UBQLN2: Difference between revisions

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Latest revision as of 09:04, 11 January 2019

Ubiquilin-2 is a protein that in humans is encoded by the UBQLN2 gene.^[1]^[2]

Function

This gene encodes a ubiquitin-like protein (ubiquilin) that shares high degree of similarity with related products in yeast, rat and frog. Ubiquilins contain a N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. They physically associate with both proteasomes and ubiquitin ligases, and are thus thought to functionally link the ubiquitination machinery to the proteasome to effect in vivo protein degradation. This ubiquilin has also been shown to bind the ATPase domain of the Hsp70-like Stch protein.^[2]

Similarity to other proteins

Human UBQLN2 shares a high degree of similarity with related ubiquilins including UBQLN1 and UBQLN4.^[3]

Clinical significance

In a small proportion of familial amyotrophic lateral sclerosis (fALS), the UBQLN2 gene is mutated, causing formation of a non-functional Ubiquilin 2 enzyme. This non-functioning enzyme leads to the accumulation of ubiquinated proteins in the lower motor neurons and upper corticospinal motor neurons, due to the fact that ubiquilin 2 normally degrades these ubiquinated proteins, but cannot if the ALS mutation is present.^[4] The same accumulations occur in patients without UBQLN2 mutations, but with mutations in other genes, including TDP-43 and C9ORF72.

Interactions

UBQLN2 has been shown to interact with HERPUD1^[5] and UBE3A.^[6]

References

↑ Kaye FJ, Modi S, Ivanovska I, Koonin EV, Thress K, Kubo A, Kornbluth S, Rose MD (Mar 2000). "A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch". FEBS Lett. 467 (2–3): 348–55. doi:10.1016/S0014-5793(00)01135-2. PMID 10675567.
↑ ^2.0 ^2.1 "Entrez Gene: UBQLN2 ubiquilin 2".
↑ Marín I (March 2014). "The ubiquilin gene family: evolutionary patterns and functional insights". BMC Evol Biol. 14: 63. doi:10.1186/1471-2148-14-63. PMC 4230246. PMID 24674348.
↑ Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N, Yang Y, Fecto F, Shi Y, Zhai H, Jiang H, Hirano M, Rampersaud E, Jansen GH, Donkervoort S, Bigio EH, Brooks BR, Ajroud K, Sufit RL, Haines JL, Mugnaini E, Pericak-Vance MA, Siddique T (August 2011). "Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia". Nature. 477 (7363): 211–215. doi:10.1038/nature10353. PMC 3169705. PMID 21857683. Lay summary – New York Times.
↑ Kim TY, Kim E, Yoon SK, Yoon JB (May 2008). "Herp enhances ER-associated protein degradation by recruiting ubiquilins". Biochem. Biophys. Res. Commun. 369 (2): 741–6. doi:10.1016/j.bbrc.2008.02.086. PMID 18307982.
↑ Kleijnen MF, Shih AH, Zhou P, Kumar S, Soccio RE, Kedersha NL, Gill G, Howley PM (August 2000). "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Mol. Cell. 6 (2): 409–19. doi:10.1016/S1097-2765(00)00040-X. PMID 10983987.

Ueki N, Oda T, Kondo M, et al. (1999). "Selection system for genes encoding nuclear-targeted proteins". Nat. Biotechnol. 16 (13): 1338–42. doi:10.1038/4315. PMID 9853615.
Kaye FJ, Shows TB (2000). "Assignment of ubiquilin2 (UBQLN2) to human chromosome xp11. 23→p11.1 by GeneBridge radiation hybrids". Cytogenet. Cell Genet. 89 (1–2): 116–7. doi:10.1159/000015588. PMID 10894951.
Kleijnen MF, Shih AH, Zhou P, et al. (2000). "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Mol. Cell. 6 (2): 409–19. doi:10.1016/S1097-2765(00)00040-X. PMID 10983987.
Murillas R, Simms KS, Hatakeyama S, et al. (2002). "Identification of developmentally expressed proteins that functionally interact with Nedd4 ubiquitin ligase". J. Biol. Chem. 277 (4): 2897–907. doi:10.1074/jbc.M110047200. PMID 11717310.
Walters KJ, Kleijnen MF, Goh AM, et al. (2002). "Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a". Biochemistry. 41 (6): 1767–77. doi:10.1021/bi011892y. PMID 11827521.
Saeki Y, Sone T, Toh-e A, Yokosawa H (2002). "Identification of ubiquitin-like protein-binding subunits of the 26S proteasome". Biochem. Biophys. Res. Commun. 296 (4): 813–9. doi:10.1016/S0006-291X(02)02002-8. PMID 12200120.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Kleijnen MF, Alarcon RM, Howley PM (2004). "The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome". Mol. Biol. Cell. 14 (9): 3868–75. doi:10.1091/mbc.E02-11-0766. PMC 196580. PMID 12972570.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
Massey LK, Mah AL, Monteiro MJ (2006). "Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrin". Biochem. J. 391 (Pt 3): 513–25. doi:10.1042/BJ20050491. PMC 1276952. PMID 15975090.
Lim J, Hao T, Shaw C, et al. (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.
Ford DL, Monteiro MJ (2006). "Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins". Biochem. J. 399 (3): 397–404. doi:10.1042/BJ20060441. PMC 1615901. PMID 16813565.
Kang Y, Zhang N, Koepp DM, Walters KJ (2007). "Ubiquitin receptor proteins hHR23a and hPLIC2 interact". J. Mol. Biol. 365 (4): 1093–101. doi:10.1016/j.jmb.2006.10.056. PMC 1994665. PMID 17098253.

