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ubiquitin conjugating/ligase activity #2679

Closed gocentral closed 9 years ago

gocentral commented 19 years ago

the Uniprot entry has the EC number 6.3.1.19 Ubiquitin--protein ligase. synonym Ubiquitin-conjugating enzyme After conferring with Viv Junker

> Hi Viv, > > I looked at this again, do you think that in GO ubiquitin conjucating > activities should be child terms of ubiquitin ligase activities? It > seems as though perhaps it should be?

Yes, I think maybe they should.

Viv

Reported by: ValWood

Original Ticket: "geneontology/ontology-requests/2688":https://sourceforge.net/p/geneontology/ontology-requests/2688

gocentral commented 19 years ago

Original comment by: jl242

gocentral commented 18 years ago

Logged In: YES user_id=516865

This isn't very clear!

I'm referring to a number of Uniprot entries O74810 O00102 P46595 etc which are ubiquitin conjugating enzymes. These have the EC number 6.3.2.19 in uniprot

EC 6.3.2.19 is Common name: ubiquitin—protein ligase

Ah, last time I looked at this EC, ubiquitin conjugating enzyme was a synonymn of Common name: ubiquitin—protein ligase...which did seem incorrect

I think this would be resolved by removing the EC numbers (then the EC2 GO mapping would be removed). I'll check witht eh Uniprot curators again.

Original comment by: ValWood

gocentral commented 18 years ago

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I'm a bit confused about this item Val - which term did you want the EC number removed from?

jane

Original comment by: jl242

gocentral commented 18 years ago

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I've done some reading up, and it seems that both ubiquitin conjugating enzyme (E2) and ubiquitin—protein ligase (E3) have ubiquitin—protein ligase activity. So I think in GO we should probably either merge ubiquitin conjugating enzyme into ubiquitin—protein ligase, or obsolete ubiquitin conjugating enzyme and the annotations can be moved to ubiquitin—protein ligase. The latter is probably safer.

There are a whole load of other small protein conjugating enzyme activities - I think that these should probably all be moved to under 'acid-amino acid ligase activity ; GO:0016881'. I'll probably have to send an email out before I do anything though...

Original comment by: jl242

gocentral commented 18 years ago

Logged In: YES user_id=451873

[off-line email thread]

> > Hi Kati, > > > > I asked Viv about this one a while ago. > > > > The problem appears to be that a number of Uniprot ubiquitin conjugating enzymes have the EC number for ubiquitin lagase activity. When I looked a while ago, this was a synonym at the EC commission, but it has since been removed. > > > > I wonder if this is a valid EC number for these entries which are > > ubiquitin conjugating enzymes. Could you take a look at some point. > > > > CCing Sandra too as some Interpro mappings are potentially affected. > > > > Thanks > > > > Val

> Hi Val, > > Sorry for being so late with my reply but > I tried to look into this one and ... > > according to our documents > > "Ubiquitin-conjugating enzymes (EC 6.3.2.19) (UBC or E2 enzymes) > catalyze the covalent attachment of ubiquitin to target proteins. An > activated ubiquitin moiety is transferred from an ubiquitin-activating > enzyme (E1) to E2 which later ligates ubiquitin directly to substrate > proteins with or without the assistance of 'N-end' recognizing proteins > (E3)." > > Also in our Enzyme database Official name is > Ubiquitin--protein ligase. > and Alternative Name(s) > Ubiquitin-activating enzyme. > Ubiquitin-conjugating enzyme. > > I hence don't see a problem with these UniProt entries, but if you still > think that there's a problem, please let me know. > > Thanks, > Kati

Hi Kati,

I still think there is a probelm that these are seperable activities. Or alternatively there is a proble with GO. I'm not enough of an expert to know where the problem lies but In GO these are 2 unrelated activities.

I'mm CCing the GO office in the hope that somebody knows the answer.

