FNBP1_HUMAN - dbPTM
FNBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FNBP1_HUMAN
UniProt AC Q96RU3
Protein Name Formin-binding protein 1
Gene Name FNBP1
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Membrane, clathrin-coated pit. Enriched in cortical regions coincident with F-actin. Also localiz
Protein Description May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL..
Protein Sequence MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS
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
27AcetylationWGIDILEKYIKFVKE
HHHHHHHHHHHHHHH		49.1619608861
27UbiquitinationWGIDILEKYIKFVKE
HHHHHHHHHHHHHHH		49.1619608861
27UbiquitinationWGIDILEKYIKFVKE
HHHHHHHHHHHHHHH		49.16-
44UbiquitinationEIELSYAKQLRNLSK
HHHHHHHHHHHHHHH		41.45-
44UbiquitinationEIELSYAKQLRNLSK
HHHHHHHHHHHHHHH		41.45-
51AcetylationKQLRNLSKKYQPKKN
HHHHHHHHHHCCCCC		59.6819809855
52AcetylationQLRNLSKKYQPKKNS
HHHHHHHHHCCCCCC		45.8219809867
57AcetylationSKKYQPKKNSKEEEE
HHHHCCCCCCHHHHH		73.4719809879
59PhosphorylationKYQPKKNSKEEEEYK
HHCCCCCCHHHHHHH		50.7728787133
66AcetylationSKEEEEYKYTSCKAF
CHHHHHHHHHHHHHH		45.3819608861
110AcetylationARYVQELKQERKSNF
HHHHHHHHHHHHHCC		49.7319608861
110UbiquitinationARYVQELKQERKSNF
HHHHHHHHHHHHHCC		49.7319608861
110AcetylationARYVQELKQERKSNF
HHHHHHHHHHHHHCC		49.73-
110UbiquitinationARYVQELKQERKSNF
HHHHHHHHHHHHHCC		49.73-
122AcetylationSNFHDGRKAQQHIET
HCCCCHHHHHHHHHH		56.9511921379
122UbiquitinationSNFHDGRKAQQHIET
HCCCCHHHHHHHHHH		56.95-
122UbiquitinationSNFHDGRKAQQHIET
HCCCCHHHHHHHHHH		56.95-
132AcetylationQHIETCWKQLESSKR
HHHHHHHHHHHHHHH		47.3419608861
132UbiquitinationQHIETCWKQLESSKR
HHHHHHHHHHHHHHH		47.3419608861
137PhosphorylationCWKQLESSKRRFERD
HHHHHHHHHHHHHHH		22.3224719451
158SulfoxidationAQQYFEKMDADINVT
HHHHHHHHCCCCCCC		3.9621406390
166UbiquitinationDADINVTKADVEKAR
CCCCCCCHHHHHHHH		38.0021906983
166UbiquitinationDADINVTKADVEKAR
CCCCCCCHHHHHHHH		38.0021906983
166 (in isoform 1)Ubiquitination-38.0021890473
166 (in isoform 2)Ubiquitination-38.0021890473
166 (in isoform 3)Ubiquitination-38.0021890473
166 (in isoform 4)Ubiquitination-38.0021890473
187UbiquitinationHQMAEDSKADYSSIL
HHHHHHCCCCHHHHH		58.56-
187UbiquitinationHQMAEDSKADYSSIL
HHHHHHCCCCHHHHH		58.56-
190PhosphorylationAEDSKADYSSILQKF
HHHCCCCHHHHHHHH		14.8028796482
191PhosphorylationEDSKADYSSILQKFN
HHCCCCHHHHHHHHC		16.0828796482
192PhosphorylationDSKADYSSILQKFNH
HCCCCHHHHHHHHCC		22.5328796482
196UbiquitinationDYSSILQKFNHEQHE
CHHHHHHHHCCCHHH		44.69-
196AcetylationDYSSILQKFNHEQHE
CHHHHHHHHCCCHHH		44.6925953088
232UbiquitinationVRMGESMKTYAEVDR
HHCCHHHHHHHHHHH		47.89-
232UbiquitinationVRMGESMKTYAEVDR
HHCCHHHHHHHHHHH		47.89-
233PhosphorylationRMGESMKTYAEVDRQ
HCCHHHHHHHHHHHH		21.2328796482
234PhosphorylationMGESMKTYAEVDRQV
CCHHHHHHHHHHHHH		8.6828796482
247UbiquitinationQVIPIIGKCLDGIVK
