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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) (CD antigen CD147)

 BASI_HUMAN              Reviewed;         385 AA.
P35613; A6NJW1; D3YLG5; Q7Z796; Q8IZL7;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 2.
20-JUN-2018, entry version 198.
RecName: Full=Basigin;
AltName: Full=5F7;
AltName: Full=Collagenase stimulatory factor;
AltName: Full=Extracellular matrix metalloproteinase inducer;
Short=EMMPRIN;
AltName: Full=Leukocyte activation antigen M6;
AltName: Full=OK blood group antigen;
AltName: Full=Tumor cell-derived collagenase stimulatory factor;
Short=TCSF;
AltName: CD_antigen=CD147;
Flags: Precursor;
Name=BSG; ORFNames=UNQ6505/PRO21383;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1634773;
Kasinrerk W., Fiebiger E., Stefanova I., Baumruker T., Knapp W.,
Stockinger H.;
"Human leukocyte activation antigen M6, a member of the Ig
superfamily, is the species homologue of rat OX-47, mouse basigin, and
chicken HT7 molecule.";
J. Immunol. 149:847-854(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=1783610;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7812975;
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).
[4]
NUCLEOTIDE SEQUENCE (ISOFORM 2).
Wakasugi H., Scamps C., Yang G., Vancong N., Bernheim A., Tursz T.,
Harada N.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE (ISOFORM 2).
Decastro R., Zhang Y., Kataoka H., Coon J., Biswas C.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=9767135; DOI=10.1016/S0378-1119(98)00400-4;
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).
[7]
NUCLEOTIDE SEQUENCE (ISOFORM 2).
Sato T., Takita M., Noguchi Y., Hirata M., Sakai T., Ito A.;
"Regulation of EMMPRIN/CD147 expression and its function of
controlling matrix metalloproteinases production and cell-surface
localization in co-culture of human uterine cervical carcinoma SKG-II
cells and human uterine cervical fibroblasts.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE (ISOFORM 2).
Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y.,
Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
TISSUE=Retina;
PubMed=12939332; DOI=10.1167/iovs.02-0995;
Ochrietor J.D., Moroz T.P., van Ekeris L., Clamp M.F., Jefferson S.C.,
deCarvalho A.C., Fadool J.M., Wistow G., Muramatsu T., Linser P.J.;
"Retina-specific expression of 5A11/Basigin-2, a member of the
immunoglobulin gene superfamily.";
Invest. Ophthalmol. Vis. Sci. 44:4086-4096(2003).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBUNIT, SUBCELLULAR
LOCATION, AND ALTERNATIVE PROMOTER USAGE.
PubMed=21536654; DOI=10.1128/MCB.05160-11;
Liao C.G., Kong L.M., Song F., Xing J.L., Wang L.X., Sun Z.J.,
Tang H., Yao H., Zhang Y., Wang L., Wang Y., Yang X.M., Li Y.,
Chen Z.N.;
"Characterization of basigin isoforms and the inhibitory function of
basigin-3 in human hepatocellular carcinoma proliferation and
invasion.";
Mol. Cell. Biol. 31:2591-2604(2011).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
PROTEIN SEQUENCE OF 22-36 (ISOFORM 1).
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[17]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
PubMed=1846736; DOI=10.1016/0003-9861(91)90332-D;
Nabeshima K., Lane W.S., Biswas C.;
"Partial sequencing and characterization of the tumor cell-derived
collagenase stimulatory factor.";
Arch. Biochem. Biophys. 285:90-96(1991).
[18]
REVIEW.
PubMed=12792908;
Muramatsu T., Miyauchi T.;
"Basigin (CD147): a multifunctional transmembrane protein involved in
reproduction, neural function, inflammation and tumor invasion.";
Histol. Histopathol. 18:981-987(2003).
[19]
GLYCOSYLATION AT ASN-160 AND ASN-268.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[20]
INTERACTION WITH PPIL2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PRO-327.
PubMed=15946952; DOI=10.1074/jbc.M503770200;
Pushkarsky T., Yurchenko V., Vanpouille C., Brichacek B., Vaisman I.,
Hatakeyama S., Nakayama K.I., Sherry B., Bukrinsky M.I.;
"Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin
60.";
J. Biol. Chem. 280:27866-27871(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[22]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[23]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SLC16A1.
