AGRIN_HUMAN - dbPTM
AGRIN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGRIN_HUMAN
UniProt AC O00468
Protein Name Agrin
Gene Name AGRN
Organism Homo sapiens (Human).
Sequence Length 2067
Subcellular Localization Isoform 1: Secreted, extracellular space, extracellular matrix . Synaptic basal lamina at the neuromuscular junction.
Isoform 2: Cell junction, synapse . Cell membrane
Single-pass type II membrane protein .
Protein Description Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.; Isoform 2: transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.; Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation.; Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity).; Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia..
Protein Sequence MAGRSHPGPLRPLLPLLVVAACVLPGAGGTCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPCQGALPDPSRSCRVNPRTRRPEMLLRPESCPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQCQGRDQCPEPCRFNAVCLSRRGRPRCSCDRVTCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPCDQAPSPCLGVQCAFGATCAVKNGQAACECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPCDRCGQCRFGALCEAETGRCVCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPCETCGDAVCAFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPCEQAECGSGGSGSGEDGDCEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGACRGPTFAPLPPVAPLHCAQTPYGCCQDNITAARGVGLAGCPSACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGRSGCTPCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDGRALGPAGCEADASAPATCAEMRCEFGARCVEESGSAHCVCPMLTCPEANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPCQEAVAPSTHPTSASVTVTTPGLLLSQALPAPPGALPLAPSSTAHSQTTPPPSSRPRTTASVPRTTVWPVLTVPPTAPSPAPSLVASAFGESGSTDGSSDEELSGDQEASGGGSGGLEPLEGSSVATPGPPVERASCYNSALGCCSDGKTPSLDAEGSNCPATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFDPTTAFRAPDVARALLRQIQVSRRRSLGVRRPLQEHVRFMDFDWFPAFITGATSGAIAAGATARATTASRLPSSAVTPRAPHPSHTSQPVAKTTAAPTTRRPPTTAPSRVPGRRPPAPQQPPKPCDSQPCFHGGTCQDWALGGGFTCSCPAGRGGAVCEKVLGAPVPAFEGRSFLAFPTLRAYHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQAAVALERTFVGAGLRGCIRLLDVNNQRLELGIGPGAATRGSGVGECGDHPCLPNPCHGGAPCQNLEAGRFHCQCPPGRVGPTCADEKSPCQPNPCHGAAPCRVLPEGGAQCECPLGREGTFCQTASGQDGSGPFLADFNGFSHLELRGLHTFARDLGEKMALEVVFLARGPSGLLLYNGQKTDGKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVLGESPKSRKVPHTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLLTPEHVLRQVDVTSFAGHPCTRASGHPCLNGASCVPREAAYVCLCPGGFSGPHCEKGLVEKSAGDVDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPCPTP
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
123PhosphorylationFVNPAPPYLWPAHKN
EECCCCCCCCHHHCC		21.9768741161
135N-linked_GlycosylationHKNELMLNSSLMRIT
HCCHHHHCHHHHHHC		18.6519159218
159O-linked_GlycosylationCVEDKPGTHFTPVPP
EECCCCCCCCCCCCC		23.4955830795
162O-linked_GlycosylationDKPGTHFTPVPPTPP
CCCCCCCCCCCCCCC		18.7755830799
167O-linked_GlycosylationHFTPVPPTPPDACRG
CCCCCCCCCCCCCCC		41.1955830805
200PhosphorylationASCVCKKSPCPSVVA
CEEEECCCCCCCEEE		19.7550564023
204PhosphorylationCKKSPCPSVVAPVCG
ECCCCCCCEEECCCC		35.6250564035
204O-linked_GlycosylationCKKSPCPSVVAPVCG
ECCCCCCCEEECCCC		35.62OGP
217PhosphorylationCGSDASTYSNECELQ