Will enter on SF later if necessary

Val

Original comment by: jl242

gocentral commented 18 years ago

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Useful review: PMID: 14998368

Original comment by: jl242

gocentral commented 18 years ago

Logged In: YES user_id=451873

An email thread relation to this topic (starts at bottom):

Looking at the docs online, particularly that related to confusion
between gene products and their functions, (http:// www.geneontology.org/GO.doc.shtml#geneProducts) I think the merge is
correct but maybe we want to rename to 'ubiquitin protein-ligase
activity'. My thought is that by changing the name from that commonly
used to refer to E3s it would indicate that this was an activity that
the gene product had and might lessen the confusion when people saw
E2s (aka ubquitin conjugating enzymes) coming back in addition to E3s
(ubiquitin protein-ligases)).

I was wondering if we should try and distinguish the ligation by E2
and E3 as child terms but I reviewed some of the literature from my
old postdoc mentor Art Haas who is probably one of the world's
experts on the Ub cycle and its kinetics and found this in a JBC
paper from a while back, the last sentence is the most relevant I
think:

http://www.fasebj.org/cgi/reprint/11/14/1257

"The half reactions of ubiquitin activation and ligation are functionally linked by ubiquitin carrier protein (E2), which acts to shuttle ubiquitin thiolester between the ternary complex of El and the isopeptide ligase (Fig. 1). Possible contributions of E2 to target protein specificity remains controversial, leading some authors to regard these proteins as distinct ubiquitin-conjugating enzymes (Ubc). Early studies in rabbit reticulocyte extracts identified several low molecular weight proteins capable of forming ubiquitin thiolesters in reactions dependent on the presence of El (30, 31), a property now accepted as a functional definition of the class. These E2.-í-ubiquitin thiolesters conjugate ubiquitin to model substrates, typically basic proteins such as histones, in the absence of E3 (30-34). Second-order kinetics for the ES-independent ligation of histones by the 14 kDa reticulocyte isoform E214K (35) and yeast Ubc4 (P. M. Bright and A. L. Haas, unpublished observation) indicates that such conjugation reflects nonspecific reaction of histone primary amines with the inherently reactive thiolester of the E2-íubiquitin intermediate. The microenvironment within which the thiolester is centered probably contributes to the reactivity of this intermediate since denaturation of the E2ubiquitin thiolester significantly ablates reactivity with nucleophiles (30). In contrast, other E2 isoforms such as yeast Cdc34 and Rad6, reticulocyte E232K, and human E2EPF exhibit properties more consistent with enzyme catalysts such as saturable kinetics, kcat values significantly above those for small organic reactions, and specificities for forming polyubiquitin chains of defined linkage that can serve as degradation signals for the 26S proteasome (35-37). These conflicting observations illustrate that E3-independent ligation by E2 isoforms should be interpreted cautiously in the absence of additional biochemical data."

This would indicate that E2-mediated ligation is more suspect so I
think going with the merge to describe the fact that all the Ub
enzymes (E1, E2 and E3) ligate ubiquitin to some other protein and
hence deserve a MF annotation 'ubiquitin-protein ligase activity' is
the way to go. If we ultimately want to get more fine grained in the
future as more info comes out we can do that but for now the merge
(and name change if you agree) seems like a good solution.

Simon.

--

Simon N. Twigger, Ph.D. Assistant Professor, Department of Physiology Medical College of Wisconsin 8701 Watertown Plank Road, Milwaukee, WI, USA tel: 414-456-8802 fax: 414-456-6595 AIM/iChat: simontatmcw

On Mar 13, 2006, at 11:40 AM, Valerie Wood wrote:

