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Protein

Basigin

Gene

Bsg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 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.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Lectin, Mannose-binding

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-210991. Basigin interactions.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-433692. Proton-coupled monocarboxylate transport.
R-MMU-70268. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Basigin
Alternative name(s):
Basic immunoglobulin superfamily
HT7 antigen
Membrane glycoprotein gp42
CD_antigen: CD147
Gene namesi
Name:Bsg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:88208. Bsg.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein
  • Melanosome By similarity

  • Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). In spermatozoa, localized on the principal piece of caput and in the middle piece during transit in the corpus and cauda epididymides (PubMed:11882021).By similarity1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 325304ExtracellularSequence analysisAdd
BLAST
Transmembranei326 – 34924HelicalSequence analysisAdd
BLAST
Topological domaini350 – 38940CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 389368BasiginPRO_0000014519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi157 ↔ 203PROSITE-ProRule annotation
Glycosylationi160 – 1601N-linked (GlcNAc...)2 Publications
Disulfide bondi242 ↔ 305PROSITE-ProRule annotation
Glycosylationi270 – 2701N-linked (GlcNAc...)2 Publications
Glycosylationi275 – 2751N-linked (GlcNAc...); atypical2 Publications
Glycosylationi306 – 3061N-linked (GlcNAc...)1 Publication
Glycosylationi309 – 3091N-linked (GlcNAc...); atypical1 Publication
Modified residuei358 – 3581PhosphothreonineCombined sources
Modified residuei372 – 3721PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated. During spermatogenesis, probably deglycosylated during epididymal transit.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP18572.
MaxQBiP18572.
PaxDbiP18572.
PeptideAtlasiP18572.
PRIDEiP18572.

PTM databases

iPTMnetiP18572.
PhosphoSiteiP18572.
SwissPalmiP18572.

Expressioni

Tissue specificityi

Isoform 1 is specifically expressed in retina. Isoform 2 is widely expressed, including adult organs, embryos and EC cells. Expressed in spermatozoa.2 Publications

Developmental stagei

In developing eye expressed at embryonic days E12, E15 and E18, and at postnatal days P1, P7, P14, and P21. Expression progressed from a more generalized distribution throughout the undifferentiated neural retina to specific staining of retina-pigmented epithilia, the MCs, photoreceptor cells and the ciliary apparatus. Expression is highest at P21. Isoform 1 and isoform 2 are expressed at equivalent levels at P7, isoform 1 is more abundant at P14, P21 and P28. In uterus during the peri-implantation period strongly expressed in luminal and glandular epithelium on day 1 of pregnancy and gradually decreased to a basal level from day 2-4 of pregnancy. Expression in the sub-luminal stroma was first detected on day 3 of pregnancy and increased on day 4 of pregnancy. On day 5 of pregnancy, the expression of basigin protein and mRNA was only detected in the implanting embryos, and the luminal epithelium and sub-luminal stroma surrounding the embryos. In ovary during sexual maturation expressed in the granulosa cells of preantral follicles at days 20 and 25 after birth. Expressed during corpus luteum formation.3 Publications

Inductioni

By estrogen in the uterine epithelium of ovariectomized animals. By eCG in ovary.2 Publications

Gene expression databases

BgeeiP18572.
CleanExiMM_BSG.
ExpressionAtlasiP18572. baseline and differential.
GenevisibleiP18572. MM.

Interactioni

Subunit structurei

Forms homooligomers in a cis-dependent manner on the plasma membrane. Forms a complex with MMP1 at the tumor cell surface (By similarity). Interacts with AJAP1 (By similarity). Interacts with ATP1B2, MAG and L1CAM. 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.By similarity2 Publications

Protein-protein interaction databases

IntActiP18572. 5 interactions.
MINTiMINT-1605342.
STRINGi10090.ENSMUSP00000070751.

Structurei

3D structure databases

ProteinModelPortaliP18572.
SMRiP18572. Positions 23-138, 140-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 21982Ig-like C2-typeAdd
BLAST
Domaini221 – 31999Ig-like V-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJET. Eukaryota.
ENOG4111V1Q. LUCA.
GeneTreeiENSGT00390000010516.
HOGENOMiHOG000263411.
HOVERGENiHBG008120.
InParanoidiP18572.
KOiK06535.
OMAiQANVFVI.
OrthoDBiEOG7V1FQN.
PhylomeDBiP18572.
TreeFamiTF326759.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR009151. Basigin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PANTHERiPTHR10075:SF12. PTHR10075:SF12. 1 hit.
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P18572-1) [UniParc]FASTAAdd to basket

