controls from a central
south Chinese population. The T allele was associated with significantly
decreased susceptibility to psoriasis (odds ratio = 0.758; p = 0.002).
Wu et al. (2011) found that the T allele of dbSNP rs8259 created a
functional binding site for microRNA-492 (MIR492; 614384), leading to
reduced translation of the BSG transcript. In contrast, the A allele
abolished the MIR492-binding site and was associated with increased
expression of BSG variant-2 in peripheral blood mononuclear cells.
ANIMAL MODEL
Naruhashi et al. (1997) generated mice deficient in basigin by targeted
disruption. Bsg -/- mice showed worse performance than their wildtype
and heterozygous littermates in the Y-maze task, which assesses
short-term memory, and in the water-finding task, which examines latent
learning, without any motor dysfunction. Moreover, the mutant mice
showed less acclimation in the habituation task compared with the
wildtype mice. The mutant mice were also more sensitive to electric foot
shock. Naruhashi et al. (1997) found these findings consistent with the
expression profile of basigin in the central nervous system and
suggested that basigin may play an important role in learning and memory
as well as in sensory functions.
Kuno et al. (1998) demonstrated that female mice deficient in basigin
are infertile due to failure of female reproductive processes including
not only implantation but also fertilization. Bsg mRNA expression in
cumulus cells and basolateral localization of the Bsg protein in the
endometrial epithelium further support the importance of Bsg in these
processes.
In Bsg -/- mice, Philp et al. (2003) found severe reduction in
accumulation of MCT1 (600682) and MCT3 (610409) proteins in the retinal
pigment epithelium and concomitant reduction in the MCT1 and MCT4
(603877) proteins in the neural retina, supporting a role for basigin in
the targeting of these transporters to the plasma membrane. The authors
concluded that decreased expression of MCT1 and MCT4 on the surfaces of
Muller and photoreceptor cells might compromise energy metabolism in the
outer retina, leading to abnormal photoreceptor cell function and
degeneration.
In order to determine the contribution of genetic background on the
Bsg-null phenotype, Chen et al. (2004) developed 3 strains of Bsg-null
mice. In 2 strains, lack of Bsg caused a high rate of embryonic
lethality, sterility in both sexes, and blindness associated with
abnormal electroretinograms and retinal degeneration predominantly in
the photoreceptor layer. The third strain showed higher embryonic
survival, but infertility and blindness persisted.
*FIELD* AV
.0001
BLOOD GROUP--OK
BSG, GLU92LYS
Spring et al. (1997) determined that a G-to-A transition at nucleotide
331 of the BSG gene, leading to a glu92-to-lys substitution, resulted in
the OK(a-) phenotype (111380) in 2 Japanese sisters and an unrelated
Japanese donor. The authors noted that the OK(a-) phenotype had only
been identified in 8 families, all of which were Japanese.
*FIELD* RF
1. Biswas, C.; Zhang, Y.; DeCastro, R.; Guo, H.; Nakamura, T.; Kataoka,
H.; Nabeshima, K.: The human tumor cell-derived collagenase stimulatory
factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer
Res. 55: 434-439, 1995.
2. Chen, S.; Kadomatsu, K.; Kondo, M.; Toyama, Y.; Toshimori, K.;
Ueno, S.; Miyake, Y.; Muramatsu, T.: Effects of flanking genes on
the phenotypes of mice deficient in basigin/CD147. Biochem. Biophys.
Res. Commun. 324: 147-153, 2004.
3. Crosnier, C.; Bustamante, L. Y.; Bartholdson, S. J.; Bei, A. K.;
Theron, M.; Uchikawa, M.; Mboup, S.; Ndir, O.; Kwiatkowski, D. P.;
Duraisingh, M. T.; Rayner, J. C.; Wright, G. J.: Basigin is a receptor
essential for erythrocyte invasion by Plasmodium falciparum. Nature 480:
534-537, 2011.
4. Guo, H.; Majmudar, G.; Jensen, T. C.; Biswas, C.; Toole, B. P.;
Gordon, M. K.: Characterization of the gene for human EMMPRIN, a
tumor cell surface inducer of matrix metalloproteinases. Gene 220:
99-108, 1998.