> > > I'm not sure either, > > But as it appears that current use of both of these two terms in > inconsistent maybe a term merge is best.... I see Simons point that
> the > community may expect the disinction, but maybe it is clearer to
> retreive > all from a search. I think I would rather see that than people > retreiving half randomly from each term. > > perhaps the 'conjugating enzyme ' designation should be only at the > gene product (rather than function level), and they will still be > retreived by synonym search?. This could all be made clear in the > comment. > > Simon what do you think? > > > Val > > > > Jane Lomax wrote: >> >> Hi Simon and Val - I'm really not sure what to do about this. I've
>> just >> had a look at the annotations for 'ubiquitin-conjugating enzyme'
>> and it's >> got some E3 proteins annotated to it (also some E1 and E4!). I'm
>> guessing >> it's because it has a vague definition and people thought they'd
>> be on the >> safe side by annotating to both. >> >> I'm thinking it may be much better to combine these into one term... >> >> jane >> >> On Fri, 10 Mar 2006, Valerie Wood wrote: >> >>> >>> >>> >>> Maybe that would be OK. >>> >>> To keep both terms as they are, but to annotate E2 's to both
>>> terms. >>> >>> If you use IEAs you will pull in a mapping to ubiquitin-protein
>>> ligase >>> activity for your E2 's >>> from EC to GO ..... >>> >>> Simon would this work, or do you think this mapping should be
>>> removed. >>> I'm pretty sure that when I first made this SF entry >>> >>> http://www.chem.qmul.ac.uk/iubmb/enzyme/EC6/3/2/19.html >>> >>> had ubiquitin conjugating enzyme as a synonym, but it doesn't
>>> now... >>> >>> >>> Jane Lomax wrote: >>>> >>>> Also, would we expect groups to annotate E2 to both 'ubiquitin
>>>> conjugating >>>> enzyme activity ; GO:0004840' and 'ubiquitin-protein ligase
>>>> activity ; >>>> GO:0004842'? Looking at the annotations, I see that quite a few
>>>> groups >>>> have, and some haven't. >>>> >>>> jane >>>> >>>> On Fri, 10 Mar 2006, Twigger Simon wrote: >>>> >>>>> Dear All, >>>>> >>>>> It would be good to find some acceptable way to keep these two
>>>>> things >>>>> separate because the ubiquitin community (which I used to
>>>>> belong to a >>>>> while back) definitely thinks of E2s as ubiquitin conjugating
>>>>> enzymes >>>>> and E3s as ubiqutin-protein ligases so to put them both as having >>>>> ubiquitin-ligase activity, whilst technically correct, will
>>>>> probably >>>>> cause confusion - people wont be expecting their E2s to come
>>>>> back as >>>>> having ubiquitin ligase activity, they will think they've been
>>>>> miss- >>>>> classified. >>>>> >>>>> From a quick look at the ontology, everywhere I could find >>>>> 'ubiquitin ligase' it looks like its being used to refer to E3s
>>>>> and >>>>> not to E2s so if we arent careful we'll have ubiquitin ligase
>>>>> meaning >>>>> E3 in a bunch of places (lots of CC are like this) and then >>>>> 'ubiquitin ligase activity' containing E2 and E3 activity in M. >>>>> Function. >>>>> >>>>> The definition of ubiquitin-protein ligase activity is also
>>>>> written >>>>> from the perspective of an E3 and would have to change:
>>>>> "Catalysis of >>>>> the reaction: ATP + ubiquitin + protein lysine = AMP +
