HERPUD1

HERPUD1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WGD
Identifiers
Aliases	HERPUD1, HERP, Mif1, SUP, homocysteine inducible ER protein with ubiquitin like domain 1
External IDs	OMIM: 608070; MGI: 1927406; HomoloGene: 40973; GeneCards: HERPUD1; OMA:HERPUD1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16q13 Start 56,932,142 bp End 56,944,864 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 C5 Start 95,113,066 bp End 95,122,005 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas palpebral conjunctiva epithelium of nasopharynx tonsil trachea tibia parietal pleura rectum olfactory bulb pylorus Top expressed in lacrimal gland parotid gland right kidney seminal vesicula submandibular gland left lobe of liver islet of Langerhans pyloric antrum calvaria gallbladder More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transmembrane transporter binding protein binding molecular function ubiquitin ligase-substrate adaptor activity Cellular component integral component of membrane Lewy body core calcium channel complex endoplasmic reticulum membrane membrane endoplasmic reticulum Biological process negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway negative regulation of cysteine-type endopeptidase activity involved in apoptotic process ubiquitin-dependent protein catabolic process negative regulation of intrinsic apoptotic signaling pathway regulation of protein ubiquitination regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway cellular calcium ion homeostasis endoplasmic reticulum calcium ion homeostasis response to endoplasmic reticulum stress PERK-mediated unfolded protein response positive regulation of ER-associated ubiquitin-dependent protein catabolic process regulation of ER-associated ubiquitin-dependent protein catabolic process response to unfolded protein retrograde protein transport, ER to cytosol positive regulation of protein binding endoplasmic reticulum unfolded protein response protein ubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9709 64209 Ensembl ENSG00000051108 ENSMUSG00000031770 UniProt Q15011 Q9JJK5 RefSeq (mRNA) NM_001010989 NM_001010990 NM_001272103 NM_014685 NM_022331 NM_001357205 RefSeq (protein) NP_001010989 NP_001259032 NP_055500 NP_001259032.1 NP_071726 NP_001344134 Location (UCSC) Chr 16: 56.93 – 56.94 Mb Chr 8: 95.11 – 95.12 Mb PubMed search
Wikidata
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Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein is a protein that in humans is encoded by the HERPUD1 gene.

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the ER stress response. This response includes the inhibition of translation to prevent further accumulation of unfolded proteins, the increased expression of proteins involved in polypeptide folding, known as the unfolded protein response (UPR), and the destruction of misfolded proteins by the ER-associated protein degradation (ERAD) system. This gene may play a role in both UPR and ERAD. Its expression is induced by UPR and it has an ER stress response element in its promoter region while the encoded protein has an N-terminal ubiquitin-like domain which may interact with the ERAD system. This protein has been shown to interact with presenilin proteins and to increase the level of amyloid-beta protein following its overexpression. Alternative splicing of this gene produces multiple transcript variants, some encoding different isoforms. The full-length nature of all transcript variants has not been determined.

Interactions

HERPUD1 has been shown to interact with UBQLN1 and UBQLN2.

Further reading

• van Laar T, van der Eb AJ, Terleth C (June 2001). "Mif1: a missing link between the unfolded protein response pathway and ER-associated protein degradation?". Current Protein & Peptide Science. 2 (2): 169–90. doi:10.2174/1389203013381189. PMID 12370023.
• Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Research. 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Kokame K, Kato H, Miyata T (March 2001). "Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response". The Journal of Biological Chemistry. 276 (12): 9199–205. doi:10.1074/jbc.M010486200. PMID 11112790.
• Sai X, Kawamura Y, Kokame K, Yamaguchi H, Shiraishi H, Suzuki R, et al. (April 2002). "Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid beta-protein". The Journal of Biological Chemistry. 277 (15): 12915–20. doi:10.1074/jbc.M112372200. PMID 11799129.
• Chtarbova S, Nimmrich I, Erdmann S, Herter P, Renner M, Kitajewski J, Müller O (November 2002). "Murine Nr4a1 and Herpud1 are up-regulated by Wnt-1, but the homologous human genes are independent from beta-catenin activation". The Biochemical Journal. 367 (Pt 3): 723–8. doi:10.1042/BJ20020699. PMC 1222938. PMID 12153396.
• Sai X, Kokame K, Shiraishi H, Kawamura Y, Miyata T, Yanagisawa K, Komano H (October 2003). "The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid beta-protein generation". FEBS Letters. 553 (1–2): 151–6. doi:10.1016/S0014-5793(03)01009-3. PMID 14550564. S2CID 1109038.
• Schulze A, Standera S, Buerger E, Kikkert M, van Voorden S, Wiertz E, et al. (December 2005). "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway". Journal of Molecular Biology. 354 (5): 1021–7. doi:10.1016/j.jmb.2005.10.020. PMID 16289116.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, et al. (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
• Liang G, Audas TE, Li Y, Cockram GP, Dean JD, Martyn AC, et al. (November 2006). "Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element". Molecular and Cellular Biology. 26 (21): 7999–8010. doi:10.1128/MCB.01046-06. PMC 1636730. PMID 16940180.
• Lenz B, Bleich S, Beutler S, Schlierf B, Schwager K, Reulbach U, et al. (December 2006). "Homocysteine regulates expression of Herp by DNA methylation involving the AARE and CREB binding sites". Experimental Cell Research. 312 (20): 4049–55. doi:10.1016/j.yexcr.2006.09.004. PMID 17020760.