| UniProt ID | BASI_HUMAN | |
|---|---|---|
| UniProt AC | P35613 | |
| Protein Name | Basigin | |
| Gene Name | BSG | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 385 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Melanosome . 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 t |
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| 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 | MAAALFVLLGFALLGTHGASGAAGFVQAPLSQQRWVGGSVELHCEAVGSPVPEIQWWFEGQGPNDTCSQLWDGARLDRVHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWVRAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSHLAALWPFLGIVAEVLVLVTIIFIYEKRRKPEDVLDDDDAGSAPLKSSGQHQNDKGKNVRQRNSS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 7 (in isoform 4) | Phosphorylation | - | 4.48 | 25159151 | |
| 44 (in isoform 2) | N-linked_Glycosylation | - | 5.85 | - | |
| 57 (in isoform 2) | Ubiquitination | - | 2.50 | 21890473 | |
| 59 (in isoform 3) | N-linked_Glycosylation | - | 36.56 | - | |
| 63 (in isoform 2) | Ubiquitination | - | 27.86 | 21890473 | |
| 70 (in isoform 3) | Phosphorylation | - | 2.30 | - | |
| 71 (in isoform 2) | Ubiquitination | - | 8.38 | 21890473 | |
| 77 | Ubiquitination | LWDGARLDRVHIHAT HHCCCCCCEEEEEEE | 45.03 | 21890473 | |
| 88 (in isoform 4) | N-linked_Glycosylation | - | 15.22 | - | |
| 99 (in isoform 4) | Phosphorylation | - | 9.10 | - | |
| 111 | Phosphorylation | GTYECRASNDPDRNH CCEEECCCCCCCCCC | 23.55 | 29449344 | |
| 111 (in isoform 2) | Ubiquitination | - | 23.55 | 21890473 | |
| 120 | Phosphorylation | DPDRNHLTRAPRVKW CCCCCCCCCCCCCCE | 19.75 | 29449344 | |
| 141 (in isoform 2) | Ubiquitination | - | 24.14 | 21890473 | |
| 141 | O-linked_Glycosylation | VLVLEPGTVFTTVED EEEECCCCEEEEHHH | 24.14 | OGP | |
| 144 | O-linked_Glycosylation | LEPGTVFTTVEDLGS ECCCCEEEEHHHHCC | 26.12 | OGP | |
| 144 | Phosphorylation | LEPGTVFTTVEDLGS ECCCCEEEEHHHHCC | 26.12 | 21601212 | |
| 145 | O-linked_Glycosylation | EPGTVFTTVEDLGSK CCCCEEEEHHHHCCE | 15.50 | 55824375 | |
| 145 | Phosphorylation | EPGTVFTTVEDLGSK CCCCEEEEHHHHCCE | 15.50 | 21601212 | |
| 148 (in isoform 2) | Ubiquitination | - | 52.58 | 21890473 | |
| 152 (in isoform 2) | N-linked_Glycosylation | - | 35.26 | - | |
| 153 (in isoform 3) | Phosphorylation | - | 4.00 | - | |
| 156 | Phosphorylation | LGSKILLTCSLNDSA HCCEEEEEEECCCCC | 9.15 | - | |
| 158 | Phosphorylation | SKILLTCSLNDSATE CEEEEEEECCCCCCE | 25.60 | 20166139 | |
| 158 (in isoform 3) | Phosphorylation | - | 25.60 | - | |
| 159 (in isoform 3) | Phosphorylation | - | 10.06 | - | |
| 160 | N-linked_Glycosylation | ILLTCSLNDSATEVT EEEEEECCCCCCEEC | 25.54 | 12754519 | |
| 160 | N-linked_Glycosylation | ILLTCSLNDSATEVT EEEEEECCCCCCEEC | 25.54 | 12754519 | |