5. Kaname, T.; Miyauchi, T.; Kuwano, A.; Matsuda, Y.; Muramatsu, T.;
Kajii, T.: Mapping basigin (BSG), a member of the immunoglobulin
superfamily, to 19p13.3. Cytogenet. Cell Genet. 64: 195-197, 1993.
6. Kanekura, T.; Miyauchi, T.; Tashiro, M.; Muramatsu, T.: Basigin,
a new member of the immunoglobulin superfamily: genes in different
mammalian species, glycosylation changes in the molecule from adult
organs and possible variation in the N-terminal sequences. Cell Struct.
Funct. 16: 23-30, 1991.
7. Kuno, N.; Kadomatsu, K.; Fan, Q.-W.; Hagihara, M.; Senda, T.; Mizutani,
S.; Muramatsu, T.: Female sterility in mice lacking the basigin gene,
which encodes a transmembrane glycoprotein belonging to the immunoglobulin
superfamily. FEBS Lett. 425: 191-194, 1998.
8. Miyauchi, T.; Kanekura, T.; Yamaoka, A.; Ozawa, M.; Miyazawa, S.;
Muramatsu, T.: Basigin, a new, broadly distributed member of the
immunoglobulin superfamily, has strong homology with both the immunoglobulin
V domain and the beta-chain of major histocompatibility complex class
II antigen. J. Biochem. 107: 316-323, 1990.
9. Miyauchi, T.; Masuzawa, Y.; Muramatsu, T.: The basigin group of
the immunoglobulin superfamily: complete conservation of a segment
in and around transmembrane domains of human and mouse basigin and
chicken HT7 antigen. J. Biochem. 110: 770-774, 1991.
10. Naruhashi, K.; Kadomatsu, K.; Igakura, T.; Fan, Q.-W.; Kuno, N.;
Muramatsu, H.; Miyauchi, T.; Hasegawa, T.; Itoh, A.; Muramatsu, T.;
Nabeshima, T.: Abnormalities of sensory and memory functions in mice
lacking Bsg gene. Biochem. Biophsy. Res. Commun. 236: 733-737, 1997.
11. Philp, N. J.; Ochrietor, J. D.; Rudoy, C.; Muramatsu, T.; Pinser,
P. J.: Loss of MCT1, MCT3, and MCT4 Expression in the retinal pigment
epithelium and neural retinal of the 5A11-basigin-null mouse. Invest.
Ophthal. Vis. Sci. 44: 1305-1311, 2003.
12. Pushkarsky, T.; Zybarth, G.; Dubrovsky, L.; Yurchenko, V.; Tang,
H.; Guo, H.; Toole, B.; Sherry, B.; Bukrinsky, M.: CD147 facilitates
HIV-1 infection by interacting with virus-associated cyclophilin A. Proc.
Nat. Acad. Sci. 98: 6360-6365, 2001.
13. Renno, T.; Wilson, A.; Dunkel, C.; Coste, I.; Maisnier-Patin,
K.; de Coignac, A. B.; Aubry, J.-P.; Lees, R. K.; Bonnefoy, J.-Y.;
MacDonald, H. R.; Gauchat, J.-F.: A role for CD147 in thymic development. J.
Immun. 168: 4946-4950, 2002.
14. Schreiner, A.; Ruonala, M.; Jakob, V.; Suthaus, J.; Boles, E.;
Wouters, F.; Starzinsi-Powitz, A.: Junction protein shrew-1 influences
cell invasion and interacts with invasion-promoting protein CD147. Molec.
Biol. Cell 18: 1272-1281, 2007.
15. Simon-Chazottes, D.; Matsubara, S.; Miyauchi, T.; Muramatsu, T.;
Guenet, J.-L.: Chromosomal localization of two cell surface-associated
molecules of potential importance in development: midkine (Mdk) and
basigin (Bsg). Mammalian Genome 2: 269-271, 1992.
