FLRT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FLRT2_HUMAN
• UniProt AC: O43155
• Protein Name: Leucine-rich repeat transmembrane protein FLRT2
• Gene Name: FLRT2
• Organism: Homo sapiens (Human).
• Sequence Length: 660
• Subcellular Localization: Cell membrane ; Single-pass membrane protein . Endoplasmic reticulum membrane . Cell junction, focal adhesion . Secreted, extracellular space, extracellular matrix . Microsome membrane . Secreted . Cell junction, synapse, synaptosome . Proteolytic cl
• Protein Description: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis..
• Protein Sequence: MGLQTTKWPSHGAFFLKSWLIISLGLYSQVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFSNLRKLERLDISNNQLRMLTQGVFDNLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNMNLLSCPTTTPGLPLFTPAPSTASPTTQPPTLSIPNPSRSYTPPTPTTSKLPTIPDWDGRERVTPPISERIQLSIHFVNDTSIQVSWLSLFTVMAYKLTWVKMGHSLVGGIVQERIVSGEKQHLSLVNLEPRSTYRICLVPLDAFNYRAVEDTICSEATTHASYLNNGSNTASSHEQTTSHSMGSPFLLAGLIGGAVIFVLVVLLSVFCWHMHKKGRYTSQKWKYNRGRRKDDYCEAGTKKDNSILEMTETSFQIVSLNNDQLLKGDFRLQPIYTPNGGINYTDCHIPNNMRYCNSSVPDLEHCHT

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
10	Phosphorylation	LQTTKWPSHGAFFLK CCCCCCCCCHHHHHH	33.18	-
202	N-linked_Glycosylation	ISDMAFQNLTSLERL ECHHHHCCCCCCHHE	38.54	19159218
284	Phosphorylation	KLERLDISNNQLRML CCEEECCCHHHHHHH	29.42	-
292	Phosphorylation	NNQLRMLTQGVFDNL HHHHHHHHHHHHHCH	17.59	-
298	N-linked_Glycosylation	LTQGVFDNLSNLKQL HHHHHHHCHHHHHHH	33.63	UniProtKB CARBOHYD
300	Phosphorylation	QGVFDNLSNLKQLTA HHHHHCHHHHHHHHH	46.50	-
395	Phosphorylation	IPNPSRSYTPPTPTT CCCCCCCCCCCCCCC	23.35	-
407	O-linked_Glycosylation	PTTSKLPTIPDWDGR CCCCCCCCCCCCCCC	56.42	OGP
418	Phosphorylation	WDGRERVTPPISERI CCCCCCCCCCHHHCE	29.57	-
422	Phosphorylation	ERVTPPISERIQLSI CCCCCCHHHCEEEEE	26.96	-
433	N-linked_Glycosylation	QLSIHFVNDTSIQVS EEEEEECCCCCCCCH	45.99	UniProtKB CARBOHYD
487	Phosphorylation	LVNLEPRSTYRICLV EECCCCCCEEEEEEE	40.27	24043423
488	Phosphorylation	VNLEPRSTYRICLVP ECCCCCCEEEEEEEE	20.35	24043423
489	Phosphorylation	NLEPRSTYRICLVPL CCCCCCEEEEEEEEC	10.14	24043423
521	N-linked_Glycosylation	THASYLNNGSNTASS CCHHHHCCCCCCCCC	53.31	UniProtKB CARBOHYD
593	Phosphorylation	DDYCEAGTKKDNSIL CCCCCCCCCCCCCHH	41.80	-
628	Phosphorylation	DFRLQPIYTPNGGIN CEEECCEECCCCCCC	23.87	-
636	Phosphorylation	TPNGGINYTDCHIPN CCCCCCCCCCCCCCC	11.31	-
647	Phosphorylation	HIPNNMRYCNSSVPD CCCCCCCCCCCCCCC	5.80	28674419
650	Phosphorylation	NNMRYCNSSVPDLEH CCCCCCCCCCCCCCC	29.20	29449344
651	Phosphorylation	NMRYCNSSVPDLEHC CCCCCCCCCCCCCCC	24.55	24670416

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

Oops, there are no upstream regulatory protein records of FLRT2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FLRT2_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 FLRT2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of FLRT2_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

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202, AND MASSSPECTROMETRY.
PubMed: 19159218