LRRN1_HUMAN - dbPTM
LRRN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRRN1_HUMAN
UniProt AC Q6UXK5
Protein Name Leucine-rich repeat neuronal protein 1
Gene Name LRRN1
Organism Homo sapiens (Human).
Sequence Length 716
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MARMSFVIAACQLVLGLLMTSLTESSIQNSECPQLCVCEIRPWFTPQSTYREATTVDCNDLRLTRIPSNLSSDTQVLLLQSNNIAKTVDELQQLFNLTELDFSQNNFTNIKEVGLANLTQLTTLHLEENQITEMTDYCLQDLSNLQELYINHNQISTISAHAFAGLKNLLRLHLNSNKLKVIDSRWFDSTPNLEILMIGENPVIGILDMNFKPLANLRSLVLAGMYLTDIPGNALVGLDSLESLSFYDNKLVKVPQLALQKVPNLKFLDLNKNPIHKIQEGDFKNMLRLKELGINNMGELVSVDRYALDNLPELTKLEATNNPKLSYIHRLAFRSVPALESLMLNNNALNAIYQKTVESLPNLREISIHSNPLRCDCVIHWINSNKTNIRFMEPLSMFCAMPPEYKGHQVKEVLIQDSSEQCLPMISHDSFPNRLNVDIGTTVFLDCRAMAEPEPEIYWVTPIGNKITVETLSDKYKLSSEGTLEISNIQIEDSGRYTCVAQNVQGADTRVATIKVNGTLLDGTQVLKIYVKQTESHSILVSWKVNSNVMTSNLKWSSATMKIDNPHITYTARVPVDVHEYNLTHLQPSTDYEVCLTVSNIHQQTQKSCVNVTTKNAAFAVDISDQETSTALAAVMGSMFAVISLASIAVYFAKRFKRKNYHHSLKKYMQKTSSIPLNELYPPLINLWEGDSEKDKDGSADTKPTQVDTSRSYYMW
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
81PhosphorylationTQVLLLQSNNIAKTV
CEEEEEECCCHHHHH
31.64-
96N-linked_GlycosylationDELQQLFNLTELDFS
HHHHHHHCCCCCCCC
55.43UniProtKB CARBOHYD
117N-linked_GlycosylationIKEVGLANLTQLTTL
HHHHCEECCCEEEEE
48.98UniProtKB CARBOHYD
306PhosphorylationELVSVDRYALDNLPE
CEEEEEHHHHHCCCH
13.67-
320PhosphorylationELTKLEATNNPKLSY
HHHHHCCCCCCCCHH
26.5926270265
326PhosphorylationATNNPKLSYIHRLAF
CCCCCCCHHHHHHHH
28.3230631047
327PhosphorylationTNNPKLSYIHRLAFR
CCCCCCHHHHHHHHC
15.9330631047
385N-linked_GlycosylationVIHWINSNKTNIRFM
EEEEECCCCCEEEEE
51.16UniProtKB CARBOHYD
468PhosphorylationTPIGNKITVETLSDK
ECCCCEEEEEECCCC
17.5621406692
471PhosphorylationGNKITVETLSDKYKL
CCEEEEEECCCCEEE
27.5021406692
473PhosphorylationKITVETLSDKYKLSS
EEEEEECCCCEEECC
39.2021406692
476PhosphorylationVETLSDKYKLSSEGT
EEECCCCEEECCCCE
23.3521406692
479PhosphorylationLSDKYKLSSEGTLEI
CCCCEEECCCCEEEE
23.38-
517N-linked_GlycosylationRVATIKVNGTLLDGT
EEEEEEECCEEECCE
32.50UniProtKB CARBOHYD
552PhosphorylationVNSNVMTSNLKWSSA
ECCCCCCCCEEEEEE
23.2830631047
557PhosphorylationMTSNLKWSSATMKID
CCCCEEEEEEEEEEC
14.4430631047
558PhosphorylationTSNLKWSSATMKIDN
CCCEEEEEEEEEECC
27.0030631047
571O-linked_GlycosylationDNPHITYTARVPVDV
CCCCEEEEEEECCEE
10.1955826169
664PhosphorylationKRKNYHHSLKKYMQK
HHCCCHHHHHHHHHH
28.6821406692
667UbiquitinationNYHHSLKKYMQKTSS
CCHHHHHHHHHHHCC
51.77-
672PhosphorylationLKKYMQKTSSIPLNE
HHHHHHHHCCCCHHH
15.7124173317
673PhosphorylationKKYMQKTSSIPLNEL
HHHHHHHCCCCHHHH
33.0524173317
674PhosphorylationKYMQKTSSIPLNELY
HHHHHHCCCCHHHHC
33.1928348404
709PhosphorylationTKPTQVDTSRSYYMW
CCCCCCCCCCCCCCC
27.4725332170

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 LRRN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRRN1_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 LRRN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTPRD_HUMANPTPRDphysical
28514442
GHITM_HUMANGHITMphysical
28514442
ST7_HUMANST7physical
28514442

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 LRRN1_HUMAN

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Related Literatures of Post-Translational Modification

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