FCHO2_HUMAN - dbPTM
FCHO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCHO2_HUMAN
UniProt AC Q0JRZ9
Protein Name F-BAR domain only protein 2
Gene Name FCHO2
Organism Homo sapiens (Human).
Sequence Length 810
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 (By similar
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 MVMAYFVENFWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIEKAAVKSKKATDTYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTVESLIQKFAESKGTGKERPGLIEFEECDTASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGYSIKPETNQNDTKENHFYSSSDSDSEDEEPKKYRIEIKPMHPNNSHHTMASLDELKVSIGNITLSPAISRHSPVQMNRNLSNEELTKSKPSAPPNEKGTSDLLAWDPLFGPSLDSSSSSSLTSSSSARPTTPLSVGTIVPPPRPASRPKLTSGKLSGINEIPRPFSPPVTSNTSPPPAAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDSNTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGVDFELVGTGYRLSLIKKRFATGRYLADC
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
22PhosphorylationNSGFDVLYHNMKHGQ
CCCCCEEEECCCCCC
7.3221253578
26MalonylationDVLYHNMKHGQISTK
CEEEECCCCCCCCHH
50.3126320211
44O-linked_GlycosylationDFVRERATIEEAYSR
HHHHHHHHHHHHHHH
34.8330379171
44PhosphorylationDFVRERATIEEAYSR
HHHHHHHHHHHHHHH
34.8318452278
55UbiquitinationAYSRSMTKLAKSASN
HHHHHHHHHHHHHCC
37.4922817900
58UbiquitinationRSMTKLAKSASNYSQ
HHHHHHHHHHCCCHH
57.9221890473
58UbiquitinationRSMTKLAKSASNYSQ
HHHHHHHHHHCCCHH
57.9222817900
58 (in isoform 1)Ubiquitination-57.9221890473
58 (in isoform 2)Ubiquitination-57.9221890473
59PhosphorylationSMTKLAKSASNYSQL
HHHHHHHHHCCCHHC
31.1828270605
61PhosphorylationTKLAKSASNYSQLGT
HHHHHHHCCCHHCCC
43.3128270605
63PhosphorylationLAKSASNYSQLGTFA
HHHHHCCCHHCCCCC
8.6928270605
64PhosphorylationAKSASNYSQLGTFAP
HHHHCCCHHCCCCCC
24.1528270605
68PhosphorylationSNYSQLGTFAPVWDV
CCCHHCCCCCCHHHH
25.8028270605
77UbiquitinationAPVWDVFKTSTEKLA
CCHHHHHHHCHHHHH
41.2232015554
82AcetylationVFKTSTEKLANCHLD
HHHHCHHHHHHCCHH
53.6526051181
992-HydroxyisobutyrylationRKLQELIKEVQKYGE
HHHHHHHHHHHHHCH
65.54-
99AcetylationRKLQELIKEVQKYGE
HHHHHHHHHHHHHCH
65.54178226245
99UbiquitinationRKLQELIKEVQKYGE
HHHHHHHHHHHHHCH
65.5429967540
103AcetylationELIKEVQKYGEEQVK
HHHHHHHHHCHHHHH
61.477711281
103UbiquitinationELIKEVQKYGEEQVK
HHHHHHHHHCHHHHH
61.4733845483
165UbiquitinationATQREIEKAAVKSKK
CCHHHHHHHHHHCCC
47.51-
174PhosphorylationAVKSKKATDTYKLYV
HHHCCCCCCHHHHHH
37.4429083192
176PhosphorylationKSKKATDTYKLYVEK
HCCCCCCHHHHHHHH
20.4329083192
