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ONTOLOGY REPORT - ANNOTATIONS


Term:histone H2A K63-linked deubiquitination
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Accession:GO:0070537 term browser browse the term
Definition:A protein deubiquitination process in which a K63-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is removed from a lysine residue in histone H2A or the variant H2AX.


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histone H2A K63-linked deubiquitination term browser
Symbol Object Name JBrowse Chr Start Stop Reference
G Brcc3 BRCA1/BRCA2-containing complex, subunit 3 JBrowse link 9 9,863,380 9,865,920 RGD:1600115
RGD:1624291
RGD:13792537
G Uimc1 ubiquitin interaction motif containing 1 JBrowse link 17 10,061,915 10,130,921 RGD:1624291
RGD:1600115
RGD:13792537
G Usp16 ubiquitin specific peptidase 16 JBrowse link 11 27,101,213 27,130,345 RGD:1624291
RGD:1600115

Term paths to the root
Path 1
Term Annotations click to browse term
  biological_process 19858
    metabolic process 12096
      primary metabolic process 10749
        protein metabolic process 6185
          proteolysis 1882
            protein modification by small protein removal 152
              protein deubiquitination 121
                protein K63-linked deubiquitination 34
                  histone H2A K63-linked deubiquitination 3
Path 2
Term Annotations click to browse term
  biological_process 19858
    metabolic process 12096
      organic substance metabolic process 11494
        macromolecule metabolic process 9943
          protein metabolic process 6185
            protein modification process 3901
              cellular protein modification process 3901
                protein modification by small protein conjugation or removal 934
                  protein modification by small protein removal 152
                    protein deubiquitination 121
                      histone deubiquitination 23
                        histone H2A K63-linked deubiquitination 3
paths to the root

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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.