PubMed=17127621; DOI=10.1080/09687860600841967;
Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.;
"The role of charged residues in the transmembrane helices of
monocarboxylate transporter 1 and its ancillary protein basigin in
determining plasma membrane expression and catalytic activity.";
Mol. Membr. Biol. 23:486-498(2006).
[24]
INTERACTION WITH AJAP1.
PubMed=17267690; DOI=10.1091/mbc.E06-07-0637;
Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
Starzinski-Powitz A.;
"junction protein shrew-1 influences cell invasion and interacts with
invasion-promoting protein CD147.";
Mol. Biol. Cell 18:1272-1281(2007).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[27]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362 AND SER-368, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[34]
FUNCTION, AND INTERACTION WITH SLC16A11.
PubMed=28666119; DOI=10.1016/j.cell.2017.06.011;
MEDIA Consortium;
SIGMA T2D Consortium;
Rusu V., Hoch E., Mercader J.M., Tenen D.E., Gymrek M., Hartigan C.R.,
DeRan M., von Grotthuss M., Fontanillas P., Spooner A., Guzman G.,
Deik A.A., Pierce K.A., Dennis C., Clish C.B., Carr S.A., Wagner B.K.,
Schenone M., Ng M.C.Y., Chen B.H., Centeno-Cruz F., Zerrweck C.,
Orozco L., Altshuler D.M., Schreiber S.L., Florez J.C., Jacobs S.B.R.,
Lander E.S.;
"Type 2 diabetes variants disrupt function of SLC16A11 through two
distinct mechanisms.";
Cell 170:199-212(2017).
[35]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-321, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=18430721; DOI=10.1074/jbc.M802694200;
Yu X.-L., Hu T., Du J.-M., Ding J.-P., Yang X.-M., Zhang J., Yang B.,
Shen X., Zhang Z., Zhong W.-D., Wen N., Jiang H., Zhu P., Chen Z.-N.;
"Crystal structure of HAb18G/CD147: implications for immunoglobulin
superfamily homophilic adhesion.";
J. Biol. Chem. 283:18056-18065(2008).
[36]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-219, IDENTIFICATION BY
MASS SPECTROMETRY, SUBUNIT, AND DISULFIDE BONDS.
PubMed=19768682; DOI=10.1002/prot.22577;
Luo J., Teplyakov A., Obmolova G., Malia T., Wu S.-J., Beil E.,
Baker A., Swencki-Underwood B., Zhao Y., Sprenkle J., Dixon K.,
Sweet R., Gilliland G.L.;
"Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-
strand swapping.";
Proteins 77:1009-1014(2009).
[37]
VARIANT LYS-208.
PubMed=9130641; DOI=10.1002/eji.1830270414;
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.";
Eur. J. Immunol. 27:891-897(1997).
-!- FUNCTION: Plays an important role in targeting the monocarboxylate
transporters SLC16A1, SLC16A3, SLC16A8 and SLC16A11 to the plasma
membrane. Plays pivotal roles in spermatogenesis, embryo
implantation, neural network formation and tumor progression.
Stimulates adjacent fibroblasts to produce matrix
metalloproteinases (MMPS). Seems to be a receptor for
oligomannosidic glycans. In vitro, promotes outgrowth of
astrocytic processes. {ECO:0000269|PubMed:17127621,
ECO:0000269|PubMed:28666119}.
-!- SUBUNIT: Forms homooligomers in a cis-dependent manner on the
plasma membrane. Forms heterooligomers of isoform 2 and isoform 3.
Forms a complex with MMP1 at the tumor cell surface. Interacts
with ATP1B2, MAG and L1CAM (By similarity). Interacts with AJAP1.
Interacts with SLC16A1, SLC16A7 and SLC1A3; probably a BSG dimer
is associated with a monocarboxylate transporter dimer. Interacts
with PPIL2; regulates BSG transport to the cell membrane.
Interacts with SLC16A11 (PubMed:28666119).
