LIGO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIGO1_HUMAN
• UniProt AC: Q96FE5
• Protein Name: Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
• Gene Name: LINGO1
• Organism: Homo sapiens (Human).
• Sequence Length: 620
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. [PubMed: 14966521]
• Protein Sequence: MQVSKRMLAGGVRSMPSPLLACWQPILLLVLGSVLSGSATGCPPRCECSAQDRAVLCHRKRFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLTSLSITHCNLTAVPYLAVRHLVYLRFLNLSYNPISTIEGSMLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESVFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTCRRARIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHVRSYSPDWPHQPNKTFAFISNQPGEGEANSTRATVPFPFDIKTLIIATTMGFISFLGVVLFCLVLLFLWSRGKGNTKHNIEIEYVPRKSDAGISSADAPRKFNMKMI

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
14	Phosphorylation	MLAGGVRSMPSPLLA HHCCCCCCCCHHHHH	32.41	-
17	Phosphorylation	GGVRSMPSPLLACWQ CCCCCCCHHHHHHHH	21.38	-
123	Phosphorylation	NNLFNLRTLGLRSNR HHHHCHHHHCCCCCC	28.48	22210691
144	N-linked_Glycosylation	GVFTGLSNLTKLDIS CHHCCCCCCCCCCCC	57.69	17005555
202	N-linked_Glycosylation	QLTLEKCNLTSIPTE HHHHHHCCCCCCCHH	58.38	17005555
264	N-linked_Glycosylation	PNCLYGLNLTSLSIT CCCEECCCCCCEEEE	36.59	17005555
274	N-linked_Glycosylation	SLSITHCNLTAVPYL CEEEECCCCCHHHHH	32.59	17005555
293	N-linked_Glycosylation	LVYLRFLNLSYNPIS HHHHHHHCCCCCCCC	24.99	17005555
295	Phosphorylation	YLRFLNLSYNPISTI HHHHHCCCCCCCCCC	23.07	-
296	Phosphorylation	LRFLNLSYNPISTIE HHHHCCCCCCCCCCC	28.29	-
300	Phosphorylation	NLSYNPISTIEGSML CCCCCCCCCCCHHHH	25.29	-
301	Phosphorylation	LSYNPISTIEGSMLH CCCCCCCCCCHHHHH	24.62	-
329	Phosphorylation	QLAVVEPYAFRGLNY EEEEECCCEECCCCE	12.59	27762562
341	N-linked_Glycosylation	LNYLRVLNVSGNQLT CCEEEEEECCCCCCE	24.05	17005555
492	N-linked_Glycosylation	RYAQVQDNGTYLCIA EEEEEECCCEEEEEE	27.84	17005555
505	N-linked_Glycosylation	IAANAGGNDSMPAHL EEEECCCCCCCCCEE	36.95	UniProtKB CARBOHYD
526	N-linked_Glycosylation	PDWPHQPNKTFAFIS CCCCCCCCCEEEEEE	49.80	UniProtKB CARBOHYD
542	N-linked_Glycosylation	QPGEGEANSTRATVP CCCCCCCCCCCCCCC	39.34	UniProtKB CARBOHYD
584	Ubiquitination	VLLFLWSRGKGNTKH HHHHHHHCCCCCCCC	38.98	32142685
590	Ubiquitination	SRGKGNTKHNIEIEY HCCCCCCCCCEEEEE	38.36	32142685
595	Ubiquitination	NTKHNIEIEYVPRKS CCCCCEEEEEECCCC	4.02	32142685
601	Ubiquitination	EIEYVPRKSDAGISS EEEEECCCCCCCCCC	46.76	32142685
602	Phosphorylation	IEYVPRKSDAGISSA EEEECCCCCCCCCCC	33.69	26657352
607	Phosphorylation	RKSDAGISSADAPRK CCCCCCCCCCCCCCC	20.68	28857561

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LIGO1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIGO1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LIGO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBXW7_HUMAN	FBXW7	physical	16169070
LIGO2_HUMAN	LINGO2	physical	28514442
H2A2C_HUMAN	HIST2H2AC	physical	28514442
LMA2L_HUMAN	LMAN2L	physical	28514442
CD032_HUMAN	C4orf32	physical	28514442
PON2_HUMAN	PON2	physical	28514442
PSMG2_HUMAN	PSMG2	physical	28514442
NGLY1_HUMAN	NGLY1	physical	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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"The structure of the Lingo-1 ectodomain, a module implicated incentral nervous system repair inhibition.";
Mosyak L., Wood A., Dwyer B., Buddha M., Johnson M., Aulabaugh A.,Zhong X., Presman E., Benard S., Kelleher K., Wilhelm J., Stahl M.L.,Kriz R., Gao Y., Cao Z., Ling H.P., Pangalos M.N., Walsh F.S.,Somers W.S.;
J. Biol. Chem. 281:36378-36390(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 40-516, FUNCTION, SUBUNIT,INTERACTION WITH NGFR AND RTN4R, DISULFIDE BONDS, MASS SPECTROMETRY,AND GLYCOSYLATION AT ASN-144; ASN-202; ASN-264; ASN-274; ASN-293;ASN-341 AND ASN-492.
PubMed: 17005555