UniProt ID | LG3BP_HUMAN | |
---|---|---|
UniProt AC | Q08380 | |
Protein Name | Galectin-3-binding protein | |
Gene Name | LGALS3BP | |
Organism | Homo sapiens (Human). | |
Sequence Length | 585 | |
Subcellular Localization | Secreted . Secreted, extracellular space, extracellular matrix . | |
Protein Description | Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells.. | |
Protein Sequence | MTPPRLFWVWLLVAGTQGVNDGDMRLADGGATNQGRVEIFYRGQWGTVCDNLWDLTDASVVCRALGFENATQALGRAAFGQGSGPIMLDEVQCTGTEASLADCKSLGWLKSNCRHERDAGVVCTNETRSTHTLDLSRELSEALGQIFDSQRGCDLSISVNVQGEDALGFCGHTVILTANLEAQALWKEPGSNVTMSVDAECVPMVRDLLRYFYSRRIDITLSSVKCFHKLASAYGARQLQGYCASLFAILLPQDPSFQMPLDLYAYAVATGDALLEKLCLQFLAWNFEALTQAEAWPSVPTDLLQLLLPRSDLAVPSELALLKAVDTWSWGERASHEEVEGLVEKIRFPMMLPEELFELQFNLSLYWSHEALFQKKTLQALEFHTVPFQLLARYKGLNLTEDTYKPRIYTSPTWSAFVTDSSWSARKSQLVYQSRRGPLVKYSSDYFQAPSDYRYYPYQSFQTPQHPSFLFQDKRVSWSLVYLPTIQSCWNYGFSCSSDELPVLGLTKSGGSDRTIAYENKALMLCEGLFVADVTDFEGWKAAIPSALDTNSSKSTSSFPCPAGHFNGFRTVIRPFYLTNSSGVD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
41 | Phosphorylation | QGRVEIFYRGQWGTV CCEEEEEECCCCCCC | 21.35 | - | |
69 | N-linked_Glycosylation | CRALGFENATQALGR HHHCCCCCHHHHHHH | 46.13 | 15084671 | |
69 | N-linked_Glycosylation | CRALGFENATQALGR HHHCCCCCHHHHHHH | 46.13 | 15084671 | |
110 | Ubiquitination | CKSLGWLKSNCRHER HHHHCHHHHHCCCCC | 32.87 | - | |
125 | N-linked_Glycosylation | DAGVVCTNETRSTHT CCCEEECCCCCCCCC | 43.44 | 17623646 | |
125 | N-linked_Glycosylation | DAGVVCTNETRSTHT CCCEEECCCCCCCCC | 43.44 | 16335952 | |
136 | Phosphorylation | STHTLDLSRELSEAL CCCCHHHHHHHHHHH | 24.31 | 29759185 | |
192 | N-linked_Glycosylation | LWKEPGSNVTMSVDA HHCCCCCCEEEEECC | 38.91 | 17623646 | |
192 | N-linked_Glycosylation | LWKEPGSNVTMSVDA HHCCCCCCEEEEECC | 38.91 | 16335952 | |
220 | Phosphorylation | YSRRIDITLSSVKCF HHHCCCEEHHHHHHH | 19.48 | 20068231 | |
229 | Ubiquitination | SSVKCFHKLASAYGA HHHHHHHHHHHHHCH | 26.04 | - | |
256 | Phosphorylation | ILLPQDPSFQMPLDL HHCCCCCCCCCCHHH | 36.08 | - | |
323 | Ubiquitination | PSELALLKAVDTWSW CCHHHHHHHHHHCCC | 47.41 | - | |
345 | Ubiquitination | EVEGLVEKIRFPMML HHHHHHHHHCCCCCC | 31.53 | - | |
345 | 2-Hydroxyisobutyrylation | EVEGLVEKIRFPMML HHHHHHHHHCCCCCC | 31.53 | - | |
362 | N-linked_Glycosylation | ELFELQFNLSLYWSH HHHHCHHHHHHEECH | 18.76 | UniProtKB CARBOHYD | |
376 | Ubiquitination | HEALFQKKTLQALEF HHHHHCCHHHHHHHH | 43.62 | - | |
395 | Ubiquitination | FQLLARYKGLNLTED HHHHHHHCCCCCCCC | 51.90 | - | |
398 | N-linked_Glycosylation | LARYKGLNLTEDTYK HHHHCCCCCCCCCCC | 54.29 | 17623646 | |
398 | N-linked_Glycosylation | LARYKGLNLTEDTYK HHHHCCCCCCCCCCC | 54.29 | 17623646 | |
405 | Ubiquitination | NLTEDTYKPRIYTSP CCCCCCCCCCEECCC | 29.88 | - | |
411 | Phosphorylation | YKPRIYTSPTWSAFV CCCCEECCCCCEEEE | 11.89 | - | |
413 | O-linked_Glycosylation | PRIYTSPTWSAFVTD CCEECCCCCEEEECC | 31.64 | OGP | |
