LRFN1_HUMAN - dbPTM
LRFN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRFN1_HUMAN
UniProt AC Q9P244
Protein Name Leucine-rich repeat and fibronectin type III domain-containing protein 1
Gene Name LRFN1
Organism Homo sapiens (Human).
Sequence Length 771
Subcellular Localization Membrane
Single-pass type I membrane protein. Cell junction, synapse. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Detected in excitatory, but not inhibitory, synaptic plasma membrane..
Protein Description Promotes neurite outgrowth in hippocampal neurons. Involved in the regulation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1 (By similarity)..
Protein Sequence MAPGPFSSALLSPPPAALPFLLLLWAGASRGQPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSLVHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRRVESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHKLVRLDMTSNRLHKLPPDGLFLRSQGTGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDDLETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLRCRAVGDPEPVVHWVAPDGRLLGNSSRTRVRGDGTLDVTITTLRDSGTFTCIASNAAGEATAPVEVCVVPLPLMAPPPAAPPPLTEPGSSDIATPGRPGANDSAAERRLVAAELTSNSVLIRWPAQRPVPGIRMYQVQYNSSVDDSLVYRMIPSTSQTFLVNDLAAGRAYDLCVLAVYDDGATALPATRVVGCVQFTTAGDPAPCRPLRAHFLGGTMIIAIGGVIVASVLVFIVLLMIRYKVYGDGDSRRVKGSRSLPRVSHVCSQTNGAGTGAAQAPALPAQDHYEALREVESQAAPAVAVEAKAMEAETASAEPEVVLGRSLGGSATSLCLLPSEETSGEESRAAVGPRRSRSGALEPPTSAPPTLALVPGGAAARPRPQQRYSFDGDYGALFQSHSYPRRARRTKRHRSTPHLDGAGGGAAGEDGDLGLGSARACLAFTSTEWMLESTV
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
87N-linked_GlycosylationVRRRDFANMTSLVHL
HHHHHCCCCCCEEEE		33.97UniProtKB CARBOHYD
95PhosphorylationMTSLVHLTLSRNTIG
CCCEEEEEECCCCHH		14.0724719451
219PhosphorylationLVRLDMTSNRLHKLP
HEEEECCCCCCCCCC		17.2019413330
318PhosphorylationVVEGQAVSLRCRAVG
EEECEEEEEEEEECC		17.0824670416
343N-linked_GlycosylationPDGRLLGNSSRTRVR
CCCCCCCCCCCCEEC		36.46UniProtKB CARBOHYD
434PhosphorylationRLVAAELTSNSVLIR
HHHEEEHHCCEEEEE		19.8419690332
435PhosphorylationLVAAELTSNSVLIRW
HHEEEHHCCEEEEEC		39.4719690332
437PhosphorylationAAELTSNSVLIRWPA
EEEHHCCEEEEECCC		20.3319690332
454PhosphorylationPVPGIRMYQVQYNSS
CCCCEEEEEEEECCC		8.8318083107
458PhosphorylationIRMYQVQYNSSVDDS
EEEEEEEECCCCCCE		20.3918083107
474O-linked_GlycosylationVYRMIPSTSQTFLVN
EEEECCCCCCEEEEC		21.35OGP
475PhosphorylationYRMIPSTSQTFLVND
EEECCCCCCEEEECH		31.40-
477PhosphorylationMIPSTSQTFLVNDLA
ECCCCCCEEEECHHH		20.78-
502O-linked_GlycosylationAVYDDGATALPATRV
EEECCCCCCCCCCEE		33.97OGP
562PhosphorylationLMIRYKVYGDGDSRR
HHHHHHHHCCCCCCC		12.83-
567PhosphorylationKVYGDGDSRRVKGSR
HHHCCCCCCCCCCCC		27.76-
573PhosphorylationDSRRVKGSRSLPRVS
CCCCCCCCCCCCCEE		16.9920068231
575PhosphorylationRRVKGSRSLPRVSHV
CCCCCCCCCCCEEEE		44.4120068231
580PhosphorylationSRSLPRVSHVCSQTN
CCCCCCEEEECCCCC		16.1026471730
584PhosphorylationPRVSHVCSQTNGAGT
CCEEEECCCCCCCCC		38.6626471730
586PhosphorylationVSHVCSQTNGAGTGA
EEEECCCCCCCCCCC		21.2326471730