HHHHHHHHHHHHHHH		22.63-
247UbiquitinationQVIPIIGKCLDGIVK
HHHHHHHHHHHHHHH		22.63-
247AcetylationQVIPIIGKCLDGIVK
HHHHHHHHHHHHHHH		22.6325953088
254UbiquitinationKCLDGIVKAAESIDQ
HHHHHHHHHHHHCCC		39.70-
287PhosphorylationGDIEFEDYTQPMKRT
CCCCCCCCCCCCEEE		10.4828796482
288PhosphorylationDIEFEDYTQPMKRTV
CCCCCCCCCCCEEEC		38.2228796482
292UbiquitinationEDYTQPMKRTVSDNS
CCCCCCCEEECCCCC		52.15-
292UbiquitinationEDYTQPMKRTVSDNS
CCCCCCCEEECCCCC		52.15-
294PhosphorylationYTQPMKRTVSDNSLS
CCCCCEEECCCCCCC		20.8822167270
296PhosphorylationQPMKRTVSDNSLSNS
CCCEEECCCCCCCCC		30.3829255136
299PhosphorylationKRTVSDNSLSNSRGE
EEECCCCCCCCCCCC		37.8629255136
301PhosphorylationTVSDNSLSNSRGEGK
ECCCCCCCCCCCCCC		32.3629255136
303PhosphorylationSDNSLSNSRGEGKPD
CCCCCCCCCCCCCCC		37.9829255136
312UbiquitinationGEGKPDLKFGGKSKG
CCCCCCCCCCCCCCC		49.71-
312UbiquitinationGEGKPDLKFGGKSKG
CCCCCCCCCCCCCCC		49.71-
320AcetylationFGGKSKGKLWPFIKK
CCCCCCCCCCHHHHH		51.6323749302
320UbiquitinationFGGKSKGKLWPFIKK
CCCCCCCCCCHHHHH		51.6321890473
320AcetylationFGGKSKGKLWPFIKK
CCCCCCCCCCHHHHH		51.63-
320UbiquitinationFGGKSKGKLWPFIKK
CCCCCCCCCCHHHHH		51.63-
320UbiquitinationFGGKSKGKLWPFIKK
CCCCCCCCCCHHHHH		51.6321890473
320 (in isoform 1)Ubiquitination-51.6321890473
320 (in isoform 2)Ubiquitination-51.6321890473
320 (in isoform 3)Ubiquitination-51.6321890473
320 (in isoform 4)Ubiquitination-51.6321890473
326UbiquitinationGKLWPFIKKNKLMSL
CCCCHHHHHCCCHHH		51.1521890473
326UbiquitinationGKLWPFIKKNKLMSL
CCCCHHHHHCCCHHH		51.15-
326UbiquitinationGKLWPFIKKNKLMSL
CCCCHHHHHCCCHHH		51.1521890473
326 (in isoform 1)Ubiquitination-51.1521890473
326 (in isoform 2)Ubiquitination-51.1521890473
332PhosphorylationIKKNKLMSLLTSPHQ
HHHCCCHHHHCCCCC		30.5723403867
335PhosphorylationNKLMSLLTSPHQPPP
CCCHHHHCCCCCCCC		45.5723403867
336PhosphorylationKLMSLLTSPHQPPPP
CCHHHHCCCCCCCCC		21.9823403867
347PhosphorylationPPPPPPASASPSAVP
CCCCCCCCCCCCCCC		34.7426055452
349PhosphorylationPPPPASASPSAVPNG
CCCCCCCCCCCCCCC		19.5222167270
351PhosphorylationPPASASPSAVPNGPQ
CCCCCCCCCCCCCCC		39.1322167270
359PhosphorylationAVPNGPQSPKQQKEP
CCCCCCCCHHHHCCC		36.8822167270
364UbiquitinationPQSPKQQKEPLSHRF
CCCHHHHCCCCCHHH		59.82-
368UbiquitinationKQQKEPLSHRFNEFM
HHHCCCCCHHHHHHH		24.27-
375SulfoxidationSHRFNEFMTSKPKIH
CHHHHHHHHCCCCCH		3.1821406390
378AcetylationFNEFMTSKPKIHCFR
HHHHHHCCCCCHHHC		40.9625953088
378UbiquitinationFNEFMTSKPKIHCFR
HHHHHHCCCCCHHHC		40.96-
386PhosphorylationPKIHCFRSLKRGLSL
CCCHHHCHHCCCCCC		20.2820068231
392PhosphorylationRSLKRGLSLKLGATP
CHHCCCCCCCCCCCH		26.7022617229
393 (in isoform 2)Phosphorylation-6.8021815630
393 (in isoform 5)Phosphorylation-6.8021815630
398PhosphorylationLSLKLGATPEDFSNL
CCCCCCCCHHHHHCC		25.9721815630
403PhosphorylationGATPEDFSNLPPEQR
CCCHHHHHCCCHHHH		50.1820068231
423UbiquitinationQKVDELNKEIQKEMD
