IFFO1_HUMAN - dbPTM
IFFO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFFO1_HUMAN
UniProt AC Q0D2I5
Protein Name Intermediate filament family orphan 1
Gene Name IFFO1
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization
Protein Description
Protein Sequence MNPLFGPNLFLLQQEQQGLAGPLGDSLGGDHFAGGGDLPPAPLSPAGPAAYSPPGPGPAPPAAMALRNDLGSNINVLKTLNLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLGRRDQAVQTGFVSPIRPLGLQLGARPAAVCSPSARVLGSPARSPAGPLAPSAASLSSSSTSTSTTYSSSARFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQDRVNELQEEAQEADACQEELALKVEQLKAELVVFKGLMSNNLSELDTKIQEKAMKVDMDICRRIDITAKLCDVAQQRNCEDMIQMFQVPSMGGRKRERKAAVEEDTSLSESEGPRQPDGDEEESTALSINEEMQRMLNQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRKSPAFTAVPLSDPPPPPSEAEDSDRDVSSDSSMR
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
78 (in isoform 5)Ubiquitination-46.84-
78UbiquitinationGSNINVLKTLNLRFR
CCCCHHHHHHCHHHH		46.84-
90UbiquitinationRFRCFLAKVHELERR
HHHHHHHHHHHHHHH		46.39-
103 (in isoform 5)Ubiquitination-57.17-
103UbiquitinationRRNRLLEKQLQQALE
HHHHHHHHHHHHHHH		57.17-
113 (in isoform 5)Ubiquitination-53.51-
113UbiquitinationQQALEEGKQGRRGLG
HHHHHHHHCCCCCCC		53.51-
128PhosphorylationRRDQAVQTGFVSPIR
HHHHHHHCCCCCCCC		26.4527732954
132PhosphorylationAVQTGFVSPIRPLGL
HHHCCCCCCCCCCCC		16.6130576142
150PhosphorylationARPAAVCSPSARVLG
CCCCEEECCCHHHHC		18.4526471730
152PhosphorylationPAAVCSPSARVLGSP
CCEEECCCHHHHCCC		16.6526471730
158PhosphorylationPSARVLGSPARSPAG
CCHHHHCCCCCCCCC		15.9526437602
170PhosphorylationPAGPLAPSAASLSSS
CCCCCCCCHHHCCCC		30.75-
173PhosphorylationPLAPSAASLSSSSTS
CCCCCHHHCCCCCCC		28.62-
177PhosphorylationSAASLSSSSTSTSTT
CHHHCCCCCCCCCCC		33.97-
235PhosphorylationGVQIDTITPEIRALY
CEECCCCCHHHHHHH		19.5724719451
247 (in isoform 1)Ubiquitination-44.0921890473
247UbiquitinationALYNVLAKVKRERDE
HHHHHHHHHHHHHHH		44.0921890473
247 (in isoform 3)Ubiquitination-44.0921890473
247 (in isoform 4)Ubiquitination-44.0921890473
247 (in isoform 5)Ubiquitination-44.0921890473
249UbiquitinationYNVLAKVKRERDEYK
HHHHHHHHHHHHHHH		48.08-
293UbiquitinationCQEELALKVEQLKAE
HHHHHHHHHHHHHHH		37.81-
293 (in isoform 5)Ubiquitination-37.81-
305 (in isoform 5)Ubiquitination-39.25-
305UbiquitinationKAELVVFKGLMSNNL
HHHHHHHHHHHHCCH		39.25-
309PhosphorylationVVFKGLMSNNLSELD
HHHHHHHHCCHHHHC		27.8429978859
313PhosphorylationGLMSNNLSELDTKIQ
HHHHCCHHHHCHHHH		37.9329978859
317PhosphorylationNNLSELDTKIQEKAM
CCHHHHCHHHHHHHH		42.5529978859
318 (in isoform 5)Ubiquitination-41.90-
318UbiquitinationNLSELDTKIQEKAMK
CHHHHCHHHHHHHHH		41.90-
325UbiquitinationKIQEKAMKVDMDICR
HHHHHHHHCCHHHHH		39.69-
337PhosphorylationICRRIDITAKLCDVA