This article on a gene on the human X chromosome and/or its associated protein is a stub. You can help Wikipedia by expanding it.

[pmid10675567-1] Kaye FJ, Modi S, Ivanovska I, Koonin EV, Thress K, Kubo A, Kornbluth S, Rose MD (Mar 2000). "A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch". FEBS Lett. 467 (2–3): 348–55. doi:10.1016/S0014-5793(00)01135-2. PMID 10675567.

[entrez-2] 2.0 ^2.1 "Entrez Gene: UBQLN2 ubiquilin 2".

[pmid24674348-3] Marín I (March 2014). "The ubiquilin gene family: evolutionary patterns and functional insights". BMC Evol Biol. 14: 63. doi:10.1186/1471-2148-14-63. PMC 4230246. PMID 24674348.

[pmid21857683-4] Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N, Yang Y, Fecto F, Shi Y, Zhai H, Jiang H, Hirano M, Rampersaud E, Jansen GH, Donkervoort S, Bigio EH, Brooks BR, Ajroud K, Sufit RL, Haines JL, Mugnaini E, Pericak-Vance MA, Siddique T (August 2011). "Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia". Nature. 477 (7363): 211–215. doi:10.1038/nature10353. PMC 3169705. PMID 21857683. Lay summary – New York Times.

[pmid18307982-5] Kim TY, Kim E, Yoon SK, Yoon JB (May 2008). "Herp enhances ER-associated protein degradation by recruiting ubiquilins". Biochem. Biophys. Res. Commun. 369 (2): 741–6. doi:10.1016/j.bbrc.2008.02.086. PMID 18307982.

