UniProt ID | LONF3_HUMAN | |
---|---|---|
UniProt AC | Q496Y0 | |
Protein Name | LON peptidase N-terminal domain and RING finger protein 3 | |
Gene Name | LONRF3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 759 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MESVRIEQMLSLPAEVSSDNLESAERGASAAQVDMGPHPKVAAEGPAPLPTREPEQEQSPGTSTPESKVLLTQADALASRGRIREALEVYRQLSERQQLVAEQLEQLVRCLAEKVPQGEALAPAPPDEGSTASGTVAAEETGAAAAAAATEVWDGFKCRKCHGFLSDPVSLSCGHTFCKLCLERGRAADRRCALCGVKLSALMVATGRARGARRAGQQPPPPLRVNVVLSGLLGKLFPGPARASQLRHEGNRLYRERQVEAALLKYNEAVKLAPNDHLLYSNRSQIYFTLESHENALHDAEIACKLRPMGFKAHFRKAQALATLGKVEEALREFLYCVSLDGKNKRARCEAQRDNLELPHCSSQEEAAARGDGSSLMDPAKVKGDGQQHHMKDQEEEEEKWDATSPKAASSKTGKCQEKKRKHCQIESQEETGMPNKASKQDPPTDQGDKPALSLPLASFDASDLECALCMRLFYEPVTTPCGHTFCLKCLERCLDHNAKCPLCKDGLSQCLASRKYSKNVIMEELIAKFLPEELKERRKLYEEEMEELSNLNKNVPIFVCTMAYPTVPCPLHIFEPCYRLMIRRCIETGTRQFGMCLGDPVKGFAEYGCILEIRNVQFFADGRSVVDSIGKRRFRVLHQSQRDGYNTADIEYIEDQKVQGEDCAELMGLHNCVYQQASLWFHSLKLSLKNRILNHFGPMPEKDADPQMNPNGPAWCWWMLAVLPLESRAQLPFLAMRSLKDRLNGIRRVLAFISRNQN | |
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 |
---|---|---|---|---|---|
59 | Phosphorylation | REPEQEQSPGTSTPE CCCCCCCCCCCCCHH | 25.25 | 25627689 | |
62 | Phosphorylation | EQEQSPGTSTPESKV CCCCCCCCCCHHHHH | 32.58 | 23663014 | |
63 | Phosphorylation | QEQSPGTSTPESKVL CCCCCCCCCHHHHHH | 48.13 | 23663014 | |
64 | Phosphorylation | EQSPGTSTPESKVLL CCCCCCCCHHHHHHH | 30.80 | 23663014 | |
67 | Phosphorylation | PGTSTPESKVLLTQA CCCCCHHHHHHHHHH | 29.30 | 23663014 | |
271 | Ubiquitination | LKYNEAVKLAPNDHL HHHHHHHHCCCCCEE | 46.08 | - | |
317 | Ubiquitination | GFKAHFRKAQALATL CHHHHHHHHHHHHHH | 43.86 | - | |
404 | Phosphorylation | EEEKWDATSPKAASS HHHHCCCCCHHHHHC | 42.99 | 24300666 | |
405 | Phosphorylation | EEKWDATSPKAASSK HHHCCCCCHHHHHCC | 26.56 | 24300666 | |
410 | Phosphorylation | ATSPKAASSKTGKCQ CCCHHHHHCCCCCCH | 36.91 | - | |
411 | Phosphorylation | TSPKAASSKTGKCQE CCHHHHHCCCCCCHH | 29.52 | - | |
413 | Phosphorylation | PKAASSKTGKCQEKK HHHHHCCCCCCHHHH | 43.77 | - | |
422 | Acetylation | KCQEKKRKHCQIESQ CCHHHHHHHCCCCCC | 58.58 | 19813285 | |
428 | Phosphorylation | RKHCQIESQEETGMP HHHCCCCCCHHHCCC | 44.51 | - | |
432 | Phosphorylation | QIESQEETGMPNKAS CCCCCHHHCCCCCCC | 37.72 | - | |
437 | Acetylation | EETGMPNKASKQDPP HHHCCCCCCCCCCCC | 48.44 | 19813293 | |
440 | Acetylation | GMPNKASKQDPPTDQ CCCCCCCCCCCCCCC | 64.68 | 19813301 | |
475 | Phosphorylation | ALCMRLFYEPVTTPC HHHHHHHCCCCCCCC | 24.74 | 22461510 | |
480 | Phosphorylation | LFYEPVTTPCGHTFC HHCCCCCCCCCCHHH | 19.47 | 22461510 | |
519 | Ubiquitination | LASRKYSKNVIMEEL HHCCCCCCCCHHHHH | 52.74 | - | |
536 | Ubiquitination | KFLPEELKERRKLYE HHCHHHHHHHHHHHH | 53.07 | - | |
589 | Phosphorylation | MIRRCIETGTRQFGM HHHHHHHHCCCCCCC | 24.76 | - | |
591 | Phosphorylation | RRCIETGTRQFGMCL HHHHHHCCCCCCCCC | 28.81 | - | |
625 | Phosphorylation | QFFADGRSVVDSIGK EEECCCCCHHHCHHH | 31.83 | 22210691 |
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 LONF3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LONF3_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 LONF3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NT2NL_HUMAN | NOTCH2NL | physical | 25416956 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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