16. Spring, F. A.; Holmes, C. H.; Simpson, K. L.; Mawby, W. J.; Mattes,
M. J.; Okubo, Y.; Parsons, S. F.: The Ok(a) blood group antigen is
a marker for the M6 leukocyte activation antigen, the human homolog
of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily
molecule that is widely expressed in human cells and tissues. Europ.
J. Immun. 27: 891-897, 1997.
17. Wu, L.-S.; Li, F.-F.; Sun, L.-D.; Li, D.; Su, J.; Kuang, Y.-H.;
Chen, G.; Chen, X.-P.; Chen, X.: A miRNA-492 binding-site polymorphism
in BSG (basigin) confers risk to psoriasis in central south Chinese
population. Hum. Genet. 130: 749-757, 2011.
18. Yurchenko, V.; O'Connor, M.; Dai, W. W.; Guo, H.; Toole, B.; Sherry,
B.; Bukrinsky, M.: CD147 is a signaling receptor for cyclophilin
B. Biochem. Biophys. Res. Commun. 288: 786-788, 2001.
19. Zhou, S.; Zhou, H.; Walian, P. J.; Jap, B. K.: CD147 is a regulatory
subunit of the gamma-secretase complex in Alzheimer's disease amyloid
beta-peptide production. Proc. Nat. Acad. Sci. 102: 7499-7504, 2005.
*FIELD* CN
Paul J. Converse - updated: 1/18/2012
Patricia A. Hartz - updated: 12/8/2011
Alan F. Scott - updated: 4/24/2007
Paul J. Converse - updated: 2/13/2006
Patricia A. Hartz - updated: 6/23/2005
Jane Kelly - updated: 3/25/2003
Paul J. Converse - updated: 2/16/2001
Ada Hamosh - updated: 8/18/2000
Ada Hamosh - updated: 7/28/2000
*FIELD* CD
Victor A. McKusick: 11/4/1993
*FIELD* ED
mgross: 01/18/2012
terry: 1/18/2012
mgross: 12/8/2011
mgross: 4/24/2007
wwang: 9/14/2006
mgross: 2/13/2006
mgross: 7/14/2005
terry: 6/23/2005
cwells: 3/25/2003
mgross: 3/16/2001
mgross: 3/13/2001
terry: 2/16/2001
carol: 8/21/2000
terry: 8/18/2000
alopez: 8/1/2000
terry: 7/28/2000
carol: 11/16/1993
carol: 11/5/1993
carol: 11/4/1993
*RECORD*
*FIELD* NO
109480
*FIELD* TI
*109480 BASIGIN; BSG
;;TCSF;;
EXTRACELLULAR MATRIX METALLOPROTEINASE INDUCER; EMMPRIN;;
read moreM6 LEUKOCYTE ACTIVATION ANTIGEN; M6;;
CD147 ANTIGEN; CD147
*FIELD* TX
DESCRIPTION
Basigin is a member of the immunoglobulin superfamily, with a structure
related to the putative primordial form of the family. As members of the
immunoglobulin superfamily play fundamental roles in intercellular
recognition involved in various immunologic phenomena, differentiation,
and development, basigin is thought also to play a role in intercellular
recognition (Miyauchi et al., 1991; Kanekura et al., 1991).
CLONING
Basigin was cloned as a carrier of an oncodevelopmental carbohydrate
marker expressed in teratocarcinoma stem cells. It is expressed broadly
in both embryos and adults. (Miyauchi et al., 1990, 1991; Kanekura et
al., 1991).
By biochemical, immunochemical, and micropeptide sequencing analyses,
Spring et al. (1997) determined that the OK blood group antigen (see
111380) is identical to the M6 leukocyte activation antigen and BSG.
Flow cytometric analysis demonstrated ubiquitous expression in
leukocytes. Immunohistochemistry indicated that OK antigen is expressed
in a number of normal human tissues as well as in malignant cells.
Immunoblot analysis showed expression of a 34-kD protein and a 50- to
70-kD protein of similar size to that seen in erythrocyte membranes.
