LRIG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LRIG2_HUMAN
• UniProt AC: O94898
• Protein Name: Leucine-rich repeats and immunoglobulin-like domains protein 2
• Gene Name: LRIG2
• Organism: Homo sapiens (Human).
• Sequence Length: 1065
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cytoplasm .
• Protein Sequence: MAPAPLGVPEEQLLGCRSRVLSRLLFIAQTALLLLPAAGAGLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPPDTAILDFSHNRLSNWNISLESQTLQEVKMNYNELTEIPYFGEPTSNITLLSLVHNIIPEINAQALQFYPALESLDLSSNIISEIKTSSFPRMQLKYLNLSNNRITTLEAGCFDNLSSSLLVVKLNRNRMSMIPPKIFKLPHLQFLELKRNRIKIVEGLTFQGLDSLRSLKMQRNGISKLKDGAFFGLNNMEELELEHNNLTRVNKGWLYGLRMLQQLYVSQNAIERISPDAWEFCQRLSELDLSYNQLTRLDESAFVGLSLLERLNLGDNRVTHIADGVFRFLSNLQTLDLRNNEISWAIEDASEAFAGLTSLTKLILQGNQIKSITKKAFIGLESLEHLDLNNNAIMSIQENAFSQTHLKELILNTSSLLCDCHLKWLLQWLVDNNFQHSVNVSCAHPEWLAGQSILNVDLKDFVCDDFLKPQIRTHPETIIALRGMNVTLTCTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQCIVTNHFGSNYSQKAKLTVNEMPSFLKTPMDLTIRTGAMARLECAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSCMAQNTAGGLSANASLTVLETPSFIRPLEDKTVTRGETAVLQCIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTCIMSNTLGTERGHIYLNVISSPNCDSSQSSIGHEDDGWTTVGIVIIVVVCCVVGTSLIWVIVIYHMRRKNEDYSITNTEELNLPADIPSYLSSQGTLSEPQEGYSNSEAGSHQQLMPPANGYIHKGTDGGTGTRVICSDCYDNANIYSRTREYCPYTYIAEEDVLDQTLSSLMVQMPKETYLVHPPQDTTALESLIPSANREPSAFPTNHERISEKKLPSTQMSGETLQRPVWNINRELGLPHPPFSQQPVHESPQLHQNEGLAGREPDCSASSMSCHRLQDHAFDFSRTRNIQDGSEGT

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
65	Phosphorylation	RRKLPAPSWRALSGL CCCCCCCCHHHHCCC	31.16	24719451
91	N-linked_Glycosylation	HNRLSNWNISLESQT CCCHHCCCEECCCHH	20.44	UniProtKB CARBOHYD
121	N-linked_Glycosylation	YFGEPTSNITLLSLV CCCCCCCCEEHHHHH	33.47	UniProtKB CARBOHYD
163	Phosphorylation	ISEIKTSSFPRMQLK HHHHHHCCCCHHEEE	44.49	24719451
171	Phosphorylation	FPRMQLKYLNLSNNR CCHHEEEEEECCCCC	14.93	-
173	N-linked_Glycosylation	RMQLKYLNLSNNRIT HHEEEEEECCCCCEE	38.03	UniProtKB CARBOHYD
175	Phosphorylation	QLKYLNLSNNRITTL EEEEEECCCCCEEEE	30.87	-
189	N-linked_Glycosylation	LEAGCFDNLSSSLLV EECCCCCCCCCCEEE	22.90	UniProtKB CARBOHYD
191	Phosphorylation	AGCFDNLSSSLLVVK CCCCCCCCCCEEEEE	24.92	28258704
192	Phosphorylation	GCFDNLSSSLLVVKL CCCCCCCCCEEEEEC	28.33	28258704
205	Phosphorylation	KLNRNRMSMIPPKIF ECCCCCCCCCCHHHH	15.43	29083192
255	Ubiquitination	RNGISKLKDGAFFGL HCCCCCCCCCCEECC	58.83	-
274	N-linked_Glycosylation	ELELEHNNLTRVNKG HHCCHHCCCCCCCHH	44.70	UniProtKB CARBOHYD
295	Phosphorylation	MLQQLYVSQNAIERI HHHHHHHCCHHHHHH	12.26	-
441	N-linked_Glycosylation	HLKELILNTSSLLCD HHHHHHHHHHHHHHH	30.81	UniProtKB CARBOHYD
468	N-linked_Glycosylation	NNFQHSVNVSCAHPE CCCCCEEEEEECCHH	24.01	UniProtKB CARBOHYD
502	Phosphorylation	FLKPQIRTHPETIIA HCCHHHCCCHHHEEE	43.33	23286773
514	N-linked_Glycosylation	IIALRGMNVTLTCTA EEEECCCCEEEEEEE	26.84	UniProtKB CARBOHYD
531	Phosphorylation	SSDSPMSTVWRKDSE CCCCCCCEEEECCCE	20.17	23286773
541	Phosphorylation	RKDSEILYDVDTENF ECCCEEEEECCCHHH	21.41	24719451
545	Phosphorylation	EILYDVDTENFVRYW EEEEECCCHHHHHHH	32.45	24719451
571	N-linked_Glycosylation	ILHLFNVNFTDEGKY EEEEEECCCCCCCCE	34.89	UniProtKB CARBOHYD
589	N-linked_Glycosylation	VTNHFGSNYSQKAKL EECCCCCCCCHHEEE	40.63	UniProtKB CARBOHYD
603	Phosphorylation	LTVNEMPSFLKTPMD EEHHHCCHHHCCCCC	41.73	24719451
607	Phosphorylation	EMPSFLKTPMDLTIR HCCHHHCCCCCEEEC	26.45	24300666
612	Phosphorylation	LKTPMDLTIRTGAMA HCCCCCEEECCCCCH	12.26	24300666
687	N-linked_Glycosylation	TAGGLSANASLTVLE CCCCCCCCCEEEEEE	27.04	UniProtKB CARBOHYD
708	Phosphorylation	PLEDKTVTRGETAVL ECCCCCCCCCCEEEH	37.88	-
728	N-linked_Glycosylation	GSPAPRLNWTKDDGP CCCCCCCCCCCCCCC	45.72	UniProtKB CARBOHYD
731	Ubiquitination	APRLNWTKDDGPLLV CCCCCCCCCCCCEEE	45.49	-
774	Phosphorylation	IMSNTLGTERGHIYL EEECCCCCCCCEEEE	26.14	24719451
903	Phosphorylation	TGTRVICSDCYDNAN CCCEEEECCCCCCCC	21.42	28796482
906	Phosphorylation	RVICSDCYDNANIYS EEEECCCCCCCCCHH	19.75	28796482
912	Phosphorylation	CYDNANIYSRTREYC CCCCCCCHHHCCHHC	7.60	25884760
913	Phosphorylation	YDNANIYSRTREYCP CCCCCCHHHCCHHCC	24.31	28796482
918	Phosphorylation	IYSRTREYCPYTYIA CHHHCCHHCCCCEEE	8.74	-
923	Phosphorylation	REYCPYTYIAEEDVL CHHCCCCEEECHHHH	7.71	-
1062	Phosphorylation	TRNIQDGSEGT---- CCCCCCCCCCC----	40.94	23312004

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

Oops, there are no upstream regulatory protein records of LRIG2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LRIG2_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 LRIG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGFR_HUMAN	EGFR	physical	25353163

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615112: Urofacial syndrome 2 (UFS2)
• 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

Phosphorylation

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-906 AND TYR-912, ANDMASS SPECTROMETRY.
PubMed: 15592455