>>>>> diphosphate + >>>>> protein N-ubiquityllysine. Catalyzes the mediation of substrate >>>>> recognition in ubiquitin-mediated protein degradation; binds
>>>>> directly >>>>> to the substrate and its cognate E2 (ubiquitin conjugating
>>>>> enzyme). " >>>>> >>>>> The existing definition for ubiquitin conjugating activity states: >>>>> "Catalysis of the linkage of ubiquitin with lysine residues on a >>>>> target protein. This function may be performed alone or in >>>>> conjunction with E3, ubiquitin-protein ligase. ". >>>>> >>>>> I actually think these definitions and the separation of the
>>>>> two ways >>>>> in which ubiquitin can be joined to other proteins looks pretty
>>>>> good >>>>> and matches the Ub cycle and the way this community thinks about >>>>> these things. Im not sure we should mess with it without a fair
>>>>> bit >>>>> more investigation. >>>>> >>>>> Simon. >>>>> >>>>> >>>>> Simon N. Twigger, Ph.D. >>>>> Assistant Professor, Department of Physiology >>>>> Medical College of Wisconsin >>>>> 8701 Watertown Plank Road, >>>>> Milwaukee, WI, USA >>>>> tel: 414-456-8802 >>>>> fax: 414-456-6595 >>>>> AIM/iChat: simontatmcw >>>>> >>>>> >>>>> On Mar 10, 2006, at 7:59 AM, Valerie Wood wrote: >>>>> >>>>>> >>>>>> >>>>>> >>>>>> Can we make 'ubiquitin conjugating activity' a child of
>>>>>> 'ubiquitin >>>>>> ligase activity' >>>>>> >>>>>> Then we could keep the distinction between the two? >>>>>> >>>>>> I think it would be good to keep both terms from an annotation >>>>>> perspective >>>>>> they just shouldn't be in different parts of the function graph. >>>>>> >>>>>> >>>>>> >>>>>> val >>>>>> >>>>>> >>>>>> >>>>>> Jane Lomax wrote: >>>>>>> >>>>>>> Hi - we've got a bit of a problem with the terms 'ubiquitin >>>>>>> conjugating >>>>>>> enzyme activity ; GO:0004840' and 'ubiquitin-protein ligase >>>>>>> activity ; >>>>>>> GO:0004842' in GO. Basically, these two terms represent the >>>>>>> enzymes E2 and >>>>>>> E3 respectively, but in the real world, both E2 and E3 possess >>>>>>> ubiquitin-protein ligase activity (EC 6.3.2.19). >>>>>>> >>>>>>> In the UniProt Enzyme database, and in the EC database they
>>>>>>> just have >>>>>>> 'ubiquitin-protein ligase', which is causing some conflicts with >>>>>>> the GO >>>>>>> mappings (Val knows more about this, or see: >>>>>>> >>>>>>> https://sourceforge.net/tracker/index.php? >>>>>>> func=detail&aid=1237306&group_id=36855&atid=440764) >>>>>>> >>>>>>> I think the best thing for us to do is obsolete 'ubiquitin >>>>>>> conjugating >>>>>>> enzyme activity ; GO:0004840' and the annotations can all be
>>>>>>> moved to >>>>>>> 'ubiquitin-protein ligase activity ; GO:0004842'. Also, we
>>>>>>> have a >>>>>>> whole >>>>>>> set of other small protein conjugating enzyme activities - I
>>>>>>> think >>>>>>> these >>>>>>> are all probably fine, but their activities are protein
>>>>>>> ligases, so I >>>>>>> think they should be moved to be children of 'acid-amino acid >>>>>>> ligase activity ; GO:0016881'. >>>>>>> >>>>>>> Does anyone have any thoughts about this? >>>>>>> >>>>>>> thanks, >>>>>>> >>>>>>> jane >>>>>>> >>>>>>> Dr Jane Lomax >>>>>>> GO Editorial Office >>>>>>> EMBL-EBI >>>>>>> Wellcome Trust Genome Campus >>>>>>> Hinxton >>>>>>> Cambridgeshire, UK >>>>>>> CB10 1SD >>>>>>> >>>>>>> p: +44 1223 492516 >>>>>>> f: +44 1223 494468

