UniProt ID | REXO4_HUMAN | |
---|---|---|
UniProt AC | Q9GZR2 | |
Protein Name | RNA exonuclease 4 | |
Gene Name | REXO4 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 422 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | ||
Protein Sequence | MGKAKVPASKRAPSSPVAKPGPVKTLTRKKNKKKKRFWKSKAREVSKKPASGPGAVVRPPKAPEDFSQNWKALQEWLLKQKSQAPEKPLVISQMGSKKKPKIIQQNKKETSPQVKGEEMPAGKDQEASRGSVPSGSKMDRRAPVPRTKASGTEHNKKGTKERTNGDIVPERGDIEHKKRKAKEAAPAPPTEEDIWFDDVDPADIEAAIGPEAAKIARKQLGQSEGSVSLSLVKEQAFGGLTRALALDCEMVGVGPKGEESMAARVSIVNQYGKCVYDKYVKPTEPVTDYRTAVSGIRPENLKQGEELEVVQKEVAEMLKGRILVGHALHNDLKVLFLDHPKKKIRDTQKYKPFKSQVKSGRPSLRLLSEKILGLQVQQAEHCSIQDAQAAMRLYVMVKKEWESMARDRRPLLTAPDHCSDDA | |
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 |
---|---|---|---|---|---|
3 | Methylation | -----MGKAKVPASK -----CCCCCCCHHH | 43.68 | 116253741 | |
5 | Methylation | ---MGKAKVPASKRA ---CCCCCCCHHHCC | 52.84 | 116253745 | |
14 | Phosphorylation | PASKRAPSSPVAKPG CHHHCCCCCCCCCCC | 46.41 | 29255136 | |
15 | Phosphorylation | ASKRAPSSPVAKPGP HHHCCCCCCCCCCCC | 23.49 | 29255136 | |
19 | Acetylation | APSSPVAKPGPVKTL CCCCCCCCCCCCCCC | 51.22 | 26051181 | |
24 | Acetylation | VAKPGPVKTLTRKKN CCCCCCCCCCCCCCC | 40.73 | 25953088 | |
25 | Phosphorylation | AKPGPVKTLTRKKNK CCCCCCCCCCCCCCH | 33.33 | 26074081 | |
27 | Phosphorylation | PGPVKTLTRKKNKKK CCCCCCCCCCCCHHH | 45.75 | 26074081 | |
46 | Phosphorylation | KSKAREVSKKPASGP HHHHHHHHCCCCCCC | 30.15 | 20860994 | |
51 | Phosphorylation | EVSKKPASGPGAVVR HHHCCCCCCCCCCCC | 54.79 | - | |
82 | Phosphorylation | EWLLKQKSQAPEKPL HHHHHCHHCCCCCCE | 29.13 | 20860994 | |
87 | Acetylation | QKSQAPEKPLVISQM CHHCCCCCCEEEEEC | 42.46 | 25953088 | |
92 | Phosphorylation | PEKPLVISQMGSKKK CCCCEEEEECCCCCC | 13.46 | 25159151 | |
96 | Phosphorylation | LVISQMGSKKKPKII EEEEECCCCCCCHHH | 35.64 | 25159151 | |
97 | Acetylation | VISQMGSKKKPKIIQ EEEECCCCCCCHHHH | 60.12 | 25953088 | |
107 | 2-Hydroxyisobutyrylation | PKIIQQNKKETSPQV CHHHHCCCCCCCCCC | 47.88 | - | |
110 | Phosphorylation | IQQNKKETSPQVKGE HHCCCCCCCCCCCCC | 55.37 | 28176443 | |
111 | Phosphorylation | QQNKKETSPQVKGEE HCCCCCCCCCCCCCC | 17.90 | 25159151 | |
115 | Sumoylation | KETSPQVKGEEMPAG CCCCCCCCCCCCCCC | 56.19 | 28112733 | |
115 (in isoform 2) | Phosphorylation | - | 56.19 | 20860994 | |
115 | Sumoylation | KETSPQVKGEEMPAG CCCCCCCCCCCCCCC | 56.19 | - | |
116 (in isoform 2) | Phosphorylation | - | 36.92 | 20860994 | |
