Description(s) found:
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gi|6319260|ref|NP_009343.1| Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet s
[NCBI NR]
gi|595528|gb|AAC04976.1| Cne1p: calnexin homolog [Saccharomyces cerevisiae]
[NCBI NR]
gi|5511|emb|CAA47100.1| calnexin homologue [Saccharomyces cerevisiae]
[NCBI NR]
gi|51013291|gb|AAT92939.1| YAL058W [Saccharomyces cerevisiae]
[NCBI NR]
pir||S29347 calnexin homolog YAL058w - yeast (Saccharomyces cerevisiae)
[NCBI NR]
gi|171153|gb|AAA65967.1| calnexin [Saccharomyces cerevisiae]
[NCBI NR]
gi|115549|sp|P27825.1|CALX_YEAST RecName: Full=Calnexin homolog; Flags: Precursor
[NCBI NR]
Calnexin homolog OS=Saccharomyces cerevisiae GN=CNE1 PE=1 SV=1
[Swiss-Prot]
CNE1 Calnexin, involved in regulation of secretion
[mips]
Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast
[SGD]
CNE1, Chr I from 37465-38973
[yeast_orfs2]
Chr I from 37465-38973
[yeastorf3.fasta]
(P27825) Calnexin homolog precursor
[4932.FASTACCERV.txt]
CNE1 SGDID:S0000054, Chr I from 37465-38973, Verified ORF
[yeastflysequest.fasta]
Cne1p [Saccharomyces cerevisiae]gi|51013291|gb|AAT92939.1| YAL058W [Saccharomyces cerevisiae]gi|5511|emb|CAA47100.1| calnexin homologue [Saccharomyces cerevisiae]gi|115549|sp|P27825|CALX_YEAST Calnexin homolog precursorgi|320646|pir||S29347 calnexin h
[nrdb_11152004_Chlamydomonas]
CNE1 SGDID:S000000054, Chr I from 37465-38973, Verified ORF, "Calnexin; integral membrane ER chaperone involved in the folding and quality control of glycoproteins, 24% identical and 31% similar to mammalian calnexin but the Ca+ binding typical of calnexi
[SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
CNE1 SGDID:S000000054, Chr I from 37465-38973, Verified ORF, "Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammali
[yeast-contam.fasta]
Calnexin homolog precursor
[nr-271106-contam.fasta]
calnexin
[nr-271106-contam.fasta]
calnexin homologue [Saccharomyces cerevisiae]
[nr-271106-contam.fasta]
Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast; Cne1p [Saccha
[nr-271106-contam.fasta]
Cne1p: calnexin homolog [Saccharomyces cerevisiae]
[nr-271106-contam.fasta]
YAL058W [Saccharomyces cerevisiae]
[nr-271106-contam.fasta]
CNE1 SGDID:S000000054, Chr I from 37465-38973, Verified ORF, "Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast"
[yeast-bovrabprots.fasta]
[chemostatdb.fasta]
Calnexin homolog OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=CNE1 PE=1 SV=1
[UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
CNE1 SGDID:S000000054, Chr I from 37464-38972, Genome Release 64-1-1, Verified ORF, "Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast"
[yeast-030211-contam.fasta]
CNE1 SGDID:S000000054, Chr I from 37464-38972, Genome Release 64-2-1, Verified ORF, "Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast"
[20141208_orf_trans.fasta]
YAL058W SGDID:S000000054, Chr I from 37464-38972, Genome Release 64-1-1, Verified ORF, "Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast"
[2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
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