LAMA_DROME - dbPTM
LAMA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMA_DROME
UniProt AC Q00174
Protein Name Laminin subunit alpha
Gene Name LanA
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 3712
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane. Cell junction, synapse. Cell projection, axon. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Major component of basement membranes. At neuromucular junctions, localiz
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. Activates presynaptic signaling involving integrin alpha-PS3/beta-nu and Fak to suppress neuromuscular junction (NMJ) growth during larval development and during low crawling activity, but not during higher-crawling conditions. Mediates, together with integrin alpha-PS3/beta-nu, glutamate receptor-modulated NMJ growth..
Protein Sequence MGHGVASIGALLVILAISYCQAELTPPYFNLATGRKIYATATCGQDTDGPELYCKLVGANTEHDHIDYSVIQGQVCDYCDPTVPERNHPPENAIDGTEAWWQSPPLSRGMKFNEVNLTINFEQEFHVAYLFIRMGNSPRPGLWTLEKSTDYGKTWTPWQHFSDTPADCETYFGKDTYKPITRDDDVICTTEYSKIVPLENGEIPVMLLNERPSSTNYFNSTVLQEWTRATNVRIRLLRTKNLLGHLMSVARQDPTVTRRYFYSIKDISIGGRCMCNGHADTCDVKDPKSPVRILACRCQHHTCGIQCNECCPGFEQKKWRQNTNARPFNCEPCNCHGHSNECKYDEEVNRKGLSLDIHGHYDGGGVCQNCQHNTVGINCNKCKPKYYRPKGKHWNETDVCSPCQCDYFFSTGHCEEETGNCECRAAFQPPSCDSCAYGYYGYPNCRECECNLNGTNGYHCEAESGQQCPCKINFAGAYCKQCAEGYYGFPECKACECNKIGSITNDCNVTTGECKCLTNFGGDNCERCKHGYFNYPTCSYCDCDNQGTESEICNKQSGQCICREGFGGPRCDQCLPGFYNYPDCKPCNCSSTGSSAITCDNTGKCNCLNNFAGKQCTLCTAGYYSYPDCLPCHCDSHGSQGVSCNSDGQCLCQPNFDGRQCDSCKEGFYNFPSCEDCNCDPAGVIDKFAGCGSVPVGELCKCKERVTGRICNECKPLYWNLNISNTEGCEICDCWTDGTISALDTCTSKSGQCPCKPHTQGRRCQECRDGTFDLDSASLFGCKDCSCDVGGSWQSVCDKISGQCKCHPRITGLACTQPLTTHFFPTLHQFQYEYEDGSLPSGTQVRYDYDEAAFPGFSSKGYVVFNAIQNDVRNEVNVFKSSLYRIVLRYVNPNAENVTATISVTSDNPLEVDQHVKVLLQPTSEPQFVTVAGPLGVKPSAIVLDPGRYVFTTKANKNVMLDYFVLLPAAYYEAGILTRHISNPCELGNMELCRHYKYASVEVFSPAATPFVIGENSKPTNPVETYTDPEHLQIVSHVGDIPVLSGSQNELHYIVDVPRSGRYIFVIDYISDRNFPDSYYINLKLKDNPDSETSVLLYPCLYSTICRTSVNEDGMEKSFYINKEDLQPVIISADIEDGSRFPIISVTAIPVDQWSIDYINPSPVCVIHDQQCATPKFRSVPDSKKIEFETDHEDRIATNKPPYASLDERVKLVHLDSQNEATIVIESKVDATKPNLFVILVKYYQPSHPKYQVYYTLTAGKNQYDGKFDIQHCPSSSGCRGVIRPAGEGSFEIDDEFKFTITTDRSQSVWLDYLVVVPLKQYNDDLLVEETFDQTKEFIQNCGHDHFHITHNASDFCKKSVFSLTADYNSGALPCNCDYAGSTSFECHPFGGQCQCKPNVIERTCGACRSRYYGFPDCKPCKCPNSAMCEPTTGECMCPPNVIGDLCEKCAPNTYGFHQVIGCEECACNPMGIANGNSQCDLFNGTCECRQNIEGRACDVCSNGYFNFPHCEQCSCHKPGTELEVCDKIDGACFCKKNVVGRDCDQCVDGTYNLQESNPDGCTTCFCFGKTSRCDSAYLRVYNVSLLKHVSITTPEFHEESIKFDMWPVPADEILLNETTLKADFTLREVNDERPAYFGVLDYLLNQNNHISAYGGDLAYTLHFTSGFDGKYIVAPDVILFSEHNALVHTSYEQPSRNEPFTNRVNIVESNFQTISGKPVSRADFMMVLRDLKVIFIRANYWEQTLVTHLSDVYLTLADEDADGTGEYQFLAVERCSCPPGYSGHSCEDCAPGYYRDPSGPYGGYCIPCECNGHSETCDCATGICSKCQHGTEGDHCERCVSGYYGNATNGTPGDCMICACPLPFDSNNFATSCEISESGDQIHCECKPGYTGPRCESCANGFYGEPESIGQVCKPCECSGNINPEDQGSCDTRTGECLRCLNNTFGAACNLCAPGFYGDAIKLKNCQSCDCDDLGTQTCDPFVGVCTCHENVIGDRCDRCKPDHYGFESGVGCRACDCGAASNSTQCDPHTGHCACKSGVTGRQCDRCAVDHWKYEKDGCTPCNCNQGYSRGFGCNPNTGKCQCLPGVIGDRCDACPNRWVLIKDEGCQECNNCHHALLDVTDRMRYQIDSVLEDFNSVTLAFFTSQKLNYYDQLADELEPKVKLLDPNSVDLSPSKKANSELESDAKSYAKQVNQTLANAFDIRERSSTTLGNITVAYDEAVKSADQAKEAIASVEALSKNLEAAASTKIDAALEQAQHILGQINGTSIELTPNEQVLEKARKLYEEVNTLVLPIKAQNKSLNALKNDIGEFSDHLEDLFNWSEASQAKSADVERRNVANQKAFDNSKFDTVSEQKLQAEKNIKDAGNFLINGDLTLNQINQKLDNLRDALNELNSFNKNVDEELPVREDQHKEADALTDQAEQKAAELAIKAQDLAAQYTDMTASAEPAIKAATAYSGIVEAVEAAQKLSQDAISAAGNATDKTDGIEERAHLADTGSTDLLQRARQSLQKVQDDLEPRLNASAGKVQKISAVNNATEHQLKDINKLIDQLPAESQRDMWKNSNANASDALEILKNVLEILEPVSVQTPKELEKAHGINRDLDLTNKDVSQANKQLDDVEGSVSKLNELAEDIEEQQHRVGSQSRQLGQEIENLKAQVEAARQLANSIKVGVNFKPSTILELKTPEKTKLLATRTNLSTYFRTTEPSGFLLYLGNDNKTAQKNNDFVAVEIVNGYPILTIDLGNGPERITSDKYVADGRWYQAVVDRMGPNAKLTIREELPNGDVVEHSKSGYLEGSQNILHVDKNSRLFVGGYPGISDFNAPPDLTTNSFSGDIEDLKIGDESVGLWNFVYGDDNDQGARERDVLLEKKKPVTGLRFKGNGYVQLNATSNLKSRSSIQFSFKADKDTSNGLLFFYGRDKHYMSIEMIDGAIFFNISLGEGGGVQSGSQDRYNDNQWHKVQAERENRNGLLKVDDIVISRTNAPLEADLELPKLRRLYFGGHPRRLNTSISLQPNFDGCIDNVVINQGVVDLTEYVTGGGVEEGCSAKFSTVVSYAPHEYGFLRMNNVSSDNNLHVVLHFKTTQPNGVLFYAANHDQSSTIGLSLQDGLLKLNSMGSQLVIDDRILNDGEDHVVTVQHTQGELRLTVDDVDNKRLGSPQPLILEGGDIFFAGLPDNYRTPRNALASLAYFVGCISDVTVNEEIINFANSAEKKNGNINGCPPHVLAYEPSLVPSYYPSGDNEVESPWSNADTLPPLKPDIESTLPPTTPTTTTTTTTTTTSTTTTSTTTTTTTPSPIVIDEEKEIEAKTPQKILTTRPPAKLNLPSDERCKLPEQPNFDVDFTEAGYRFYGLREQRLQINSLPVKVRRHHDIGISFRTERPNGLLIYAGSKQRDDFIAVYLLDGRVTYEIRVGAQLQAKITTEAELNDGTWHTVEVVRTQRKVSLLIDKLEQPGSVDLNAERSAPVLAVELPIYLGGVNKFLESEVKNLTDFKTEVPYFNGCLKNIKFDAMDLETPPEEFGVVPCSEQVERGLFFNNQKAFVKIFDHFDVGTEMKISFDFRPRDPNGLLFSVHGKNSYAILELVDNTLYFTVKTDLKNIVSTNYKLPNNESFCDGKTRNVQAIKSKFVINIAVDFISSNPGVGNEGSVITRTNRPLFLGGHVAFQRAPGIKTKKSFKGCISKVEVNQRMINITPNMVVGDIWQGYCPLN
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
116N-linked_GlycosylationGMKFNEVNLTINFEQ
CCEECEEEEEEECEE		25.86-
219N-linked_GlycosylationPSSTNYFNSTVLQEW
CCCCCCCCHHHHHHH		26.81-
395N-linked_GlycosylationRPKGKHWNETDVCSP
CCCCCCCCCCCCCCH		41.85-
453N-linked_GlycosylationRECECNLNGTNGYHC
CEEEEECCCCCCCEE		41.05-
