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organism-gene
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 PR:P11021 |
   endoplasmic reticulum chaperone BiP (human)
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   hHSPA5
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  "An endoplasmic reticulum chaperone BiP that is encoded in the genome of human." [PRO:DAN]
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organism-sequence
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 PR:P11021-1 |
   endoplasmic reticulum chaperone BiP isoform 1 (human)
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   hHSPA5/iso:1
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  "An endoplasmic reticulum chaperone BiP isoform 1 that is encoded in the genome of human." [PRO:DNx]
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organism-modification
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 PR:000047915 |
   endoplasmic reticulum chaperone BiP, signal peptide removed form (human)
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   hHSPA5/SigPep-
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  "An endoplasmic reticulum chaperone BiP (human) that has had the signal peptide removed. UniProtKB:P11021, 19-654." [PRO:DNx, Reactome:R-HSA-351315, Reactome:R-HSA-351322, Reactome:R-HSA-387190, Reactome:R-HSA-5252042, Reactome:R-HSA-5252115, Reactome:R-HSA-985498]
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organism-modification
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 PR:000066394 |
   endoplasmic reticulum chaperone BiP citrullinated 1 (human)
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   hHSPA5/Cit:1
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-439 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-439, MOD:00219." [IEDB_epitope:1777526, PRO:DNx]
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organism-modification
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 PR:000067089 |
   endoplasmic reticulum chaperone BiP deaminated 1 (human)
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   hHSPA5/Deam:1
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  "An endoplasmic reticulum chaperone BiP (human) that has been deaminated on the residue at the position equivalent to Asn-331 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Asn-331, MOD:00684." [IEDB_epitope:1814293, PRO:DNx]
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organism-modification
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 PR:000068879 |
   endoplasmic reticulum chaperone BiP citrullinated 2 (human)
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   hHSPA5/Cit:2
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-17 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-17, MOD:00219." [IEDB_epitope:1797378, PRO:DNx]
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organism-modification
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 PR:000069333 |
   endoplasmic reticulum chaperone BiP deaminated 2 (human)
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   hHSPA5/Deam:2
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  "An endoplasmic reticulum chaperone BiP (human) that has been deaminated on the residue at the position equivalent to Gln-628 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Gln-628, MOD:00685." [IEDB_epitope:1738565, PRO:DNx]
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organism-modification
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 PR:000069532 |
   endoplasmic reticulum chaperone BiP deaminated 3 (human)
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   hHSPA5/Deam:3
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  "An endoplasmic reticulum chaperone BiP (human) that has been deaminated on the residue at the position equivalent to Asn-380 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Asn-380, MOD:00684." [IEDB_epitope:1769058, IEDB_epitope:1807351, PRO:DNx]
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organism-modification
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 PR:000069548 |
   endoplasmic reticulum chaperone BiP methylated 1 (human)
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   hHSPA5/Me:1
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  "An endoplasmic reticulum chaperone BiP (human) that has been methylated on the residue at the position equivalent to Arg-492 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-492, MOD:00658." [IEDB_epitope:1857914, PRO:DNx]
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organism-modification
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 PR:000071676 |
   endoplasmic reticulum chaperone BiP citrullinated 3 (human)
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   hHSPA5/Cit:3
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-197 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-197, MOD:00219." [IEDB_epitope:858100, PRO:DNx]
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organism-modification
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 PR:000073571 |
   endoplasmic reticulum chaperone BiP deaminated 4 (human)
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   hHSPA5/Deam:4
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  "An endoplasmic reticulum chaperone BiP (human) that has been deaminated on the residue at the position equivalent to Gln-458 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Gln-458, MOD:00685." [IEDB_epitope:1996011, PRO:DNx]
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organism-modification
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 PR:000079115 |
   endoplasmic reticulum chaperone BiP deaminated 5 (human)
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   hHSPA5/Deam:5
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  "An endoplasmic reticulum chaperone BiP (human) that has been deaminated on the residue at the position equivalent to Gln-409 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Gln-409, MOD:00685." [IEDB_epitope:1976205, PRO:DNx]
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organism-modification
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 PR:000079369 |
   endoplasmic reticulum chaperone BiP citrullinated 4 (human)
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   hHSPA5/Cit:4
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-306 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-306, MOD:00219." [IEDB_epitope:1721815, PRO:DNx]
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organism-modification
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 PR:000080220 |
   endoplasmic reticulum chaperone BiP citrullinated 5 (human)
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   hHSPA5/Cit:5
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-261 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-261, MOD:00219." [IEDB_epitope:1820693, PRO:DNx]
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organism-modification
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 PR:000081710 |
   endoplasmic reticulum chaperone BiP citrullinated 6 (human)
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   hHSPA5/Cit:6
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-297 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-297, MOD:00219." [IEDB_epitope:590605, PRO:DNx]
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organism-modification
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 PR:000083938 |
   endoplasmic reticulum chaperone BiP deaminated 6 (human)
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   hHSPA5/Deam:6
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  "An endoplasmic reticulum chaperone BiP (human) that has been deaminated on the residue at the position equivalent to Gln-304 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Gln-304, MOD:00685." [IEDB_epitope:1366773, PRO:DNx]
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organism-modification
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 PR:000084736 |
   endoplasmic reticulum chaperone BiP citrullinated 7 (human)
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   hHSPA5/Cit:7
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-367 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-367, MOD:00219." [IEDB_epitope:1841978, PRO:DNx]
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organism-modification
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 PR:000085575 |
   endoplasmic reticulum chaperone BiP citrullinated 8 (human)
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   hHSPA5/Cit:8
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  "An endoplasmic reticulum chaperone BiP (human) that has been citrullinated on the residue at the position equivalent to Arg-510 of the amino acid sequence represented by UniProtKB:P11021. UniProtKB:P11021, Arg-510, MOD:00219." [IEDB_epitope:1739931, IEDB_epitope:857878, IEDB_epitope:858056, PRO:DNx]
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