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Protein Ontology report - follistatin, signal peptide removed form (human)
PR:000047454 -
http://purl.obolibrary.org/obo/PR_000047454
Protein Forms
Annotations
Ontology Information
Show OBO stanza
/
GPI
PRO ID
PR:000047454
PRO name
follistatin, signal peptide removed form (human)
Synonyms
PRO-Short-label
:
EXACT:
hFST/SigPep-
PRO-proteoform-std
:
EXACT:
UniProtKB:P19883
, 30-344
PRO-proteoform-ftid
:
EXACT:
PRO_0000010103
Definition
"A follistatin (human) that has had the signal peptide removed.
UniProtKB:P19883
, 30-344." [PRO:DNx,
Reactome:R-HSA-2473211
]
PRO Category
organism-modification
Parent
PR:000018268
follistatin, signal peptide removed form
PR:P19883
follistatin (human)
Taxon
NCBITaxon:9606
Homo sapiens
Terms by PRO Category
Organism-Independent
Organism-Specific
Category
Number of Terms
Category
Number of Terms
Modification
0
Organism-Modification
4
Term Hierarchy
Visualization
DAG:
OLS:
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Protein Forms
Switch to
Compact View
Category
PRO ID
Name
Short Name
Definition
Ann.
Has Annotation?
comp.
In Complex?
organism-modification
PR:000047454
follistatin, signal peptide removed form (human)
hFST/SigPep-
"A follistatin (human) that has had the signal peptide removed. UniProtKB:P19883, 30-344." [PRO:DNx, Reactome:R-HSA-2473211]
organism-modification
PR:000036412
follistatin isoform 1, signal peptide removed glycosylated form (human)
hFST/iso:1/SigPep-/GlycoRes+
"A follistatin isoform 1, signal peptide removed glycosylated form in human. UniProtKB:P19883-1, 30-344, MOD:00693." [PMID:16150905, PRO:CNA]
Yes
organism-modification
PR:000036414
follistatin isoform 1 cleaved and N-glycosylated 2 (human)
hFST/iso:1/ClvNGlyco:2
"A follistatin isoform 1 cleaved and N-glycosylated 2 in human. UniProtKB:P19883-1, 30-332, Asn-124/Asn-288, MOD:00160." [PMID:16150905, PRO:CNA, PRO:DAN]
Yes
organism-modification
PR:000036415
follistatin isoform 2, signal peptide removed N-glycosylated 1 (human)
hFST/iso:2/SigPep-/NGlyco:1
"A follistatin isoform 2, signal peptide removed glycosylated form that is in human and has been N-glycosylated at residues equivalent to Asn-124 and Asn-288 of the amino acid sequence represented by UniProtKB:P19883-2. UniProtKB:P19883-2, 30-317, Asn-124/Asn-288, MOD:00160." [PMID:15454184, PMID:16150905, PMID:1906804, PRO:CNA, PRO:DAN]
Yes
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Functional Annotation (PRO-centric view)
Switch to
GO Centric View
PRO Term
GO Annotation
Evidence
PR:000036412
hFST/iso:1/SigPep-/GlycoRes+
UniProtKB:P19883-1, 30-344, MOD:00693
located_in
GO:0005615
extracellular space
PMID:16150905
PR:000036414
hFST/iso:1/ClvNGlyco:2
UniProtKB:P19883-1, 30-332, Asn-124/Asn-288, MOD:00160
located_in
GO:0005615
extracellular space
PMID:16150905
PR:000036415
hFST/iso:2/SigPep-/NGlyco:1
UniProtKB:P19883-2, 30-317, Asn-124/Asn-288, MOD:00160
acts_upstream_of_or_within
GO:0032926
negative regulation of activin receptor signaling pathway
PMID:1906804
located_in
GO:0005615
extracellular space
PMID:16150905