LAMB2_HUMAN - dbPTM
LAMB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMB2_HUMAN
UniProt AC P55268
Protein Name Laminin subunit beta-2
Gene Name LAMB2
Organism Homo sapiens (Human).
Sequence Length 1798
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane. S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.
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 MELTSRERGRGQPLPWELRLGLLLSVLAATLAQAPAPDVPGCSRGSCYPATGDLLVGRADRLTASSTCGLNGPQPYCIVSHLQDEKKCFLCDSRRPFSARDNPHSHRIQNVVTSFAPQRRAAWWQSENGIPAVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFPGVPLAPPRHWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPDPYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVVRGNCFCYGHASECAPAPGAPAHAEGMVHGACICKHNTRGLNCEQCQDFYRDLPWRPAEDGHSHACRKCECHGHTHSCHFDMAVYLASGNVSGGVCDGCQHNTAGRHCELCRPFFYRDPTKDLRDPAVCRSCDCDPMGSQDGGRCDSHDDPALGLVSGQCRCKEHVVGTRCQQCRDGFFGLSISDRLGCRRCQCNARGTVPGSTPCDPNSGSCYCKRLVTGRGCDRCLPGHWGLSHDLLGCRPCDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFRPFLDHLIWEAEDTRGQVLDVVERLVTPGETPSWTGSGFVRLQEGQTLEFLVASVPKAMDYDLLLRLEPQVPEQWAELELIVQRPGPVPAHSLCGHLVPKDDRIQGTLQPHARYLIFPNPVCLEPGISYKLHLKLVRTGGSAQPETPYSGPGLLIDSLVLLPRVLVLEMFSGGDAAALERQATFERYQCHEEGLVPSKTSPSEACAPLLISLSTLIYNGALPCQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGFGPTGCQACQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWGFPSCRPCVCNGHADECNTHTGACLGCRDHTGGEHCERCIAGFHGDPRLPYGGQCRPCPCPEGPGSQRHFATSCHQDEYSQQIVCHCRAGYTGLRCEACAPGHFGDPSRPGGRCQLCECSGNIDPMDPDACDPHTGQCLRCLHHTEGPHCAHCKPGFHGQAARQSCHRCTCNLLGTNPQQCPSPDQCHCDPSSGQCPCLPNVQGPSCDRCAPNFWNLTSGHGCQPCACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDPGLQCHACDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGIFPACHPCHACFGDWDRVVQDLAARTQRLEQRAQELQQTGVLGAFESSFWHMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIGEATEHLTQLEADLTDVQDENFNANHALSGLERDRLALNLTLRQLDQHLDLLKHSNFLGAYDSIRHAHSQSAEAERRANTSALAVPSPVSNSASARHRTEALMDAQKEDFNSKHMANQRALGKLSAHTHTLSLTDINELVCGAPGDAPCATSPCGGAGCRDEDGQPRCGGLSCNGAAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTCQ
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
86UbiquitinationVSHLQDEKKCFLCDS
EEECCCCCEEEEECC		64.2329967540
232PhosphorylationAIPIPDPYSSRIQNL
CCCCCCCCHHHHHHH		27.02-
241UbiquitinationSRIQNLLKITNLRVN
HHHHHHHHHHCCCCC		51.1321906983
243PhosphorylationIQNLLKITNLRVNLT
HHHHHHHHCCCCCEE		26.9830622161
248N-linked_GlycosylationKITNLRVNLTRLHTL
HHHCCCCCEEEEECC		29.30UniProtKB CARBOHYD
368N-linked_GlycosylationAVYLASGNVSGGVCD
EEEHHCCCCCCCCCC		23.45UniProtKB CARBOHYD
399UbiquitinationFFYRDPTKDLRDPAV
CCCCCCCCCCCCCHH		61.2229967540
464MethylationFGLSISDRLGCRRCQ
CCCCHHHHHCCCCCC		26.62115385939
468MethylationISDRLGCRRCQCNAR
HHHHHCCCCCCCCCC		40.38115385947
477PhosphorylationCQCNARGTVPGSTPC
CCCCCCCCCCCCCCC		20.27-
498PhosphorylationCYCKRLVTGRGCDRC
EECCEECCCCCCCCC		26.2524719451
614PhosphorylationTLEFLVASVPKAMDY
EEEEEEECCCCCCCH		31.32-
690UbiquitinationLEPGISYKLHLKLVR
ECCCEEEEEEEEEEE		23.7329967540
1085N-linked_GlycosylationRCAPNFWNLTSGHGC