By PCR using primers designed from purified peptide fragments, followed
by RACE, Biswas et al. (1995) cloned EMMPRIN. The deduced 269-amino acid
protein encodes a 21-amino acid N-terminal signal peptide, followed by a
185-amino acid extracellular domain, a putative transmembrane region,
and a short C-terminal domain. The extracellular domain contains 2
immunoglobulin-like subdomains, and the putative transmembrane region
has features of a leucine zipper motif. Northern blot analysis detected
a 1.7-kb EMMPRIN transcript in a human hepatic stellate cell line.
Wu et al. (2011) stated that there are 4 splice variants of BSG. RT-PCR
showed that only variant-2 was expressed in peripheral blood mononuclear
cells. Variant-2 lacks exon 3 and encodes a protein with a deletion in
its N-terminal region compared with the full-length protein.
GENE STRUCTURE
Guo et al. (1998) determined that the BSG gene contains 8 exons and
spans 10.8 kb. Exon 1 contains the 5-prime UTR and the translation start
site, which falls within a CpG island. The 5-prime flanking sequence
contains 3 consensus binding sites for SP1 (189906) and 2 sites for AP2
(107580), but no TATA or CAAT boxes.
Wu et al. (2011) reported that the BSG gene contains 10 exons. The first
4 exons, including 2 alternative first exons, are subject to alternative
splicing.
MAPPING
Kaname et al. (1993) mapped the human BSG gene to 19p13.3 by
fluorescence in situ hybridization. Using an interspecific backcross
panel and microsatellite polymorphisms as markers, Simon-Chazottes et
al. (1992) mapped the gene for basigin (Bsg) to mouse chromosome 10.
GENE FUNCTION
Pushkarsky et al. (2001) identified CD147 as a receptor for
extracellular cyclophilin A (CYPA; 123840). They found that CD147
enhanced human immunodeficiency virus (HIV)-1 infection through
interaction with CYPA incorporated into virions. Virus-associated CYPA
coimmunoprecipitated with CD147 from infected cells, and antibody to
CD147 inhibited HIV-1 entry. Viruses whose replication did not require
CYPA were resistant to the inhibitory effect of anti-CD147 antibody.
Pushkarsky et al. (2001) concluded that HIV-1 entry depends on an
interaction between virus-associated CYPA and CD147 on a target cell.
Yurchenko et al. (2001) determined that CD147 also serves as a receptor
for cyclophilin B (CYPB; 123841). CYPB induced Ca(2+) flux, ERK (see
MAPK3; 601795) phosphorylation, and chemotaxis in CD147-transfected
Chinese hamster ovary cells, but not in control cells. The chemotactic
response of primary human neutrophils to CYPB was blocked by antibodies
to CD147.
Using expression cloning, Renno et al. (2002) identified CD147 as a
molecule expressed on the surface of cycling thymocytes. CD147
expression correlated with immature thymocyte cycling, and ligation of
the molecule on these cells inhibited their development into mature T
cells.
Zhou et al. (2005) identified CD147 as a subunit of native
gamma-secretase complexes (see PSEN1; 104311) purified from HeLa cell
membranes. Coimmunoprecipitation studies confirmed the presence of CD147
in HeLa cell complexes and in soluble complexes from a human neural cell
line and embryonic kidney cells. Depletion of CD147 by RNA interference
increased production of amyloid-beta (see APP; 104760) peptides without
changing the expression of other gamma-secretase components or APP
substrates. Zhou et al. (2005) concluded that the presence of CD147
within the gamma-secretase complex downmodulates production of
amyloid-beta peptides.
Schreiner et al. (2007) found that SHREW1 (AJAP1; 610972), a protein
associated with cellular invasion, interacted with CD147 in epithelial
cells. Downregulation of SHREW1 or CD147 using small interfering RNA in
HeLa cells decreased invasiveness without affecting proliferation.
Schreiner et al. (2007) concluded that SHREW1-CD147 interaction is
associated with regulation of cellular invasion.
By systematic screening of a library of erythrocyte proteins, Crosnier
et al. (2011) identified basigin as a receptor for PfRh5, a Plasmodium
falciparum ligand essential for blood stage growth of the parasite, the
causative agent of malaria (see 611162). Soluble basigin or basigin
knockdown inhibited erythrocyte invasion by all P. falciparum strains,
and complete blocking was achieved by anti-basigin antibodies. OK(a-)
red blood cells, which express the glu92-to-lys (E92K; 109480.0001)
variant of basigin, had reduced binding to PfRh5 due to slower
association and faster dissociation rates. Another basigin variant,
leu90 to pro (L90P), did not interact with PfRh5 at all. Crosnier et al.