CCCCHHHCCCHHHHH		13.6550564047
218PhosphorylationGSDASTYSNECELQR
CCCHHHCCCHHHHHH		26.6650564053
250N-linked_GlycosylationGSRDPCSNVTCSFGS
CCCCCCCCCEECCCC		39.57UniProtKB CARBOHYD
257PhosphorylationNVTCSFGSTCARSAD
CCEECCCCCCCCCCC		20.5050564029
258PhosphorylationVTCSFGSTCARSADG
CEECCCCCCCCCCCC		15.5750564041
330PhosphorylationALPDPSRSCRVNPRT
CCCCCCCCCCCCCCC		15.6028188228
405S-nitrosocysteinePCRFNAVCLSRRGRP
CCCCCEEEECCCCCC		2.37-
405S-nitrosylationPCRFNAVCLSRRGRP
CCCCCEEEECCCCCC		2.3719483679
455PhosphorylationRQQRAIPSKHQGPCD
HHHHCCCCCCCCCCC		36.3424719451
496O-linked_GlycosylationECLQACSSLYDPVCG
HHHHHHHHCCCCCCC		30.72OGP
674PhosphorylationAECGSGGSGSGEDGD
CCCCCCCCCCCCCCC		33.0528348404
676PhosphorylationCGSGGSGSGEDGDCE
CCCCCCCCCCCCCHH		40.4824505115
754O-linked_GlycosylationQGACRGPTFAPLPPV
CCCCCCCCCCCCCCC		34.9455830683
777N-linked_GlycosylationPYGCCQDNITAARGV
CCCCCCCCCCCCCCC		13.97UniProtKB CARBOHYD
838PhosphorylationWNFRGIVTDGRSGCT
CCEEEEEECCCCCCC		30.7121888424
842PhosphorylationGIVTDGRSGCTPCSC
EEEECCCCCCCCCCC		43.6921888424
845PhosphorylationTDGRSGCTPCSCDPQ
ECCCCCCCCCCCCCC		30.7521888424
896PhosphorylationAGCEADASAPATCAE
CCCCCCCCCCCCHHH		35.0224275569
896O-linked_GlycosylationAGCEADASAPATCAE
CCCCCCCCCCCCHHH		35.02OGP
932N-linked_GlycosylationMLTCPEANATKVCGS
CEECCCCCCCEEECC		46.62UniProtKB CARBOHYD
985O-linked_GlycosylationHPTSASVTVTTPGLL
CCCCCEEEEECCCHH		15.05OGP
987O-linked_GlycosylationTSASVTVTTPGLLLS
CCCEEEEECCCHHHH		20.22OGP
994O-linked_GlycosylationTTPGLLLSQALPAPP
ECCCHHHHCCCCCCC		17.24OGP
1029PhosphorylationSRPRTTASVPRTTVW
CCCCCCCCCCCCCEE		30.4824719451
1095O-linked_GlycosylationLEGSSVATPGPPVER
CCCCCCCCCCCCCCC		26.99OGP
1159PhosphorylationPEMADPKSELFGETA
HHHCCCHHHHHHHHH		44.9446160591
1165PhosphorylationKSELFGETARSIEST
HHHHHHHHHHHHHHH		27.9646160597
1258O-linked_GlycosylationDWFPAFITGATSGAI
CCHHHHHCCCCCHHH		17.82OGP
1261O-linked_GlycosylationPAFITGATSGAIAAG
HHHHCCCCCHHHHHC		29.10OGP
1274PhosphorylationAGATARATTASRLPS
HCCCHHCCCHHCCCC		19.83-
1274O-linked_GlycosylationAGATARATTASRLPS
HCCCHHCCCHHCCCC		19.8355830621
1275O-linked_GlycosylationGATARATTASRLPSS
CCCHHCCCHHCCCCC		22.9646160603
1275PhosphorylationGATARATTASRLPSS
CCCHHCCCHHCCCCC		22.9646160603
1277O-linked_GlycosylationTARATTASRLPSSAV
CHHCCCHHCCCCCCC		32.0555830633
1277PhosphorylationTARATTASRLPSSAV
CHHCCCHHCCCCCCC		32.05-
1281PhosphorylationTTASRLPSSAVTPRA
CCHHCCCCCCCCCCC		35.2126852163
1281O-linked_GlycosylationTTASRLPSSAVTPRA
CCHHCCCCCCCCCCC		35.2155825251
1282PhosphorylationTASRLPSSAVTPRAP
CHHCCCCCCCCCCCC		25.4826852163
1282O-linked_GlycosylationTASRLPSSAVTPRAP
CHHCCCCCCCCCCCC		25.4855825255
1285O-linked_GlycosylationRLPSSAVTPRAPHPS
CCCCCCCCCCCCCCC		13.5355825261
1285PhosphorylationRLPSSAVTPRAPHPS
CCCCCCCCCCCCCCC		13.5324719451
1292O-linked_GlycosylationTPRAPHPSHTSQPVA
CCCCCCCCCCCCCCC		36.0455824689
1294O-linked_GlycosylationRAPHPSHTSQPVAKT
CCCCCCCCCCCCCCC		33.1355824695
1295O-linked_GlycosylationAPHPSHTSQPVAKTT
CCCCCCCCCCCCCCC		27.3655824701
1301O-linked_GlycosylationTSQPVAKTTAAPTTR
CCCCCCCCCCCCCCC		16.3655824707
1302O-linked_GlycosylationSQPVAKTTAAPTTRR