591PhosphorylationSQTNGAGTGAAQAPA
CCCCCCCCCCCCCCC		24.1026471730
605PhosphorylationALPAQDHYEALREVE
CCCCHHHHHHHHHHH		15.9329978859
613PhosphorylationEALREVESQAAPAVA
HHHHHHHHCCCCEEH		30.2317525332
624UbiquitinationPAVAVEAKAMEAETA
CEEHHHHHHHHHHHC		34.4621906983
632PhosphorylationAMEAETASAEPEVVL
HHHHHHCCCCCEEEE		40.3528985074
642PhosphorylationPEVVLGRSLGGSATS
CEEEEEECCCCCCEE		29.5730576142
646PhosphorylationLGRSLGGSATSLCLL
EEECCCCCCEEEEEC		26.9522617229
648PhosphorylationRSLGGSATSLCLLPS
ECCCCCCEEEEECCC		24.7530631047
649PhosphorylationSLGGSATSLCLLPSE
CCCCCCEEEEECCCC		19.4630576142
655PhosphorylationTSLCLLPSEETSGEE
EEEEECCCCCCCCHH		48.2926074081
658PhosphorylationCLLPSEETSGEESRA
EECCCCCCCCHHHHH		37.6726074081
659PhosphorylationLLPSEETSGEESRAA
ECCCCCCCCHHHHHC		47.7026074081
672PhosphorylationAAVGPRRSRSGALEP
HCCCCCCCCCCCCCC		31.8830576142
674PhosphorylationVGPRRSRSGALEPPT
CCCCCCCCCCCCCCC		29.6629255136
681PhosphorylationSGALEPPTSAPPTLA
CCCCCCCCCCCCEEE		48.5129255136
682PhosphorylationGALEPPTSAPPTLAL
CCCCCCCCCCCEEEE		44.5529255136
686PhosphorylationPPTSAPPTLALVPGG
CCCCCCCEEEECCCC		24.4929255136
704PhosphorylationRPRPQQRYSFDGDYG
CCCCCCCCCCCCCHH		14.8928152594
705PhosphorylationPRPQQRYSFDGDYGA
CCCCCCCCCCCCHHH		21.0322617229
710PhosphorylationRYSFDGDYGALFQSH
CCCCCCCHHHHHCCC		15.1628152594
716PhosphorylationDYGALFQSHSYPRRA
CHHHHHCCCCCCCCC		13.6828450419
718PhosphorylationGALFQSHSYPRRARR
HHHHCCCCCCCCCCC		41.9225849741
719PhosphorylationALFQSHSYPRRARRT
HHHCCCCCCCCCCCC		8.7128450419
731PhosphorylationRRTKRHRSTPHLDGA
CCCCCCCCCCCCCCC		39.9230266825
732PhosphorylationRTKRHRSTPHLDGAG
CCCCCCCCCCCCCCC		18.0630266825
753PhosphorylationDGDLGLGSARACLAF
CCCCCCCCHHHHHHH		21.4423312004
761PhosphorylationARACLAFTSTEWMLE
HHHHHHHHCHHHHHH		29.1824719451
762PhosphorylationRACLAFTSTEWMLES
HHHHHHHCHHHHHHC		20.2028348404
763PhosphorylationACLAFTSTEWMLEST
HHHHHHCHHHHHHCC		30.5228348404
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 LRFN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRFN1_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 LRFN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KI13B_HUMANKIF13Bphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
CING_HUMANCGNphysical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
CBY1_HUMANCBY1physical
27173435
F110B_HUMANFAM110Bphysical
27173435
GGYF2_HUMANGIGYF2physical
27173435
NGAP_HUMANRASAL2physical
27173435
F110A_HUMANFAM110Aphysical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
NAV1_HUMANNAV1physical
27173435
RPTOR_HUMANRPTORphysical
27173435
HDAC7_HUMANHDAC7physical
27173435
KIF1B_HUMANKIF1Bphysical
27173435
SH3B4_HUMANSH3BP4physical
27173435
REEP3_HUMANREEP3physical
27173435
PANK2_HUMANPANK2physical
27173435
CRTC2_HUMANCRTC2physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRFN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, AND MASSSPECTROMETRY.

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