FCHO2_MOUSE - dbPTM
FCHO2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCHO2_MOUSE
UniProt AC Q3UQN2
Protein Name F-BAR domain only protein 2
Gene Name Fcho2
Organism Mus musculus (Mouse).
Sequence Length 809
Subcellular Localization Membrane, clathrin-coated pit
Peripheral membrane protein
Cytoplasmic side . Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2.
Protein Description Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor..
Protein Sequence MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPMWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYTAKCVEQERLKKEGATQREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAVKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGFSIKPEANQNDTKENHFYSSSDSDSEDEEPKRYRIEIKPAHPNNLHHTMASLDELKVSIGNITLSPAVSRHSPVQMNRNSSNEELTKSKPSSLPTEKGTNDLLAWDPLFGSSLESSSAPLTSSSSARPTTPLSLGTLVPPPRPASRPKLASGKLSGINEIPRPFSPPVTSNTSPPPTAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAIALTESVNAYFKGADPTKCIVKITGDVTISFPSGIIKVFTSNPSPAVLCFRVKNISRLEQILPNSQLVFSDPSQCDSNTKDFWMNMQAVTIYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSGISEKSDSGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGNTLSGVDIELVGTGYRLSLVKKRFATGRYLADC
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
78UbiquitinationPMWDVFKTSTEKLAN
CHHHHHHHCHHHHHH		29.4427667366
103UbiquitinationELIKEVQKYGEEQVK
HHHHHHHHHCHHHHH		61.4722790023
258AcetylationIQKFAESKGTGKERP
HHHHHHHCCCCCCCC		52.586568933
272UbiquitinationPGLIEFEECDPASAV
CCCEEEEECCHHHHC		49.9327667366
288UbiquitinationGIKPRKRKTFALPGI
CCCCCCCCCCCCCCC		51.5422790023
289PhosphorylationIKPRKRKTFALPGII
CCCCCCCCCCCCCCE		20.4126370283
297UbiquitinationFALPGIIKKEKDAES
CCCCCCEECCCCCCC		53.6222790023
304PhosphorylationKKEKDAESVECPDAD
ECCCCCCCCCCCCCC		25.5730352176
312PhosphorylationVECPDADSLNIPDVD
CCCCCCCCCCCCCCC		25.6527087446
324PhosphorylationDVDEEGFSIKPEANQ
CCCCCCCCCCCCCCC		40.3325619855
340PhosphorylationDTKENHFYSSSDSDS
CCCCCCCCCCCCCCC		10.4922324799
341PhosphorylationTKENHFYSSSDSDSE
CCCCCCCCCCCCCCC		23.5622324799
342PhosphorylationKENHFYSSSDSDSED
CCCCCCCCCCCCCCC		27.1322324799
343PhosphorylationENHFYSSSDSDSEDE
CCCCCCCCCCCCCCC		34.8822324799
345PhosphorylationHFYSSSDSDSEDEEP
CCCCCCCCCCCCCCC		45.0122324799
347PhosphorylationYSSSDSDSEDEEPKR
CCCCCCCCCCCCCCE		51.3922324799
370PhosphorylationHPNNLHHTMASLDEL
CCCCHHHCCCCHHHC		12.0429472430
373PhosphorylationNLHHTMASLDELKVS
CHHHCCCCHHHCEEE		26.0726824392
380PhosphorylationSLDELKVSIGNITLS
CHHHCEEEECCEEEC		24.1626643407
385PhosphorylationKVSIGNITLSPAVSR
EEEECCEEECCCHHC		25.7827087446
387PhosphorylationSIGNITLSPAVSRHS
EECCEEECCCHHCCC		11.3625521595
391PhosphorylationITLSPAVSRHSPVQM
EEECCCHHCCCCCCC		26.7827087446
394PhosphorylationSPAVSRHSPVQMNRN
CCCHHCCCCCCCCCC		26.1725521595
402PhosphorylationPVQMNRNSSNEELTK
CCCCCCCCCCHHHHC		31.1627087446
403PhosphorylationVQMNRNSSNEELTKS
CCCCCCCCCHHHHCC		52.3825521595
408PhosphorylationNSSNEELTKSKPSSL
CCCCHHHHCCCCCCC		36.2326643407
410PhosphorylationSNEELTKSKPSSLPT
CCHHHHCCCCCCCCC		44.5629472430
413PhosphorylationELTKSKPSSLPTEKG
HHHCCCCCCCCCCCC		48.5229472430
414PhosphorylationLTKSKPSSLPTEKGT
HHCCCCCCCCCCCCC		47.0629472430
417PhosphorylationSKPSSLPTEKGTNDL
CCCCCCCCCCCCCCC		56.4729472430
447PhosphorylationAPLTSSSSARPTTPL
CCCCCCCCCCCCCCC		30.19-
451PhosphorylationSSSSARPTTPLSLGT
CCCCCCCCCCCCCCC		35.1829472430
452PhosphorylationSSSARPTTPLSLGTL
CCCCCCCCCCCCCCC		25.5527742792
455PhosphorylationARPTTPLSLGTLVPP
