Protein Ubiquitination

Question 1

Ubiquitin is an alternative option to

Answer 1

Phosphorylation

Question 2

What does ubiquitin mainly modify?

Answer 2

Lys (and Met)

Question 3

Ubiquitination is the addition of:

Answer 3

A 7kDa protein

Question 4

What enzymes add ubiquitin?

Answer 4

E1, E2, and E3

Question 5

What enzymes remove ubiquitin?

Answer 5

DUBs

Question 6

Is the addition of ubiquitin chains generally reversible or irreversible?

Answer 6

Irreversible

Question 7

Ubiqutination

Answer 7

The post-translational addition of ubiquitin to lysine (or Met) residues

Question 8

Writer

Answer 8

Ubiquitin ligase

Question 9

Reader

Answer 9

UIM domain

Question 10

Eraser

Answer 10

Deubiquitinase

Question 11

Output

Answer 11

DNA damage response

Question 12

Ubiquitin

Answer 12

A short protein (76 amino acids)
97% conserved in eukaryotes

Question 13

3 steps to protein ubiquitination

Answer 13

Activation
Conjunction
Ligation

Question 14

Activating

Answer 14

Ubiquitin-activating enzymes (E1s) use ATP (molecular currencies) to add ubiquitin onto Cystic residue

Question 15

Conjugation

Answer 15

Activated ubiquitin is transferred to an E2 enzyme via a Cys residue

Question 16

Ligation

Answer 16

Ubiquitin-ligases (E3s) catalyse the transfer of ubiquitin to the Lys (or Met) amino group

Question 17

2 types of covalent bonds in ubiquitin

Answer 17

Peptide bond
Isopeptide bond