LRIG1_HUMAN - dbPTM
LRIG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRIG1_HUMAN
UniProt AC Q96JA1
Protein Name Leucine-rich repeats and immunoglobulin-like domains protein 1
Gene Name LRIG1 {ECO:0000303|PubMed:15282549}
Organism Homo sapiens (Human).
Sequence Length 1093
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation..
Protein Sequence MARPVRGGLGAPRRSPCLLLLWLLLLRLEPVTAAAGPRAPCAAACTCAGDSLDCGGRGLAALPGDLPSWTRSLNLSYNKLSEIDPAGFEDLPNLQEVYLNNNELTAVPSLGAASSHVVSLFLQHNKIRSVEGSQLKAYLSLEVLDLSLNNITEVRNTCFPHGPPIKELNLAGNRIGTLELGAFDGLSRSLLTLRLSKNRITQLPVRAFKLPRLTQLDLNRNRIRLIEGLTFQGLNSLEVLKLQRNNISKLTDGAFWGLSKMHVLHLEYNSLVEVNSGSLYGLTALHQLHLSNNSIARIHRKGWSFCQKLHELVLSFNNLTRLDEESLAELSSLSVLRLSHNSISHIAEGAFKGLRSLRVLDLDHNEISGTIEDTSGAFSGLDSLSKLTLFGNKIKSVAKRAFSGLEGLEHLNLGGNAIRSVQFDAFVKMKNLKELHISSDSFLCDCQLKWLPPWLIGRMLQAFVTATCAHPESLKGQSIFSVPPESFVCDDFLKPQIITQPETTMAMVGKDIRFTCSAASSSSSPMTFAWKKDNEVLTNADMENFVHVHAQDGEVMEYTTILHLRQVTFGHEGRYQCVITNHFGSTYSHKARLTVNVLPSFTKTPHDITIRTTTMARLECAATGHPNPQIAWQKDGGTDFPAARERRMHVMPDDDVFFITDVKIDDAGVYSCTAQNSAGSISANATLTVLETPSLVVPLEDRVVSVGETVALQCKATGNPPPRITWFKGDRPLSLTERHHLTPDNQLLVVQNVVAEDAGRYTCEMSNTLGTERAHSQLSVLPAAGCRKDGTTVGIFTIAVVSSIVLTSLVWVCIIYQTRKKSEEYSVTNTDETVVPPDVPSYLSSQGTLSDRQETVVRTEGGPQANGHIESNGVCPRDASHFPEPDTHSVACRQPKLCAGSAYHKEPWKAMEKAEGTPGPHKMEHGGRVVCSDCNTEVDCYSRGQAFHPQPVSRDSAQPSAPNGPEPGGSDQEHSPHHQCSRTAAGSCPECQGSLYPSNHDRMLTAVKKKPMASLDGKGDSSWTLARLYHPDSTELQPASSLTSGSPERAEAQYLLVSNGHLPKACDASPESTPLTGQLPGKQRVPLLLAPKS
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
72PhosphorylationDLPSWTRSLNLSYNK
CCCHHHHHCCCCCCC
17.7723403867
74N-linked_GlycosylationPSWTRSLNLSYNKLS
CHHHHHCCCCCCCCC
28.3425765764
150N-linked_GlycosylationVLDLSLNNITEVRNT
HHHHHCCCHHHHHHH
48.1025765764
177PhosphorylationLAGNRIGTLELGAFD
CCCCCCEEEECCCCC
18.0623312004
187PhosphorylationLGAFDGLSRSLLTLR
CCCCCCCCHHHHHHH
25.9223312004
236PhosphorylationLTFQGLNSLEVLKLQ
CEECCCCHHHHHHHH
30.83-
246N-linked_GlycosylationVLKLQRNNISKLTDG
HHHHHHCCHHHHCCC
41.9425765764
259PhosphorylationDGAFWGLSKMHVLHL
CCCCHHHCCCEEEEE
24.80-
292N-linked_GlycosylationLHQLHLSNNSIARIH
HEEHHCCCCCHHHHH
53.2625765764
318N-linked_GlycosylationELVLSFNNLTRLDEE
HHHHCCCCCCCCCHH
40.5625765764
331PhosphorylationEESLAELSSLSVLRL
HHHHHHHHCCHHHHC
22.27-
332PhosphorylationESLAELSSLSVLRLS
HHHHHHHCCHHHHCC
36.97-
334PhosphorylationLAELSSLSVLRLSHN
HHHHHCCHHHHCCCC
22.5124719451
594PhosphorylationYSHKARLTVNVLPSF
CCCEEEEEEEECCCC
12.41-
600PhosphorylationLTVNVLPSFTKTPHD
EEEEECCCCCCCCCC
41.1924719451
602PhosphorylationVNVLPSFTKTPHDIT
EEECCCCCCCCCCEE
38.0424670416
603UbiquitinationNVLPSFTKTPHDITI
EECCCCCCCCCCEEE
59.03-
623O-linked_GlycosylationARLECAATGHPNPQI
EEEHHHHHCCCCCCE
19.9455832991
634UbiquitinationNPQIAWQKDGGTDFP
CCCEEEECCCCCCCH
47.87-
684N-linked_GlycosylationSAGSISANATLTVLE
CCCEEEECEEEEEEE
27.0225765764
715UbiquitinationETVALQCKATGNPPP
CEEEEEEHHHCCCCC
35.70-
728UbiquitinationPPRITWFKGDRPLSL
CCCEEEEECCCCCCC
52.00-
734PhosphorylationFKGDRPLSLTERHHL