508N-linked_GlycosylationGSITNDCNVTTGECK
CCCCCCCCCCCCCCE		36.71-
588N-linked_GlycosylationYPDCKPCNCSSTGSS
CCCCCCCCCCCCCCC		36.91-
722N-linked_GlycosylationKPLYWNLNISNTEGC
CCEEEEEECCCCCCC		32.22-
897N-linked_GlycosylationYVNPNAENVTATISV
HCCCCCCCEEEEEEE		33.75-
1352N-linked_GlycosylationDHFHITHNASDFCKK
CCEEECCCHHHHHCH		32.27-
1484N-linked_GlycosylationNSQCDLFNGTCECRQ
CCCCCCCCCEEEECC		52.76-
1583N-linked_GlycosylationSAYLRVYNVSLLKHV
CEEEEEEEHHHEEEE		17.66-
1617N-linked_GlycosylationPADEILLNETTLKAD
CHHHHEECCCEECCC		40.92-
1847N-linked_GlycosylationCVSGYYGNATNGTPG
CCCCCCCCCCCCCCC		27.72-
1943N-linked_GlycosylationGECLRCLNNTFGAAC
CHHHHHHHCCCCHHH		49.47-
2024N-linked_GlycosylationCDCGAASNSTQCDPH
CCCCCCCCCCCCCCC		44.33-
2196N-linked_GlycosylationKSYAKQVNQTLANAF
HHHHHHHHHHHHHHH		26.9917893096
2215N-linked_GlycosylationRSSTTLGNITVAYDE
CCCCCCCCEEEEHHH		29.85-
2267N-linked_GlycosylationQHILGQINGTSIELT
HHHHHHCCCCEEECC		39.54-
2301N-linked_GlycosylationVLPIKAQNKSLNALK
EEEHHHCCHHHHHHH		40.52-
2323N-linked_GlycosylationDHLEDLFNWSEASQA
HHHHHHHCCHHHHHH		48.97-
2482N-linked_GlycosylationDAISAAGNATDKTDG
HHHHHCCCCCCCCCC		34.63-
2524N-linked_GlycosylationDDLEPRLNASAGKVQ
HHHHHHHCCCCCCEE		32.88-
2538N-linked_GlycosylationQKISAVNNATEHQLK
EEEHHHCCCCHHHHH		41.4617893096
2569N-linked_GlycosylationMWKNSNANASDALEI
HHHHCCCCHHHHHHH		44.20-
2699N-linked_GlycosylationKLLATRTNLSTYFRT
EEEEECCCCCCCEEC		28.80-
2720N-linked_GlycosylationLLYLGNDNKTAQKNN
EEEECCCCCCCCCCC		47.80-
2890N-linked_GlycosylationGNGYVQLNATSNLKS
CCCEEEEECCCCCCC		24.87-
2938N-linked_GlycosylationIDGAIFFNISLGEGG
ECCEEEEEEEECCCC		16.52-
3010N-linked_GlycosylationGGHPRRLNTSISLQP
CCCCCCCCCCEECCC		29.93-
3070N-linked_GlycosylationYGFLRMNNVSSDNNL
CCEEEEECCCCCCCE		26.21-
3491N-linked_GlycosylationFLESEVKNLTDFKTE
HHHHHHCCCCCCCCC		54.04-
3612N-linked_GlycosylationTNYKLPNNESFCDGK
CCCCCCCCCCCCCCC		44.33-
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 LAMA_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMA_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 LAMA_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERM_DROMEtermphysical
14605208
LAMC1_DROMELanB2physical
22036573
ITA3_DROMEscbgenetic
12040052
SLIT_DROMEsligenetic
12040052
LAMB1_DROMELanB1physical
22036573
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMA_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-2196 AND ASN-2538, ANDMASS SPECTROMETRY.

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