LRRN3_HUMAN - dbPTM
LRRN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRRN3_HUMAN
UniProt AC Q9H3W5
Protein Name Leucine-rich repeat neuronal protein 3
Gene Name LRRN3
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MKDMPLRIHVLLGLAITTLVQAVDKKVDCPRLCTCEIRPWFTPRSIYMEASTVDCNDLGLLTFPARLPANTQILLLQTNNIAKIEYSTDFPVNLTGLDLSQNNLSSVTNINVKKMPQLLSVYLEENKLTELPEKCLSELSNLQELYINHNLLSTISPGAFIGLHNLLRLHLNSNRLQMINSKWFDALPNLEILMIGENPIIRIKDMNFKPLINLRSLVIAGINLTEIPDNALVGLENLESISFYDNRLIKVPHVALQKVVNLKFLDLNKNPINRIRRGDFSNMLHLKELGINNMPELISIDSLAVDNLPDLRKIEATNNPRLSYIHPNAFFRLPKLESLMLNSNALSALYHGTIESLPNLKEISIHSNPIRCDCVIRWMNMNKTNIRFMEPDSLFCVDPPEFQGQNVRQVHFRDMMEICLPLIAPESFPSNLNVEAGSYVSFHCRATAEPQPEIYWITPSGQKLLPNTLTDKFYVHSEGTLDINGVTPKEGGLYTCIATNLVGADLKSVMIKVDGSFPQDNNGSLNIKIRDIQANSVLVSWKASSKILKSSVKWTAFVKTENSHAAQSARIPSDVKVYNLTHLNPSTEYKICIDIPTIYQKNRKKCVNVTTKGLHPDQKEYEKNNTTTLMACLGGLLGIIGVICLISCLSPEMNCDGGHSYVRNYLQKPTFALGELYPPLINLWEAGKEKSTSLKVKATVIGLPTNMS
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
93N-linked_GlycosylationYSTDFPVNLTGLDLS
EECCCCCCCCCCCCC
31.93UniProtKB CARBOHYD
103N-linked_GlycosylationGLDLSQNNLSSVTNI
CCCCCCCCCCCCCCC
33.39UniProtKB CARBOHYD
120PhosphorylationKKMPQLLSVYLEENK
HCCHHHHHHHHHCCC
19.8029396449
122PhosphorylationMPQLLSVYLEENKLT
CHHHHHHHHHCCCCC
12.6729396449
223N-linked_GlycosylationSLVIAGINLTEIPDN
HEEEECCCCCCCCCC
39.74UniProtKB CARBOHYD
338PhosphorylationFRLPKLESLMLNSNA
CCCCCHHHHHCCCHH
29.5229759185
350PhosphorylationSNALSALYHGTIESL
CHHHHHHHHCCHHHC
9.6429759185
382N-linked_GlycosylationVIRWMNMNKTNIRFM
EEEEECCCCCCEEEE
42.89UniProtKB CARBOHYD
522N-linked_GlycosylationGSFPQDNNGSLNIKI
CCCCCCCCCCEEEEE
50.12UniProtKB CARBOHYD
579N-linked_GlycosylationPSDVKVYNLTHLNPS
CCCCEEEECCCCCCC
41.26UniProtKB CARBOHYD
608N-linked_GlycosylationKNRKKCVNVTTKGLH
HCCHHCCCCCCCCCC
34.58UniProtKB CARBOHYD
624N-linked_GlycosylationDQKEYEKNNTTTLMA
CHHHHHHCCHHHHHH
38.86UniProtKB CARBOHYD
625N-linked_GlycosylationQKEYEKNNTTTLMAC
HHHHHHCCHHHHHHH
50.28UniProtKB CARBOHYD

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 LRRN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRRN3_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 LRRN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALL5_HUMANCALML5physical
28514442
SPB4_HUMANSERPINB4physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRRN3_HUMAN

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Related Literatures of Post-Translational Modification

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