177PhosphorylationSKKATDTYKLYVEKY
CCCCCCHHHHHHHHH
11.2129083192
180PhosphorylationATDTYKLYVEKYALA
CCCHHHHHHHHHHHH
11.4729083192
188UbiquitinationVEKYALAKADFEQKM
HHHHHHHHCHHHHHH
49.7129967540
194UbiquitinationAKADFEQKMTETAQK
HHCHHHHHHHHHHHH
40.3632015554
223UbiquitinationIIGSLSNAIKEIHLQ
HHHHHHHHHHHHHHH
15.7422817900
225UbiquitinationGSLSNAIKEIHLQIG
HHHHHHHHHHHHHHH
48.4822817900
227UbiquitinationLSNAIKEIHLQIGQV
HHHHHHHHHHHHHHH
3.1421963094
229UbiquitinationNAIKEIHLQIGQVHE
HHHHHHHHHHHHHHH
4.9521963094
248UbiquitinationNMANTTVESLIQKFA
HHCCHHHHHHHHHHH
37.4223000965
250UbiquitinationANTTVESLIQKFAES
CCHHHHHHHHHHHHH
2.8123000965
251UbiquitinationNTTVESLIQKFAESK
CHHHHHHHHHHHHHC
6.1123000965
253UbiquitinationTVESLIQKFAESKGT
HHHHHHHHHHHHCCC
39.2823000965
255UbiquitinationESLIQKFAESKGTGK
HHHHHHHHHHCCCCC
27.4723000965
258UbiquitinationIQKFAESKGTGKERP
HHHHHHHCCCCCCCC
52.5822817900
262AcetylationAESKGTGKERPGLIE
HHHCCCCCCCCCCEE
50.8426051181
262UbiquitinationAESKGTGKERPGLIE
HHHCCCCCCCCCCEE
50.8421890473
264UbiquitinationSKGTGKERPGLIEFE
HCCCCCCCCCCEEEE
33.7921890473
264UbiquitinationSKGTGKERPGLIEFE
HCCCCCCCCCCEEEE
33.7921890473
283AcetylationASAVEGIKPRKRKTF
CHHCCCCCCCCCCCC
50.0226051181
283UbiquitinationASAVEGIKPRKRKTF
CHHCCCCCCCCCCCC
50.0223000965
286UbiquitinationVEGIKPRKRKTFALP
CCCCCCCCCCCCCCC
67.7723000965
288UbiquitinationGIKPRKRKTFALPGI
CCCCCCCCCCCCCCC
51.5423000965
289PhosphorylationIKPRKRKTFALPGII
CCCCCCCCCCCCCCE
20.4127422710
297SumoylationFALPGIIKKEKDAES
CCCCCCEECCCCCCC
53.6228112733
297UbiquitinationFALPGIIKKEKDAES
CCCCCCEECCCCCCC
53.6221890473
297 (in isoform 1)Ubiquitination-53.6221890473
297 (in isoform 2)Ubiquitination-53.6221890473
304PhosphorylationKKEKDAESVECPDAD
ECCCCCCCCCCCCHH
25.5726657352
312PhosphorylationVECPDADSLNIPDVD
CCCCCHHHCCCCCCC
25.6525159151
323PhosphorylationPDVDEEGYSIKPETN
CCCCCCCCCCCCCCC
15.5320873877
324PhosphorylationDVDEEGYSIKPETNQ
CCCCCCCCCCCCCCC
34.6920873877
329PhosphorylationGYSIKPETNQNDTKE
CCCCCCCCCCCCCCC
51.1123927012
334PhosphorylationPETNQNDTKENHFYS
CCCCCCCCCCCCCCC
48.0523927012
340PhosphorylationDTKENHFYSSSDSDS
CCCCCCCCCCCCCCC
10.4924275569
341PhosphorylationTKENHFYSSSDSDSE
CCCCCCCCCCCCCCC
23.5625849741
342PhosphorylationKENHFYSSSDSDSED
CCCCCCCCCCCCCCC
27.1325849741
343PhosphorylationENHFYSSSDSDSEDE
CCCCCCCCCCCCCCC
34.8825849741
345PhosphorylationHFYSSSDSDSEDEEP
CCCCCCCCCCCCCCC
45.0125849741
347PhosphorylationYSSSDSDSEDEEPKK
CCCCCCCCCCCCCCE