Original comment by: jl242

gocentral commented 18 years ago

Logged In: YES user_id=451873

An email thread relation to this topic (starts at bottom):

Looking at the docs online, particularly that related to confusion
between gene products and their functions, (http:// www.geneontology.org/GO.doc.shtml#geneProducts) I think the merge is
correct but maybe we want to rename to 'ubiquitin protein-ligase
activity'. My thought is that by changing the name from that commonly
used to refer to E3s it would indicate that this was an activity that
the gene product had and might lessen the confusion when people saw
E2s (aka ubquitin conjugating enzymes) coming back in addition to E3s
(ubiquitin protein-ligases)).

I was wondering if we should try and distinguish the ligation by E2
and E3 as child terms but I reviewed some of the literature from my
old postdoc mentor Art Haas who is probably one of the world's
experts on the Ub cycle and its kinetics and found this in a JBC
paper from a while back, the last sentence is the most relevant I
think:

http://www.fasebj.org/cgi/reprint/11/14/1257

"The half reactions of ubiquitin activation and ligation are functionally linked by ubiquitin carrier protein (E2), which acts to shuttle ubiquitin thiolester between the ternary complex of El and the isopeptide ligase (Fig. 1). Possible contributions of E2 to target protein specificity remains controversial, leading some authors to regard these proteins as distinct ubiquitin-conjugating enzymes (Ubc). Early studies in rabbit reticulocyte extracts identified several low molecular weight proteins capable of forming ubiquitin thiolesters in reactions dependent on the presence of El (30, 31), a property now accepted as a functional definition of the class. These E2.-í-ubiquitin thiolesters conjugate ubiquitin to model substrates, typically basic proteins such as histones, in the absence of E3 (30-34). Second-order kinetics for the ES-independent ligation of histones by the 14 kDa reticulocyte isoform E214K (35) and yeast Ubc4 (P. M. Bright and A. L. Haas, unpublished observation) indicates that such conjugation reflects nonspecific reaction of histone primary amines with the inherently reactive thiolester of the E2-íubiquitin intermediate. The microenvironment within which the thiolester is centered probably contributes to the reactivity of this intermediate since denaturation of the E2ubiquitin thiolester significantly ablates reactivity with nucleophiles (30). In contrast, other E2 isoforms such as yeast Cdc34 and Rad6, reticulocyte E232K, and human E2EPF exhibit properties more consistent with enzyme catalysts such as saturable kinetics, kcat values significantly above those for small organic reactions, and specificities for forming polyubiquitin chains of defined linkage that can serve as degradation signals for the 26S proteasome (35-37). These conflicting observations illustrate that E3-independent ligation by E2 isoforms should be interpreted cautiously in the absence of additional biochemical data."

This would indicate that E2-mediated ligation is more suspect so I
think going with the merge to describe the fact that all the Ub
enzymes (E1, E2 and E3) ligate ubiquitin to some other protein and
hence deserve a MF annotation 'ubiquitin-protein ligase activity' is
the way to go. If we ultimately want to get more fine grained in the
future as more info comes out we can do that but for now the merge
(and name change if you agree) seems like a good solution.

Simon.

--

Simon N. Twigger, Ph.D. Assistant Professor, Department of Physiology Medical College of Wisconsin 8701 Watertown Plank Road, Milwaukee, WI, USA tel: 414-456-8802 fax: 414-456-6595 AIM/iChat: simontatmcw

On Mar 13, 2006, at 11:40 AM, Valerie Wood wrote:

