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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
4 | Phosphorylation | ----MKRTPTAEERE ----CCCCCCHHHHH | 21.33 | 25159151 | |
6 | Phosphorylation | --MKRTPTAEERERE --CCCCCCHHHHHHH | 46.19 | 26074081 | |
32 | Phosphorylation | DTWLPYLTPKDDEFY HCCCCCCCCCCCHHH | 23.58 | - | |
45 | Ubiquitination | FYQQWQLKYPKLILR HHHHHHHHCCHHHHH | 44.39 | 21890473 | |
45 (in isoform 1) | Ubiquitination | - | 44.39 | 21890473 | |
48 | Ubiquitination | QWQLKYPKLILREAS HHHHHCCHHHHHHCC | 45.10 | 21890473 | |
48 (in isoform 1) | Ubiquitination | - | 45.10 | 21890473 | |
55 | Phosphorylation | KLILREASSVSEELH HHHHHHCCCCCHHHH | 26.90 | 25159151 | |
88 | Ubiquitination | DLVRIQGKDLLTPVS HHHHHCCCCCCCCCH | 28.91 | 21890473 | |
88 (in isoform 1) | Ubiquitination | - | 28.91 | 21890473 | |
104 | S-nitrosylation | ILIGNPGCTYKYLNT HHCCCCCCCCEEECC | 3.86 | 19483679 | |
104 | S-nitrosocysteine | ILIGNPGCTYKYLNT HHCCCCCCCCEEECC | 3.86 | - | |
106 | Phosphorylation | IGNPGCTYKYLNTRL CCCCCCCCEEECCCE | 11.17 | - | |
107 (in isoform 1) | Ubiquitination | - | 25.71 | 21890473 | |
107 | Ubiquitination | GNPGCTYKYLNTRLF CCCCCCCEEECCCEE | 25.71 | 21890473 | |
108 | Phosphorylation | NPGCTYKYLNTRLFT CCCCCCEEECCCEEE | 8.51 | - | |
121 | Ubiquitination | FTVPWPVKGSNIKHT EEECCCCCCCCCCCC | 53.17 | 21890473 | |
121 (in isoform 1) | Ubiquitination | - | 53.17 | 21890473 | |
126 | Ubiquitination | PVKGSNIKHTEAEIA CCCCCCCCCCHHHHH | 49.04 | - | |
150 | Phosphorylation | NDYLQIETIQALEEL HHHHHHHHHHHHHHH | 21.73 | - | |
160 | Ubiquitination | ALEELAAKEKANEDA HHHHHHHHHHCCCCC | 54.89 | - | |
162 | Ubiquitination | EELAAKEKANEDAVP HHHHHHHHCCCCCCC | 56.67 | - | |
173 | Phosphorylation | DAVPLCMSADFPRVG CCCCCCCCCCCCCCC | 24.56 | 25159151 | |
183 | Phosphorylation | FPRVGMGSSYNGQDE CCCCCCCCCCCCCCC | 22.28 | 22199227 | |
184 | Phosphorylation | PRVGMGSSYNGQDEV CCCCCCCCCCCCCCC | 19.52 | 21815630 | |
185 | Phosphorylation | RVGMGSSYNGQDEVD CCCCCCCCCCCCCCC | 25.63 | 22199227 | |
194 (in isoform 1) | Ubiquitination | - | 29.44 | 21890473 | |
194 | Ubiquitination | GQDEVDIKSRAAYNV CCCCCCCHHHHHEEE | 29.44 | 21906983 | |
199 | Phosphorylation | DIKSRAAYNVTLLNF CCHHHHHEEEEEEEC | 14.80 | 20068231 | |
202 | Phosphorylation | SRAAYNVTLLNFMDP HHHHEEEEEEECCCC | 23.14 | 20068231 | |
211 | Ubiquitination | LNFMDPQKMPYLKEE EECCCCCCCCCCCCC | 47.43 | 21890473 | |
211 (in isoform 1) | Ubiquitination | - | 47.43 | 21890473 | |
216 | Ubiquitination | PQKMPYLKEEPYFGM CCCCCCCCCCCCCCC | 54.94 | 19608861 | |
216 | Acetylation | PQKMPYLKEEPYFGM CCCCCCCCCCCCCCC | 54.94 | 19608861 | |
