LRFN4_HUMAN - dbPTM
LRFN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRFN4_HUMAN
UniProt AC Q6PJG9
Protein Name Leucine-rich repeat and fibronectin type-III domain-containing protein 4
Gene Name LRFN4
Organism Homo sapiens (Human).
Sequence Length 635
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Promotes neurite outgrowth in hippocampal neurons. May play a role in redistributing DLG4 to the cell periphery (By similarity)..
Protein Sequence MAPPLLLLLLASGAAACPLPCVCQNLSESLSTLCAHRGLLFVPPNVDRRTVELRLADNFIQALGPPDFRNMTGLVDLTLSRNAITRIGARAFGDLESLRSLHLDGNRLVELGTGSLRGPVNLQHLILSGNQLGRIAPGAFDDFLESLEDLDLSYNNLRQVPWAGIGAMPALHTLNLDHNLIDALPPGAFAQLGQLSRLDLTSNRLATLAPDPLFSRGRDAEASPAPLVLSFSGNPLHCNCELLWLRRLARPDDLETCASPPGLAGRYFWAVPEGEFSCEPPLIARHTQRLWVLEGQRATLRCRALGDPAPTMHWVGPDDRLVGNSSRARAFPNGTLEIGVTGAGDAGGYTCIATNPAGEATARVELRVLALPHGGNSSAEGGRPGPSDIAASARTAAEGEGTLESEPAVQVTEVTATSGLVSWGPGRPADPVWMFQIQYNSSEDETLIYRIVPASSHHFLLKHLVPGADYDLCLLALSPAAGPSDLTATRLLGCAHFSTLPASPLCHALQAHVLGGTLTVAVGGVLVAALLVFTVALLVRGRGAGNGRLPLKLSHVQSQTNGGPSPTPKAHPPRSPPPRPQRSCSLDLGDAGCYGYARRLGGAWARRSHSVHGGLLGAGCRGVGGSAERLEESVV
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
25N-linked_GlycosylationPLPCVCQNLSESLST
CHHHHHCCHHHHHHH		40.17UniProtKB CARBOHYD
50PhosphorylationPPNVDRRTVELRLAD
CCCCCCCCEEEHHHH		21.1622210691
70N-linked_GlycosylationLGPPDFRNMTGLVDL
HCCCCHHCCCCCEEE		32.15UniProtKB CARBOHYD
78PhosphorylationMTGLVDLTLSRNAIT
CCCCEEEECCCCHHH		20.4424719451
324N-linked_GlycosylationPDDRLVGNSSRARAF
CCCCCCCCCCCCEEC		29.36UniProtKB CARBOHYD
333N-linked_GlycosylationSRARAFPNGTLEIGV
CCCEECCCCCEEEEC		50.02UniProtKB CARBOHYD
376N-linked_GlycosylationLALPHGGNSSAEGGR
EECCCCCCCCCCCCC		37.07UniProtKB CARBOHYD
377PhosphorylationALPHGGNSSAEGGRP
ECCCCCCCCCCCCCC		33.9122210691
378PhosphorylationLPHGGNSSAEGGRPG
CCCCCCCCCCCCCCC		34.0522210691
440N-linked_GlycosylationWMFQIQYNSSEDETL
EEEEEEECCCCCCEE		23.76UniProtKB CARBOHYD
558PhosphorylationLKLSHVQSQTNGGPS
EEEECEECCCCCCCC		37.5727732954
560PhosphorylationLSHVQSQTNGGPSPT
EECEECCCCCCCCCC		40.8727732954
565PhosphorylationSQTNGGPSPTPKAHP
CCCCCCCCCCCCCCC		44.6825159151
567PhosphorylationTNGGPSPTPKAHPPR
CCCCCCCCCCCCCCC		41.5828387310
575PhosphorylationPKAHPPRSPPPRPQR
CCCCCCCCCCCCCCC		47.7526329039
583PhosphorylationPPPRPQRSCSLDLGD
CCCCCCCCCCCCCCC		11.6522617229
585PhosphorylationPRPQRSCSLDLGDAG
CCCCCCCCCCCCCCH		26.6023401153
594PhosphorylationDLGDAGCYGYARRLG
CCCCCHHHHHHHHHC		16.5622817900
608PhosphorylationGGAWARRSHSVHGGL
CCCCCCCCCCCCCCC		17.9830576142
610PhosphorylationAWARRSHSVHGGLLG
CCCCCCCCCCCCCCC		19.6323401153
626PhosphorylationGCRGVGGSAERLEES
CCCCCCCCHHHHHHH		22.4923401153
633PhosphorylationSAERLEESVV-----
CHHHHHHHCC-----		20.8523401153
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 LRFN4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRFN4_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 LRFN4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NT2NL_HUMANNOTCH2NLphysical
25416956
CYTSA_HUMANSPECC1Lphysical
26186194
MY18A_HUMANMYO18Aphysical
26186194
AP2A1_HUMANAP2A1physical
26186194
AP2A2_HUMANAP2A2physical
26186194
AP1B1_HUMANAP1B1physical
26186194
FBX46_HUMANFBXO46physical
26186194
REPS1_HUMANREPS1physical
26186194
NCK2_HUMANNCK2physical
28514442
DYL1_HUMANDYNLL1physical
28514442
NCK1_HUMANNCK1physical
28514442
LEG1_HUMANLGALS1physical
28514442
GCP60_HUMANACBD3physical
28514442
DYL2_HUMANDYNLL2physical
28514442
LIGO1_HUMANLINGO1physical
28514442
DEP1A_HUMANDEPDC1physical
28514442
CE051_HUMANC5orf51physical
28514442
NSUN3_HUMANNSUN3physical
28514442
AT5G1_HUMANATP5G1physical
28514442
CHSS3_HUMANCHSY3physical
28514442
VINEX_HUMANSORBS3physical
28514442
TRIP6_HUMANTRIP6physical
28514442
UBP30_HUMANUSP30physical
28514442
UBP25_HUMANUSP25physical
28514442
CISD3_HUMANCISD3physical
28514442
TM39B_HUMANTMEM39Bphysical
28514442
LMBR1_HUMANLMBR1physical
28514442
S27A3_HUMANSLC27A3physical
28514442
HIP1R_HUMANHIP1Rphysical
28514442
MD2L2_HUMANMAD2L2physical
28514442
CIP2A_HUMANKIAA1524physical
28514442
LRFN1_HUMANLRFN1physical
28514442
HEAT3_HUMANHEATR3physical
28514442
SLIK5_HUMANSLITRK5physical
28514442
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.
Regulatory Network of LRFN4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASSSPECTROMETRY.

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