HERPUD1: Difference between revisions

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{{Infobox_gene}}
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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]].<ref name="pmid10922362">{{cite journal |vauthors=Kokame K, Agarwala KL, Kato H, Miyata T | title = Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress | journal = J Biol Chem | volume = 275 | issue = 42 | pages = 32846–53 |date=Nov 2000 | pmid = 10922362 | pmc =  | doi = 10.1074/jbc.M002063200 }}</ref><ref name="pmid10708769">{{cite journal |vauthors=van Laar T, Schouten T, Hoogervorst E, van Eck M, van der Eb AJ, Terleth C | title = The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway | journal = FEBS Lett | volume = 469 | issue = 1 | pages = 123–31 |date=Apr 2000 | pmid = 10708769 | pmc =  | doi =10.1016/S0014-5793(00)01253-9 }}</ref><ref name="entrez"/>
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{{GNF_Protein_box
| image = PBB_Protein_HERPUD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wgd.
| PDB = {{PDB2|1wgd}}
| Name = Homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1
| HGNCid = 13744
| Symbol = HERPUD1
| AltSymbols =; HERP; KIAA0025; Mif1; SUP
| OMIM = 608070
| ECnumber =
| Homologene = 40973
| MGIid = 1927406
  | GeneAtlas_image1 = PBB_GE_HERPUD1_217168_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}  
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9709
    | Hs_Ensembl = ENSG00000051108
    | Hs_RefseqProtein = NP_001010989
    | Hs_RefseqmRNA = NM_001010989
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 55523249
    | Hs_GenLoc_end = 55535294
    | Hs_Uniprot = Q15011
    | Mm_EntrezGene = 64209
    | Mm_Ensembl = ENSMUSG00000031770
    | Mm_RefseqmRNA = NM_022331
    | Mm_RefseqProtein = NP_071726
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 97275629
    | Mm_GenLoc_end = 97284487
    | Mm_Uniprot = Q3TMN9
  }}
}}
'''Homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1''', also known as '''HERPUD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HERPUD1 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9709| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: HERPUD1 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9709| accessdate = }}</ref>
| summary_text = 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 [[Endoplasmic-reticulum-associated protein degradation|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.<ref name="entrez">{{cite web | title = Entrez Gene: HERPUD1 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9709| accessdate = }}</ref>
}}
}}
==Interactions==
HERPUD1 has been shown to [[Protein-protein interaction|interact]] with [[UBQLN1]]<ref name=pmid18307982>{{cite journal |last=Kim |first=Tae-Yeon |authorlink= |author2=Kim Eunmin |author3=Yoon Sungjoo Kim |author4=Yoon Jong-Bok  |date=May 2008 |title=Herp enhances ER-associated protein degradation by recruiting ubiquilins |journal=Biochem. Biophys. Res. Commun. |volume=369 |issue=2 |pages=741–6 |publisher= |location = United States| pmid = 18307982 |doi = 10.1016/j.bbrc.2008.02.086 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[UBQLN2]].<ref name="pmid18307982" />