> > > I'm not sure either, > > But as it appears that current use of both of these two terms in > inconsistent maybe a term merge is best.... I see Simons point that
> the > community may expect the disinction, but maybe it is clearer to
> retreive > all from a search. I think I would rather see that than people > retreiving half randomly from each term. > > perhaps the 'conjugating enzyme ' designation should be only at the > gene product (rather than function level), and they will still be > retreived by synonym search?. This could all be made clear in the > comment. > > Simon what do you think? > > > Val > > > > Jane Lomax wrote: >> >> Hi Simon and Val - I'm really not sure what to do about this. I've
>> just >> had a look at the annotations for 'ubiquitin-conjugating enzyme'
>> and it's >> got some E3 proteins annotated to it (also some E1 and E4!). I'm
>> guessing >> it's because it has a vague definition and people thought they'd
>> be on the >> safe side by annotating to both. >> >> I'm thinking it may be much better to combine these into one term... >> >> jane >> >> On Fri, 10 Mar 2006, Valerie Wood wrote: >> >>> >>> >>> >>> Maybe that would be OK. >>> >>> To keep both terms as they are, but to annotate E2 's to both
>>> terms. >>> >>> If you use IEAs you will pull in a mapping to ubiquitin-protein
>>> ligase >>> activity for your E2 's >>> from EC to GO ..... >>> >>> Simon would this work, or do you think this mapping should be
>>> removed. >>> I'm pretty sure that when I first made this SF entry >>> >>> http://www.chem.qmul.ac.uk/iubmb/enzyme/EC6/3/2/19.html >>> >>> had ubiquitin conjugating enzyme as a synonym, but it doesn't
>>> now... >>> >>> >>> Jane Lomax wrote: >>>> >>>> Also, would we expect groups to annotate E2 to both 'ubiquitin
>>>> conjugating >>>> enzyme activity ; GO:0004840' and 'ubiquitin-protein ligase
>>>> activity ; >>>> GO:0004842'? Looking at the annotations, I see that quite a few
>>>> groups >>>> have, and some haven't. >>>> >>>> jane >>>> >>>> On Fri, 10 Mar 2006, Twigger Simon wrote: >>>> >>>>> Dear All, >>>>> >>>>> It would be good to find some acceptable way to keep these two
>>>>> things >>>>> separate because the ubiquitin community (which I used to
>>>>> belong to a >>>>> while back) definitely thinks of E2s as ubiquitin conjugating
>>>>> enzymes >>>>> and E3s as ubiqutin-protein ligases so to put them both as having >>>>> ubiquitin-ligase activity, whilst technically correct, will
>>>>> probably >>>>> cause confusion - people wont be expecting their E2s to come
>>>>> back as >>>>> having ubiquitin ligase activity, they will think they've been
>>>>> miss- >>>>> classified. >>>>> >>>>> From a quick look at the ontology, everywhere I could find >>>>> 'ubiquitin ligase' it looks like its being used to refer to E3s
>>>>> and >>>>> not to E2s so if we arent careful we'll have ubiquitin ligase
>>>>> meaning >>>>> E3 in a bunch of places (lots of CC are like this) and then >>>>> 'ubiquitin ligase activity' containing E2 and E3 activity in M. >>>>> Function. >>>>> >>>>> The definition of ubiquitin-protein ligase activity is also
>>>>> written >>>>> from the perspective of an E3 and would have to change:
>>>>> "Catalysis of >>>>> the reaction: ATP + ubiquitin + protein lysine = AMP +
>>>>> diphosphate + >>>>> protein N-ubiquityllysine. Catalyzes the mediation of substrate >>>>> recognition in ubiquitin-mediated protein degradation; binds
>>>>> directly >>>>> to the substrate and its cognate E2 (ubiquitin conjugating
>>>>> enzyme). " >>>>> >>>>> The existing definition for ubiquitin conjugating activity states: >>>>> "Catalysis of the linkage of ubiquitin with lysine residues on a >>>>> target protein. This function may be performed alone or in >>>>> conjunction with E3, ubiquitin-protein ligase. ". >>>>> >>>>> I actually think these definitions and the separation of the
>>>>> two ways >>>>> in which ubiquitin can be joined to other proteins looks pretty