{ECO:0000250|UniProtKB:P18572, ECO:0000250|UniProtKB:P26453,
ECO:0000269|PubMed:15946952, ECO:0000269|PubMed:17127621,
ECO:0000269|PubMed:17267690, ECO:0000269|PubMed:18430721,
ECO:0000269|PubMed:19768682, ECO:0000269|PubMed:21536654,
ECO:0000269|PubMed:28666119}.
-!- INTERACTION:
B2L3N7:- (xeno); NbExp=5; IntAct=EBI-11037868, EBI-16118096;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15946952,
ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:21536654}; Single-
pass type I membrane protein {ECO:0000303|PubMed:15946952}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV. In
spermatozoa, localized on the principal piece of caput and in the
middle piece during transit in the corpus and cauda epididymides
(By similarity). {ECO:0000250|UniProtKB:P18572,
ECO:0000269|PubMed:17081065}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long, Basigin-2;
IsoId=P35613-1; Sequence=Displayed;
Name=2; Synonyms=Basigin-1;
IsoId=P35613-2; Sequence=VSP_011501;
Name=3; Synonyms=Basigin-3;
IsoId=P35613-3; Sequence=VSP_043225;
Note=Produced by alternative promoter usage. N-glycosylated.;
Name=4; Synonyms=Basigin-4;
IsoId=P35613-4; Sequence=VSP_043226, VSP_043227;
Note=Produced by alternative promoter usage. N-glycosylated.;
-!- TISSUE SPECIFICITY: Present only in vascular endothelium in non-
neoplastic regions of the brain, whereas it is present in tumor
cells but not in proliferating blood vessels in malignant gliomas.
-!- INDUCTION: Enriched on the surface of tumor cells. Up-regulated in
gliomas. Its expression levels correlate with malignant potential
of the tumor.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973}.
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=ok";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/bsg/";
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EMBL; X64364; CAA45716.1; -; mRNA.
EMBL; D45131; BAA08109.1; -; mRNA.
EMBL; L10240; AAA68936.1; -; mRNA.
EMBL; M87879; AAA91084.1; -; mRNA.
EMBL; L20471; AAB41120.1; -; mRNA.
EMBL; AF042854; AAD10704.1; -; Genomic_DNA.
EMBL; AF042848; AAD10704.1; JOINED; Genomic_DNA.
EMBL; AF042849; AAD10704.1; JOINED; Genomic_DNA.
EMBL; AF042850; AAD10704.1; JOINED; Genomic_DNA.
EMBL; AF042851; AAD10704.1; JOINED; Genomic_DNA.
EMBL; AF042852; AAD10704.1; JOINED; Genomic_DNA.
EMBL; AF042853; AAD10704.1; JOINED; Genomic_DNA.
EMBL; AB072923; BAB88938.1; -; mRNA.
EMBL; AB085790; BAC76828.1; -; mRNA.
EMBL; AF548371; AAN40694.1; -; mRNA.
EMBL; GU557064; ADD31881.1; -; mRNA.
EMBL; GU557065; ADD31882.1; -; mRNA.
EMBL; AY358113; AAQ88480.1; -; mRNA.
EMBL; AY942196; AAX20110.1; -; Genomic_DNA.
EMBL; AC005559; AAC33279.1; -; Genomic_DNA.
EMBL; CH471242; EAW61181.1; -; Genomic_DNA.
EMBL; CH471242; EAW61185.1; -; Genomic_DNA.
EMBL; BC009040; AAH09040.1; -; mRNA.
CCDS; CCDS12032.1; -. [P35613-4]
CCDS; CCDS12033.1; -. [P35613-1]
CCDS; CCDS12034.1; -. [P35613-2]
CCDS; CCDS58635.1; -. [P35613-3]
PIR; A46506; A46506.
RefSeq; NP_001309172.1; NM_001322243.1. [P35613-2]
RefSeq; NP_001719.2; NM_001728.3. [P35613-1]
RefSeq; NP_940991.1; NM_198589.2. [P35613-2]
RefSeq; NP_940992.1; NM_198590.2. [P35613-3]
RefSeq; NP_940993.1; NM_198591.2. [P35613-4]
RefSeq; XP_016882662.1; XM_017027173.1. [P35613-1]
UniGene; Hs.501293; -.
