BASI_MOUSE - dbPTM
BASI_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BASI_MOUSE
UniProt AC P18572
Protein Name Basigin
Gene Name Bsg
Organism Mus musculus (Mouse).
Sequence Length 389
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Melanosome . 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 duri
Protein Description 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..
Protein Sequence MAAALLLALAFTLLSGQGACAAAGFLKAPLSQERWAGGSVVLHCEAVGSPIPEIQWWFEGNAPNDSCSQLWDGARLDRVHIHAAYRQHAASSLSVDGLTAEDTGTYECRASSDPDRNHLTRPPRVKWVRAQASVVVLEPGTIQTSVQEVNSKTQLTCSLNSSGVDIVGHRWMRGGKVLQEDTLPDLHTKYIVDADDRSGEYSCIFLPEPVGRSEINVEGPPRIKVGKKSEHSSEGELAKLVCKSDASYPPITDWFWFKTSDTGEEEAITNSTEANGKYVVVSTPEKSQLTISNLDVNVDPGTYVCNATNAQGTTRETISLRVRSRMAALWPFLGIVAEVLVLVTIIFIYEKRRKPDQTLDEDDPGAAPLKGSGTHMNDKDKNVRQRNAT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
160N-linked_GlycosylationTQLTCSLNSSGVDIV
CEEEEEECCCCCEEC
20.1719656770
190PhosphorylationLPDLHTKYIVDADDR
CCCCCCEEEEECCCC
13.8223984901
198PhosphorylationIVDADDRSGEYSCIF
EEECCCCCCCEEEEE
42.8626239621
201PhosphorylationADDRSGEYSCIFLPE
CCCCCCCEEEEEECC
16.6223984901
202PhosphorylationDDRSGEYSCIFLPEP
CCCCCCEEEEEECCC
9.0923984901
203S-palmitoylationDRSGEYSCIFLPEPV
CCCCCEEEEEECCCC
2.2028526873
203S-nitrosylationDRSGEYSCIFLPEPV
CCCCCEEEEEECCCC
2.2022588120
203GlutathionylationDRSGEYSCIFLPEPV
CCCCCEEEEEECCCC
2.2024333276
238UbiquitinationHSSEGELAKLVCKSD
CCCHHHHHHHHHCCC
9.9927667366
269PhosphorylationTGEEEAITNSTEANG
CCCEEEEECCCEECC
30.1123140645
270N-linked_GlycosylationGEEEAITNSTEANGK
CCEEEEECCCEECCE
40.6019656770
271PhosphorylationEEEAITNSTEANGKY
CEEEEECCCEECCEE
20.9723140645
272PhosphorylationEEAITNSTEANGKYV
EEEEECCCEECCEEE
40.9823140645
275N-linked_GlycosylationITNSTEANGKYVVVS
EECCCEECCEEEEEE
41.0619656770
278PhosphorylationSTEANGKYVVVSTPE
CCEECCEEEEEECCC
10.4023140645
282PhosphorylationNGKYVVVSTPEKSQL
CCEEEEEECCCCCCE
27.0023140645
283PhosphorylationGKYVVVSTPEKSQLT
CEEEEEECCCCCCEE
24.6923140645
306N-linked_GlycosylationDPGTYVCNATNAQGT
CCCEEEEECCCCCCC
39.4919349973
309N-linked_GlycosylationTYVCNATNAQGTTRE
EEEEECCCCCCCCCC
28.0519349973
354UbiquitinationFIYEKRRKPDQTLDE
HHHHHHCCCCCCCCC
57.9127667366
358PhosphorylationKRRKPDQTLDEDDPG
HHCCCCCCCCCCCCC
43.4825521595
372PhosphorylationGAAPLKGSGTHMNDK
CCCCCCCCCCCCCHH
38.6427742792
374PhosphorylationAPLKGSGTHMNDKDK
CCCCCCCCCCCHHCC
21.4625159016

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BASI_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BASI_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BASI_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BASI_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BASI_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-270; ASN-275;ASN-306 AND ASN-309, AND MASS SPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-270 AND ASN-275,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358, AND MASSSPECTROMETRY.

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