216 | Sumoylation | PQKMPYLKEEPYFGM CCCCCCCCCCCCCCC | 54.94 | 19608861 | |
216 | Sumoylation | PQKMPYLKEEPYFGM CCCCCCCCCCCCCCC | 54.94 | - | |
216 (in isoform 1) | Ubiquitination | - | 54.94 | 21890473 | |
220 | Phosphorylation | PYLKEEPYFGMGKMA CCCCCCCCCCCCCEE | 18.95 | - | |
229 | Phosphorylation | GMGKMAVSWHHDENL CCCCEECEECCCCCC | 15.91 | 27251275 | |
240 | O-linked_Glycosylation | DENLVDRSAVAVYSY CCCCCCHHHEEEEEE | 23.72 | 28510447 | |
240 | Phosphorylation | DENLVDRSAVAVYSY CCCCCCHHHEEEEEE | 23.72 | 23312004 | |
245 | Phosphorylation | DRSAVAVYSYSCEGP CHHHEEEEEEECCCC | 7.67 | 27732954 | |
246 | Phosphorylation | RSAVAVYSYSCEGPE HHHEEEEEEECCCCC | 12.17 | 27732954 | |
246 | O-linked_Glycosylation | RSAVAVYSYSCEGPE HHHEEEEEEECCCCC | 12.17 | 28510447 | |
247 | Phosphorylation | SAVAVYSYSCEGPEE HHEEEEEEECCCCCC | 10.31 | 28985074 | |
248 | Phosphorylation | AVAVYSYSCEGPEEE HEEEEEEECCCCCCC | 10.35 | 30206219 | |
256 | Phosphorylation | CEGPEEESEDDSHLE CCCCCCCCCCCCCCC | 49.99 | 23401153 | |
260 | Phosphorylation | EEESEDDSHLEGRDP CCCCCCCCCCCCCCC | 42.15 | 25159151 | |
355 | Phosphorylation | DVDNDDVSLKSFEPA CCCCCCCCHHHCCCC | 36.75 | 20873877 | |
414 | Phosphorylation | WKKMEGVTNAVLHEV HHHHCCHHHHHHHHH | 28.46 | 22210691 | |
422 | 2-Hydroxyisobutyrylation | NAVLHEVKREGLPVE HHHHHHHHHCCCCHH | 41.57 | - | |
441 | Phosphorylation | ILTAILASLTARQNL HHHHHHHHHHHHHHH | 23.86 | 22210691 | |
443 | Phosphorylation | TAILASLTARQNLRR HHHHHHHHHHHHHHH | 19.80 | 22210691 | |
458 | Phosphorylation | EWHARCQSRIARTLP HHHHHHHHHHHHHCC | 29.31 | - | |
469 | Acetylation | RTLPADQKPECRPYW HHCCCCCCCCCCCCC | 43.24 | 26822725 | |
475 | Phosphorylation | QKPECRPYWEKDDAS CCCCCCCCCCCCCCC | 13.57 | 29396449 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
150 | T | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FTO_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
BCCIP_HUMAN | BCCIP | physical | 22863883 | |
KCRB_HUMAN | CKB | physical | 22863883 | |
CNDP2_HUMAN | CNDP2 | physical | 22863883 | |
TKFC_HUMAN | DAK | physical | 22863883 | |
EF2_HUMAN | EEF2 | physical | 22863883 | |
LDHA_HUMAN | LDHA | physical | 22863883 | |
LDHB_HUMAN | LDHB | physical | 22863883 | |
MVD1_HUMAN | MVD | physical | 22863883 | |
NDRG1_HUMAN | NDRG1 | physical | 22863883 | |
PSA_HUMAN | NPEPPS | physical | 22863883 | |
NHRF1_HUMAN | SLC9A3R1 | physical | 22863883 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
612938 | Growth 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. |
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Acetylation | |
Reference | PubMed |
"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. |