51.3925849741
354PhosphorylationSEDEEPKKYRIEIKP
CCCCCCCEEEEEEEC
50.9432142685
361PhosphorylationKYRIEIKPMHPNNSH
EEEEEEECCCCCCCC
31.7932142685
367PhosphorylationKPMHPNNSHHTMASL
ECCCCCCCCCCCCCH
24.2428348404
370PhosphorylationHPNNSHHTMASLDEL
CCCCCCCCCCCHHHC
14.7132645325
380O-linked_GlycosylationSLDELKVSIGNITLS
CHHHCEEEECCEEEC
24.1630379171
380PhosphorylationSLDELKVSIGNITLS
CHHHCEEEECCEEEC
24.1625159151
385PhosphorylationKVSIGNITLSPAISR
EEEECCEEECCCHHH
25.7830266825
387PhosphorylationSIGNITLSPAISRHS
EECCEEECCCHHHCC
12.0219664994
391O-linked_GlycosylationITLSPAISRHSPVQM
EEECCCHHHCCCCCC
26.5030379171
391PhosphorylationITLSPAISRHSPVQM
EEECCCHHHCCCCCC
26.5029255136
394PhosphorylationSPAISRHSPVQMNRN
CCCHHHCCCCCCCCC
26.1722167270
403PhosphorylationVQMNRNLSNEELTKS
CCCCCCCCHHHHHCC
45.8329255136
408PhosphorylationNLSNEELTKSKPSAP
CCCHHHHHCCCCCCC
36.2330266825
410PhosphorylationSNEELTKSKPSAPPN
CHHHHHCCCCCCCCC
44.5624275569
444PhosphorylationSSSSSSLTSSSSARP
CCCCCCCCCCCCCCC
28.6327251275
445PhosphorylationSSSSSLTSSSSARPT
CCCCCCCCCCCCCCC
33.2527251275
446PhosphorylationSSSSLTSSSSARPTT
CCCCCCCCCCCCCCC
24.0727251275
447PhosphorylationSSSLTSSSSARPTTP
CCCCCCCCCCCCCCC
27.9928348404
448PhosphorylationSSLTSSSSARPTTPL
CCCCCCCCCCCCCCC
30.1928348404
452PhosphorylationSSSSARPTTPLSVGT
CCCCCCCCCCCCCEE
35.1825850435
453PhosphorylationSSSARPTTPLSVGTI
CCCCCCCCCCCCEEE
25.5526657352
455PhosphorylationSARPTTPLSVGTIVP
CCCCCCCCCCEEECC
6.4332142685
456PhosphorylationARPTTPLSVGTIVPP
CCCCCCCCCEEECCC
21.5020873877
459PhosphorylationTTPLSVGTIVPPPRP
CCCCCCEEECCCCCC
19.3520873877
460PhosphorylationTPLSVGTIVPPPRPA
CCCCCEEECCCCCCC
3.4432142685
468PhosphorylationVPPPRPASRPKLTSG
CCCCCCCCCCCCCCC
52.3726657352
473PhosphorylationPASRPKLTSGKLSGI
CCCCCCCCCCCCCCC
41.3721406692
474PhosphorylationASRPKLTSGKLSGIN
CCCCCCCCCCCCCCC
44.3522496350
478PhosphorylationKLTSGKLSGINEIPR
CCCCCCCCCCCCCCC
40.9023927012
488PhosphorylationNEIPRPFSPPVTSNT
CCCCCCCCCCCCCCC
30.8629255136
492PhosphorylationRPFSPPVTSNTSPPP
CCCCCCCCCCCCCCC
23.2529255136
493PhosphorylationPFSPPVTSNTSPPPA
CCCCCCCCCCCCCCC
38.0429255136
495PhosphorylationSPPVTSNTSPPPAAP
CCCCCCCCCCCCCCC
42.2329255136
496PhosphorylationPPVTSNTSPPPAAPL
CCCCCCCCCCCCCCC
39.3925159151
508PhosphorylationAPLARAESSSSISSS
CCCCCCCCCCCCCCC
34.2430278072
509PhosphorylationPLARAESSSSISSSA
CCCCCCCCCCCCCCC
21.4330278072
510PhosphorylationLARAESSSSISSSAS
CCCCCCCCCCCCCCC
40.7630278072