| 163 (in isoform 2) | Phosphorylation | - | 15.62 | - | |
| 173 (in isoform 1) | Ubiquitination | - | 46.81 | 21890473 | |
| 173 | Ubiquitination | VTGHRWLKGGVVLKE ECCCCEEECCEEEEC | 46.81 | 21890473 | |
| 179 (in isoform 1) | Ubiquitination | - | 41.77 | 21890473 | |
| 179 | Ubiquitination | LKGGVVLKEDALPGQ EECCEEEECCCCCCC | 41.77 | 21890473 | |
| 179 | Succinylation | LKGGVVLKEDALPGQ EECCEEEECCCCCCC | 41.77 | 23954790 | |
| 179 | Acetylation | LKGGVVLKEDALPGQ EECCEEEECCCCCCC | 41.77 | 26051181 | |
| 182 (in isoform 4) | Phosphorylation | - | 19.42 | - | |
| 187 (in isoform 1) | Ubiquitination | - | 56.81 | 21890473 | |
| 187 (in isoform 4) | Phosphorylation | - | 56.81 | - | |
| 187 | Ubiquitination | EDALPGQKTEFKVDS CCCCCCCCEEEEECC | 56.81 | 21906983 | |
| 188 (in isoform 4) | Phosphorylation | - | 38.47 | - | |
| 191 | Ubiquitination | PGQKTEFKVDSDDQW CCCCEEEEECCCCCC | 38.61 | - | |
| 203 | Glutathionylation | DQWGEYSCVFLPEPM CCCEEEEEEEECCCC | 2.16 | 22555962 | |
| 212 | O-linked_Glycosylation | FLPEPMGTANIQLHG EECCCCCCCEEEECC | 15.41 | OGP | |
| 224 | Ubiquitination | LHGPPRVKAVKSSEH ECCCCCEEEEECCCC | 49.06 | - | |
| 227 | Ubiquitination | PPRVKAVKSSEHINE CCCEEEEECCCCCCC | 53.80 | 21906983 | |
| 227 (in isoform 1) | Ubiquitination | - | 53.80 | 21890473 | |
| 227 | Acetylation | PPRVKAVKSSEHINE CCCEEEEECCCCCCC | 53.80 | 27452117 | |
| 228 | Phosphorylation | PRVKAVKSSEHINEG CCEEEEECCCCCCCC | 34.07 | 26434776 | |
| 229 | Phosphorylation | RVKAVKSSEHINEGE CEEEEECCCCCCCCC | 27.72 | 26434776 | |
| 234 (in isoform 2) | Ubiquitination | - | 58.78 | 21890473 | |
| 237 | Phosphorylation | EHINEGETAMLVCKS CCCCCCCCEEEEEEC | 28.37 | 26434776 | |
| 239 | Sulfoxidation | INEGETAMLVCKSES CCCCCCEEEEEECCC | 3.63 | 21406390 | |
| 242 | Glutathionylation | GETAMLVCKSESVPP CCCEEEEEECCCCCC | 3.36 | 22555962 | |
| 243 | Ubiquitination | ETAMLVCKSESVPPV CCEEEEEECCCCCCC | 50.18 | - | |
| 244 | Phosphorylation | TAMLVCKSESVPPVT CEEEEEECCCCCCCC | 29.94 | 28258704 | |
| 246 (in isoform 2) | Phosphorylation | - | 47.19 | - | |
| 246 | Phosphorylation | MLVCKSESVPPVTDW EEEEECCCCCCCCCE | 47.19 | 20166139 | |
| 250 (in isoform 2) | Ubiquitination | - | 6.58 | 21890473 | |
| 251 (in isoform 2) | Phosphorylation | - | 31.43 | - | |
| 251 | O-linked_Glycosylation | SESVPPVTDWAWYKI CCCCCCCCCEEEEEE | 31.43 | OGP | |
| 252 (in isoform 2) | Phosphorylation | - | 33.07 | - | |
| 257 (in isoform 1) | Ubiquitination | - | 28.55 | 21890473 | |
| 257 | Ubiquitination | VTDWAWYKITDSEDK CCCEEEEEECCCHHH | 28.55 | 21890473 | |
| 257 | Sumoylation | VTDWAWYKITDSEDK CCCEEEEEECCCHHH | 28.55 | - | |