123 | Acetylation | GEEMPAGKDQEASRG CCCCCCCCCCCHHCC | 59.34 | 26051181 | |
128 | Phosphorylation | AGKDQEASRGSVPSG CCCCCCHHCCCCCCC | 36.10 | 24732914 | |
129 | Methylation | GKDQEASRGSVPSGS CCCCCHHCCCCCCCC | 48.75 | 115491155 | |
131 | Phosphorylation | DQEASRGSVPSGSKM CCCHHCCCCCCCCCC | 29.73 | 25159151 | |
136 | Phosphorylation | RGSVPSGSKMDRRAP CCCCCCCCCCCCCCC | 29.19 | 20860994 | |
163 | Phosphorylation | KKGTKERTNGDIVPE CCCCCCCCCCCCCCC | 44.65 | 21406692 | |
214 | Ubiquitination | AIGPEAAKIARKQLG HHCHHHHHHHHHHHC | 43.90 | - | |
223 | Phosphorylation | ARKQLGQSEGSVSLS HHHHHCCCCCCEEHH | 41.97 | 25159151 | |
226 | Phosphorylation | QLGQSEGSVSLSLVK HHCCCCCCEEHHHHH | 12.41 | 25159151 | |
228 | Phosphorylation | GQSEGSVSLSLVKEQ CCCCCCEEHHHHHHH | 17.59 | 24043423 | |
230 | Phosphorylation | SEGSVSLSLVKEQAF CCCCEEHHHHHHHHC | 24.50 | 24719451 | |
256 | Ubiquitination | EMVGVGPKGEESMAA EEECCCCCCCHHHHH | 73.38 | - | |
273 | Acetylation | SIVNQYGKCVYDKYV HHHHHCCCEECCCCC | 18.65 | 26051181 | |
278 | Acetylation | YGKCVYDKYVKPTEP CCCEECCCCCCCCCC | 33.97 | 26051181 | |
281 | Ubiquitination | CVYDKYVKPTEPVTD EECCCCCCCCCCCCC | 43.03 | - | |
294 | Phosphorylation | TDYRTAVSGIRPENL CCHHHHHCCCCHHHC | 26.49 | 23607784 | |
302 | Acetylation | GIRPENLKQGEELEV CCCHHHCCCCCCCHH | 68.77 | 26051181 | |
302 | Ubiquitination | GIRPENLKQGEELEV CCCHHHCCCCCCCHH | 68.77 | - | |
333 | Acetylation | HALHNDLKVLFLDHP EHHHCCEEEEEECCC | 39.49 | 26051181 | |
355 | Phosphorylation | QKYKPFKSQVKSGRP CCCCCCHHHHHCCCC | 40.35 | 30576142 | |
359 | Phosphorylation | PFKSQVKSGRPSLRL CCHHHHHCCCCHHHH | 40.97 | 30576142 | |
363 | Phosphorylation | QVKSGRPSLRLLSEK HHHCCCCHHHHHHHH | 25.43 | 30576142 | |
368 | Phosphorylation | RPSLRLLSEKILGLQ CCHHHHHHHHHHCCH | 41.24 | 24719451 | |
398 | Acetylation | MRLYVMVKKEWESMA HHHHHHHHHHHHHHH | 27.21 | 26051181 | |
413 | Phosphorylation | RDRRPLLTAPDHCSD CCCCCCCCCCCCCCC | 43.77 | 23186163 | |
419 | Phosphorylation | LTAPDHCSDDA---- CCCCCCCCCCC---- | 34.80 | 23401153 |
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 REXO4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of REXO4_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 REXO4_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ESR1_HUMAN | ESR1 | physical | 10908561 | |
ESR2_HUMAN | ESR2 | physical | 10908561 |
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. |
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Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY. |