HHHHHHHHHHHHHHH		69.67-
448SulfoxidationVYLKNPQMGDPASLD
HHHCCCCCCCHHHHH		7.4821406390
453PhosphorylationPQMGDPASLDHKLAE
CCCCCHHHHHHHHHH		39.4527251275
457UbiquitinationDPASLDHKLAEVSQN
CHHHHHHHHHHHHHC		49.40-
457AcetylationDPASLDHKLAEVSQN
CHHHHHHHHHHHHHC		49.4025953088
467UbiquitinationEVSQNIEKLRVETQK
HHHHCHHHHHHHHHH		37.48-
467AcetylationEVSQNIEKLRVETQK
HHHHCHHHHHHHHHH		37.4825953088
497PhosphorylationSEQARRQSGLYDSQN
CHHHHHHCCCCCCCC		29.0223401153
500PhosphorylationARRQSGLYDSQNPPT
HHHHCCCCCCCCCCC		19.6429255136
502PhosphorylationRQSGLYDSQNPPTVN
HHCCCCCCCCCCCCC		20.5023927012
507PhosphorylationYDSQNPPTVNNCAQD
CCCCCCCCCCCCCCC		36.8023927012
517PhosphorylationNCAQDRESPDGSYTE
CCCCCCCCCCCCCCH		29.2322115753
521PhosphorylationDRESPDGSYTEEQSQ
CCCCCCCCCCHHHHH		35.9425159151
522PhosphorylationRESPDGSYTEEQSQE
CCCCCCCCCHHHHHH		24.5722115753
523PhosphorylationESPDGSYTEEQSQES
CCCCCCCCHHHHHHH		34.4422115753
527PhosphorylationGSYTEEQSQESEMKV
CCCCHHHHHHHHHEE		38.9128796482
530PhosphorylationTEEQSQESEMKVLAT
CHHHHHHHHHEEECC		35.0428796482
537PhosphorylationSEMKVLATDFDDEFD
HHHEEECCCCCCCCC		32.7926552605
554PhosphorylationEPLPAIGTCKALYTF
CCCCCCEEEEEEEEE		12.5326552605
578PhosphorylationVVEGETLYVIEEDKG
EEECCEEEEEEECCC		13.55-
600PhosphorylationRNEDEEGYVPTSYVE
CCCCCCCCCCCHHEE		13.41-
612UbiquitinationYVEVCLDKNAKDS--
HEEEEECCCCCCC--		45.95-
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 FNBP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FNBP1_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 FNBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNKS1_HUMANTNKSphysical
14596906
AKAP9_HUMANAKAP9physical
15047863
FNBP1_HUMANFNBP1physical
15252009
DYN1_HUMANDNM1physical
15252009
EGF_HUMANEGFphysical
15252009
TRFE_HUMANTFphysical
15252009
SNX2_HUMANSNX2physical
14596906
TNFL6_HUMANFASLGphysical
12023017
SNX2_HUMANSNX2physical
11438682
TBB5_HUMANTUBBphysical
19041431
WASP_HUMANWASphysical
19041431
WASL_HUMANWASLphysical
22939629
DYN2_HUMANDNM2physical
16418535
WASL_HUMANWASLphysical
16418535
FCHO1_HUMANFCHO1physical
26344197
MYO1E_HUMANMYO1Ephysical
26344197
SF3A1_HUMANSF3A1physical
26344197
DYN2_HUMANDNM2physical
15252009
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 FNBP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-66; LYS-110 ANDLYS-132, AND MASS SPECTROMETRY.
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-296; SER-299 ANDSER-359, AND MASS SPECTROMETRY.
"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-296 AND SER-299, ANDMASS SPECTROMETRY.
"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-296; SER-299; SER-349AND SER-359, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294; SER-296 ANDSER-299, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-522, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory