NP_001029197.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
51.0 kDa
NCBI Official Full Name
endoplasmic reticulum resident protein 29 isoform 2
NCBI Official Synonym Full Names
endoplasmic reticulum protein 29
NCBI Official Synonym Symbols
ERp28; ERp31; PDIA9; PDI-DB; C12orf8; HEL-S-107 [Similar Products]
NCBI Protein Information
endoplasmic reticulum resident protein 29
UniProt Protein Name
Endoplasmic reticulum resident protein 29
UniProt Synonym Protein Names
Endoplasmic reticulum resident protein 28; ERp28; Endoplasmic reticulum resident protein 31; ERp31
UniProt Synonym Gene Names
UniProt Entry Name
ERP29_HUMAN
NCBI Summary for ERP29
This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]
UniProt Comments for ERP29
ERP29: Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
Protein type: Chaperone
Chromosomal Location of Human Ortholog: 12q24.13
Cellular Component: cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome; membrane; smooth endoplasmic reticulum; transport vesicle
Molecular Function: chaperone binding; protein binding; protein disulfide isomerase activity; protein homodimerization activity
Biological Process: activation of MAPK activity; intracellular protein transport; negative regulation of protein secretion; positive regulation of protein amino acid phosphorylation; protein folding; protein secretion; protein unfolding
Product References and Citations for ERP29 recombinant protein
ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif.Ferrari D.M., van Nguyen P., Kratzin H.D., Soeling H.D.Eur. J. Biochem. 255:570-579(1998)
The WashU-Merck EST project.Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M., Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., Rifkin L., Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A., Wohldmann P., Wilson R.
Human liver protein map
update 1993.Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.Electrophoresis 14:1216-1222(1993)
Human liver protein map
a reference database established by microsequencing and gel comparison.Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.Electrophoresis 13:992-1001(1992)
Lubec G., Vishwanath V.Submitted (MAR-2007)
to UniProtKB
Hubbard M.J.Submitted (DEC-1998)
to UniProtKB
Human ERp29
isolation, primary structural characterisation and two-dimensional gel mapping.Hubbard M.J., McHugh N.J.3.0.CO;2-2>Electrophoresis 21:3785-3796(2000)
A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.Mol. Biol. Cell 13:4456-4469(2002)
Proteomic analysis of early melanosomes
identification of novel melanosomal proteins.Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.J. Proteome Res. 2:69-79(2003)
Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.J. Proteome Res. 5:3135-3144(2006)
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
A secreted tyrosine kinase acts in the extracellular environment.Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr., Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.Cell 158:1033-1044(2014)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Research Articles on ERP29
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Products associated with ERP29 recombinant protein
Pathways associated with ERP29 recombinant protein
Diseases associated with ERP29 recombinant protein
Organs/Tissues associated with ERP29 recombinant protein
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