[pmid10983987-6] Kleijnen MF, Shih AH, Zhou P, Kumar S, Soccio RE, Kedersha NL, Gill G, Howley PM (August 2000). "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Mol. Cell. 6 (2): 409–19. doi:10.1016/S1097-2765(00)00040-X. PMID 10983987.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''Ubiquilin-2''' is a [[protein]] that in humans is encoded by the ''UBQLN2'' [[gene]].<ref name="pmid10675567">{{cite journal |vauthors=Kaye FJ, Modi S, Ivanovska I, Koonin EV, Thress K, Kubo A, Kornbluth S, Rose MD | title = A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch | journal = FEBS Lett | volume = 467 | issue = 2–3 | pages = 348–55 |date=Mar 2000 | pmid = 10675567 | pmc =  | doi =10.1016/S0014-5793(00)01135-2  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBQLN2 ubiquilin 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29978| accessdate = }}</ref>
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{GNF_Protein_box
- | image = PBB_Protein_UBQLN2_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j8c.
- | PDB = {{PDB2|1j8c}}
- | Name = Ubiquilin 2
- | HGNCid = 12509
- | Symbol = UBQLN2
- | AltSymbols =; CHAP1; CHAP1/DSK2; Dsk2; HRIHFB2157; LIC-2; N4BP4; PLIC-2; PLIC2; RIHFB2157
- | OMIM = 300264
- | ECnumber =
- | Homologene = 81830
- | MGIid = 1860283
- | GeneAtlas_image1 = PBB_GE_UBQLN2_215884_s_at_tn.png
- | Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
- | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
- | Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 29978
-    | Hs_Ensembl = ENSG00000188021
-    | Hs_RefseqProtein = NP_038472
-    | Hs_RefseqmRNA = NM_013444
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = X
-    | Hs_GenLoc_start = 56606797
-    | Hs_GenLoc_end = 56611026
-    | Hs_Uniprot = Q9UHD9
-    | Mm_EntrezGene = 54609
-    | Mm_Ensembl = ENSMUSG00000050148
-    | Mm_RefseqmRNA = NM_018798
-    | Mm_RefseqProtein = NP_061268
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = X
-    | Mm_GenLoc_start = 148838948
-    | Mm_GenLoc_end = 148842286
-    | Mm_Uniprot = Q9QZM0
-  }}
-}}
-'''Ubiquilin 2''', also known as '''UBQLN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBQLN2 ubiquilin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29978| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+This gene encodes a [[ubiquitin-like protein]] ([[ubiquilin]]) that shares high degree of similarity with related products in yeast, rat and frog. Ubiquilins contain a [[N-terminus|N-terminal]] ubiquitin-like domain and a [[C-terminus|C-terminal]] ubiquitin-associated domain. They physically associate with both [[proteasome]]s and [[ubiquitin ligase]]s, and are thus thought to functionally link the ubiquitination machinery to the proteasome to effect ''in vivo'' protein degradation. This ubiquilin has also been shown to bind the [[ATPase]] domain of the [[Hsp70]]-like [[STCH|Stch]] protein.<ref name="entrez"/>
-{{PBB_Summary
-| section_title =
+==Similarity to other proteins==
-| summary_text = This gene encodes an ubiquitin-like protein (ubiquilin) that shares high degree of similarity with related products in yeast, rat and frog. Ubiquilins contain a N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. They physically associate with both proteasomes and ubiquitin ligases, and thus thought to functionally link the ubiquitination machinery to the proteasome to affect in vivo protein degradation. This ubiquilin has also been shown to bind the ATPase domain of the Hsp70-like Stch protein.<ref name="entrez">{{cite web | title = Entrez Gene: UBQLN2 ubiquilin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29978| accessdate = }}</ref>
-}}
+Human UBQLN2 shares a high degree of similarity with related ubiquilins including [[UBQLN1]] and [[UBQLN4]].<ref name="pmid24674348">{{cite journal | author = Marín I | title = The ubiquilin gene family: evolutionary patterns and functional insights | journal = BMC Evol Biol | volume = 14| pages = 63 | date=March 2014 | pmid = 24674348 | doi = 10.1186/1471-2148-14-63 | pmc=4230246}}</ref>
+== Clinical significance ==