511PhosphorylationARAESSSSISSSASL
CCCCCCCCCCCCCCC
28.5623911959
513PhosphorylationAESSSSISSSASLSA
CCCCCCCCCCCCCCC
21.8630278072
514PhosphorylationESSSSISSSASLSAA
CCCCCCCCCCCCCCC
28.4030576142
515PhosphorylationSSSSISSSASLSAAN
CCCCCCCCCCCCCCC
18.3230278072
517PhosphorylationSSISSSASLSAANTP
CCCCCCCCCCCCCCC
25.4630278072
519PhosphorylationISSSASLSAANTPTV
CCCCCCCCCCCCCCE
23.8830278072
523PhosphorylationASLSAANTPTVGVSR
CCCCCCCCCCEECCC
18.6628857561
525PhosphorylationLSAANTPTVGVSRGP
CCCCCCCCEECCCCC
28.0523186163
529PhosphorylationNTPTVGVSRGPSPVS
CCCCEECCCCCCCCC
26.1223186163
533PhosphorylationVGVSRGPSPVSLGNQ
EECCCCCCCCCCCCC
40.5330278072
536PhosphorylationSRGPSPVSLGNQDTL
CCCCCCCCCCCCCCC
33.6630278072
542PhosphorylationVSLGNQDTLPVAVAL
CCCCCCCCCCHHHHH
24.1723663014
550PhosphorylationLPVAVALTESVNAYF
CCHHHHHHHHHHHHH
19.2425850435
552PhosphorylationVAVALTESVNAYFKG
HHHHHHHHHHHHHCC
18.5525850435
556PhosphorylationLTESVNAYFKGADPT
HHHHHHHHHCCCCCC
10.7126330541
608UbiquitinationISRLEQILPNAQLVF
HHHHHHHCCCCEEEE
2.4029967540
616PhosphorylationPNAQLVFSDPSQCDS
CCCEEEECCHHHCCC
40.9228387310
641UbiquitinationAVTVYLKKLSEQNPA
HHHHHHHHHHHCCCC
55.4329967540
651PhosphorylationEQNPAASYYNVDVLK
HCCCCHHEECEEEEE
8.37-
676PhosphorylationTPLNLATYWKCSAST
CCEEEECEEECCCCC
9.39-
678AcetylationLNLATYWKCSASTTD
EEEECEEECCCCCCC
14.117704225
682PhosphorylationTYWKCSASTTDLRVD
CEEECCCCCCCCEEE
18.6222798277
683PhosphorylationYWKCSASTTDLRVDY
EEECCCCCCCCEEEC
24.8528348404
684PhosphorylationWKCSASTTDLRVDYK
EECCCCCCCCEEECC
30.4624961811
711UbiquitinationSNIQVVVPVDGGVTN
HCCEEEEECCCCCCC
13.5832015554
739PhosphorylationMKAFWKLSSISEKSE
HHHHHHHHHCCCCCC
23.1527251275
740PhosphorylationKAFWKLSSISEKSEN
HHHHHHHHCCCCCCC
40.3427251275
744UbiquitinationKLSSISEKSENGGSG
HHHHCCCCCCCCCCC
57.1732015554
795PhosphorylationVGTGYRLSLIKKRFA
ECCCEEHHHHHHHHC
21.0324719451

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCHO2_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 FCHO2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPS15_HUMANEPS15physical
21762413
DAB2_HUMANDAB2physical
22323290

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 FCHO2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-403, 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-488; SER-510 ANDSER-511, 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-387 AND SER-403, ANDMASS SPECTROMETRY.

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