Also known as: 5A11/Basigin-2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAALLLALA FTLLSGQGAC AAAGFLKAPL SQERWAGGSV VLHCEAVGSP
60 70 80 90 100
IPEIQWWFEG NAPNDSCSQL WDGARLDRVH IHAAYRQHAA SSLSVDGLTA
110 120 130 140 150
EDTGTYECRA SSDPDRNHLT RPPRVKWVRA QASVVVLEPG TIQTSVQEVN
160 170 180 190 200
SKTQLTCSLN SSGVDIVGHR WMRGGKVLQE DTLPDLHTKY IVDADDRSGE
210 220 230 240 250
YSCIFLPEPV GRSEINVEGP PRIKVGKKSE HSSEGELAKL VCKSDASYPP
260 270 280 290 300
ITDWFWFKTS DTGEEEAITN STEANGKYVV VSTPEKSQLT ISNLDVNVDP
310 320 330 340 350
GTYVCNATNA QGTTRETISL RVRSRMAALW PFLGIVAEVL VLVTIIFIYE
360 370 380
KRRKPDQTLD EDDPGAAPLK GSGTHMNDKD KNVRQRNAT
Length:389
Mass (Da):42,445
Last modified:August 31, 2004 - v2
Checksum:iB1E484C3386BEB20
GO
Isoform 2 (identifier: P18572-2) [UniParc]FASTAAdd to basket

Also known as: 5A11/Basigin

The sequence of this isoform differs from the canonical sequence as follows:
     24-139: Missing.

Show »
Length:273
Mass (Da):29,674
Checksum:i0FE654472A619094
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei24 – 139116Missing in isoform 2. 4 PublicationsVSP_011502Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00611 mRNA. Translation: BAA00486.1.
D82019 Genomic DNA. Translation: BAA11508.1.
S63813 mRNA. Translation: AAB27567.2.
Y16256 mRNA. Translation: CAA76140.1.
AY089967 mRNA. Translation: AAM09957.1.
AK002332 mRNA. Translation: BAB22018.1.
BC010270 mRNA. Translation: AAH10270.1.
CCDSiCCDS23985.1. [P18572-1]
CCDS35967.1. [P18572-2]
PIRiJX0107.
S43512.
RefSeqiNP_001070652.1. NM_001077184.1. [P18572-2]
NP_033898.1. NM_009768.2. [P18572-1]
UniGeneiMm.726.

Genome annotation databases

EnsembliENSMUST00000067036; ENSMUSP00000070751; ENSMUSG00000023175. [P18572-1]
ENSMUST00000179781; ENSMUSP00000136487; ENSMUSG00000023175. [P18572-2]
GeneIDi12215.
KEGGimmu:12215.
UCSCiuc007fzl.1. mouse. [P18572-1]
uc007fzm.1. mouse. [P18572-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00611 mRNA. Translation: BAA00486.1.
D82019 Genomic DNA. Translation: BAA11508.1.
S63813 mRNA. Translation: AAB27567.2.
Y16256 mRNA. Translation: CAA76140.1.
AY089967 mRNA. Translation: AAM09957.1.
AK002332 mRNA. Translation: BAB22018.1.
BC010270 mRNA. Translation: AAH10270.1.
CCDSiCCDS23985.1. [P18572-1]
CCDS35967.1. [P18572-2]
PIRiJX0107.
S43512.
RefSeqiNP_001070652.1. NM_001077184.1. [P18572-2]
NP_033898.1. NM_009768.2. [P18572-1]
UniGeneiMm.726.

3D structure databases

ProteinModelPortaliP18572.
SMRiP18572. Positions 23-138, 140-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18572. 5 interactions.
MINTiMINT-1605342.
STRINGi10090.ENSMUSP00000070751.

PTM databases

iPTMnetiP18572.
PhosphoSiteiP18572.
SwissPalmiP18572.

Proteomic databases

EPDiP18572.
MaxQBiP18572.
PaxDbiP18572.
PeptideAtlasiP18572.
PRIDEiP18572.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067036; ENSMUSP00000070751; ENSMUSG00000023175. [P18572-1]
ENSMUST00000179781; ENSMUSP00000136487; ENSMUSG00000023175. [P18572-2]
GeneIDi12215.
KEGGimmu:12215.
UCSCiuc007fzl.1. mouse. [P18572-1]
uc007fzm.1. mouse. [P18572-2]

Organism-specific databases

CTDi682.
MGIiMGI:88208. Bsg.

Phylogenomic databases

eggNOGiENOG410IJET. Eukaryota.
ENOG4111V1Q. LUCA.
GeneTreeiENSGT00390000010516.
HOGENOMiHOG000263411.
HOVERGENiHBG008120.
InParanoidiP18572.
KOiK06535.
OMAiQANVFVI.
OrthoDBiEOG7V1FQN.
PhylomeDBiP18572.
TreeFamiTF326759.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-210991. Basigin interactions.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-433692. Proton-coupled monocarboxylate transport.
R-MMU-70268. Pyruvate metabolism.

Miscellaneous databases

PROiP18572.
SOURCEiSearch...

Gene expression databases

BgeeiP18572.
CleanExiMM_BSG.
ExpressionAtlasiP18572. baseline and differential.
GenevisibleiP18572. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR009151. Basigin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PANTHERiPTHR10075:SF12. PTHR10075:SF12. 1 hit.
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Miyauchi T., Kanekura T., Yamaoka A., Ozawa M., Miyazawa S., Muramatsu T.
    J. Biochem. 107:316-323(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: 129/Sv.
  2. "Cloning of cDNA for a novel mouse membrane glycoprotein (gp42): shared identity to histocompatibility antigens, immunoglobulins and neural-cell adhesion molecules."
    Altruda F., Cervella P., Gaeta M.L., Daniele A., Giancotti F., Tarone G., Stefanuto G., Silengo L.
    Gene 85:445-452(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    Tissue: Fibroblast.
  3. "Expression of the HT7 gene in blood-brain barrier."
    Unger C.M., Seulberger H., Breier G., Albrecht U., Achen M.G., Risau W.
    Adv. Exp. Med. Biol. 331:211-215(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Kidney.
  4. "Structure of the mouse basigin gene, a unique member of the immunoglobulin superfamily."
    Miyauchi T., Jimma F., Igakura T., Yu S., Ozawa M., Muramatsu T.
    J. Biochem. 118:717-724(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    Strain: BALB/cJ.
    Tissue: Liver.
  5. "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."
    Kanekura T., Miyauchi T., Tahior M., Muramatsu T.
    Cell Struct. Funct. 16:23-30(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
  6. Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Retina.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Kidney.
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: Czech II.
    Tissue: Mammary gland.
  9. "The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach."
    Heller M., von der Ohe M., Kleene R., Mohajeri M.H., Schachner M.
    J. Neurochem. 84:557-565(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS (ISOFORM 2), PROTEIN SEQUENCE OF 278-286, FUNCTION, INTERACTION WITH ATP1B2; MAG AND L1CAM, GLYCOSYLATION.
    Tissue: Brain.
  10. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 278-286, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  11. "Loss of MCT1, MCT3, and MCT4 expression in the retinal pigment epithelium and neural retina of the 5A11/basigin-null mouse."
    Philp N.J., Ochrietor J.D., Rudoy C., Muramatsu T., Linser P.J.
    Invest. Ophthalmol. Vis. Sci. 44:1305-1311(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Basigin expression and hormonal regulation in mouse uterus during the peri-implantation period."
    Xiao L.J., Chang H., Ding N.Z., Ni H., Kadomatsu K., Yang Z.M.
    Mol. Reprod. Dev. 63:47-54(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, INDUCTION.
  13. "Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice."
    Saxena D.K., Oh-Oka T., Kadomatsu K., Muramatsu T., Toshimori K.
    Reproduction 123:435-444(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEGLYCOSYLATION.
  14. "Developmental analyses of 5A11/Basigin, 5A11/Basigin-2 and their putative binding partner MCT1 in the mouse eye."
    Clamp M.F., Ochrietor J.D., Moroz T.P., Linser P.J.
    Exp. Eye Res. 78:777-789(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  15. "Basigin expression and regulation in mouse ovary during the sexual maturation and development of corpus luteum."
    Chang H., Ni H., Ma X.-H., Xu L.-B., Kadomatsu K., Muramatsu T., Yang Z.-M.
    Mol. Reprod. Dev. 68:135-141(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, INDUCTION.
  16. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-270 AND ASN-275.
    Tissue: Myoblast.
  18. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-270; ASN-275; ASN-306 AND ASN-309.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  20. "Basigin interacts with both MCT1 and MCT2 in murine spermatozoa."
    Mannowetz N., Wandernoth P., Wennemuth G.
    J. Cell. Physiol. 227:2154-2162(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC16A1 AND SLC16A7, TISSUE SPECIFICITY, FUNCTION.

Entry informationi

Entry nameiBASI_MOUSE
AccessioniPrimary (citable) accession number: P18572
Secondary accession number(s): Q6LDB0, Q7TSC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 31, 2004
Last modified: July 6, 2016
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.