User:Flounlackerkm

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
updatedbyinstructor	BPSPP:Q38152	2016-04-11 11:32:59 CDT	GO:0036121 double-stranded DNA-dependent ATP-dependent DNA helicase activity (F)	PMID:18157148	ECO:0000315 mutant phenotype evidence used in manual assertion	Fig 4, Table 1.	challenge
updatedbyinstructor	9CAUD:W8EEZ1	2016-04-25 09:42:18 CDT	GO:0036121 double-stranded DNA-dependent ATP-dependent DNA helicase activity (F)	GO_REF:0000100	ECO:0000247 sequence alignment evidence used in manual assertion	blastp e value of 1.8e-171, with percent identity of 57.6%, and query coverage of 99.54%	challenge
updatedbyinstructor	BPSPP:Q38152	2016-04-25 10:13:47 CDT	GO:0006268 DNA unwinding involved in DNA replication (P)	PMID:18157148	ECO:0000315 mutant phenotype evidence used in manual assertion	Figure 4 shows the effect of mutated residues on the protein and how the mutations effect the binding ability of the protein to primase using gel electrophoresus. Helicase binds to and unwinds the DNA prior to replication, and in complex with primase, puts down the DNA primer to initiate replication. When mutated the protein does no properly function and complex with primase to activate primase and initiate replication. Table 1 shows the series of deletions and mutations done to assess the helicase and ATPase activity in the presence and absence primase. DeltaN92 is the first series of deletions performed, deleting amino acids 1 to 92, this mutation decreased the DNA unwinding ability of the protein from 100% to 66% activity. DeltaN112 deleted amino acids 1-112. This deletion caused the DNA unwinding ability of helicase to stop almost completely, with a drop from 100% activity to 3% activity with this deletion. The double point mutation mt1 changed the amino acids I121A and E122A, resulting in a decrease in helicase activity to 7%.	challenge
updatedbyinstructor	STREE:A0A0U0BZQ2	2016-05-08 16:09:43 CDT	GO:0036121 double-stranded DNA helicase activity (F)	GO_REF:0000100	ECO:0000247 sequence alignment evidence used in manual assertion	blastp e-value of 1.4e-144, query coverage of 99.32, with a percent identity of 51.4%	challenge
updatedbyinstructor	9BACI:A0A0K9GSD2	2016-05-08 16:14:30 CDT	GO:0036121 double-stranded DNA-dependent ATP-dependent DNA helicase activity (F)	GO_REF:0000100	ECO:0000247 sequence alignment evidence used in manual assertion	blastp e-value of 1.6e-157, query coverage of 98.87, and percent identity of 54.9%	challenge
unacceptable	BPSPP:Q38152	2016-05-11 08:10:51 CDT	GO:1990077 primosome complex (C)	PMID:18157148	ECO:0000314 direct assay evidence used in manual assertion	figure 1 shows the hexameric structure of the SPP1 helicase, determined with x-ray crystallography. Helicase binds to and unwinds the DNA prior to replication, and in complex with primase, puts down the DNA primer to initiate replication. Figure 4d shows the binding of primase and helicase into a complex by gel shift, in the presence of primase the helicase complexes with the primase and migrates more slowly and a shorter distacne through the gel than in the absence of primase. Only the full length helicase is able to form a complex with primase. Helicase binds to and unwinds the DNA prior to replication, and in complex with primase, puts down the DNA primer to initiate replication. When mutated the protein does no properly function and complex with primase to activate primase and initiate replication. Table 1 shows the series of deletions and mutations done to assess the helicase and ATPase activity in the presence and absence primase. In the presence of primase, the ATPase activity more than doubles (1 to 2.3) and the helicase activity quadruples (1 to 4.6).	challenge

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unacceptable:1
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Annotations challenged by Flounlackerkm

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history
unacceptable	Gilliabb, Team ContaminatorZ	9CAUD:A0A024AZP1	GO:0098015 - virus tail (C)	PMID:25100842	ECO:0000314 direct assay evidence used in manual assertion	challenge	C: 5
unacceptable	Amariam1, Team You can't B. cereus	9CAUD:A0A0K2D089	GO:0046798 - viral portal complex (C)	PMID:12239300	ECO:0000316 genetic interaction evidence used in manual assertion	challenge	C: 5
unacceptable	Di46616, Team Red A	BACSU:RPSB	GO:0080134 - regulation of response to stress (P)	PMID:10383961	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 4
unacceptable	Mnguy1, Team Blue B	HAEIN:COAE	GO:0004140 - dephospho-CoA kinase activity (F)	PMID:11292795	ECO:0000314 direct assay evidence used in manual assertion	challenge	C: 1
unacceptable	Nitika1, Team Purple A	ECOLI:CRL	GO:0016987 - sigma factor activity (F)	PMID:9878355	ECO:0000314 direct assay evidence used in manual assertion	challenge	C: 1

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