+In a small proportion of familial [[amyotrophic lateral sclerosis]] (fALS), the UBQLN2 gene is mutated, causing formation of a non-functional Ubiquilin 2 enzyme. This non-functioning enzyme leads to the accumulation of ubiquinated proteins in the lower motor neurons and upper corticospinal motor neurons, due to the fact that ubiquilin 2 normally degrades these ubiquinated proteins, but cannot if the ALS mutation is present.<ref name="pmid21857683">{{cite journal |vauthors=Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N, Yang Y, Fecto F, Shi Y, Zhai H, Jiang H, Hirano M, Rampersaud E, Jansen GH, Donkervoort S, Bigio EH, Brooks BR, Ajroud K, Sufit RL, Haines JL, Mugnaini E, Pericak-Vance MA, Siddique T | title = Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia | journal = Nature | volume = 477| issue = 7363| pages = 211–215|date=August 2011 | pmid = 21857683 | doi = 10.1038/nature10353 | laysummary = https://www.nytimes.com/2011/08/30/health/30theory.html | laysource = New York Times | pmc=3169705}}</ref> The same accumulations occur in patients without UBQLN2 mutations, but with mutations in other genes, including TDP-43 and [[C9orf72|C9ORF72]].<!-- Citation needed. -->
+==Interactions==
+UBQLN2 has been shown to [[Protein-protein interaction|interact]] with [[HERPUD1]]<ref name="pmid18307982">{{cite journal |vauthors=Kim TY, Kim E, Yoon SK, Yoon JB | title = Herp enhances ER-associated protein degradation by recruiting ubiquilins | journal = Biochem. Biophys. Res. Commun. | volume = 369 | issue = 2 | pages = 741–6 |date=May 2008 | pmid = 18307982 | doi = 10.1016/j.bbrc.2008.02.086 }}</ref> and [[UBE3A]].<ref name="pmid10983987">{{cite journal |vauthors=Kleijnen MF, Shih AH, Zhou P, Kumar S, Soccio RE, Kedersha NL, Gill G, Howley PM | title = The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome | journal = Mol. Cell | volume = 6 | issue = 2 | pages = 409–19 |date=August 2000 | pmid = 10983987 | doi = 10.1016/S1097-2765(00)00040-X }}</ref>
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
-{{PBB_Further_reading
+*{{cite journal  | author=Ueki N |title=Selection system for genes encoding nuclear-targeted proteins |journal=Nat. Biotechnol. |volume=16 |issue= 13 |pages= 1338–42 |year= 1999 |pmid= 9853615 |doi= 10.1038/4315  |name-list-format=vanc| author2=Oda T  | author3=Kondo M  | display-authors=3  | last4=Yano  | first4=Kazuhiro  | last5=Noguchi  | first5=Teruhisa  | last6=Muramatsu  | first6=Masa-aki }}
-| citations =
+*{{cite journal  |vauthors=Kaye FJ, Shows TB |title=Assignment of ubiquilin2 (UBQLN2) to human chromosome xp11. 23→p11.1 by GeneBridge radiation hybrids |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1–2 |pages= 116–7 |year= 2000 |pmid= 10894951 |doi=10.1159/000015588  }}
-*{{cite journal  | author=Ueki N, Oda T, Kondo M, ''et al.'' |title=Selection system for genes encoding nuclear-targeted proteins. |journal=Nat. Biotechnol. |volume=16 |issue= 13 |pages= 1338-42 |year= 1999 |pmid= 9853615 |doi= 10.1038/4315 }}
+*{{cite journal  | author=Kleijnen MF |title=The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome |journal=Mol. Cell |volume=6 |issue= 2 |pages= 409–19 |year= 2000 |pmid= 10983987 |doi=10.1016/S1097-2765(00)00040-X  |name-list-format=vanc| author2=Shih AH  | author3=Zhou P  | display-authors=3  | last4=Kumar  | first4=Sushant  | last5=Soccio  | first5=Raymond E.  | last6=Kedersha  | first6=Nancy L.  | last7=Gill  | first7=Grace  | last8=Howley  | first8=Peter M.  }}
-*{{cite journal  | author=Kaye FJ, Modi S, Ivanovska I, ''et al.'' |title=A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. |journal=FEBS Lett. |volume=467 |issue= 2-3 |pages= 348-55 |year= 2000 |pmid= 10675567 |doi=  }}
+*{{cite journal  | author=Murillas R |title=Identification of developmentally expressed proteins that functionally interact with Nedd4 ubiquitin ligase |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2897–907 |year= 2002 |pmid= 11717310 |doi= 10.1074/jbc.M110047200  |name-list-format=vanc| author2=Simms KS  | author3=Hatakeyama S  | display-authors=3  | last4=Weissman  | first4=AM  | last5=Kuehn  | first5=MR }}
-*{{cite journal  | author=Kaye FJ, Shows TB |title=Assignment of ubiquilin2 (UBQLN2) to human chromosome xp11. 23-->p11.1 by GeneBridge radiation hybrids. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1-2 |pages= 116-7 |year= 2000 |pmid= 10894951 |doi=  }}
+*{{cite journal  | author=Walters KJ |title=Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a |journal=Biochemistry |volume=41 |issue= 6 |pages= 1767–77 |year= 2002 |pmid= 11827521 |doi=10.1021/bi011892y  |name-list-format=vanc| author2=Kleijnen MF  | author3=Goh AM  | display-authors=3  | last4=Wagner  | first4=Gerhard  | last5=Howley  | first5=Peter M.  }}
-*{{cite journal  | author=Kleijnen MF, Shih AH, Zhou P, ''et al.'' |title=The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 409-19 |year= 2000 |pmid= 10983987 |doi=  }}
+*{{cite journal  |vauthors=Saeki Y, Sone T, Toh-e A, Yokosawa H |title=Identification of ubiquitin-like protein-binding subunits of the 26S proteasome |journal=Biochem. Biophys. Res. Commun. |volume=296 |issue= 4 |pages= 813–9 |year= 2002 |pmid= 12200120 |doi=10.1016/S0006-291X(02)02002-8  }}