413 | Phosphorylation | PRIYTSPTWSAFVTD CCEECCCCCEEEECC | 31.64 | - | |
415 | Phosphorylation | IYTSPTWSAFVTDSS EECCCCCEEEECCCC | 17.82 | - | |
427 | Ubiquitination | DSSWSARKSQLVYQS CCCHHHCHHHHHEEE | 42.12 | - | |
428 | Phosphorylation | SSWSARKSQLVYQSR CCHHHCHHHHHEEEC | 24.16 | 20639409 | |
432 | Phosphorylation | ARKSQLVYQSRRGPL HCHHHHHEEECCCCC | 14.90 | - | |
434 | Phosphorylation | KSQLVYQSRRGPLVK HHHHHEEECCCCCEE | 13.27 | 20639409 | |
441 | Acetylation | SRRGPLVKYSSDYFQ ECCCCCEECCCCCCC | 47.28 | 26051181 | |
441 | Ubiquitination | SRRGPLVKYSSDYFQ ECCCCCEECCCCCCC | 47.28 | 21890473 | |
442 | Phosphorylation | RRGPLVKYSSDYFQA CCCCCEECCCCCCCC | 13.11 | 20639409 | |
443 | Phosphorylation | RGPLVKYSSDYFQAP CCCCEECCCCCCCCC | 15.83 | 25884760 | |
443 | O-linked_Glycosylation | RGPLVKYSSDYFQAP CCCCEECCCCCCCCC | 15.83 | OGP | |
444 | Phosphorylation | GPLVKYSSDYFQAPS CCCEECCCCCCCCCC | 32.99 | 26657352 | |
444 | O-linked_Glycosylation | GPLVKYSSDYFQAPS CCCEECCCCCCCCCC | 32.99 | 55817675 | |
446 | Phosphorylation | LVKYSSDYFQAPSDY CEECCCCCCCCCCCC | 10.27 | 20639409 | |
451 | O-linked_Glycosylation | SDYFQAPSDYRYYPY CCCCCCCCCCCCCCC | 50.74 | OGP | |
451 | Phosphorylation | SDYFQAPSDYRYYPY CCCCCCCCCCCCCCC | 50.74 | 20639409 | |
453 | Phosphorylation | YFQAPSDYRYYPYQS CCCCCCCCCCCCCCC | 12.59 | 20639409 | |
458 | Phosphorylation | SDYRYYPYQSFQTPQ CCCCCCCCCCCCCCC | 10.73 | - | |
463 | Phosphorylation | YPYQSFQTPQHPSFL CCCCCCCCCCCCCCC | 23.94 | - | |
474 | Ubiquitination | PSFLFQDKRVSWSLV CCCCCCCCCCEEEEE | 43.87 | 21890473 | |
550 | O-linked_Glycosylation | AIPSALDTNSSKSTS HCCCCCCCCCCCCCC | 37.54 | 23301498 | |
551 | N-linked_Glycosylation | IPSALDTNSSKSTSS CCCCCCCCCCCCCCC | 43.91 | 18638581 | |
551 | N-linked_Glycosylation | IPSALDTNSSKSTSS CCCCCCCCCCCCCCC | 43.91 | 18780401 | |
554 | Ubiquitination | ALDTNSSKSTSSFPC CCCCCCCCCCCCCCC | 58.54 | - | |
580 | N-linked_Glycosylation | IRPFYLTNSSGVD-- EEEEECCCCCCCC-- | 31.42 | 16740002 |
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 LG3BP_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LG3BP_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 LG3BP_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 |
"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-69; ASN-125; ASN-192;ASN-398 AND ASN-551, AND MASS SPECTROMETRY. | |
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-551, AND MASSSPECTROMETRY. | |
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry."; Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.; J. Proteome Res. 5:1493-1503(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-398; ASN-551 ANDASN-580, AND MASS SPECTROMETRY. | |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192;ASN-398; ASN-551 AND ASN-580, AND MASS SPECTROMETRY. | |
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69, AND MASS SPECTROMETRY. |