CCCCCCCCCCCCCCC		21.8155824713
1306O-linked_GlycosylationAKTTAAPTTRRPPTT
CCCCCCCCCCCCCCC		28.3655824719
1307O-linked_GlycosylationKTTAAPTTRRPPTTA
CCCCCCCCCCCCCCC		24.5055824725
1312O-linked_GlycosylationPTTRRPPTTAPSRVP
CCCCCCCCCCCCCCC		37.9755824017
1313O-linked_GlycosylationTTRRPPTTAPSRVPG
CCCCCCCCCCCCCCC		42.2055824023
1316O-linked_GlycosylationRPPTTAPSRVPGRRP
CCCCCCCCCCCCCCC		43.3755824029
1381PhosphorylationVPAFEGRSFLAFPTL
CCCCCCCCEEHHHHH		35.1528857561
1418UbiquitinationYNGNARGKDFLALAL
ECCCCCCCCEEEEEE		39.4923000965
1510PhosphorylationAAVALERTFVGAGLR
HHHHHHHHHHCCHHH		17.1969101621
1540PhosphorylationGIGPGAATRGSGVGE
ECCCCCCCCCCCCCC		34.7221406692
1540O-linked_GlycosylationGIGPGAATRGSGVGE
ECCCCCCCCCCCCCC		34.7237817119
1584O-linked_GlycosylationPPGRVGPTCADEKSP
CCCCCCCCCCCCCCC		17.8855833095
1687AcetylationNGQKTDGKGDFVSLA
CCEECCCCCCCEEEE		59.1030586801
1720O-linked_GlycosylationIRSREPVTLGAWTRV
EECCCCEEECCEEEE		30.1455823799
1720PhosphorylationIRSREPVTLGAWTRV
EECCCCEEECCEEEE		30.14-
1725PhosphorylationPVTLGAWTRVSLERN
CEEECCEEEEEEHHC		22.2146160609
1725O-linked_GlycosylationPVTLGAWTRVSLERN
CEEECCEEEEEEHHC		22.2146160609
1728PhosphorylationLGAWTRVSLERNGRK
ECCEEEEEEHHCCCC		22.6324719451
1735AcetylationSLERNGRKGALRVGD
EEHHCCCCCCEEECC		50.357822923
1750 (in isoform 6)O-linked_Glycosylation-29.42OGP
1811O-linked_GlycosylationTPEHVLRQVDVTSFA
CHHHHHHHCCCCCCC		17.42-
1811 (in isoform 6)O-linked_Glycosylation-17.42OGP
1815O-linked_GlycosylationVLRQVDVTSFAGHPC
HHHHCCCCCCCCCCC		24.2255832849
1835O-linked_GlycosylationHPCLNGASCVPREAA
CCCCCCCCCCCCCCE		26.28-
1859UbiquitinationSGPHCEKGLVEKSAG
CCCCHHCCCEECCCC		37.8229967540
1860 (in isoform 6)Phosphorylation-24.7928387310
1863UbiquitinationCEKGLVEKSAGDVDT
HHCCCEECCCCCCCE		34.5329967540
1864 (in isoform 3)Phosphorylation-6.2328387310
1882 (in isoform 6)O-linked_Glycosylation-31.23OGP
1890 (in isoform 6)O-linked_Glycosylation-32.87OGP
1896O-linked_GlycosylationELANEIPVPETLDSG
HHHHCCCCCCCCCCC		14.49-
1899O-linked_GlycosylationNEIPVPETLDSGALH
HCCCCCCCCCCCHHC		34.95-
1902O-linked_GlycosylationPVPETLDSGALHEKA
CCCCCCCCCHHCHHH		19.55-
1909 (in isoform 6)O-linked_Glycosylation-26.67OGP
1909O-linked_GlycosylationSGALHEKALQSNHFE
CCHHCHHHHHCCCEE		26.67-
1912O-linked_GlycosylationLHEKALQSNHFELSL
HCHHHHHCCCEEEEE		20.4455833149
1918PhosphorylationQSNHFELSLRTEATQ
HCCCEEEEECCCCCC		6.1424719451
1918O-linked_GlycosylationQSNHFELSLRTEATQ
HCCCEEEEECCCCCC		6.1455833155
1921O-linked_GlycosylationHFELSLRTEATQGLV
CEEEEECCCCCCEEE		2.0855827137
1924O-linked_GlycosylationLSLRTEATQGLVLWS
EEECCCCCCEEEEEE		6.3255827143
1931O-linked_GlycosylationTQGLVLWSGKATERA
CCEEEEEECCCCCCC		10.0655827149
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 AGRIN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of AGRIN_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00770 Congenital myasthenic syndrome
OMIM Disease
615120Myasthenic syndrome, congenital, 8 (CMS8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGRIN_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-135, AND MASSSPECTROMETRY.

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