FLOT2_HUMAN - dbPTM
FLOT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLOT2_HUMAN
UniProt AC Q14254
Protein Name Flotillin-2
Gene Name FLOT2
Organism Homo sapiens (Human).
Sequence Length 428
Subcellular Localization Cell membrane
Peripheral membrane protein . Membrane, caveola
Peripheral membrane protein . Endosome . Membrane
Lipid-anchor . Membrane-associated protein of caveolae.
Protein Description May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. May be involved in epidermal cell adhesion and epidermal structure and function..
Protein Sequence MGNCHTVGPNEALVVSGGCCGSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAELPASVHALTGVDLSKIPLIKKATGVQV
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
2Myristoylation------MGNCHTVGP
------CCCCCCCCC		45.5325255805
4S-palmitoylation----MGNCHTVGPNE
----CCCCCCCCCCC		2.0522081607
19S-palmitoylationALVVSGGCCGSDYKQ
EEEEECCCCCCCHHH		2.4422081607
20S-palmitoylationLVVSGGCCGSDYKQY
EEEECCCCCCCHHHH		7.0822081607
81UbiquitinationQVKIMTEKELLAVAC
EEEECCHHHHHHHHH		44.4921890473
812-HydroxyisobutyrylationQVKIMTEKELLAVAC
EEEECCHHHHHHHHH		44.49-
88S-palmitoylationKELLAVACEQFLGKN
HHHHHHHHHHHCCCC		3.2029575903
942-HydroxyisobutyrylationACEQFLGKNVQDIKN
HHHHHCCCCHHHHHH		56.97-
100UbiquitinationGKNVQDIKNVVLQTL
CCCHHHHHHHHHHHH		52.5621890473
124PhosphorylationTLTVEQIYQDRDQFA
CCCHHHHHCCHHHHH		12.21-
127MethylationVEQIYQDRDQFAKLV
HHHHHCCHHHHHHHH		24.89-
132UbiquitinationQDRDQFAKLVREVAA
CCHHHHHHHHHHHHC		49.13-
1322-HydroxyisobutyrylationQDRDQFAKLVREVAA
CCHHHHHHHHHHHHC		49.13-
155UbiquitinationEILSFTIKDVYDKVD
EEEEEEHHHHHHHHH		37.7821890473
158PhosphorylationSFTIKDVYDKVDYLS
EEEHHHHHHHHHHHH		21.8527307780
160AcetylationTIKDVYDKVDYLSSL
EHHHHHHHHHHHHHC		21.2226051181
1602-HydroxyisobutyrylationTIKDVYDKVDYLSSL
EHHHHHHHHHHHHHC		21.22-
160UbiquitinationTIKDVYDKVDYLSSL
EHHHHHHHHHHHHHC		21.2221890473
163PhosphorylationDVYDKVDYLSSLGKT
HHHHHHHHHHHCCCC		16.0919258392
165PhosphorylationYDKVDYLSSLGKTQT
HHHHHHHHHCCCCEE		19.7928450419
166PhosphorylationDKVDYLSSLGKTQTA
HHHHHHHHCCCCEEE		38.2528355574
1692-HydroxyisobutyrylationDYLSSLGKTQTAVVQ
HHHHHCCCCEEEEHH		42.63-
169UbiquitinationDYLSSLGKTQTAVVQ
HHHHHCCCCEEEEHH		42.6321890473
170PhosphorylationYLSSLGKTQTAVVQR
HHHHCCCCEEEEHHC		29.3821406692
172PhosphorylationSSLGKTQTAVVQRDA
HHCCCCEEEEHHCCC		27.0121406692
192PhosphorylationEAERDAGIREAECKK
HHHHHHCCCHHHHHH		3.7417389395
197S-palmitoylationAGIREAECKKEMLDV
HCCCHHHHHHHHHCC		11.1329575903
210PhosphorylationDVKFMADTKIADSKR
CCCHHCCCCCCCHHH		18.1420726782
2112-HydroxyisobutyrylationVKFMADTKIADSKRA
CCHHCCCCCCCHHHH		36.12-
227PhosphorylationELQKSAFSEEVNIKT
HHHHHHCCCCCCHHH		32.3423917254
234PhosphorylationSEEVNIKTAEAQLAY
CCCCCHHHHHHHHHH		26.4021945579
241PhosphorylationTAEAQLAYELQGARE
HHHHHHHHHHHCHHH		26.2621945579
285PhosphorylationTDKELIATVRRPAEA
CCHHHHHHCCCHHHH		13.93-
305UbiquitinationQQIAEGEKVKQVLLA
HHHHCCCCHHHHHHH		66.64-