PDB; 3B5H; X-ray; 2.80 A; A/B/C/D=140-321.
PDB; 3I84; X-ray; 2.00 A; A/B=13-219.
PDB; 3I85; X-ray; 2.50 A; A/B=13-219.
PDB; 3QQN; X-ray; 2.31 A; A/B=23-138.
PDB; 3QR2; X-ray; 2.30 A; A/B=23-138.
PDB; 4U0Q; X-ray; 3.10 A; B/D=1-385.
PDB; 5X0T; X-ray; 2.50 A; E/F=138-217.
PDB; 5XF0; NMR; -; A=215-321.
PDBsum; 3B5H; -.
PDBsum; 3I84; -.
PDBsum; 3I85; -.
PDBsum; 3QQN; -.
PDBsum; 3QR2; -.
PDBsum; 4U0Q; -.
PDBsum; 5X0T; -.
PDBsum; 5XF0; -.
ProteinModelPortal; P35613; -.
SMR; P35613; -.
BioGrid; 107147; 159.
CORUM; P35613; -.
DIP; DIP-50310N; -.
IntAct; P35613; 40.
MINT; P35613; -.
STRING; 9606.ENSP00000333769; -.
ChEMBL; CHEMBL3580492; -.
TCDB; 8.A.23.1.1; the basigin (basigin) family.
iPTMnet; P35613; -.
PhosphoSitePlus; P35613; -.
SwissPalm; P35613; -.
BioMuta; BSG; -.
DMDM; 51704273; -.
EPD; P35613; -.
MaxQB; P35613; -.
PaxDb; P35613; -.
PeptideAtlas; P35613; -.
PRIDE; P35613; -.
ProteomicsDB; 55113; -.
ProteomicsDB; 55114; -. [P35613-2]
ProteomicsDB; 55115; -. [P35613-3]
ProteomicsDB; 55116; -. [P35613-4]
TopDownProteomics; P35613-1; -. [P35613-1]
TopDownProteomics; P35613-2; -. [P35613-2]
TopDownProteomics; P35613-3; -. [P35613-3]
DNASU; 682; -.
Ensembl; ENST00000333511; ENSP00000333769; ENSG00000172270. [P35613-1]
Ensembl; ENST00000346916; ENSP00000344707; ENSG00000172270. [P35613-4]
Ensembl; ENST00000353555; ENSP00000343809; ENSG00000172270. [P35613-2]
Ensembl; ENST00000545507; ENSP00000473664; ENSG00000172270. [P35613-3]
GeneID; 682; -.
KEGG; hsa:682; -.
UCSC; uc002loy.5; human. [P35613-1]
CTD; 682; -.
DisGeNET; 682; -.
EuPathDB; HostDB:ENSG00000172270.18; -.
GeneCards; BSG; -.
HGNC; HGNC:1116; BSG.
HPA; CAB002427; -.
HPA; HPA036048; -.
HPA; HPA074870; -.
MIM; 109480; gene.
MIM; 111380; phenotype.
neXtProt; NX_P35613; -.
OpenTargets; ENSG00000172270; -.
PharmGKB; PA25433; -.
eggNOG; ENOG410IJET; Eukaryota.
eggNOG; ENOG4111V1Q; LUCA.
GeneTree; ENSGT00390000010516; -.
HOGENOM; HOG000263411; -.
HOVERGEN; HBG008120; -.
InParanoid; P35613; -.
KO; K06535; -.
OMA; QWWFEGN; -.
OrthoDB; EOG091G07LY; -.
PhylomeDB; P35613; -.
TreeFam; TF326759; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
Reactome; R-HSA-70268; Pyruvate metabolism.
ChiTaRS; BSG; human.
EvolutionaryTrace; P35613; -.
GeneWiki; Basigin; -.
GenomeRNAi; 682; -.
PMAP-CutDB; P35613; -.
PRO; PR:P35613; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000172270; -.
CleanEx; HS_BSG; -.
ExpressionAtlas; P35613; baseline and differential.
Genevisible; P35613; HS.
GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR009151; Basigin.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
PANTHER; PTHR10075:SF12; PTHR10075:SF12; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Blood group antigen; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Lectin; Mannose-binding; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 21
CHAIN 22 385 Basigin.
/FTId=PRO_0000014518.
TOPO_DOM 138 323 Extracellular. {ECO:0000255}.
TRANSMEM 324 344 Helical. {ECO:0000255}.
TOPO_DOM 345 385 Cytoplasmic. {ECO:0000255}.
DOMAIN 138 219 Ig-like C2-type.
DOMAIN 221 315 Ig-like V-type.
COMPBIAS 356 359 Poly-Asp.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 157 203 {ECO:0000244|PDB:3B5H,
ECO:0000244|PDB:3I84,
ECO:0000269|PubMed:18430721,
ECO:0000269|PubMed:19768682}.
DISULFID 242 301 {ECO:0000244|PDB:3B5H,
ECO:0000269|PubMed:18430721}.
VAR_SEQ 1 209 Missing (in isoform 3).
{ECO:0000303|PubMed:21536654}.
/FTId=VSP_043225.
VAR_SEQ 1 11 MAAALFVLLGF -> MKQSDASPQER (in isoform
4). {ECO:0000303|PubMed:21536654}.
/FTId=VSP_043226.
VAR_SEQ 12 191 Missing (in isoform 4).
{ECO:0000303|PubMed:21536654}.
/FTId=VSP_043227.
VAR_SEQ 24 139 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1634773,
ECO:0000303|PubMed:7812975}.
/FTId=VSP_011501.
VARIANT 208 208 E -> K (in Ok(A-); dbSNP:rs104894669).
{ECO:0000269|PubMed:9130641}.
/FTId=VAR_013574.
VARIANT 269 269 G -> V (in dbSNP:rs1803203).
/FTId=VAR_011720.
MUTAGEN 327 327 P->A: Loss of interaction with PPIL2.
{ECO:0000269|PubMed:15946952}.
CONFLICT 328 328 F -> L (in Ref. 2; BAC76828).
{ECO:0000305}.
STRAND 24 27 {ECO:0000244|PDB:3QR2}.
STRAND 32 35 {ECO:0000244|PDB:3QR2}.
STRAND 40 47 {ECO:0000244|PDB:3QR2}.
STRAND 53 62 {ECO:0000244|PDB:3QR2}.
HELIX 74 77 {ECO:0000244|PDB:3QR2}.
STRAND 79 95 {ECO:0000244|PDB:3QR2}.
HELIX 100 102 {ECO:0000244|PDB:3QR2}.
STRAND 104 111 {ECO:0000244|PDB:3QR2}.
STRAND 116 118 {ECO:0000244|PDB:3QR2}.
STRAND 128 137 {ECO:0000244|PDB:3QR2}.
STRAND 142 149 {ECO:0000244|PDB:3I84}.
STRAND 152 159 {ECO:0000244|PDB:3I84}.
STRAND 166 173 {ECO:0000244|PDB:3I84}.
STRAND 176 181 {ECO:0000244|PDB:3I84}.
STRAND 186 192 {ECO:0000244|PDB:3I84}.
HELIX 194 196 {ECO:0000244|PDB:3I84}.
STRAND 199 207 {ECO:0000244|PDB:3I84}.
STRAND 210 217 {ECO:0000244|PDB:3I84}.
STRAND 224 226 {ECO:0000244|PDB:3B5H}.
STRAND 228 233 {ECO:0000244|PDB:3B5H}.
STRAND 238 243 {ECO:0000244|PDB:3B5H}.
STRAND 252 257 {ECO:0000244|PDB:3B5H}.
STRAND 260 262 {ECO:0000244|PDB:3B5H}.
STRAND 264 266 {ECO:0000244|PDB:4U0Q}.
HELIX 270 272 {ECO:0000244|PDB:3B5H}.
STRAND 274 279 {ECO:0000244|PDB:3B5H}.
STRAND 282 287 {ECO:0000244|PDB:3B5H}.
TURN 292 294 {ECO:0000244|PDB:3B5H}.
STRAND 295 305 {ECO:0000244|PDB:3B5H}.
STRAND 308 319 {ECO:0000244|PDB:3B5H}.
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


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