FTO_HUMAN - dbPTM
FTO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FTO_HUMAN
UniProt AC Q9C0B1
Protein Name Alpha-ketoglutarate-dependent dioxygenase FTO
Gene Name FTO
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Dioxygenase that repairs alkylated DNA and RNA by oxidative demethylation. Has highest activity towards single-stranded RNA containing 3-methyluracil, followed by single-stranded DNA containing 3-methylthymine. Has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. [PubMed: 18775698]
Protein Sequence MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCDDVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLPVEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP
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----MKRTPTAEERE
----CCCCCCHHHHH		21.3325159151
6Phosphorylation--MKRTPTAEERERE
--CCCCCCHHHHHHH		46.1926074081
32PhosphorylationDTWLPYLTPKDDEFY
HCCCCCCCCCCCHHH		23.58-
45UbiquitinationFYQQWQLKYPKLILR
HHHHHHHHCCHHHHH		44.3921890473
45 (in isoform 1)Ubiquitination-44.3921890473
48UbiquitinationQWQLKYPKLILREAS
HHHHHCCHHHHHHCC		45.1021890473
48 (in isoform 1)Ubiquitination-45.1021890473
55PhosphorylationKLILREASSVSEELH
HHHHHHCCCCCHHHH		26.9025159151
88UbiquitinationDLVRIQGKDLLTPVS
HHHHHCCCCCCCCCH		28.9121890473
88 (in isoform 1)Ubiquitination-28.9121890473
104S-nitrosylationILIGNPGCTYKYLNT
HHCCCCCCCCEEECC		3.8619483679
104S-nitrosocysteineILIGNPGCTYKYLNT
HHCCCCCCCCEEECC		3.86-
106PhosphorylationIGNPGCTYKYLNTRL
CCCCCCCCEEECCCE		11.17-
107 (in isoform 1)Ubiquitination-25.7121890473
107UbiquitinationGNPGCTYKYLNTRLF
CCCCCCCEEECCCEE		25.7121890473
108PhosphorylationNPGCTYKYLNTRLFT
CCCCCCEEECCCEEE		8.51-
121UbiquitinationFTVPWPVKGSNIKHT
EEECCCCCCCCCCCC		53.1721890473
121 (in isoform 1)Ubiquitination-53.1721890473
126UbiquitinationPVKGSNIKHTEAEIA
CCCCCCCCCCHHHHH		49.04-
150PhosphorylationNDYLQIETIQALEEL
HHHHHHHHHHHHHHH		21.73-
160UbiquitinationALEELAAKEKANEDA
HHHHHHHHHHCCCCC		54.89-
162UbiquitinationEELAAKEKANEDAVP
HHHHHHHHCCCCCCC		56.67-
173PhosphorylationDAVPLCMSADFPRVG
CCCCCCCCCCCCCCC		24.5625159151
183PhosphorylationFPRVGMGSSYNGQDE
CCCCCCCCCCCCCCC		22.2822199227
184PhosphorylationPRVGMGSSYNGQDEV
CCCCCCCCCCCCCCC		19.5221815630
185PhosphorylationRVGMGSSYNGQDEVD
CCCCCCCCCCCCCCC		25.6322199227
194 (in isoform 1)Ubiquitination-29.4421890473
194UbiquitinationGQDEVDIKSRAAYNV
CCCCCCCHHHHHEEE		29.4421906983
199PhosphorylationDIKSRAAYNVTLLNF
CCHHHHHEEEEEEEC		14.8020068231
202PhosphorylationSRAAYNVTLLNFMDP
HHHHEEEEEEECCCC		23.1420068231
211UbiquitinationLNFMDPQKMPYLKEE
EECCCCCCCCCCCCC		47.4321890473
211 (in isoform 1)Ubiquitination-47.4321890473
216UbiquitinationPQKMPYLKEEPYFGM
CCCCCCCCCCCCCCC		54.9419608861
216AcetylationPQKMPYLKEEPYFGM
CCCCCCCCCCCCCCC		54.9419608861
216SumoylationPQKMPYLKEEPYFGM
CCCCCCCCCCCCCCC		54.9419608861
216SumoylationPQKMPYLKEEPYFGM
CCCCCCCCCCCCCCC		54.94-
216 (in isoform 1)Ubiquitination-54.9421890473
220PhosphorylationPYLKEEPYFGMGKMA
CCCCCCCCCCCCCEE		18.95-
229PhosphorylationGMGKMAVSWHHDENL
CCCCEECEECCCCCC		15.9127251275
240O-linked_GlycosylationDENLVDRSAVAVYSY
CCCCCCHHHEEEEEE		23.7228510447
240PhosphorylationDENLVDRSAVAVYSY
CCCCCCHHHEEEEEE		23.7223312004
245PhosphorylationDRSAVAVYSYSCEGP
CHHHEEEEEEECCCC		7.6727732954
246PhosphorylationRSAVAVYSYSCEGPE
HHHEEEEEEECCCCC		12.1727732954
246O-linked_GlycosylationRSAVAVYSYSCEGPE
HHHEEEEEEECCCCC		12.1728510447
247PhosphorylationSAVAVYSYSCEGPEE
HHEEEEEEECCCCCC		10.3128985074
248PhosphorylationAVAVYSYSCEGPEEE
HEEEEEEECCCCCCC		10.3530206219
256PhosphorylationCEGPEEESEDDSHLE
CCCCCCCCCCCCCCC		49.9923401153
260PhosphorylationEEESEDDSHLEGRDP
CCCCCCCCCCCCCCC		42.1525159151
355PhosphorylationDVDNDDVSLKSFEPA
CCCCCCCCHHHCCCC		36.7520873877
414PhosphorylationWKKMEGVTNAVLHEV
HHHHCCHHHHHHHHH		28.4622210691
4222-HydroxyisobutyrylationNAVLHEVKREGLPVE
HHHHHHHHHCCCCHH		41.57-
441PhosphorylationILTAILASLTARQNL
HHHHHHHHHHHHHHH		23.8622210691
443PhosphorylationTAILASLTARQNLRR
HHHHHHHHHHHHHHH		19.8022210691
458PhosphorylationEWHARCQSRIARTLP
HHHHHHHHHHHHHCC		29.31-
469AcetylationRTLPADQKPECRPYW
HHCCCCCCCCCCCCC		43.2426822725
475PhosphorylationQKPECRPYWEKDDAS
CCCCCCCCCCCCCCC		13.5729396449
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
150TPhosphorylationKinaseCK2A1P68400
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FTO_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 FTO_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCCIP_HUMANBCCIPphysical
22863883
KCRB_HUMANCKBphysical
22863883
CNDP2_HUMANCNDP2physical
22863883
TKFC_HUMANDAKphysical
22863883
EF2_HUMANEEF2physical
22863883
LDHA_HUMANLDHAphysical
22863883
LDHB_HUMANLDHBphysical
22863883
MVD1_HUMANMVDphysical
22863883
NDRG1_HUMANNDRG1physical
22863883
PSA_HUMANNPEPPSphysical
22863883
NHRF1_HUMANSLC9A3R1physical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612938Growth retardation developmental delay coarse facies early death (GDFD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FTO_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND MASS SPECTROMETRY.

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