(2011) concluded that the dependence on a single receptor-ligand pair
across many P. falciparum strains may provide novel possibilities for
therapeutic intervention.
MOLECULAR GENETICS
Wu et al. (2011) noted that a psoriasis susceptibility locus, PSORS6
(605364), is located on chromosome 19p13, where the BSG gene maps. They
genotyped a T-to-A SNP, dbSNP rs8259, in the 3-prime UTR of the BSG gene
in 668 psoriasis patients and 1,143 healthy controls from a central
south Chinese population. The T allele was associated with significantly
decreased susceptibility to psoriasis (odds ratio = 0.758; p = 0.002).
Wu et al. (2011) found that the T allele of dbSNP rs8259 created a
functional binding site for microRNA-492 (MIR492; 614384), leading to
reduced translation of the BSG transcript. In contrast, the A allele
abolished the MIR492-binding site and was associated with increased
expression of BSG variant-2 in peripheral blood mononuclear cells.
ANIMAL MODEL
Naruhashi et al. (1997) generated mice deficient in basigin by targeted
disruption. Bsg -/- mice showed worse performance than their wildtype
and heterozygous littermates in the Y-maze task, which assesses
short-term memory, and in the water-finding task, which examines latent
learning, without any motor dysfunction. Moreover, the mutant mice
showed less acclimation in the habituation task compared with the
wildtype mice. The mutant mice were also more sensitive to electric foot
shock. Naruhashi et al. (1997) found these findings consistent with the
expression profile of basigin in the central nervous system and
suggested that basigin may play an important role in learning and memory
as well as in sensory functions.
Kuno et al. (1998) demonstrated that female mice deficient in basigin
are infertile due to failure of female reproductive processes including
not only implantation but also fertilization. Bsg mRNA expression in
cumulus cells and basolateral localization of the Bsg protein in the
endometrial epithelium further support the importance of Bsg in these
processes.
In Bsg -/- mice, Philp et al. (2003) found severe reduction in
accumulation of MCT1 (600682) and MCT3 (610409) proteins in the retinal
pigment epithelium and concomitant reduction in the MCT1 and MCT4
(603877) proteins in the neural retina, supporting a role for basigin in
the targeting of these transporters to the plasma membrane. The authors
concluded that decreased expression of MCT1 and MCT4 on the surfaces of
Muller and photoreceptor cells might compromise energy metabolism in the
outer retina, leading to abnormal photoreceptor cell function and
degeneration.
In order to determine the contribution of genetic background on the
Bsg-null phenotype, Chen et al. (2004) developed 3 strains of Bsg-null
mice. In 2 strains, lack of Bsg caused a high rate of embryonic
lethality, sterility in both sexes, and blindness associated with
abnormal electroretinograms and retinal degeneration predominantly in
the photoreceptor layer. The third strain showed higher embryonic
survival, but infertility and blindness persisted.
*FIELD* AV
.0001
BLOOD GROUP--OK
BSG, GLU92LYS
Spring et al. (1997) determined that a G-to-A transition at nucleotide
331 of the BSG gene, leading to a glu92-to-lys substitution, resulted in
the OK(a-) phenotype (111380) in 2 Japanese sisters and an unrelated
Japanese donor. The authors noted that the OK(a-) phenotype had only
been identified in 8 families, all of which were Japanese.
*FIELD* RF
1. Biswas, C.; Zhang, Y.; DeCastro, R.; Guo, H.; Nakamura, T.; Kataoka,
H.; Nabeshima, K.: The human tumor cell-derived collagenase stimulatory
factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer
Res. 55: 434-439, 1995.
2. Chen, S.; Kadomatsu, K.; Kondo, M.; Toyama, Y.; Toshimori, K.;
Ueno, S.; Miyake, Y.; Muramatsu, T.: Effects of flanking genes on
the phenotypes of mice deficient in basigin/CD147. Biochem. Biophys.
