LRFN3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LRFN3_HUMAN
• UniProt AC: Q9BTN0
• Protein Name: Leucine-rich repeat and fibronectin type-III domain-containing protein 3
• Gene Name: LRFN3
• Organism: Homo sapiens (Human).
• Sequence Length: 628
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Cell projection, axon. Cell projection, dendrite. Cell junction, synapse. Cell junction, synapse, presynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane.
• Protein Description: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity)..
• Protein Sequence: MAILPLLLCLLPLAPASSPPQSATPSPCPRRCRCQTQSLPLSVLCPGAGLLFVPPSLDRRAAELRLADNFIASVRRRDLANMTGLLHLSLSRNTIRHVAAGAFADLRALRALHLDGNRLTSLGEGQLRGLVNLRHLILSNNQLAALAAGALDDCAETLEDLDLSYNNLEQLPWEALGRLGNVNTLGLDHNLLASVPAGAFSRLHKLARLDMTSNRLTTIPPDPLFSRLPLLARPRGSPASALVLAFGGNPLHCNCELVWLRRLAREDDLEACASPPALGGRYFWAVGEEEFVCEPPVVTHRSPPLAVPAGRPAALRCRAVGDPEPRVRWVSPQGRLLGNSSRARAFPNGTLELLVTEPGDGGIFTCIAANAAGEATAAVELTVGPPPPPQLANSTSCDPPRDGDPDALTPPSAASASAKVADTGPPTDRGVQVTEHGATAALVQWPDQRPIPGIRMYQIQYNSSADDILVYRMIPAESRSFLLTDLASGRTYDLCVLAVYEDSATGLTATRPVGCARFSTEPALRPCGAPHAPFLGGTMIIALGGVIVASVLVFIFVLLMRYKVHGGQPPGKAKIPAPVSSVCSQTNGALGPTPTPAPPAPEPAALRAHTVVQLDCEPWGPGHEPVGP

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
24	O-linked_Glycosylation	SSPPQSATPSPCPRR CCCCCCCCCCCCCCC	29.55	OGP
81	N-linked_Glycosylation	VRRRDLANMTGLLHL HHHHHHHHCHHHEHH	35.53	UniProtKB CARBOHYD
89	Phosphorylation	MTGLLHLSLSRNTIR CHHHEHHHCCHHHHH	17.35	24719451
91	Phosphorylation	GLLHLSLSRNTIRHV HHEHHHCCHHHHHHH	21.80	22210691
218	Phosphorylation	MTSNRLTTIPPDPLF CCCCCCCCCCCCCHH	35.76	-
339	N-linked_Glycosylation	PQGRLLGNSSRARAF CCCCCCCCCHHCEEC	36.46	UniProtKB CARBOHYD
348	N-linked_Glycosylation	SRARAFPNGTLELLV HHCEECCCCCEEEEE	50.02	UniProtKB CARBOHYD
393	N-linked_Glycosylation	PPPPQLANSTSCDPP CCCCCCCCCCCCCCC	55.18	UniProtKB CARBOHYD
409	Phosphorylation	DGDPDALTPPSAASA CCCCCCCCCCCHHHH	34.57	27732954
412	Phosphorylation	PDALTPPSAASASAK CCCCCCCCHHHHCCE	37.36	27732954
415	Phosphorylation	LTPPSAASASAKVAD CCCCCHHHHCCEECC	23.60	27732954
417	Phosphorylation	PPSAASASAKVADTG CCCHHHHCCEECCCC	26.57	27732954
457	Phosphorylation	PIPGIRMYQIQYNSS CCCCEEEEEEEECCC	7.82	-
462	N-linked_Glycosylation	RMYQIQYNSSADDIL EEEEEEECCCCCCEE	17.08	UniProtKB CARBOHYD
463	Phosphorylation	MYQIQYNSSADDILV EEEEEECCCCCCEEE	23.20	-
464	Phosphorylation	YQIQYNSSADDILVY EEEEECCCCCCEEEE	31.89	-
503	Phosphorylation	VLAVYEDSATGLTAT EEEEEECCCCCCEEC	18.78	-
505	Phosphorylation	AVYEDSATGLTATRP EEEECCCCCCEECCC	36.35	-
580	Phosphorylation	AKIPAPVSSVCSQTN CCCCCCHHHHHCCCC	18.92	-

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

Oops, there are no upstream regulatory protein records of LRFN3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LRFN3_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 LRFN3_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LRFN3_HUMAN !!

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

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASSSPECTROMETRY.
PubMed: 17081983