SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

NEDD8; Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex uba-3-ula-1 and linkage to the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

Nuclear Pore complex Protein.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

Ran GTPase-activating protein 2; GTPase system comprising ran-1, ran-2 and ran-3 is essential in nucleocytoplasmic trafficking. Ran-2 is a GTPase activator for the nuclear RAS-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. Required for correct chromosome alignment and segregation on the metaphase plate.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

Small ubiquitin-related modifier; Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic dev [...]

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

SUMO-activating enzyme subunit uba-2; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

SUMO-conjugating enzyme UBC9; Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1 and the Polycomb protein sop-2. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates. Belongs to the ubiquitin-conjugating enzyme family.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

UBIQUITIN_CONJUGAT_2 domain-containing protein.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

Sentrin-specific protease; Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

Ubiquitin-like protease 2; Protease that catalyzes two essential functions in the smo-1 pathway: processing of full-length smo-1 to their mature forms and deconjugation of smo-1 from targeted proteins (By similarity). May deconjugate smo-1 from the cadherin protein hmr-1 and plays a role in its recruitment to and the maintenance of adherens junctions. Required for epidermal morphogenesis during embryonic development ; Belongs to the peptidase C48 family.

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

Small ubiquitin-related modifier; Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic dev [...]

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

SUMO-activating enzyme subunit uba-2; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

SUMO-conjugating enzyme UBC9; Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1 and the Polycomb protein sop-2. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates. Belongs to the ubiquitin-conjugating enzyme family.

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

UBIQUITIN_CONJUGAT_2 domain-containing protein.

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

Sentrin-specific protease; Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form.

E3 SUMO-protein ligase gei-17; Functions as an E3-type smo-1 ligase. Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment. In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation. In embryos, plays a role in determining telomere localization in the nucleus.

Ubiquitin-like protease 2; Protease that catalyzes two essential functions in the smo-1 pathway: processing of full-length smo-1 to their mature forms and deconjugation of smo-1 from targeted proteins (By similarity). May deconjugate smo-1 from the cadherin protein hmr-1 and plays a role in its recruitment to and the maintenance of adherens junctions. Required for epidermal morphogenesis during embryonic development ; Belongs to the peptidase C48 family.

NEDD8; Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex uba-3-ula-1 and linkage to the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

SUMO-activating enzyme subunit aos-1; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).

NEDD8; Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex uba-3-ula-1 and linkage to the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

Small ubiquitin-related modifier; Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic dev [...]

NEDD8; Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex uba-3-ula-1 and linkage to the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

SUMO-activating enzyme subunit uba-2; The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).