FCHO1_HUMAN - dbPTM
FCHO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCHO1_HUMAN
UniProt AC O14526
Protein Name F-BAR domain only protein 1
Gene Name FCHO1
Organism Homo sapiens (Human).
Sequence Length 889
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. Accordi
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. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors..
Protein Sequence MSYFGEHFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLLRKFAESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTCPEVDEEGFTVRPDVTQNSTAEPSRFSSSDSDFDDEEPRKFYVHIKPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQRPRSAPRTSSCAERLQSEEQVSKNLFGPPLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDSWVPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAGGDLMPAPADPTAREGLAAPPRRLRSRKVSCPLTRSNGDLSRSLSPSPLGSSAASTALERPSFLSQTGHGVSRGPSPVVLGSQDALPIATAFTEYVHAYFRGHSPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDPETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPLTNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEAGGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGVDLELVGSGYRMSLVKRRFATGMYLVSC
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
20PhosphorylationNHGFEVLYHSVKQGP
CCCEEEEEEEHHCCC		9.3823917254
30PhosphorylationVKQGPISTKELADFI
HHCCCCCHHHHHHHH		29.29-
31UbiquitinationKQGPISTKELADFIR
HCCCCCHHHHHHHHH		43.89-
80AcetylationVFRVSSDKLALCHLE
HHEECCCHHHHHHHH		37.297975485
97UbiquitinationRKLQDLIKDVLRYGE
HHHHHHHHHHHHHCH		49.43-
141PhosphorylationLPKSRENYLNRCMDQ
CCCCHHHHHHHHHHH		10.7019664994
155PhosphorylationQERLRRESTSQKEMD
HHHHHHHCCCHHHHH		31.39-
174PhosphorylationKTKKAAESLRRSVEK
HHHHHHHHHHHHHHH		23.5825999147
192UbiquitinationARADFEQKMLDSALR
HHHHHHHHHHHHHHH		33.94-
262UbiquitinationSKGTGREKPGPLDFE
HCCCCCCCCCCCCHH		54.64-
295PhosphorylationAFRLPGLSRREREPE
HHCCCCCCCCCCCCC		34.9023917254
343PhosphorylationTAEPSRFSSSDSDFD
CCCCCCCCCCCCCCC		28.0225262027
344PhosphorylationAEPSRFSSSDSDFDD
CCCCCCCCCCCCCCC		35.1430108239
345PhosphorylationEPSRFSSSDSDFDDE
CCCCCCCCCCCCCCC		39.6825262027
347PhosphorylationSRFSSSDSDFDDEEP
CCCCCCCCCCCCCCC		41.9730108239
358PhosphorylationDEEPRKFYVHIKPAP
CCCCCEEEEEEECCC		8.3129978859
372PhosphorylationPARAPACSPEAAAAQ
CCCCCCCCHHHHHHH		28.0723401153
386PhosphorylationQLRATAGSLILPPGP
HHHHHCCCEECCCCC		15.12-
396PhosphorylationLPPGPGGTMKRHSSR
CCCCCCCCCCCCCCC		25.9927251275
397SulfoxidationPPGPGGTMKRHSSRD
CCCCCCCCCCCCCCC		3.9821406390
420PhosphorylationRSAPRTSSCAERLQS
CCCCCCCHHHHHHHC		19.41-
427PhosphorylationSCAERLQSEEQVSKN
HHHHHHHCHHHHHHH		47.9326552605
432PhosphorylationLQSEEQVSKNLFGPP
HHCHHHHHHHCCCCC		18.6027251275
475PhosphorylationSPENVEDSGLDSPSH
CCCCCCCCCCCCCCC		27.9626074081
479PhosphorylationVEDSGLDSPSHAAPG
CCCCCCCCCCCCCCC		33.0926074081
481PhosphorylationDSGLDSPSHAAPGPS
CCCCCCCCCCCCCCC		29.7026074081
491PhosphorylationAPGPSPDSWVPRPGT
CCCCCCCCCCCCCCC		33.1026074081
