LAM2_CAEEL - dbPTM
LAM2_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAM2_CAEEL
UniProt AC Q18823
Protein Name Laminin-like protein lam-2
Gene Name lam-2
Organism Caenorhabditis elegans.
Sequence Length 1633
Subcellular Localization
Protein Description During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably downstream of the integrin complex formed by pat-2 and pat-3..
Protein Sequence MTSILWLFSLAVLWHMGQPQPAELYPSVDPNHFGADGNPCYDRATRQPQRCVPDFVNAAFNLEVQVTNTCGTKRPTKFCVQSGHTGQRSVCETCDDRHEGFSHPAKYLTDFNVGNNETWWQSDTMQEGQQYPTTTNLTLVLGKSFDITYVRLKFISPRPESFTIYKKTHTDSEWEPWQFYSGSCRATYGLSDRAPILPGNEATAQCTKEFSDISPITGGNIAFSTLEGRPSAHAFEESEVLQKWVTASAIRISLNRMNTFGDEVFKDPQVLRSYYYAISDFAVGGRCKCNGHASECVGSSSVDGENRLVCRCEHNTQGADCNECLPFYNDRPWRSGTSVEANECIACNCSQLSNRCYFDQQLFEETGHGGHCIDCQGNTQGVHCEQCIANHWRRPGENYCVACGCNEIGSLSTQCDNEGKCQCKPGVTGRFCDQCLDGFYDFSTNGCKNCGCETSGSLNNQPRCDSSSGSCSCKLNVEGRQCDKCKPGYFDLSTENQFGCTPCFCFGHSSICNTADGYFAMNVSSVFDQDKQKWAGQNRIGLQDTQWAELDKAVAVSDTDNSPVYFVAPEQFLGDQRSSYNQDLVFTLKVAKHVTNQDVKDIIIVGADRQELSTSITAQGNPFPTTEAQTYRFRVHADPYFGWYPRINELDFIGILSNITAIKIRGTYSYKDIGYLSNVNLGTAGVAPSAANPKQATWIEHCECLPGFVGQFCESCESGFRRETKFGGPFNHCIKCDCHNHSNSCEAESGSCICEHNTAGDTCERCARGYYGDALQGTEEDCQKCPCPNDGPCILHADGDVICTECPNGYTGRRCDECSDGYFGNPKDGTECVECACSGNTDPNSIGNCDKITGECKKCIFNTHGFNCENCKPGYWGDALIEPKGNCQSCGCFAAGTRRPNNDYTLLECNQQDGQCDCLPNVIGIQCDQCAHGFYNITSGLGCQECNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFSANGCQPCDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGITQGCLPCDDCYTLIQSRVNVFREKVKSLDNTLQEIIENPAPVNDTKFDEKVKETSRAASEVWEAVKQKTKEGGGTIKTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNLPTKCFNVINLEQEGQK
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_GlycosylationTDFNVGNNETWWQSD
ECCCCCCCCCEEECC		41.9912754521
136N-linked_GlycosylationQQYPTTTNLTLVLGK
CCCCCCCCEEEEECC		29.01-
348N-linked_GlycosylationANECIACNCSQLSNR
CCCEEEECHHHHCCC		21.3217761667
522N-linked_GlycosylationADGYFAMNVSSVFDQ
CCCEEEEEHHHHCCC		27.39-
658N-linked_GlycosylationDFIGILSNITAIKIR
CEEEHHHCCEEEEEE		31.9817761667
740N-linked_GlycosylationCIKCDCHNHSNSCEA
EEEECCCCCCCCCEE		46.7617761667
936N-linked_GlycosylationQCAHGFYNITSGLGC
CCCCCCCCCCCCCCC		28.88-
1077N-linked_GlycosylationIENPAPVNDTKFDEK
HHCCCCCCCCCHHHH		50.6117761667
1183N-linked_GlycosylationERAQIAYNASQKYGE
HHHHHHHHHHHHHHH		24.8817761667
1226N-linked_GlycosylationLSEQAIANATQANKE
HHHHHHHHHHHHCHH		37.0917761667
1259N-linked_GlycosylationKEKQNQLNESIHRTL
HHHHHHHHHHHHHHH		31.0717761667
1336N-linked_GlycosylationDELFDEVNRSVADAR
HHHHHHHHHHHHHHH		28.58-
1452N-linked_GlycosylationKSADVLLNETHALAD
HHHHHHHHHHHHHHH		48.2117761667
1528N-linked_GlycosylationKNSAIEANATILAEE
HHHCHHHCCEEEECH		25.48-
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 LAM2_CAEEL !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAM2_CAEEL !!
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 LAM2_CAEEL !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LAM2_CAEEL !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAM2_CAEEL

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins.";
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.;
Mol. Cell. Proteomics 6:2100-2109(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348; ASN-658; ASN-740;ASN-1077; ASN-1183; ASN-1226; ASN-1259 AND ASN-1452, AND MASSSPECTROMETRY.
"Identification of the hydrophobic glycoproteins of Caenorhabditiselegans.";
Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H.,Mahuran D.J.;
Glycobiology 15:952-964(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-658; ASN-1077; ASN-1226;ASN-1259 AND ASN-1452, AND MASS SPECTROMETRY.
"Lectin affinity capture, isotope-coded tagging and mass spectrometryto identify N-linked glycoproteins.";
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,Kasai K., Takahashi N., Isobe T.;
Nat. Biotechnol. 21:667-672(2003).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116, AND MASSSPECTROMETRY.

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