UniProt ID | LAMB1_DROME | |
---|---|---|
UniProt AC | P11046 | |
Protein Name | Laminin subunit beta-1 | |
Gene Name | LanB1 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1788 | |
Subcellular Localization | Secreted, extracellular space, extracellular matrix, basement membrane. | |
Protein Description | Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.. | |
Protein Sequence | MLELRLIVVIVLALLSWQWDPVDSQRPPQHGRRDRPKYPPNKFIKTHPCERSSCYPATGNLLIGRENRLTASSTCGLHSPERFCILSHLQDKKCFLCDTREETKHDPYKNHRIGQIIYKTKPGTNIPTWWQSENGKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTDPYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYGISNMVVRGSCSCYGHASQCLPLDPAFSQADNEDGMVHGRCECTHNTKGMNCEECEDFFNDLPWKPAFGKKTNACKKCECNDHAVSCHFDEAVFTASGFVSGGVCDNCLHNTRGQHCEECMPYFYRDPEQDITSERVCQPCDCDPQGSSDDGICDSLNELEEGAVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGCEPCTCNPLGTLNNSGCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGCSLCNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYFIPLLPEVHEAEVVDECISYGANGNCSLVAETPDGSFTGIGFTRVPENSELVFTVGDIPRSMPYDAVIRYQSTSRGDWENAFITLVRPDQVDPEGGCGELAAATSSETRIPFSLPDRSRQVVALNEVCLEAGKVYKFRIYFERKRHDVDSPTATILVDSLTLIPRIDVTPIFQGSVLADIRKKDYEKYNCKSSLYDMNYKSDPKCQNLDNILSVFVHDGASMCNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGCKACDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRVCQCNGHAATCDPIQGTCIDCQDSTTGYSCDSCLDGYYGNPLFGSEIGCRPCRCPETVASGLAHADGCSLDTRNNNMLCHCQEGYSGSRCEICADNFFGNPDNGGTCSKCECSNNVDLYDTGNCDRQTGACLKCLYQTTGDHCELCKDGFFGDALQQNCQQCECDFLGTNNTIAHCDRFTGQCPCLPNVQGVRCDQCAENHWKIASGEGCESCNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQPCECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGQFPHCSPCGECFNNWDLILSALEDATTATILRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQVCGKPGDPCDSLCGGAGCGHCGGFLSCEHGAKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQCYT | |
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 |
---|---|---|---|---|---|
138 | N-linked_Glycosylation | QSENGKENATIQLDL ECCCCCCCEEEEEEE | 45.96 | - | |
201 | N-linked_Glycosylation | GVPTVLENITDVMCT CCCCHHHHHCHHHCC | 38.00 | - | |
232 | N-linked_Glycosylation | RVLPPNINVTDPYAE EECCCCCCCCCHHHH | 36.96 | - | |
267 | Phosphorylation | LGDNLLDSRLENEEK HCCCHHHHHCCCCCC | 38.44 | 27794539 | |
487 | N-linked_Glycosylation | CNPLGTLNNSGCVMR CCCCCCCCCCCCEEE | 40.22 | - | |
591 | N-linked_Glycosylation | ISYGANGNCSLVAET HHCCCCCCEEEEEEC | 16.41 | - | |
1051 | N-linked_Glycosylation | ECDFLGTNNTIAHCD CCCCCCCCCCEEEEC | 41.68 | - | |
1246 | N-linked_Glycosylation | HIRNLLQNTSVSLVD HHHHHHHCCCEEEEE | 34.00 | - | |
1301 | N-linked_Glycosylation | VELESLQNHSRLVQQ CCHHHHHHHHHHHHH | 40.16 | - | |
1330 | N-linked_Glycosylation | SNIEGALNLTRHAYE HCHHHHHHHHHHHHH | 38.54 | - | |
1341 | N-linked_Glycosylation | HAYERVSNLSTLKDE HHHHHHHCHHHHHHH | 34.84 | - | |
1473 | N-linked_Glycosylation | ALTQAKLNASEAYEK HHHHHHCCHHHHHHH | 40.49 | - | |
1493 | N-linked_Glycosylation | EQSERYLNQTNANIK HHHHHHHHHCCCCHH | 37.38 | 17893096 | |
1515 | N-linked_Glycosylation | ALNNFQENKTASPSE HHHCCCCCCCCCHHH | 35.87 | - | |
1581 | N-linked_Glycosylation | NNLQSIANATKEKAD HCHHHHHHHCHHHHH | 46.61 | - | |
1644 | N-linked_Glycosylation | YSAEAPANNTAQQVE CCCCCCCCCHHHHHH | 45.38 | - | |
1703 | N-linked_Glycosylation | QSATSATNQTLTDRA HHHHHHHHHHHHHHH | 32.34 | - | |
1746 | Phosphorylation | KDLNDLQTVYLNKNQ CCCHHCEEEEECCCH | 20.58 | 22668510 | |
1748 | Phosphorylation | LNDLQTVYLNKNQQL CHHCEEEEECCCHHH | 14.14 | 22668510 |
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 LAMB1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LAMB1_DROME !! |
* 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 LAMB1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
WWOX_DROME | Wwox | physical | 14605208 | |
LAMC1_DROME | LanB2 | physical | 22036573 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster."; Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.; Glycobiology 17:1388-1403(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1493, AND MASSSPECTROMETRY. |