307UbiquitinationIAEGEKVKQVLLAQA
HHCCCCHHHHHHHHH		45.84-
3072-HydroxyisobutyrylationIAEGEKVKQVLLAQA
HHCCCCHHHHHHHHH		45.84-
335UbiquitinationAVIEAMGKAEAERMK
HHHHHCCHHHHHHHH		29.93-
344UbiquitinationEAERMKLKAEAYQKY
HHHHHHHHHHHHHHH		38.37-
3442-HydroxyisobutyrylationEAERMKLKAEAYQKY
HHHHHHHHHHHHHHH		38.37-
348PhosphorylationMKLKAEAYQKYGDAA
HHHHHHHHHHHHHHH		9.31-
350AcetylationLKAEAYQKYGDAAKM
HHHHHHHHHHHHHHH		38.2327452117
3502-HydroxyisobutyrylationLKAEAYQKYGDAAKM
HHHHHHHHHHHHHHH		38.23-
350UbiquitinationLKAEAYQKYGDAAKM
HHHHHHHHHHHHHHH		38.23-
351PhosphorylationKAEAYQKYGDAAKMA
HHHHHHHHHHHHHHH		12.5218180459
370UbiquitinationALPQIAAKIAAPLTK
HHHHHHHHHHCCCCC		24.6921890473
377UbiquitinationKIAAPLTKVDEIVVL
HHHCCCCCCCEEEEE		56.20-
385PhosphorylationVDEIVVLSGDNSKVT
CCEEEEECCCCHHHH		32.2730266825
389PhosphorylationVVLSGDNSKVTSEVN
EEECCCCHHHHHHHH		32.9930266825
390UbiquitinationVLSGDNSKVTSEVNR
EECCCCHHHHHHHHH		56.65-
392PhosphorylationSGDNSKVTSEVNRLL
CCCCHHHHHHHHHHH		23.94-
405PhosphorylationLLAELPASVHALTGV
HHHHCCCCHHHHCCC		16.7025255805
421UbiquitinationLSKIPLIKKATGVQV
HHHCCCCCCCCCCCC		44.00-
425UbiquitinationPLIKKATGVQV----
CCCCCCCCCCC----		16.8421890473
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
163YPhosphorylationKinaseFYNP06241
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
4CPalmitoylation

22081607
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 FLOT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RT14_HUMANMRPS14physical
22939629
VDAC2_HUMANVDAC2physical
22939629
CAVN1_HUMANPTRFphysical
22939629
HNRL2_HUMANHNRNPUL2physical
22939629
RAB2A_HUMANRAB2Aphysical
22939629
MMGT1_HUMANMMGT1physical
22939629
SSRA_HUMANSSR1physical
22939629
TOM40_HUMANTOMM40physical
22939629
GBG12_HUMANGNG12physical
22939629
VAMP2_HUMANVAMP2physical
22939629
PTH2_HUMANPTRH2physical
22939629
MAVS_HUMANMAVSphysical
22939629
VDAC1_HUMANVDAC1physical
22939629
NMNA1_HUMANNMNAT1physical
21988832
SPA24_HUMANSPATA24physical
21988832
TMM79_HUMANTMEM79physical
26186194
ABCB6_HUMANABCB6physical
26186194
TBC15_HUMANTBC1D15physical
26186194
MPZL3_HUMANMPZL3physical
26186194
DEGS1_HUMANDEGS1physical
26186194
MPC2_HUMANMPC2physical
26186194
S26A6_HUMANSLC26A6physical
26186194
TMM79_HUMANTMEM79physical
28514442
MPC2_HUMANMPC2physical
28514442
TBC15_HUMANTBC1D15physical
28514442
MPZL3_HUMANMPZL3physical
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 FLOT2_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded oninduction of neuronal differentiation in cultured cells.";
Li Y., Martin B.R., Cravatt B.F., Hofmann S.L.;
J. Biol. Chem. 287:523-530(2012).
Cited for: PALMITOYLATION AT CYS-4; CYS-19 AND CYS-20, AND MUTAGENESIS OF CYS-4;CYS-19 AND CYS-20.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-241, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-241, AND MASSSPECTROMETRY.

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