Res. Commun. 324: 147-153, 2004.
3. Crosnier, C.; Bustamante, L. Y.; Bartholdson, S. J.; Bei, A. K.;
Theron, M.; Uchikawa, M.; Mboup, S.; Ndir, O.; Kwiatkowski, D. P.;
Duraisingh, M. T.; Rayner, J. C.; Wright, G. J.: Basigin is a receptor
essential for erythrocyte invasion by Plasmodium falciparum. Nature 480:
534-537, 2011.
4. Guo, H.; Majmudar, G.; Jensen, T. C.; Biswas, C.; Toole, B. P.;
Gordon, M. K.: Characterization of the gene for human EMMPRIN, a
tumor cell surface inducer of matrix metalloproteinases. Gene 220:
99-108, 1998.
5. Kaname, T.; Miyauchi, T.; Kuwano, A.; Matsuda, Y.; Muramatsu, T.;
Kajii, T.: Mapping basigin (BSG), a member of the immunoglobulin
superfamily, to 19p13.3. Cytogenet. Cell Genet. 64: 195-197, 1993.
6. Kanekura, T.; Miyauchi, T.; Tashiro, M.; Muramatsu, T.: Basigin,
a new member of the immunoglobulin superfamily: genes in different
mammalian species, glycosylation changes in the molecule from adult
organs and possible variation in the N-terminal sequences. Cell Struct.
Funct. 16: 23-30, 1991.
7. Kuno, N.; Kadomatsu, K.; Fan, Q.-W.; Hagihara, M.; Senda, T.; Mizutani,
S.; Muramatsu, T.: Female sterility in mice lacking the basigin gene,
which encodes a transmembrane glycoprotein belonging to the immunoglobulin
superfamily. FEBS Lett. 425: 191-194, 1998.
8. Miyauchi, T.; Kanekura, T.; Yamaoka, A.; Ozawa, M.; Miyazawa, S.;
Muramatsu, T.: Basigin, a new, broadly distributed member of the
immunoglobulin superfamily, has strong homology with both the immunoglobulin
V domain and the beta-chain of major histocompatibility complex class
II antigen. J. Biochem. 107: 316-323, 1990.
9. Miyauchi, T.; Masuzawa, Y.; Muramatsu, T.: The basigin group of
the immunoglobulin superfamily: complete conservation of a segment
in and around transmembrane domains of human and mouse basigin and
chicken HT7 antigen. J. Biochem. 110: 770-774, 1991.
10. Naruhashi, K.; Kadomatsu, K.; Igakura, T.; Fan, Q.-W.; Kuno, N.;
Muramatsu, H.; Miyauchi, T.; Hasegawa, T.; Itoh, A.; Muramatsu, T.;
Nabeshima, T.: Abnormalities of sensory and memory functions in mice
lacking Bsg gene. Biochem. Biophsy. Res. Commun. 236: 733-737, 1997.
11. Philp, N. J.; Ochrietor, J. D.; Rudoy, C.; Muramatsu, T.; Pinser,
P. J.: Loss of MCT1, MCT3, and MCT4 Expression in the retinal pigment
epithelium and neural retinal of the 5A11-basigin-null mouse. Invest.
Ophthal. Vis. Sci. 44: 1305-1311, 2003.
12. Pushkarsky, T.; Zybarth, G.; Dubrovsky, L.; Yurchenko, V.; Tang,
H.; Guo, H.; Toole, B.; Sherry, B.; Bukrinsky, M.: CD147 facilitates
HIV-1 infection by interacting with virus-associated cyclophilin A. Proc.
Nat. Acad. Sci. 98: 6360-6365, 2001.
13. Renno, T.; Wilson, A.; Dunkel, C.; Coste, I.; Maisnier-Patin,
K.; de Coignac, A. B.; Aubry, J.-P.; Lees, R. K.; Bonnefoy, J.-Y.;
MacDonald, H. R.; Gauchat, J.-F.: A role for CD147 in thymic development. J.
Immun. 168: 4946-4950, 2002.