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=van Laar T, van der Eb AJ, Terleth C |title=Mif1: a missing link between the unfolded protein response pathway and ER-associated protein degradation? |journal=Curr. Protein Pept. Sci. |volume=2 |issue= 2 |pages= 169-90 |year= 2002 |pmid= 12370023 |doi=  }}
*{{cite journal  |vauthors=van Laar T, van der Eb AJ, Terleth C |title=Mif1: a missing link between the unfolded protein response pathway and ER-associated protein degradation? |journal=Curr. Protein Pept. Sci. |volume=2 |issue= 2 |pages= 169–90 |year= 2002 |pmid= 12370023 |doi=10.2174/1389203013381189 }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=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. |journal=DNA Res. |volume=1 |issue= 1 |pages= 27-35 |year= 1995 |pmid= 7584026 |doi=  }}
*{{cite journal   |vauthors=Nomura N, Miyajima N, Sazuka T, etal |title=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. |journal=DNA Res. |volume=1 |issue= 1 |pages= 27–35 |year= 1995 |pmid= 7584026 |doi=10.1093/dnares/1.1.27 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal   |vauthors=Andersson B, Wentland MA, Ricafrente JY, etal |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
*{{cite journal   |vauthors=Yu W, Andersson B, Worley KC, etal |title=Large-Scale Concatenation cDNA Sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi= 10.1101/gr.7.4.353| pmc=139146 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal  | author=van Laar T, Schouten T, Hoogervorst E, ''et al.'' |title=The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway. |journal=FEBS Lett. |volume=469 |issue= 1 |pages= 123-31 |year= 2000 |pmid= 10708769 |doi= }}
*{{cite journal  |vauthors=Kokame K, Kato H, Miyata T |title=Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9199–205 |year= 2001 |pmid= 11112790 |doi= 10.1074/jbc.M010486200 }}
*{{cite journal | author=Kokame K, Agarwala KL, Kato H, Miyata T |title=Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32846-53 |year= 2000 |pmid= 10922362 |doi= 10.1074/jbc.M002063200 }}
*{{cite journal   |vauthors=Sai X, Kawamura Y, Kokame K, etal |title=Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid beta-protein |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12915–20 |year= 2002 |pmid= 11799129 |doi= 10.1074/jbc.M112372200 }}
*{{cite journal | author=Kokame K, Kato H, Miyata T |title=Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9199-205 |year= 2001 |pmid= 11112790 |doi= 10.1074/jbc.M010486200 }}
*{{cite journal   |vauthors=Chtarbova S, Nimmrich I, Erdmann S, etal |title=Murine Nr4a1 and Herpud1 are up-regulated by Wnt-1, but the homologous human genes are independent from beta-catenin activation |journal=Biochem. J. |volume=367 |issue= Pt 3 |pages= 723–8 |year= 2002 |pmid= 12153396 |doi= 10.1042/BJ20020699  | pmc=1222938 }}
*{{cite journal | author=Sai X, Kawamura Y, Kokame K, ''et al.'' |title=Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid beta-protein. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12915-20 |year= 2002 |pmid= 11799129 |doi= 10.1074/jbc.M112372200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal | author=Chtarbova S, Nimmrich I, Erdmann S, ''et al.'' |title=Murine Nr4a1 and Herpud1 are up-regulated by Wnt-1, but the homologous human genes are independent from beta-catenin activation. |journal=Biochem. J. |volume=367 |issue= Pt 3 |pages= 723-8 |year= 2002 |pmid= 12153396 |doi= 10.1042/BJ20020699 }}
*{{cite journal   |vauthors=Sai X, Kokame K, Shiraishi H, etal |title=The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid beta-protein generation |journal=FEBS Lett. |volume=553 |issue= 1–2 |pages= 151–6 |year= 2003 |pmid= 14550564 |doi=10.1016/S0014-5793(03)01009-3  }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal | author=Sai X, Kokame K, Shiraishi H, ''et al.'' |title=The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid beta-protein generation. |journal=FEBS Lett. |volume=553 |issue= 1-2 |pages= 151-6 |year= 2003 |pmid= 14550564 |doi= }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Schulze A, Standera S, Buerger E, etal |title=The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway |journal=J. Mol. Biol. |volume=354 |issue= 5 |pages= 1021–7 |year= 2006 |pmid= 16289116 |doi= 10.1016/j.jmb.2005.10.020 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal   |vauthors=Lim J, Hao T, Shaw C, etal |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=Schulze A, Standera S, Buerger E, ''et al.'' |title=The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. |journal=J. Mol. Biol. |volume=354 |issue= 5 |pages= 1021-7 |year= 2006 |pmid= 16289116 |doi= 10.1016/j.jmb.2005.10.020 }}
*{{cite journal   |vauthors=Liang G, Audas TE, Li Y, etal |title=Luman/CREB3 Induces Transcription of the Endoplasmic Reticulum (ER) Stress Response Protein Herp through an ER Stress Response Element |journal=Mol. Cell. Biol. |volume=26 |issue= 21 |pages= 7999–8010 |year= 2007 |pmid= 16940180 |doi= 10.1128/MCB.01046-06 | pmc=1636730 }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal   |vauthors=Lenz B, Bleich S, Beutler S, etal |title=Homocysteine regulates expression of Herp by DNA methylation involving the AARE and CREB binding sites |journal=Exp. Cell Res. |volume=312 |issue= 20 |pages= 4049–55 |year= 2007 |pmid= 17020760 |doi= 10.1016/j.yexcr.2006.09.004 }}
*{{cite journal  | author=Liang G, Audas TE, Li Y, ''et al.'' |title=Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element. |journal=Mol. Cell. Biol. |volume=26 |issue= 21 |pages= 7999-8010 |year= 2007 |pmid= 16940180 |doi= 10.1128/MCB.01046-06 }}
*{{cite journal | author=Lenz B, Bleich S, Beutler S, ''et al.'' |title=Homocysteine regulates expression of Herp by DNA methylation involving the AARE and CREB binding sites. |journal=Exp. Cell Res. |volume=312 |issue= 20 |pages= 4049-55 |year= 2007 |pmid= 17020760 |doi= 10.1016/j.yexcr.2006.09.004 }}
}}
}}
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{{refend}}
{{PDB Gallery|geneid=9709}}
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Revision as of 13:34, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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View/Edit Human

Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein is a protein that in humans is encoded by the HERPUD1 gene.[1][2][3]

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.[3]

Interactions

HERPUD1 has been shown to interact with UBQLN1[4] and UBQLN2.[4]

References

  1. ↑ Kokame K, Agarwala KL, Kato H, Miyata T (Nov 2000). "Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress". J Biol Chem. 275 (42): 32846–53. doi:10.1074/jbc.M002063200. PMID 10922362.
  2. ↑ van Laar T, Schouten T, Hoogervorst E, van Eck M, van der Eb AJ, Terleth C (Apr 2000). "The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway". FEBS Lett. 469 (1): 123–31. doi:10.1016/S0014-5793(00)01253-9. PMID 10708769.
  3. ↑ 3.0 3.1 "Entrez Gene: HERPUD1 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1".
  4. ↑ 4.0 4.1 Kim, Tae-Yeon; Kim Eunmin; Yoon Sungjoo Kim; Yoon Jong-Bok (May 2008). "Herp enhances ER-associated protein degradation by recruiting ubiquilins". Biochem. Biophys. Res. Commun. United States. 369 (2): 741–6. doi:10.1016/j.bbrc.2008.02.086. PMID 18307982.

Further reading



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