FBP1L_HUMAN - dbPTM
FBP1L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBP1L_HUMAN
UniProt AC Q5T0N5
Protein Name Formin-binding protein 1-like
Gene Name FNBP1L
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cytoplasmic vesicle. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens..
Protein Sequence MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSVKMGPALEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS
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
2Phosphorylation------MSWGTELWD
------CCCCHHHHH		33.9228348404
5Phosphorylation---MSWGTELWDQFD
---CCCCHHHHHHHH		22.9628348404
44UbiquitinationEIEQNYAKQLRNLVK
HHHHHHHHHHHHHHH		39.23-
98PhosphorylationEEMAHRVYGELMRYA
HHHHHHHHHHHHHHH		12.58-
104PhosphorylationVYGELMRYAHDLKTE
HHHHHHHHHHHHHHH		8.36-
109UbiquitinationMRYAHDLKTERKMHL
HHHHHHHHHHHHHHH		55.16-
109AcetylationMRYAHDLKTERKMHL
HHHHHHHHHHHHHHH		55.1627452117
109UbiquitinationMRYAHDLKTERKMHL
HHHHHHHHHHHHHHH		55.16-
121UbiquitinationMHLQEGRKAQQYLDM
HHHHHHHHHHHHHHH		62.50-
121UbiquitinationMHLQEGRKAQQYLDM
HHHHHHHHHHHHHHH		62.50-
149UbiquitinationRECREAEKAQQSYER
HHHHHHHHHHHHHHH		59.55-
153PhosphorylationEAEKAQQSYERLDND
HHHHHHHHHHHHHCC		19.5128102081
154PhosphorylationAEKAQQSYERLDNDT
HHHHHHHHHHHHCCC		10.7528102081
161PhosphorylationYERLDNDTNATKADV
HHHHHCCCCCCHHHH		32.7628102081
165UbiquitinationDNDTNATKADVEKAK
HCCCCCCHHHHHHHH		39.93-
165UbiquitinationDNDTNATKADVEKAK
HCCCCCCHHHHHHHH		39.9321906983
165 (in isoform 1)Ubiquitination-39.9321906983
165 (in isoform 2)Ubiquitination-39.9321906983
165 (in isoform 3)Ubiquitination-39.9321906983
165 (in isoform 4)Ubiquitination-39.9321906983
165 (in isoform 5)Ubiquitination-39.9321906983
172UbiquitinationKADVEKAKQQLNLRT
HHHHHHHHHHHCHHH		50.04-
172UbiquitinationKADVEKAKQQLNLRT
HHHHHHHHHHHCHHH		50.04-
186 (in isoform 1)Ubiquitination-49.4621906983
186 (in isoform 2)Ubiquitination-49.4621906983
186UbiquitinationTHMADENKNEYAAQL
HHCCCCCHHHHHHHH		49.462190698
186 (in isoform 3)Ubiquitination-49.4621906983
186 (in isoform 4)Ubiquitination-49.4621906983
186 (in isoform 5)Ubiquitination-49.4621906983
186UbiquitinationTHMADENKNEYAAQL
HHCCCCCHHHHHHHH		49.46-
225UbiquitinationMDERRTIKLSECYRG
HHHHHCEEHHHHHCC		45.40-
264PhosphorylationSVDERRDSQMVVDSF
CCCCCHHHHHHHHHH		20.5428348404
266SulfoxidationDERRDSQMVVDSFKS
CCCHHHHHHHHHHHC		3.5221406390
272UbiquitinationQMVVDSFKSGFEPPG
HHHHHHHHCCCCCCC		54.33-
286PhosphorylationGDFPFEDYSQHIYRT
CCCCCCCCCHHEEEE		11.7521945579
287PhosphorylationDFPFEDYSQHIYRTI
CCCCCCCCHHEEEEC		27.8321945579
291PhosphorylationEDYSQHIYRTISDGT
CCCCHHEEEECCCCC		10.2821945579
293PhosphorylationYSQHIYRTISDGTIS
CCHHEEEECCCCCCC		14.0930266825
295PhosphorylationQHIYRTISDGTISAS
HHEEEECCCCCCCCC		29.4019664994
298PhosphorylationYRTISDGTISASKQE
EEECCCCCCCCCHHC		19.4230266825
300PhosphorylationTISDGTISASKQESG
ECCCCCCCCCHHCCC		26.7423927012
302PhosphorylationSDGTISASKQESGKM
CCCCCCCCHHCCCCC		28.2523927012
303UbiquitinationDGTISASKQESGKMD
CCCCCCCHHCCCCCC		58.77-
306PhosphorylationISASKQESGKMDAKT
CCCCHHCCCCCCCCC		41.0223403867
314PhosphorylationGKMDAKTTVGKAKGK
CCCCCCCCCCCCCCE		26.9330576142
321AcetylationTVGKAKGKLWLFGKK
CCCCCCCEEEECCCC		35.4625953088
321UbiquitinationTVGKAKGKLWLFGKK
CCCCCCCEEEECCCC		35.46-
422PhosphorylationNRELQKESDQKDALN
HHHHHHHHHHHHHHH		52.9924275569
441SulfoxidationVYEKNPQMGDPGSLQ
HHHHCCCCCCCCCCC		7.4821406390
473PhosphorylationHKNEAWLSEVEGKTG
HCCCHHHHHHCCCCC		28.97-
478UbiquitinationWLSEVEGKTGGRGDR
HHHHHCCCCCCCCCC		30.41-
488PhosphorylationGRGDRRHSSDINHLV
CCCCCCCHHHCCHHH		28.0929255136
489PhosphorylationRGDRRHSSDINHLVT
CCCCCCHHHCCHHHC		36.0629255136
496PhosphorylationSDINHLVTQGRESPE
HHCCHHHCCCCCCCC		31.5023927012
501PhosphorylationLVTQGRESPEGSYTD
HHCCCCCCCCCCCCC		27.2219664994
505PhosphorylationGRESPEGSYTDDANQ
CCCCCCCCCCCCCCC		24.1730266825
506PhosphorylationRESPEGSYTDDANQE
CCCCCCCCCCCCCCC		25.6630266825
507PhosphorylationESPEGSYTDDANQEV
CCCCCCCCCCCCCCC		29.1530266825
566PhosphorylationMKEGEVLYIIEEDKG
EECCEEEEEEEECCC		12.6724927040
577PhosphorylationEDKGDGWTRARRQNG
ECCCCCCCCCCCCCC		21.71-
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 FBP1L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBP1L_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 FBP1L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATG3_HUMANATG3physical
19342671
DYN2_HUMANDNM2physical
16418535
WASL_HUMANWASLphysical
16418535
PACN3_HUMANPACSIN3physical
26344197
SF3A1_HUMANSF3A1physical
26344197
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 FBP1L_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-295, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, 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-295; SER-488 ANDSER-501, AND MASS SPECTROMETRY.

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