FLOT1_HUMAN - dbPTM
FLOT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLOT1_HUMAN
UniProt AC O75955
Protein Name Flotillin-1
Gene Name FLOT1
Organism Homo sapiens (Human).
Sequence Length 427
Subcellular Localization Cell membrane
Peripheral membrane protein . Endosome . Membrane, caveola
Peripheral membrane protein . Melanosome . Membrane raft . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Membrane-associ
Protein Description May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles..
Protein Sequence MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA
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
4Phosphorylation----MFFTCGPNEAM
----CCCCCCCCCEE		12.8024719451
19PhosphorylationVVSGFCRSPPVMVAG
EEECCCCCCCEEEEC		34.4323911959
23SulfoxidationFCRSPPVMVAGGRVF
CCCCCCEEEECCEEE		1.7928465586
34S-palmitoylationGRVFVLPCIQQIQRI
CEEEEEHHHHHHHHC		3.7129575903
51UbiquitinationNTLTLNVKSEKVYTR
CCEEEEECCCEEEEC		52.3921890473
51AcetylationNTLTLNVKSEKVYTR
CCEEEEECCCEEEEC		52.3926051181
51UbiquitinationNTLTLNVKSEKVYTR
CCEEEEECCCEEEEC		52.3921890473
56PhosphorylationNVKSEKVYTRHGVPI
EECCCEEEECCCCEE		14.77-
78UbiquitinationVKIQGQNKEMLAAAC
EEECCCCHHHHHHHH		36.29-
128PhosphorylationYKDRQKFSEQVFKVA
HHCHHHHHHHHHHHH		33.8720068231
136PhosphorylationEQVFKVASSDLVNMG
HHHHHHHHHHHHHCC		27.6328851738
137PhosphorylationQVFKVASSDLVNMGI
HHHHHHHHHHHHCCE		25.8128851738
145PhosphorylationDLVNMGISVVSYTLK
HHHHCCEEEEEEECC		15.6724260401
148PhosphorylationNMGISVVSYTLKDIH
HCCEEEEEEECCCCC		15.3928851738
149PhosphorylationMGISVVSYTLKDIHD
CCEEEEEEECCCCCC		12.41-
150PhosphorylationGISVVSYTLKDIHDD
CEEEEEEECCCCCCC		21.5928851738
160PhosphorylationDIHDDQDYLHSLGKA
CCCCCCHHHHHCCCH		10.7327794612
163PhosphorylationDDQDYLHSLGKARTA
CCCHHHHHCCCHHCH		35.9026055452
166MalonylationDYLHSLGKARTAQVQ
HHHHHCCCHHCHHHH		39.7326320211
166UbiquitinationDYLHSLGKARTAQVQ
HHHHHCCCHHCHHHH		39.73-
169PhosphorylationHSLGKARTAQVQKDA
HHCCCHHCHHHHHHH		26.7123532336
195UbiquitinationGIREAKAKQEKVSAQ
CHHHHHHHHHHHCHH		59.28-
200PhosphorylationKAKQEKVSAQYLSEI
HHHHHHHCHHHHHHH		22.2621945579
203PhosphorylationQEKVSAQYLSEIEMA
HHHHCHHHHHHHHHH		16.3521945579
205PhosphorylationKVSAQYLSEIEMAKA
HHCHHHHHHHHHHHH		31.4321945579
211UbiquitinationLSEIEMAKAQRDYEL
HHHHHHHHHHCCHHH		43.68-
216PhosphorylationMAKAQRDYELKKAAY
HHHHHCCHHHHHHHH		25.91-
220MethylationQRDYELKKAAYDIEV
HCCHHHHHHHHCCCC		51.37-
223PhosphorylationYELKKAAYDIEVNTR
HHHHHHHHCCCCCCH		23.4725884760
238PhosphorylationRAQADLAYQLQVAKT
HHHHHHHHHHHHHHH		19.6321945579
292PhosphorylationKPAEAERYKLERLAE
CHHHHHHHHHHHHHH		16.07-
302UbiquitinationERLAEAEKSQLIMQA
HHHHHHHHHHHHHHH		51.02-
303PhosphorylationRLAEAEKSQLIMQAE
HHHHHHHHHHHHHHH		23.0220068231
315PhosphorylationQAEAEAASVRMRGEA
HHHHHHHHHHHHHHH		19.8021399631
348PhosphorylationKAEAFQLYQEAAQLD
HHHHHHHHHHHHHHH		8.1027259358
374UbiquitinationEISGPLTSANKITLV
HHCCCCCCCCEEEEE		37.2121890473
379PhosphorylationLTSANKITLVSSGSG
CCCCCEEEEEECCCC		23.7920068231
