LRC4B_HUMAN - dbPTM
LRC4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC4B_HUMAN
UniProt AC Q9NT99
Protein Name Leucine-rich repeat-containing protein 4B
Gene Name LRRC4B
Organism Homo sapiens (Human).
Sequence Length 713
Subcellular Localization Membrane
Single-pass membrane protein. Cell junction, synapse, presynaptic cell membrane.
Protein Description Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity)..
Protein Sequence MARARGSPCPPLPPGRMSWPHGALLFLWLFSPPLGAGGGGVAVTSAAGGGSPPATSCPVACSCSNQASRVICTRRDLAEVPASIPVNTRYLNLQENGIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRYIGELDQSHFTCYAPVIVEPPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNVSAVDPVAAGGTGSGGGGPGGSGGVGGGSGGYTYFTTVTVETLETQPGEEALQPRGTEKEPPGPTTDGVWGGGRPGDAAGPASSSTTAPAPRSSRPTEKAFTVPITDVTENALKDLDDVMKTTKIIIGCFVAITFMAAVMLVAFYKLRKQHQLHKHHGPTRTVEIINVEDELPAASAVSVAAAAAVASGGGVGGDSHLALPALERDHLNHHHYVAAAFKAHYSSNPSGGGCGGKGPPGLNSIHEPLLFKSGSKENVQETQI
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
88PhosphorylationPASIPVNTRYLNLQE
CCCCCCCCCEEECHH		22.4120068231
147PhosphorylationELFDNRLTTVPTQAF
HHHCCCCCCCCHHHH		23.6225072903
148PhosphorylationLFDNRLTTVPTQAFE
HHCCCCCCCCHHHHH		29.1325072903
151PhosphorylationNRLTTVPTQAFEYLS
CCCCCCCHHHHHHHH		28.3525072903
156PhosphorylationVPTQAFEYLSKLREL
CCHHHHHHHHHHHHH		15.1525072903
158PhosphorylationTQAFEYLSKLRELWL
HHHHHHHHHHHHHHH		28.8325072903
183PhosphorylationYAFNRVPSLRRLDLG
HHHCCCCCCCCCCHH		31.4824719451
211PhosphorylationEGLVNLRYLNLGMCN
HHHCCCCEEECCCCC		11.78-
224N-linked_GlycosylationCNLKDIPNLTALVRL
CCCCCCCCCEEEEEH		50.81UniProtKB CARBOHYD
248PhosphorylationLDLIRPGSFQGLTSL
EEEECCCCCCCHHHH		19.6527174698
253PhosphorylationPGSFQGLTSLRKLWL
CCCCCCHHHHHHHHH		32.3227174698
254PhosphorylationGSFQGLTSLRKLWLM
CCCCCHHHHHHHHHH		31.0827174698
283N-linked_GlycosylationLKSLEELNLSHNNLM
HHCHHHHCCCCCCCC		42.66UniProtKB CARBOHYD
333N-linked_GlycosylationLKETVPSNTTCCARC
HHHCCCCCCCEECCC		33.08UniProtKB CARBOHYD
374N-linked_GlycosylationVEPPTDLNVTEGMAA
ECCCCCCCCCCCCEE		41.28UniProtKB CARBOHYD
387PhosphorylationAAELKCRTGTSMTSV
EEEEEECCCCCCCEE		55.0424719451
389PhosphorylationELKCRTGTSMTSVNW
EEEECCCCCCCEEEE		18.0824719451
400N-linked_GlycosylationSVNWLTPNGTLMTHG
EEEEECCCCEEEECC		51.34UniProtKB CARBOHYD
422N-linked_GlycosylationVLHDGTLNFTNVTVQ
EEECCCEEEEEEEEE		41.35UniProtKB CARBOHYD
425N-linked_GlycosylationDGTLNFTNVTVQDTG
CCCEEEEEEEEEECC		24.27UniProtKB CARBOHYD
444N-linked_GlycosylationMVTNSAGNTTASATL
EEECCCCCEEEEEEE		33.69UniProtKB CARBOHYD
452N-linked_GlycosylationTTASATLNVSAVDPV
EEEEEEECCCCCCCE		22.73UniProtKB CARBOHYD
497O-linked_GlycosylationVTVETLETQPGEEAL
EEEEEECCCCCCHHC		43.08OGP
648PhosphorylationGGGVGGDSHLALPAL
CCCCCCCCCCCCCCC		24.5524173317
665PhosphorylationDHLNHHHYVAAAFKA
CCCCCHHHHHHHHHH		6.34-
674PhosphorylationAAAFKAHYSSNPSGG
HHHHHHHHCCCCCCC		20.7525884760
676PhosphorylationAFKAHYSSNPSGGGC
HHHHHHCCCCCCCCC		45.66-
693PhosphorylationKGPPGLNSIHEPLLF
CCCCCCCCCCCCEEC		30.3024173317
702PhosphorylationHEPLLFKSGSKENVQ
CCCEECCCCCCCCCC		40.7524114839
704PhosphorylationPLLFKSGSKENVQET
CEECCCCCCCCCCCC		43.8423911959
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 LRC4B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC4B_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 LRC4B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LRC4B_HUMAN !!
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 LRC4B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704, AND MASSSPECTROMETRY.

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