Description(s) found:
SHOW ONLY BEST
|
gi|6319546|ref|NP_009628.1| Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires a heat-induced conformational change; not expressed in uns
[NCBI NR]
pir||S45465 heat shock protein HSP26 - yeast (Saccharomyces cerevisiae)
[NCBI NR]
gi|536324|emb|CAA85016.1| HSP26 [Saccharomyces cerevisiae]
[NCBI NR]
gi|433836|emb|CAA53929.1| unnamed protein product [Saccharomyces cerevisiae]
[NCBI NR]
gi|171716|gb|AAA66914.1| heat shock protein 26 [Saccharomyces cerevisiae]
[NCBI NR]
gi|123568|sp|P15992.3|HSP26_YEAST RecName: Full=Heat shock protein 26; AltName: Full=26 kDa heat shock protein
[NCBI NR]
Heat shock protein 26 OS=Saccharomyces cerevisiae GN=HSP26 PE=1 SV=3
[Swiss-Prot]
HSP26 Heat shock protein
[mips]
Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires a heat-induced conformational change; not expressed in unstressed cells
[SGD]
HSP26, Chr II from 381989-382633
[yeast_orfs2]
Chr II from 381989-382633
[yeastorf3.fasta]
HSP26 SGDID:S0000276, Chr II from 381990-382634, Verified ORF
[yeastflysequest.fasta]
HSP26 SGDID:S0000276, Chr II from 382027-382671, Verified ORF
[10112005cervSGD.fasta]
Hsp26p [Saccharomyces cerevisiae]gi|433836|emb|CAA53929.1| unnamed protein product [Saccharomyces cerevisiae]gi|536324|emb|CAA85016.1| HSP26 [Saccharomyces cerevisiae]gi|625517|pir||S45465 heat shock protein HSP26 - yeast (Saccharomyces cerevisiae)gi|
[nrdb_11152004_Chlamydomonas]
HSP26 SGDID:S000000276, Chr II from 382027-382671, Verified ORF, "Small heat shock protein with chaperone activity that is regulated by a heat induced transition from an inactive oligomeric (24-mer) complex to an active dimer; induced by heat, upon entry
[SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
HSP26 SGDID:S000000276, Chr II from 382027-382671, Verified ORF, "Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires a heat-induced confo
[SGD_S-cerevisiae_na_08-19-2008_con_reversed.fasta]
Heat shock protein 26 (26 kDa heat shock protein)
[nr-271106-contam.fasta]
Small heat shock protein with chaperone activity that is regulated by a heat induced transition from an inactive oligomeric (24-mer) complex to an active dimer; induced by heat, upon entry into stationary phase, and during sporulation; Hsp26p [Saccharomyc
[nr-271106-contam.fasta]
unnamed protein product [Saccharomyces cerevisiae]
[nr-271106-contam.fasta]
HSP26 [Saccharomyces cerevisiae]
[nr-271106-contam.fasta]
heat shock protein 26
[nr-271106-contam.fasta]
HSP26 SGDID:S000000276, Chr II from 382027-382671, Verified ORF, "Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires a heat-induced conformational change; not expressed in unstressed cells"
[yeast-bovrabprots.fasta]
HSP26 SGDID:S000000276, Chr II from 382027-382671, Verified ORF, "Small heat shock protein with chaperone activity that is regulated by a heat induced transition from an inactive oligomeric (24-mer) complex to an active dimer; induced by heat, upon entry into stationary phase, and during sporulation"
[yeast-contam_custom.fasta]
[chemostatdb.fasta]
Heat shock protein 26 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=HSP26 PE=1 SV=3
[UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
HSP26 SGDID:S000000276, Chr II from 382030-382674, Genome Release 64-1-1, Verified ORF, "Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires heat-induced conformational change; also has mRNA binding activity"
[yeast-030211-contam.fasta]
HSP26 SGDID:S000000276, Chr II from 382030-382674, Genome Release 64-2-1, Verified ORF, "Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; long-lived protein that is preferentially retained in mother cells and forms cytoplasmic foci; oligomer activation requires heat-induced conformational change; also has mRNA binding activity"
[20141208_orf_trans.fasta]
YBR072W SGDID:S000000276, Chr II from 382030-382674, Genome Release 64-1-1, Verified ORF, "Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires heat-induced conformational change; also has mRNA binding activity"
[2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
|