382PhosphorylationANKITLVSSGSGTMG
CCEEEEEECCCCCCC		31.9029255136
383PhosphorylationNKITLVSSGSGTMGA
CEEEEEECCCCCCCC		29.5129255136
385PhosphorylationITLVSSGSGTMGAAK
EEEEECCCCCCCCHH		32.7929255136
387PhosphorylationLVSSGSGTMGAAKVT
EEECCCCCCCCHHHH		17.7129255136
392UbiquitinationSGTMGAAKVTGEVLD
CCCCCCHHHHHHHHH		39.53-
402PhosphorylationGEVLDILTRLPESVE
HHHHHHHHCCCHHHH		30.4128102081
407PhosphorylationILTRLPESVERLTGV
HHHCCCHHHHHHHCC		27.6020068231
422UbiquitinationSISQVNHKPLRTA--
CHHHCCCCCCCCC--		40.3121890473
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
56YPhosphorylationKinaseSRCP12931
PSP
149YPhosphorylationKinaseSRCP12931
PSP
160YPhosphorylationKinaseFYNP06241
PSP
315SPhosphorylationKinasePKCAP17252
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLOT1_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 FLOT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRBS1_HUMANSORBS1physical
15128873
SRBS2_HUMANSORBS2physical
15128873
CBL_HUMANCBLphysical
11001060
SRBS1_HUMANSORBS1physical
11001060
SRBS1_HUMANSORBS1physical
11481476
VINEX_HUMANSORBS3physical
11481476
SRBS1_HUMANSORBS1physical
17548467
FRS2_HUMANFRS2physical
22235335
TRIM5_MACMUTRIM5physical
20810659
FLOT2_HUMANFLOT2physical
22939629
RAB5C_HUMANRAB5Cphysical
22939629
LTOR2_HUMANLAMTOR2physical
22939629
S12A4_HUMANSLC12A4physical
22939629
CERS2_HUMANCERS2physical
22939629
S38A2_HUMANSLC38A2physical
22939629
PTH2_HUMANPTRH2physical
22939629
THIL_HUMANACAT1physical
22939629
NDUS6_HUMANNDUFS6physical
22939629
ILVBL_HUMANILVBLphysical
22939629
SE1L1_HUMANSEL1Lphysical
22939629
NPL4_HUMANNPLOC4physical
22939629
GBG12_HUMANGNG12physical
22939629
M2OM_HUMANSLC25A11physical
22939629
HM13_HUMANHM13physical
22939629
RT05_HUMANMRPS5physical
22939629
PICAL_HUMANPICALMphysical
22939629
ICT1_HUMANICT1physical
22939629
RM55_HUMANMRPL55physical
22939629
SCMC1_HUMANSLC25A24physical
22939629
VAMP2_HUMANVAMP2physical
22939629
OCAD1_HUMANOCIAD1physical
22939629
MRP1_HUMANABCC1physical
22939629
RT31_HUMANMRPS31physical
22939629
TBA1C_HUMANTUBA1Cphysical
22939629
LMAN2_HUMANLMAN2physical
22939629
RS15_HUMANRPS15physical
22939629
RAB31_HUMANRAB31physical
22939629
RM50_HUMANMRPL50physical
22939629
S10AA_HUMANS100A10physical
22939629
MAEA_HUMANMAEAphysical
22939629
YBOX1_HUMANYBX1physical
22939629
EMC1_HUMANEMC1physical
22939629
MA2A1_HUMANMAN2A1physical
22939629
RM38_HUMANMRPL38physical
22939629
CAV1_HUMANCAV1physical
22936677
YES_HUMANYES1physical
22936677
AURKB_HUMANAURKBphysical
20430883
INCE_HUMANINCENPphysical
20430883
CAV1_HUMANCAV1physical
25204797
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 FLOT1_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-385, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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 THR-387, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, AND MASSSPECTROMETRY.

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