| 259 (in isoform 2) | Ubiquitination | - | 29.35 | 21890473 | |
| 264 (in isoform 1) | Ubiquitination | - | 39.09 | 21890473 | |
| 264 | Ubiquitination | KITDSEDKALMNGSE EECCCHHHHHHCCCC | 39.09 | 21906983 | |
| 268 | N-linked_Glycosylation | SEDKALMNGSESRFF CHHHHHHCCCCCEEE | 52.25 | 12754519 | |
| 268 | N-linked_Glycosylation | SEDKALMNGSESRFF CHHHHHHCCCCCEEE | 52.25 | 12754519 | |
| 277 | Phosphorylation | SESRFFVSSSQGRSE CCCEEEEECCCCCCE | 21.08 | 29214152 | |
| 278 | Phosphorylation | ESRFFVSSSQGRSEL CCEEEEECCCCCCEE | 22.75 | 20068231 | |
| 279 | Phosphorylation | SRFFVSSSQGRSELH CEEEEECCCCCCEEE | 29.19 | 20068231 | |
| 283 | Phosphorylation | VSSSQGRSELHIENL EECCCCCCEEEEEEC | 51.87 | 22210691 | |
| 283 | O-linked_Glycosylation | VSSSQGRSELHIENL EECCCCCCEEEEEEC | 51.87 | OGP | |
| 292 | Sulfoxidation | LHIENLNMEADPGQY EEEEECCCCCCCCCE | 5.18 | 30846556 | |
| 299 | Phosphorylation | MEADPGQYRCNGTSS CCCCCCCEEECCCCC | 24.05 | - | |
| 302 | N-linked_Glycosylation | DPGQYRCNGTSSKGS CCCCEEECCCCCCCC | 48.02 | UniProtKB CARBOHYD | |
| 304 | Phosphorylation | GQYRCNGTSSKGSDQ CCEEECCCCCCCCCE | 18.81 | 22210691 | |
| 307 | Ubiquitination | RCNGTSSKGSDQAII EECCCCCCCCCEEEE | 63.30 | - | |
| 309 | Phosphorylation | NGTSSKGSDQAIITL CCCCCCCCCEEEEEE | 30.22 | 21712546 | |
| 315 | Phosphorylation | GSDQAIITLRVRSHL CCCEEEEEEEHHHHH | 11.46 | - | |
| 350 | Ubiquitination | FIYEKRRKPEDVLDD HHHHHCCCHHHCCCC | 57.71 | 21906983 | |
| 350 (in isoform 1) | Ubiquitination | - | 57.71 | 21890473 | |
| 362 | Phosphorylation | LDDDDAGSAPLKSSG CCCCCCCCCCCCCCC | 28.56 | 29255136 | |
| 366 (in isoform 1) | Ubiquitination | - | 41.33 | 21890473 | |
| 366 | Ubiquitination | DAGSAPLKSSGQHQN CCCCCCCCCCCCCCC | 41.33 | 22053931 | |
| 367 | Phosphorylation | AGSAPLKSSGQHQND CCCCCCCCCCCCCCC | 47.59 | 21955146 | |
| 368 | Phosphorylation | GSAPLKSSGQHQNDK CCCCCCCCCCCCCCC | 40.67 | 21955146 | |
| 375 | Ubiquitination | SGQHQNDKGKNVRQR CCCCCCCCCCCHHHH | 78.36 | 2190698 | |
| 375 (in isoform 1) | Ubiquitination | - | 78.36 | 21890473 | |
| 384 | Phosphorylation | KNVRQRNSS------ CCHHHHCCC------ | 39.35 | 29514088 | |
| 385 | Phosphorylation | NVRQRNSS------- CHHHHCCC------- | 48.03 | 29514088 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BASI_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "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 AND ASN-268, AND MASSSPECTROMETRY. | |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268, AND MASSSPECTROMETRY. | |
| "Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-160 AND ASN-268. | |
| Phosphorylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY. | |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY. | |