14. Schreiner, A.; Ruonala, M.; Jakob, V.; Suthaus, J.; Boles, E.;
Wouters, F.; Starzinsi-Powitz, A.: Junction protein shrew-1 influences
cell invasion and interacts with invasion-promoting protein CD147. Molec.
Biol. Cell 18: 1272-1281, 2007.
15. Simon-Chazottes, D.; Matsubara, S.; Miyauchi, T.; Muramatsu, T.;
Guenet, J.-L.: Chromosomal localization of two cell surface-associated
molecules of potential importance in development: midkine (Mdk) and
basigin (Bsg). Mammalian Genome 2: 269-271, 1992.
16. Spring, F. A.; Holmes, C. H.; Simpson, K. L.; Mawby, W. J.; Mattes,
M. J.; Okubo, Y.; Parsons, S. F.: The Ok(a) blood group antigen is
a marker for the M6 leukocyte activation antigen, the human homolog
of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily
molecule that is widely expressed in human cells and tissues. Europ.
J. Immun. 27: 891-897, 1997.
17. Wu, L.-S.; Li, F.-F.; Sun, L.-D.; Li, D.; Su, J.; Kuang, Y.-H.;
Chen, G.; Chen, X.-P.; Chen, X.: A miRNA-492 binding-site polymorphism
in BSG (basigin) confers risk to psoriasis in central south Chinese
population. Hum. Genet. 130: 749-757, 2011.
18. Yurchenko, V.; O'Connor, M.; Dai, W. W.; Guo, H.; Toole, B.; Sherry,
B.; Bukrinsky, M.: CD147 is a signaling receptor for cyclophilin
B. Biochem. Biophys. Res. Commun. 288: 786-788, 2001.
19. Zhou, S.; Zhou, H.; Walian, P. J.; Jap, B. K.: CD147 is a regulatory
subunit of the gamma-secretase complex in Alzheimer's disease amyloid
beta-peptide production. Proc. Nat. Acad. Sci. 102: 7499-7504, 2005.
*FIELD* CN
Paul J. Converse - updated: 1/18/2012
Patricia A. Hartz - updated: 12/8/2011
Alan F. Scott - updated: 4/24/2007
Paul J. Converse - updated: 2/13/2006
Patricia A. Hartz - updated: 6/23/2005
Jane Kelly - updated: 3/25/2003
Paul J. Converse - updated: 2/16/2001
Ada Hamosh - updated: 8/18/2000
Ada Hamosh - updated: 7/28/2000
*FIELD* CD
Victor A. McKusick: 11/4/1993
*FIELD* ED
mgross: 01/18/2012
terry: 1/18/2012
mgross: 12/8/2011
mgross: 4/24/2007
wwang: 9/14/2006
mgross: 2/13/2006
mgross: 7/14/2005
terry: 6/23/2005
cwells: 3/25/2003
mgross: 3/16/2001
mgross: 3/13/2001
terry: 2/16/2001
carol: 8/21/2000
terry: 8/18/2000
alopez: 8/1/2000
terry: 7/28/2000
carol: 11/16/1993
carol: 11/5/1993
carol: 11/4/1993
MIM
111380
*RECORD*
*FIELD* NO
111380
*FIELD* TI
#111380 BLOOD GROUP--OK; OK
*FIELD* TX
A number sign (#) is used with this entry because the OK(a-) phenotype
read moreresults from a mutation in the gene encoding basigin (BSG; 109480).
A murine monoclonal antibody produced in response to immunization with a
human teratocarcinoma cell line recognizes a cell surface antigen
expressed by all human cells, including red blood cells. All red cell
samples tested reacted positively with the monoclonal antibody except
those of a very rare phenotype called OK(a-). Only 3 unrelated OK(a-)
propositi were known to Williams et al. (1987), who found that the cells
in all 3 were negative for the monoclonal antibody. Further tests
suggested that the immune antibody found in the serum of some OK(a-)
persons recognized the same cell surface determinant as did the
monoclonal antibody. The determinant was found on the red cells of
gorillas and chimpanzees but not on the red cells of rhesus monkeys,
baboons, and marmosets. Indirect radioimmunoassay of reactivity to the
monoclonal antibody by somatic cell hybrids located the gene to
19pter-p13.2.