498PhosphorylationSWVPRPGTPQSPPSC
CCCCCCCCCCCCCCC		22.3426074081
501PhosphorylationPRPGTPQSPPSCRAP
CCCCCCCCCCCCCCC		39.7326074081
504PhosphorylationGTPQSPPSCRAPPPE
CCCCCCCCCCCCCCC		21.4426074081
523PhosphorylationRAPPLPDSPQPLASS
CCCCCCCCCCCCCCC		24.4028464451
529PhosphorylationDSPQPLASSPGPWGL
CCCCCCCCCCCCCCC		44.7628450419
530PhosphorylationSPQPLASSPGPWGLE
CCCCCCCCCCCCCCH		28.4128464451
552PhosphorylationMPAPADPTAREGLAA
CCCCCCCCHHCCCCC		38.6028122231
570PhosphorylationRLRSRKVSCPLTRSN
HHHCCCCCCCCCCCC		17.0423401153
574PhosphorylationRKVSCPLTRSNGDLS
CCCCCCCCCCCCCCC		19.7328450419
576PhosphorylationVSCPLTRSNGDLSRS
CCCCCCCCCCCCCCC		39.6724850871
581PhosphorylationTRSNGDLSRSLSPSP
CCCCCCCCCCCCCCC		25.2728985074
583PhosphorylationSNGDLSRSLSPSPLG
CCCCCCCCCCCCCCC		29.8022617229
585PhosphorylationGDLSRSLSPSPLGSS
CCCCCCCCCCCCCCC		25.2822115753
587PhosphorylationLSRSLSPSPLGSSAA
CCCCCCCCCCCCCHH		29.4022115753
591PhosphorylationLSPSPLGSSAASTAL
CCCCCCCCCHHHHHH		25.2025262027
592PhosphorylationSPSPLGSSAASTALE
CCCCCCCCHHHHHHH		26.5126074081
595PhosphorylationPLGSSAASTALERPS
CCCCCHHHHHHHCCH		17.5826074081
596PhosphorylationLGSSAASTALERPSF
CCCCHHHHHHHCCHH		30.4526074081
602PhosphorylationSTALERPSFLSQTGH
HHHHHCCHHHHCCCC		45.0726074081
605PhosphorylationLERPSFLSQTGHGVS
HHCCHHHHCCCCCCC		24.5626074081
607PhosphorylationRPSFLSQTGHGVSRG
CCHHHHCCCCCCCCC		27.9826074081
612PhosphorylationSQTGHGVSRGPSPVV
HCCCCCCCCCCCCEE		35.7929978859
616PhosphorylationHGVSRGPSPVVLGSQ
CCCCCCCCCEEECCC		32.9022115753
622PhosphorylationPSPVVLGSQDALPIA
CCCEEECCCCHHHHH		22.2628464451
630PhosphorylationQDALPIATAFTEYVH
CCHHHHHHHHHHHHH		24.0326074081
644PhosphorylationHAYFRGHSPSCLARV
HHHHCCCCHHHHHHC		22.7228122231
652PhosphorylationPSCLARVTGELTMTF
HHHHHHCCCEEEEEE		21.27-
677PhosphorylationTPPPPVLSFRLVHTT
CCCCCEEEEEEEEEH		14.4624719451
744PhosphorylationVLLRYQFSRPGPQSV
EEEEEEECCCCCCCC		23.2624719451
808PhosphorylationVRLQPAATWNLEEKR
EEECCCCCCCCCCCE		19.59-
814UbiquitinationATWNLEEKRLTWRLP
CCCCCCCCEEEEECC		43.25-
817PhosphorylationNLEEKRLTWRLPDVS
CCCCCEEEEECCCHH		16.75-
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 FCHO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCHO1_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 FCHO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT16_HUMANZBTB16physical
16169070
A4_HUMANAPPphysical
21832049
PPL13_HUMANLGALS14physical
25416956
EXOS5_HUMANEXOSC5physical
25416956
FCHO2_HUMANFCHO2physical
28514442
PCGF1_HUMANPCGF1physical
28514442
EPS15_HUMANEPS15physical
28514442
EP15R_HUMANEPS15L1physical
28514442
AP2A1_HUMANAP2A1physical
28514442
AP2A2_HUMANAP2A2physical
28514442
SRR_HUMANSRRphysical
28514442
AP1B1_HUMANAP1B1physical
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 FCHO1_HUMAN

loading...

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-616, AND MASSSPECTROMETRY.

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