>>>>> good >>>>> and matches the Ub cycle and the way this community thinks about >>>>> these things. Im not sure we should mess with it without a fair
>>>>> bit >>>>> more investigation. >>>>> >>>>> Simon. >>>>> >>>>> >>>>> Simon N. Twigger, Ph.D. >>>>> Assistant Professor, Department of Physiology >>>>> Medical College of Wisconsin >>>>> 8701 Watertown Plank Road, >>>>> Milwaukee, WI, USA >>>>> tel: 414-456-8802 >>>>> fax: 414-456-6595 >>>>> AIM/iChat: simontatmcw >>>>> >>>>> >>>>> On Mar 10, 2006, at 7:59 AM, Valerie Wood wrote: >>>>> >>>>>> >>>>>> >>>>>> >>>>>> Can we make 'ubiquitin conjugating activity' a child of
>>>>>> 'ubiquitin >>>>>> ligase activity' >>>>>> >>>>>> Then we could keep the distinction between the two? >>>>>> >>>>>> I think it would be good to keep both terms from an annotation >>>>>> perspective >>>>>> they just shouldn't be in different parts of the function graph. >>>>>> >>>>>> >>>>>> >>>>>> val >>>>>> >>>>>> >>>>>> >>>>>> Jane Lomax wrote: >>>>>>> >>>>>>> Hi - we've got a bit of a problem with the terms 'ubiquitin >>>>>>> conjugating >>>>>>> enzyme activity ; GO:0004840' and 'ubiquitin-protein ligase >>>>>>> activity ; >>>>>>> GO:0004842' in GO. Basically, these two terms represent the >>>>>>> enzymes E2 and >>>>>>> E3 respectively, but in the real world, both E2 and E3 possess >>>>>>> ubiquitin-protein ligase activity (EC 6.3.2.19). >>>>>>> >>>>>>> In the UniProt Enzyme database, and in the EC database they
>>>>>>> just have >>>>>>> 'ubiquitin-protein ligase', which is causing some conflicts with >>>>>>> the GO >>>>>>> mappings (Val knows more about this, or see: >>>>>>> >>>>>>> https://sourceforge.net/tracker/index.php? >>>>>>> func=detail&aid=1237306&group_id=36855&atid=440764) >>>>>>> >>>>>>> I think the best thing for us to do is obsolete 'ubiquitin >>>>>>> conjugating >>>>>>> enzyme activity ; GO:0004840' and the annotations can all be
>>>>>>> moved to >>>>>>> 'ubiquitin-protein ligase activity ; GO:0004842'. Also, we
>>>>>>> have a >>>>>>> whole >>>>>>> set of other small protein conjugating enzyme activities - I
>>>>>>> think >>>>>>> these >>>>>>> are all probably fine, but their activities are protein
>>>>>>> ligases, so I >>>>>>> think they should be moved to be children of 'acid-amino acid >>>>>>> ligase activity ; GO:0016881'. >>>>>>> >>>>>>> Does anyone have any thoughts about this? >>>>>>> >>>>>>> thanks, >>>>>>> >>>>>>> jane >>>>>>> >>>>>>> Dr Jane Lomax >>>>>>> GO Editorial Office >>>>>>> EMBL-EBI >>>>>>> Wellcome Trust Genome Campus >>>>>>> Hinxton >>>>>>> Cambridgeshire, UK >>>>>>> CB10 1SD >>>>>>> >>>>>>> p: +44 1223 492516 >>>>>>> f: +44 1223 494468

Original comment by: jl242

gocentral commented 17 years ago

Logged In: YES user_id=436423 Originator: NO

Hi,

This item has been open for a long time. Please comment to let us know whether you would like it to remain assigned to you, or would prefer it to be reassigned. (You don't necessarily have to work on it immediately if you keep it; we just need to know whether it's still on your list.)

Thanks, Midori & David Ontology development group managers

Original comment by: mah11

gocentral commented 17 years ago

Logged In: YES user_id=451873 Originator: NO

Merged 'ubiquitin conjugating enzyme activity ; GO:0004840' into 'ubiquitin-protein ligase activity ; GO:0004842'. New definition is:"Catalysis of the reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine."

Original comment by: jl242

gocentral commented 17 years ago

Original comment by: jl242

gocentral commented 17 years ago

Logged In: YES user_id=516865 Originator: YES

Hi

Rama and Rob have proposed to unmerge these.

The new SF item is 1669585

Val

Original comment by: ValWood

gocentral commented 17 years ago

Original comment by: ValWood

gocentral commented 17 years ago

Logged In: YES user_id=436423 Originator: NO

SF 1669585 has been sorted, so closing this too. m

Original comment by: mah11

gocentral commented 17 years ago

Original comment by: mah11