FLRT3_HUMAN - dbPTM
FLRT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLRT3_HUMAN
UniProt AC Q9NZU0
Protein Name Leucine-rich repeat transmembrane protein FLRT3
Gene Name FLRT3
Organism Homo sapiens (Human).
Sequence Length 649
Subcellular Localization Cell membrane
Single-pass membrane protein . Endoplasmic reticulum membrane . Cell junction, focal adhesion . Secreted . Cell projection, axon . Detected on dendritic punctae that colocalize in part with glutamaergic synapses, but not with GABAergi
Protein Description Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion via its interaction with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. [PubMed: 26235030 Interaction with the intracellular domain of ROBO1 mediates axon attraction towards cells expressing NTN1. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5B, and possibly also other UNC-5 family members (By similarity Promotes neurite outgrowth (in vitro)]
Protein Sequence MISAAWSIFLIGTKIGLFLQVAPLSVMAKSCPSVCRCDAGFIYCNDRFLTSIPTGIPEDATTLYLQNNQINNAGIPSDLKNLLKVERIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPWGLPRTIEELRLDDNRISTISSPSLQGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTNLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWLQSLPVKVNVRGLMCQAPEKVRGMAIKDLNAELFDCKDSGIVSTIQITTAIPNTVYPAQGQWPAPVTKQPDIKNPKLTKDHQTTGSPSRKTITITVKSVTSDTIHISWKLALPMTALRLSWLKLGHSPAFGSITETIVTGERSEYLVTALEPDSPYKVCMVPMETSNLYLFDETPVCIETETAPLRMYNPTTTLNREQEKEPYKNPNLPLAAIIGGAVALVTIALLALVCWYVHRNGSLFSRNCAYSKGRRRKDDYAEAGTKKDNSILEIRETSFQMLPISNEPISKEEFVIHTIFPPNGMNLYKNNHSESSSNRSYRDSGIPDSDHSHS
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 Orthologous
Protein Cluster
3Phosphorylation-----MISAAWSIFL
-----CCHHHHHHHH		15.61-
7Phosphorylation-MISAAWSIFLIGTK
-CCHHHHHHHHHHCC		9.95-
13PhosphorylationWSIFLIGTKIGLFLQ
HHHHHHHCCHHHHHE		16.7030631047
84UbiquitinationSDLKNLLKVERIYLY
HHHHHHHHHEEEEEE		45.26-
191PhosphorylationDNRISTISSPSLQGL
CCCEECCCCCCHHCH		35.9623917254
192PhosphorylationNRISTISSPSLQGLT
CCEECCCCCCHHCHH		18.0423917254
194PhosphorylationISTISSPSLQGLTSL
EECCCCCCHHCHHHC		34.9623917254
226N-linked_GlycosylationKVFFNLVNLTELSLV
HHEEECCCHHHHHHH		44.4026235030
231PhosphorylationLVNLTELSLVRNSLT
CCCHHHHHHHHCCCC		20.7024719451
282N-linked_GlycosylationRLDMSNNNLSNLPQG
HHCCCCCCCCCCCCC		49.44UniProtKB CARBOHYD
296N-linked_GlycosylationGIFDDLDNITQLILR
CHHCCHHHHHHHHHH		46.64UniProtKB CARBOHYD
322PhosphorylationWVRDWLQSLPVKVNV
HHHHHHHHCCCEEEC		32.2522817900
358PhosphorylationELFDCKDSGIVSTIQ
HHHCCCCCCCEEEEE		18.86-
363PhosphorylationKDSGIVSTIQITTAI
CCCCCEEEEEEEECC		13.15-
402PhosphorylationKLTKDHQTTGSPSRK
CCCCCCCCCCCCCCC		29.7028270605
403PhosphorylationLTKDHQTTGSPSRKT
CCCCCCCCCCCCCCE		29.1428270605
405PhosphorylationKDHQTTGSPSRKTIT
CCCCCCCCCCCCEEE		20.0128270605
407PhosphorylationHQTTGSPSRKTITIT
CCCCCCCCCCEEEEE		48.3720068231
410PhosphorylationTGSPSRKTITITVKS
CCCCCCCEEEEEEEE		23.4228270605
412PhosphorylationSPSRKTITITVKSVT
CCCCCEEEEEEEECC		18.8128270605
414PhosphorylationSRKTITITVKSVTSD
CCCEEEEEEEECCCC		17.1528270605
417PhosphorylationTITITVKSVTSDTIH
EEEEEEEECCCCEEE		26.7020068231
419PhosphorylationTITVKSVTSDTIHIS
EEEEEECCCCEEEEE		28.1620068231
420PhosphorylationITVKSVTSDTIHISW
EEEEECCCCEEEEEE		30.5120068231
422PhosphorylationVKSVTSDTIHISWKL
EEECCCCEEEEEEEH		17.7720068231
426PhosphorylationTSDTIHISWKLALPM
CCCEEEEEEEHHHCH		12.1920068231
434PhosphorylationWKLALPMTALRLSWL
EEHHHCHHHHHHHHH		22.1720068231
510O-linked_GlycosylationPLRMYNPTTTLNREQ
CCCCCCCCCCCCHHH		28.8655824143
511O-linked_GlycosylationLRMYNPTTTLNREQE
CCCCCCCCCCCHHHH		30.4655824149
512O-linked_GlycosylationRMYNPTTTLNREQEK
CCCCCCCCCCHHHHC		25.2355824155
522PhosphorylationREQEKEPYKNPNLPL
HHHHCCCCCCCCCCH		25.21-
575PhosphorylationGRRRKDDYAEAGTKK
CCCCCCCCCCCCCCC		19.24-
580PhosphorylationDDYAEAGTKKDNSIL
CCCCCCCCCCCCCEE		41.80-
581UbiquitinationDYAEAGTKKDNSILE
CCCCCCCCCCCCEEE		58.1533845483
585PhosphorylationAGTKKDNSILEIRET
CCCCCCCCEEEEEEC		38.3930266825
592PhosphorylationSILEIRETSFQMLPI
CEEEEEECEEEEEEC		25.6230266825
593PhosphorylationILEIRETSFQMLPIS
EEEEEECEEEEEECC		14.5530266825
600PhosphorylationSFQMLPISNEPISKE
EEEEEECCCCCCCCC		32.9530266825
605PhosphorylationPISNEPISKEEFVIH
ECCCCCCCCCCEEEE		44.7425850435
606UbiquitinationISNEPISKEEFVIHT
CCCCCCCCCCEEEEE		63.08-
635PhosphorylationSESSSNRSYRDSGIP
CCCCCCCCCCCCCCC		28.8628857561
636PhosphorylationESSSNRSYRDSGIPD
CCCCCCCCCCCCCCC		18.4025002506
639PhosphorylationSNRSYRDSGIPDSDH
CCCCCCCCCCCCCCC		29.6225849741
644PhosphorylationRDSGIPDSDHSHS--
CCCCCCCCCCCCC--		31.6924719451
647PhosphorylationGIPDSDHSHS-----
CCCCCCCCCC-----		30.3424719451
649PhosphorylationPDSDHSHS-------
CCCCCCCC-------		44.9525627689
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of FLRT3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLRT3_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FLRT3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FLRT3_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615271Hypogonadotropic hypogonadism 21 with or without anosmia (HH21)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLRT3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND MASSSPECTROMETRY.

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