CCCCCCCCCCCCCCC		26.4228066266
458PhosphorylationTTPLSLGTLVPPPRP
CCCCCCCCCCCCCCC		29.8520469934
467PhosphorylationVPPPRPASRPKLASG
CCCCCCCCCCCCCCC		52.3726824392
473PhosphorylationASRPKLASGKLSGIN
CCCCCCCCCCCCCCC		47.0724759943
477PhosphorylationKLASGKLSGINEIPR
CCCCCCCCCCCCCCC		40.9022942356
487PhosphorylationNEIPRPFSPPVTSNT
CCCCCCCCCCCCCCC		30.8625521595
491PhosphorylationRPFSPPVTSNTSPPP
CCCCCCCCCCCCCCC		23.2525521595
492PhosphorylationPFSPPVTSNTSPPPT
CCCCCCCCCCCCCCC		38.0422942356
494PhosphorylationSPPVTSNTSPPPTAP
CCCCCCCCCCCCCCC		42.2325521595
495PhosphorylationPPVTSNTSPPPTAPL
CCCCCCCCCCCCCCC		39.3925521595
499PhosphorylationSNTSPPPTAPLARAE
CCCCCCCCCCCCCCC		46.8320469934
507PhosphorylationAPLARAESSSSISSS
CCCCCCCCCCCCCCC		34.2427087446
508PhosphorylationPLARAESSSSISSSA
CCCCCCCCCCCCCCC		21.4325521595
509PhosphorylationLARAESSSSISSSAS
CCCCCCCCCCCCCCC		40.7625521595
510PhosphorylationARAESSSSISSSASL
CCCCCCCCCCCCCCC		28.5621082442
512PhosphorylationAESSSSISSSASLSA
CCCCCCCCCCCCCCC		21.8626239621
513PhosphorylationESSSSISSSASLSAA
CCCCCCCCCCCCCCC		28.4021082442
514PhosphorylationSSSSISSSASLSAAN
CCCCCCCCCCCCCCC		18.3221082442
516PhosphorylationSSISSSASLSAANTP
CCCCCCCCCCCCCCC		25.4621082442
518PhosphorylationISSSASLSAANTPTV
CCCCCCCCCCCCCCE		23.8826239621
522PhosphorylationASLSAANTPTVGVSR
CCCCCCCCCCEECCC		18.6623984901
524PhosphorylationLSAANTPTVGVSRGP
CCCCCCCCEECCCCC		28.0523984901
528PhosphorylationNTPTVGVSRGPSPVS
CCCCEECCCCCCCCC		26.1221183079
532PhosphorylationVGVSRGPSPVSLGNQ
EECCCCCCCCCCCCC		40.5326824392
535PhosphorylationSRGPSPVSLGNQDTL
CCCCCCCCCCCCCCC		33.6626745281
541PhosphorylationVSLGNQDTLPVAIAL
CCCCCCCCCCHHEEE		24.1726745281
562PhosphorylationYFKGADPTKCIVKIT
HHCCCCCCCEEEEEE		38.8128059163
585PhosphorylationSGIIKVFTSNPSPAV
CCEEEEEECCCCCEE		30.4923737553
586PhosphorylationGIIKVFTSNPSPAVL
CEEEEEECCCCCEEE		34.9723737553
589PhosphorylationKVFTSNPSPAVLCFR
EEEECCCCCEEEEEE		29.7323737553
679PhosphorylationLATYWKCSASTTDLR
EECEEECCCCCCCCE		22.8723737553
681PhosphorylationTYWKCSASTTDLRVD
CEEECCCCCCCCEEE		18.6230352176
682PhosphorylationYWKCSASTTDLRVDY
EEECCCCCCCCEEEC		24.8523737553
683PhosphorylationWKCSASTTDLRVDYK
EECCCCCCCCEEECC		30.4623737553
718UbiquitinationVDGGVTNMQSLPPAI
CCCCCCCHHHCCHHC		1.7727667366
743UbiquitinationKLSGISEKSDSGGSG
HHHCCCCCCCCCCCC		53.4222790023
794PhosphorylationVGTGYRLSLVKKRFA
ECCCEEEHHHHHHHC		23.3224719451
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 FCHO2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCHO2_MOUSE !!
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 FCHO2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FCHO2_MOUSEFcho2physical
21762413
ITSN1_RATItsn1physical
20448150
SYNJ1_RATSynj1physical
20448150
DYN1_RATDnm1physical
20448150
UBA1_RATUba1physical
20448150
DAB2_RATDab2physical
20448150
AP2A_HUMANTFAP2Aphysical
20448150
DAB2_HUMANDAB2physical
20448150
ITSN1_HUMANITSN1physical
20448150
ITSN2_HUMANITSN2physical
20448150
EPS15_HUMANEPS15physical
20448150
MYH9_HUMANMYH9physical
20448150
CLH1_HUMANCLTCphysical
20448150
FILA2_HUMANFLG2physical
20448150
ACTN4_HUMANACTN4physical
20448150
EP15R_HUMANEPS15L1physical
20448150
DYN1_HUMANDNM1physical
20448150
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FCHO2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-402; SER-403AND SER-508, AND MASS SPECTROMETRY.

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