CCCCCCCCCCCCCCC		29.33UniProtKB CARBOHYD
1181O-linked_GlycosylationDQCARGFSGIFPACH
CCCCCCCCCCCCCCC		33.5328657654
1249N-linked_GlycosylationQGIVGARNTSAASTA
CHHHCCCCCCHHHHH		37.54UniProtKB CARBOHYD
1250O-linked_GlycosylationGIVGARNTSAASTAQ
HHHCCCCCCHHHHHH		17.7528657654
1308N-linked_GlycosylationERDRLALNLTLRQLD
HHHHHHHHCHHHHHH		25.9319159218
1310PhosphorylationDRLALNLTLRQLDQH
HHHHHHCHHHHHHHH		20.8724719451
1322UbiquitinationDQHLDLLKHSNFLGA
HHHHHHHHCCCHHHH		52.8923503661
1348N-linked_GlycosylationAEAERRANTSALAVP
HHHHHHHCCCCEECC		32.5219159218
1349PhosphorylationEAERRANTSALAVPS
HHHHHHCCCCEECCC		17.8723312004
1350PhosphorylationAERRANTSALAVPSP
HHHHHCCCCEECCCC		22.5423312004
1356PhosphorylationTSALAVPSPVSNSAS
CCCEECCCCCCCCHH		31.1923312004
1356O-linked_GlycosylationTSALAVPSPVSNSAS
CCCEECCCCCCCCHH		31.19OGP
1359PhosphorylationLAVPSPVSNSASARH
EECCCCCCCCHHHHH		28.5723312004
1361PhosphorylationVPSPVSNSASARHRT
CCCCCCCCHHHHHHH		18.9823312004
1363PhosphorylationSPVSNSASARHRTEA
CCCCCCHHHHHHHHH		26.1723312004
1368PhosphorylationSASARHRTEALMDAQ
CHHHHHHHHHHHHHH		21.3423312004
1472PhosphorylationRALAEGGSILSRVAE
HHHHHCCCHHHHHHH		31.0821406692
1475PhosphorylationAEGGSILSRVAETRR
HHCCCHHHHHHHHHH		24.0421406692
1497UbiquitinationRAQAALDKANASRGQ
HHHHHHHHHHHCHHH		44.3729967540
1499N-linked_GlycosylationQAALDKANASRGQVE
HHHHHHHHHCHHHHH		44.1619159218
1532PhosphorylationQEGADPDSIEMVATR
HCCCCHHHHHHHHHH		26.3215367484
1548PhosphorylationLELSIPASAEQIQHL
HHHCCCCCHHHHHHH		27.3026657352
1603UbiquitinationWAEDEKQKAETVQAA
HHHHHHHHHHHHHHH		60.2929967540
1654PhosphorylationAGAERALSSAGERAR
HHHHHHHHHHHHHHH		19.7021406692
1655PhosphorylationGAERALSSAGERARQ
HHHHHHHHHHHHHHH		40.9421406692
1671UbiquitinationDALLEALKLKRAGNS
HHHHHHHHHHHHCCC		60.0423000965
1673UbiquitinationLLEALKLKRAGNSLA
HHHHHHHHHHCCCCC		38.3223000965
1674MethylationLEALKLKRAGNSLAA
HHHHHHHHHCCCCCH		59.15115481549
1714UbiquitinationGDQYQTVKALAERKA
HHHHHHHHHHHHHHH		40.8621906983
1720UbiquitinationVKALAERKAQGVLAA
HHHHHHHHHHHHHHH		36.2423503661
1720SumoylationVKALAERKAQGVLAA
HHHHHHHHHHHHHHH		36.24-
1720SumoylationVKALAERKAQGVLAA
HHHHHHHHHHHHHHH		36.24-
1748UbiquitinationLLQAAQDKLQRLQEL
HHHHHHHHHHHHHHH		34.1423503661
1759PhosphorylationLQELEGTYEENERAL
HHHHHCCHHHHHHHH		31.91-
1769UbiquitinationNERALESKAAQLDGL
HHHHHHHHHHHHHHH		38.0621906983
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
1532SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMB2_HUMAN !!
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 LAMB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBL1_HUMANRBL1physical
21988832
ORC5_HUMANORC5physical
21988832
P85B_HUMANPIK3R2physical
21988832
STAT3_HUMANSTAT3physical
21988832
SAP_HUMANPSAPphysical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609049Pierson syndrome (PIERSS)
614199Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMB2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-1308; ASN-1348 ANDASN-1499, AND MASS SPECTROMETRY.

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