EECCCCCCCCCCCCC
35.6126699800
771PhosphorylationEMSNTLGTERAHSQL
EEECCCCCCCCCCEE
25.9724719451
833PhosphorylationSVTNTDETVVPPDVP
CCCCCCCCCCCCCCC
29.6127282143
844PhosphorylationPDVPSYLSSQGTLSD
CCCCHHHHCCCCCCC
16.6327282143
848PhosphorylationSYLSSQGTLSDRQET
HHHHCCCCCCCCCCE
18.5627282143
901PhosphorylationQPKLCAGSAYHKEPW
CCCCCCCCCCCCCHH
13.7126437602
941PhosphorylationCNTEVDCYSRGQAFH
CCCEEEEECCCCCCC
9.2829978859
942PhosphorylationNTEVDCYSRGQAFHP
CCEEEEECCCCCCCC
35.9429978859
956PhosphorylationPQPVSRDSAQPSAPN
CCCCCCCCCCCCCCC
27.9123312004
960PhosphorylationSRDSAQPSAPNGPEP
CCCCCCCCCCCCCCC
44.2523312004
970PhosphorylationNGPEPGGSDQEHSPH
CCCCCCCCCCCCCCC
41.8728555341
975PhosphorylationGGSDQEHSPHHQCSR
CCCCCCCCCCCCCCC
25.7730177828
981PhosphorylationHSPHHQCSRTAAGSC
CCCCCCCCCCCCCCC
26.5430177828
996PhosphorylationPECQGSLYPSNHDRM
CCCCCCCCCCCCHHC
13.30-
1029PhosphorylationSWTLARLYHPDSTEL
CEEEEEECCCCCCCC
13.0223312004
1033PhosphorylationARLYHPDSTELQPAS
EEECCCCCCCCCCCH
28.3828348404
1034PhosphorylationRLYHPDSTELQPASS
EECCCCCCCCCCCHH
48.3624719451
1040PhosphorylationSTELQPASSLTSGSP
CCCCCCCHHCCCCCH
32.3427251275
1041PhosphorylationTELQPASSLTSGSPE
CCCCCCHHCCCCCHH
37.4627251275
1043PhosphorylationLQPASSLTSGSPERA
CCCCHHCCCCCHHHH
32.7523312004
1044PhosphorylationQPASSLTSGSPERAE
CCCHHCCCCCHHHHH
42.4323312004
1046PhosphorylationASSLTSGSPERAEAQ
CHHCCCCCHHHHHCE
24.2923312004
1054PhosphorylationPERAEAQYLLVSNGH
HHHHHCEEEEEECCC
14.7322817900
1069PhosphorylationLPKACDASPESTPLT
CCCCCCCCCCCCCCC
18.8922199227
1072PhosphorylationACDASPESTPLTGQL
CCCCCCCCCCCCCCC
38.4130266825
1073PhosphorylationCDASPESTPLTGQLP
CCCCCCCCCCCCCCC
22.2130266825
1076PhosphorylationSPESTPLTGQLPGKQ
CCCCCCCCCCCCCCC
24.8823403867
1093PhosphorylationPLLLAPKS-------
CEEECCCC-------
44.3829214152

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
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:15282549

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRIG1_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 LRIG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET_HUMANMETphysical
17178829
EGFR_HUMANEGFRphysical
15345710
ERBB4_HUMANERBB4physical
15345710
EGFR_HUMANEGFRphysical
15282549
ERBB2_HUMANERBB2physical
15282549
ERBB3_HUMANERBB3physical
15282549
ERBB4_HUMANERBB4physical
15282549
CBL_HUMANCBLphysical
15282549
EGFR_HUMANEGFRphysical
18542056
UBP8_HUMANUSP8physical
24828152
LRIG3_HUMANLRIG3physical
28514442
LRC40_HUMANLRRC40physical
28514442
RAB4A_HUMANRAB4Aphysical
28514442
CNPY4_HUMANCNPY4physical
28514442
SCRIB_HUMANSCRIBphysical
28514442
MFR1L_HUMANMTFR1Lphysical
28514442
LRIG2_HUMANLRIG2physical
28514442
PON2_HUMANPON2physical
28514442
TBB8_HUMANTUBB8physical
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 LRIG1_HUMAN

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Related Literatures of Post-Translational Modification

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