LAMB1_DROME - dbPTM
LAMB1_DROME - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
138N-linked_GlycosylationQSENGKENATIQLDL
ECCCCCCCEEEEEEE
45.96-
201N-linked_GlycosylationGVPTVLENITDVMCT
CCCCHHHHHCHHHCC
38.00-
232N-linked_GlycosylationRVLPPNINVTDPYAE
EECCCCCCCCCHHHH
36.96-
267PhosphorylationLGDNLLDSRLENEEK
HCCCHHHHHCCCCCC
38.4427794539
487N-linked_GlycosylationCNPLGTLNNSGCVMR
CCCCCCCCCCCCEEE
40.22-
591N-linked_GlycosylationISYGANGNCSLVAET
HHCCCCCCEEEEEEC
16.41-
1051N-linked_GlycosylationECDFLGTNNTIAHCD
CCCCCCCCCCEEEEC
41.68-
1246N-linked_GlycosylationHIRNLLQNTSVSLVD
HHHHHHHCCCEEEEE
34.00-
1301N-linked_GlycosylationVELESLQNHSRLVQQ
CCHHHHHHHHHHHHH
40.16-
1330N-linked_GlycosylationSNIEGALNLTRHAYE
HCHHHHHHHHHHHHH
38.54-
1341N-linked_GlycosylationHAYERVSNLSTLKDE
HHHHHHHCHHHHHHH
34.84-
1473N-linked_GlycosylationALTQAKLNASEAYEK
HHHHHHCCHHHHHHH
40.49-
1493N-linked_GlycosylationEQSERYLNQTNANIK
HHHHHHHHHCCCCHH
37.3817893096
1515N-linked_GlycosylationALNNFQENKTASPSE
HHHCCCCCCCCCHHH
35.87-
1581N-linked_GlycosylationNNLQSIANATKEKAD
HCHHHHHHHCHHHHH
46.61-
1644N-linked_GlycosylationYSAEAPANNTAQQVE
CCCCCCCCCHHHHHH
45.38-
1703N-linked_GlycosylationQSATSATNQTLTDRA
HHHHHHHHHHHHHHH
32.34-
1746PhosphorylationKDLNDLQTVYLNKNQ
CCCHHCEEEEECCCH
20.5822668510
1748PhosphorylationLNDLQTVYLNKNQQL
CHHCEEEEECCCHHH
14.1422668510

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 LAMB1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMB1_DROME !!

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 LAMB1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WWOX_DROMEWwoxphysical
14605208
LAMC1_DROMELanB2physical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMB1_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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