-*{{cite journal  | author=Murillas R, Simms KS, Hatakeyama S, ''et al.'' |title=Identification of developmentally expressed proteins that functionally interact with Nedd4 ubiquitin ligase. |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2897-907 |year= 2002 |pmid= 11717310 |doi= 10.1074/jbc.M110047200 }}
+*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
-*{{cite journal  | author=Walters KJ, Kleijnen MF, Goh AM, ''et al.'' |title=Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a. |journal=Biochemistry |volume=41 |issue= 6 |pages= 1767-77 |year= 2002 |pmid= 11827521 |doi=  }}
+*{{cite journal  |vauthors=Kleijnen MF, Alarcon RM, Howley PM |title=The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome |journal=Mol. Biol. Cell |volume=14 |issue= 9 |pages= 3868–75 |year= 2004 |pmid= 12972570 |doi= 10.1091/mbc.E02-11-0766  | pmc=196580 }}
-*{{cite journal  | author=Saeki Y, Sone T, Toh-e A, Yokosawa H |title=Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. |journal=Biochem. Biophys. Res. Commun. |volume=296 |issue= 4 |pages= 813-9 |year= 2002 |pmid= 12200120 |doi=  }}
+*{{cite journal  | author=Colland F |title=Functional proteomics mapping of a human signaling pathway |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104  | pmc=442148  |name-list-format=vanc| author2=Jacq X  | author3=Trouplin V  | display-authors=3  | last4=Mougin  | first4=C  | last5=Groizeleau  | first5=C  | last6=Hamburger  | first6=A  | last7=Meil  | first7=A  | last8=Wojcik  | first8=J  | last9=Legrain  | first9=P }}
-*{{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  | author=Ross MT |title=The DNA sequence of the human X chromosome |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440  | pmc=2665286  |name-list-format=vanc| author2=Grafham DV  | author3=Coffey AJ  | display-authors=3  | last4=Scherer  | first4=Steven  | last5=McLay  | first5=Kirsten  | last6=Muzny  | first6=Donna  | last7=Platzer  | first7=Matthias  | last8=Howell  | first8=Gareth R.  | last9=Burrows  | first9=Christine }}
-*{{cite journal  | author=Kleijnen MF, Alarcon RM, Howley PM |title=The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. |journal=Mol. Biol. Cell |volume=14 |issue= 9 |pages= 3868-75 |year= 2004 |pmid= 12972570 |doi= 10.1091/mbc.E02-11-0766 }}
+*{{cite journal  |vauthors=Massey LK, Mah AL, Monteiro MJ |title=Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrin |journal=Biochem. J. |volume=391 |issue= Pt 3 |pages= 513–25 |year= 2006 |pmid= 15975090 |doi= 10.1042/BJ20050491  | pmc=1276952 }}
-*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
+*{{cite journal  | author=Lim J |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  |name-list-format=vanc| author2=Hao T  | author3=Shaw C  | display-authors=3  | last4=Patel  | first4=Akash J.  | last5=Szabó  | first5=Gábor  | last6=Rual  | first6=Jean-François  | last7=Fisk  | first7=C. Joseph  | last8=Li  | first8=Ning  | last9=Smolyar  | first9=Alex }}
-*{{cite journal  | author=Ross MT, Grafham DV, Coffey AJ, ''et al.'' |title=The DNA sequence of the human X chromosome. |journal=Nature |volume=434 |issue= 7031 |pages= 325-37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 }}
+*{{cite journal  |vauthors=Ford DL, Monteiro MJ |title=Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins |journal=Biochem. J. |volume=399 |issue= 3 |pages= 397–404 |year= 2006 |pmid= 16813565 |doi= 10.1042/BJ20060441  | pmc=1615901 }}
-*{{cite journal  | author=Massey LK, Mah AL, Monteiro MJ |title=Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrin. |journal=Biochem. J. |volume=391 |issue= Pt 3 |pages= 513-25 |year= 2006 |pmid= 15975090 |doi= 10.1042/BJ20050491 }}
+*{{cite journal  |vauthors=Kang Y, Zhang N, Koepp DM, Walters KJ |title=Ubiquitin receptor proteins hHR23a and hPLIC2 interact |journal=J. Mol. Biol. |volume=365 |issue= 4 |pages= 1093–101 |year= 2007 |pmid= 17098253 |doi= 10.1016/j.jmb.2006.10.056  | pmc=1994665 }}
-*{{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  | author=Ford DL, Monteiro MJ |title=Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins. |journal=Biochem. J. |volume=399 |issue= 3 |pages= 397-404 |year= 2006 |pmid= 16813565 |doi= 10.1042/BJ20060441 }}
-*{{cite journal  | author=Kang Y, Zhang N, Koepp DM, Walters KJ |title=Ubiquitin receptor proteins hHR23a and hPLIC2 interact. |journal=J. Mol. Biol. |volume=365 |issue= 4 |pages= 1093-101 |year= 2007 |pmid= 17098253 |doi= 10.1016/j.jmb.2006.10.056 }}
-}}
 {{refend}}
-{{protein-stub}}
+{{PDB Gallery|geneid=29978}}
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+{{gene-X-stub}}