LIGO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIGO2_HUMAN
• UniProt AC: Q7L985
• Protein Name: Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 2
• Gene Name: LINGO2
• Organism: Homo sapiens (Human).
• Sequence Length: 606
• Subcellular Localization: Membrane ; Single-pass type I membrane protein .
• Protein Sequence: MLHTAISCWQPFLGLAVVLIFMGSTIGCPARCECSAQNKSVSCHRRRLIAIPEGIPIETKILDLSKNRLKSVNPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLKLVPLGVFTGLSNLTKLDISENKIVILLDYMFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEKCNLTAVPTEALSHLRSLISLHLKHLNINNMPVYAFKRLFHLKHLEIDYWPLLDMMPANSLYGLNLTSLSVTNTNLSTVPFLAFKHLVYLTHLNLSYNPISTIEAGMFSDLIRLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENVFSSPRALEVLSINNNPLACDCRLLWILQRQPTLQFGGQQPMCAGPDTIRERSFKDFHSTALSFYFTCKKPKIREKKLQHLLVDEGQTVQLECSADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLTVKGFASDRFLYANRTPMYMTDSNDTISNGTNANTFSLDLKTILVSTAMGCFTFLGVVLFCFLLLFVWSRGKGKHKNSIDLEYVPRKNNGAVVEGEVAGPRRFNMKMI

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
38	N-linked_Glycosylation	RCECSAQNKSVSCHR CCCCCCCCCCCEEEE	37.98	UniProtKB CARBOHYD
130	N-linked_Glycosylation	GVFTGLSNLTKLDIS CHHCCCCCCCCCCCC	57.69	UniProtKB CARBOHYD
188	N-linked_Glycosylation	QLTLEKCNLTAVPTE HHHHHHCCCCCCCHH	52.04	UniProtKB CARBOHYD
279	N-linked_Glycosylation	LVYLTHLNLSYNPIS HHHHHHCCCCCCCCC	21.24	UniProtKB CARBOHYD
311	Phosphorylation	IVGAQLRTIEPHSFQ EEEEEEEECCCCCCC	37.98	22167270
316	Phosphorylation	LRTIEPHSFQGLRFL EEECCCCCCCHHHHH	29.94	22167270
327	N-linked_Glycosylation	LRFLRVLNVSQNLLE HHHHHHEECCHHHHH	28.65	UniProtKB CARBOHYD
471	Methylation	GDGTLEIRFAQDQDS CCCEEEEEEEECCCC	16.09	24384539
574	Acetylation	SRGKGKHKNSIDLEY HCCCCCCCCCCCCEE	56.74	7460677
576	Phosphorylation	GKGKHKNSIDLEYVP CCCCCCCCCCCEEEC	23.45	27732954

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

Oops, there are no upstream regulatory protein records of LIGO2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIGO2_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 LIGO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
SMUF2_HUMAN	SMURF2	physical	28514442
LEG1_HUMAN	LGALS1	physical	28514442
NPT2B_HUMAN	SLC34A2	physical	28514442
G3PT_HUMAN	GAPDHS	physical	28514442
PTPRD_HUMAN	PTPRD	physical	28514442
S11IP_HUMAN	STK11IP	physical	28514442
LMA2L_HUMAN	LMAN2L	physical	28514442
TRI11_HUMAN	TRIM11	physical	28514442
CNPY3_HUMAN	CNPY3	physical	28514442
NNRD_HUMAN	CARKD	physical	28514442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.