By biochemical, immunochemical, and micropeptide sequencing analyses,
Spring et al. (1997) determined that the OK blood group antigen is
identical to the M6 leukocyte activation antigen, also called BSG. They
identified a mutation in the BSG gene (109480.0001) that resulted in the
OK(a-) phenotype in 2 Japanese sisters and an unrelated Japanese donor.
The authors noted that the OK(a-) phenotype had only been identified in
8 families, all which were Japanese.
*FIELD* RF
1. Spring, F. A.; Holmes, C. H.; Simpson, K. L.; Mawby, W. J.; Mattes,
M. J.; Okubo, Y.; Parsons, S. F.: The Ok(a) blood group antigen is
a marker for the M6 leukocyte activation antigen, the human homolog
of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily
molecule that is widely expressed in human cells and tissues. Europ.
J. Immun. 27: 891-897, 1997.
2. Williams, B. P.; Pym, B.; Tippett, P.; Sher, D.; Povey, S.; Andrews,
P. W.; Goodfellow, P. N.; Daniels, G.; Okubo, Y.: Another red cell
surface antigen, OK(a), is encoded by a gene on chromosome 19. (Abstract) Cyto
genet. Cell Genet. 46: 717 only, 1987.
*FIELD* CD
Victor A. McKusick: 8/31/1987
*FIELD* ED
terry: 04/14/2003
mgross: 3/13/2001
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 10/13/1989
root: 6/9/1988
marie: 3/25/1988
*RECORD*
*FIELD* NO
111380
*FIELD* TI
#111380 BLOOD GROUP--OK; OK
*FIELD* TX
A number sign (#) is used with this entry because the OK(a-) phenotype
read moreresults from a mutation in the gene encoding basigin (BSG; 109480).
A murine monoclonal antibody produced in response to immunization with a
human teratocarcinoma cell line recognizes a cell surface antigen
expressed by all human cells, including red blood cells. All red cell
samples tested reacted positively with the monoclonal antibody except
those of a very rare phenotype called OK(a-). Only 3 unrelated OK(a-)
propositi were known to Williams et al. (1987), who found that the cells
in all 3 were negative for the monoclonal antibody. Further tests
suggested that the immune antibody found in the serum of some OK(a-)
persons recognized the same cell surface determinant as did the
monoclonal antibody. The determinant was found on the red cells of
gorillas and chimpanzees but not on the red cells of rhesus monkeys,
baboons, and marmosets. Indirect radioimmunoassay of reactivity to the
monoclonal antibody by somatic cell hybrids located the gene to
19pter-p13.2.
By biochemical, immunochemical, and micropeptide sequencing analyses,
Spring et al. (1997) determined that the OK blood group antigen is
identical to the M6 leukocyte activation antigen, also called BSG. They
identified a mutation in the BSG gene (109480.0001) that resulted in the
OK(a-) phenotype in 2 Japanese sisters and an unrelated Japanese donor.
The authors noted that the OK(a-) phenotype had only been identified in
8 families, all which were Japanese.
*FIELD* RF
1. Spring, F. A.; Holmes, C. H.; Simpson, K. L.; Mawby, W. J.; Mattes,
M. J.; Okubo, Y.; Parsons, S. F.: The Ok(a) blood group antigen is
a marker for the M6 leukocyte activation antigen, the human homolog
of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily
molecule that is widely expressed in human cells and tissues. Europ.
J. Immun. 27: 891-897, 1997.
2. Williams, B. P.; Pym, B.; Tippett, P.; Sher, D.; Povey, S.; Andrews,
P. W.; Goodfellow, P. N.; Daniels, G.; Okubo, Y.: Another red cell
surface antigen, OK(a), is encoded by a gene on chromosome 19. (Abstract) Cyto
genet. Cell Genet. 46: 717 only, 1987.
*FIELD* CD
Victor A. McKusick: 8/31/1987
*FIELD* ED
terry: 04/14/2003
mgross: 3/13/2001
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 10/13/1989
root: 6/9/1988
marie: 3/25/1988