HHHHCHHHHHHHHHH		17.62-
339UbiquitinationRRIDITAKLCDVAQQ
HHCHHHHHHHHHHHH		40.78-
358 (in isoform 5)Ubiquitination-2.31-
359 (in isoform 5)Ubiquitination-14.07-
362 (in isoform 7)Phosphorylation-36.7727251275
363PhosphorylationFQVPSMGGRKRERKA
HCCCCCCCCHHHHHH		24.2427251275
363 (in isoform 5)Phosphorylation-24.2427251275
363 (in isoform 4)Phosphorylation-24.2427251275
376PhosphorylationKAAVEEDTSLSESEG
HHHHCCCCCCCCCCC		34.5426471730
377PhosphorylationAAVEEDTSLSESEGP
HHHCCCCCCCCCCCC		42.0725850435
379PhosphorylationVEEDTSLSESEGPRQ
HCCCCCCCCCCCCCC		38.5525850435
381PhosphorylationEDTSLSESEGPRQPD
CCCCCCCCCCCCCCC		44.4725850435
382PhosphorylationDTSLSESEGPRQPDG
CCCCCCCCCCCCCCC		69.99-
464UbiquitinationKVIKDTESLFKTREK
HHHHHHHHHHHHCHH		40.99-
464PhosphorylationKVIKDTESLFKTREK
HHHHHHHHHHHHCHH		40.9924719451
464 (in isoform 5)Ubiquitination-40.99-
471UbiquitinationSLFKTREKEYQETID
HHHHHCHHHHHHHHH		59.43-
471 (in isoform 5)Ubiquitination-59.43-
488UbiquitinationELELATAKNDMNRHL
HHHHHHHCHHHHHHH		49.48-
492UbiquitinationATAKNDMNRHLHEYM
HHHCHHHHHHHHHHH		30.96-
492 (in isoform 5)Ubiquitination-30.96-
498PhosphorylationMNRHLHEYMEMCSMK
HHHHHHHHHHHHHHH		6.39-
503PhosphorylationHEYMEMCSMKRGLDV
HHHHHHHHHHCCCCH		26.48-
509UbiquitinationCSMKRGLDVQMETCR
HHHHCCCCHHHHHHH		31.27-
527PhosphorylationTQSGDRKSPAFTAVP
HCCCCCCCCCEEEEE		23.5026471730
531PhosphorylationDRKSPAFTAVPLSDP
CCCCCCEEEEECCCC		28.9326471730
536PhosphorylationAFTAVPLSDPPPPPS
CEEEEECCCCCCCCC		41.8426471730
543PhosphorylationSDPPPPPSEAEDSDR
CCCCCCCCCCCCCCC		56.0326471730
548PhosphorylationPPSEAEDSDRDVSSD
CCCCCCCCCCCCCCC		26.5026471730
553PhosphorylationEDSDRDVSSDSSMR-
CCCCCCCCCCCCCC-		32.4926471730
554PhosphorylationDSDRDVSSDSSMR--
CCCCCCCCCCCCC--		41.1626471730
556PhosphorylationDRDVSSDSSMR----
CCCCCCCCCCC----		28.1626471730
557PhosphorylationRDVSSDSSMR-----
CCCCCCCCCC-----		24.4626471730
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 IFFO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFFO1_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 IFFO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RN183_HUMANRNF183physical
16189514
TCHP_HUMANTCHPphysical
21516116
AMOL1_HUMANAMOTL1physical
27173435
COBL1_HUMANCOBLL1physical
27173435
CDAC1_HUMANCDADC1physical
27173435
SCML1_HUMANSCML1physical
27173435
HMBX1_HUMANHMBOX1physical
27173435
DDHD1_HUMANDDHD1physical
27173435
UH1BL_HUMANUHRF1BP1Lphysical
27173435
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFFO1_HUMAN

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Related Literatures of Post-Translational Modification

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