Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB Subcellular Location vocabulary mapping

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:9738895

ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif.

ERp28/ERp29 is an ER-lumenal protein with a KEEL retention signal that is a PDI-family member but lacks the CXXC (CGHC) thioredoxin-box motif, hence is not a disulfide isomerase.

PMID:12475965

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

ERp29 is part of a large ER chaperone multiprotein complex (BiP, GRP94, PDI, ERdj3, cyclophilin B, ERp72, GRP170, UGGT, SDF2-L1) that binds unassembled, incompletely folded immunoglobulin heavy chains.

PMID:19946888

Defining the membrane proteome of NK cells.

PMID:19995400

Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation.

ERP29 is among thiol-isomerase-family proteins released by platelets and recruited to the platelet surface following activation.

PMID:22064321

ERp29 induces breast cancer cell growth arrest and survival through modulation of activation of p38 and upregulation of ER stress protein p58IPK.

In breast cancer cells, ERp29 (an ER luminal protein with a role in protein unfolding and secretion) overexpression induces growth arrest via p38 MAPK activation and upregulation of p58IPK, modulating gene expression and protein secretion.

PMID:23864651

The identification of novel proteins that interact with the GLP-1 receptor and restrain its activity.

PMID:32296183

A reference map of the human binary protein interactome.

file:human/ERP29/ERP29-uniprot.txt

UniProt entry P30040 (ERP29_HUMAN), Endoplasmic reticulum resident protein 29

Non-catalytic (no CXXC) PDI-family ER-lumenal homodimeric chaperone that assists processing/folding of secretory proteins; part of a large ER chaperone complex; KEEL ER-retention signal; also detected in melanosomes and at the cell surface.

file:human/ERP29/ERP29-deep-research-falcon.md

Falcon deep research report for ERP29

ERP29 lacks the characteristic CXXC catalytic motif of classical PDIs and acts as a chaperone rather than a catalyst; it is recruited to the calnexin/calreticulin cycle, its C-terminal D domain being the principal interface that binds the CNX/CRT P domains, and it cycles between ER and Golgi via the KDEL receptor (KEEL motif) to assist early-secretory-pathway folding/trafficking of clients such as thyroglobulin and ENaC.