Ubiquitin D

Ubiquitin D is a protein that in humans is encoded by the UBD gene.[5][6][7]

UBD
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2MBE
Identifiers
Aliases	UBD, FAT10, GABBR1, UBD-3, ubiquitin D
External IDs	OMIM: 606050 MGI: 1344410 HomoloGene: 4665 GeneCards: UBD
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p22.1 Start 29,555,515 bp[1] End 29,559,732 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 B1 Start 37,193,892 bp[2] End 37,196,095 bp[2]
Gene ontology Molecular function • proteasome binding • GO:0001948 protein binding Cellular component • cytoplasm • aggresome • cell nucleus • fibrillar center • cytosol Biological process • positive regulation of I-kappaB kinase/NF-kappaB signaling • response to tumor necrosis factor • myeloid dendritic cell differentiation • protein modification by small protein conjugation • protein ubiquitination • ubiquitin-dependent protein catabolic process • response to interferon-gamma • proteolysis • aggresome assembly • positive regulation of apoptotic process • post-translational modification • regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10537	24108
Ensembl	ENSG00000228913 ENSG00000231968 ENSG00000206468 ENSG00000206513 ENSG00000224654 ENSG00000213886 ENSG00000226898	ENSMUSG00000035186
UniProt	O15205	P63072
RefSeq (mRNA)	NM_006398	NM_023137
RefSeq (protein)	NP_006389	NP_075626
Location (UCSC)	Chr 6: 29.56 – 29.56 Mb	Chr 17: 37.19 – 37.2 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

UBD (gene) has been shown to interact with NUB1[8] and MAD2L1.[9]

References

1. ENSG00000231968, ENSG00000206468, ENSG00000206513, ENSG00000224654, ENSG00000213886, ENSG00000226898 GRCh38: Ensembl release 89: ENSG00000228913, ENSG00000231968, ENSG00000206468, ENSG00000206513, ENSG00000224654, ENSG00000213886, ENSG00000226898 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000035186 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Bates EE, Ravel O, Dieu MC, Ho S, Guret C, Bridon JM, Ait-Yahia S, Brière F, Caux C, Banchereau J, Lebecque S (Oct 1997). "Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells". European Journal of Immunology. 27 (10): 2471–7. doi:10.1002/eji.1830271002. PMID 9368598.
6. Fan W, Cai W, Parimoo S, Schwarz DC, Lennon GG, Weissman SM (Aug 1996). "Identification of seven new human MHC class I region genes around the HLA-F locus". Immunogenetics. 44 (2): 97–103. doi:10.1007/BF02660056. PMID 8662070.
7. "Entrez Gene: UBD ubiquitin D".
8. Hipp MS, Raasi S, Groettrup M, Schmidtke G (Apr 2004). "NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation". The Journal of Biological Chemistry. 279 (16): 16503–10. doi:10.1074/jbc.M310114200. PMID 14757770.
9. Liu YC, Pan J, Zhang C, Fan W, Collinge M, Bender JR, Weissman SM (Apr 1999). "A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2". Proceedings of the National Academy of Sciences of the United States of America. 96 (8): 4313–8. doi:10.1073/pnas.96.8.4313. PMC 16329. PMID 10200259.

Further reading

• Mazzé FM, Degrève L (2006). "The role of viral and cellular proteins in the budding of human immunodeficiency virus". Acta Virologica. 50 (2): 75–85. PMID 16808324.
• Ott DE, Coren LV, Copeland TD, Kane BP, Johnson DG, Sowder RC, Yoshinaka Y, Oroszlan S, Arthur LO, Henderson LE (Apr 1998). "Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus". Journal of Virology. 72 (4): 2962–8. doi:10.1128/JVI.72.4.2962-2968.1998. PMC 109742. PMID 9525617.
• Liu YC, Pan J, Zhang C, Fan W, Collinge M, Bender JR, Weissman SM (Apr 1999). "A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2". Proceedings of the National Academy of Sciences of the United States of America. 96 (8): 4313–8. doi:10.1073/pnas.96.8.4313. PMC 16329. PMID 10200259.
• Schubert U, Ott DE, Chertova EN, Welker R, Tessmer U, Princiotta MF, Bennink JR, Krausslich HG, Yewdell JW (Nov 2000). "Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2". Proceedings of the National Academy of Sciences of the United States of America. 97 (24): 13057–62. Bibcode:2000PNAS...9713057S. doi:10.1073/pnas.97.24.13057. PMC 27177. PMID 11087859.
• Strack B, Calistri A, Accola MA, Palu G, Gottlinger HG (Nov 2000). "A role for ubiquitin ligase recruitment in retrovirus release". Proceedings of the National Academy of Sciences of the United States of America. 97 (24): 13063–8. Bibcode:2000PNAS...9713063S. doi:10.1073/pnas.97.24.13063. PMC 27178. PMID 11087860.
• Ott DE, Coren LV, Chertova EN, Gagliardi TD, Schubert U (Dec 2000). "Ubiquitination of HIV-1 and MuLV Gag". Virology. 278 (1): 111–21. doi:10.1006/viro.2000.0648. PMID 11112487.
• Strack B, Calistri A, Göttlinger HG (Jun 2002). "Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis". Journal of Virology. 76 (11): 5472–9. doi:10.1128/JVI.76.11.5472-5479.2002. PMC 137019. PMID 11991975.
• Ott DE, Coren LV, Sowder RC, Adams J, Schubert U (Mar 2003). "Retroviruses have differing requirements for proteasome function in the budding process". Journal of Virology. 77 (6): 3384–93. doi:10.1128/JVI.77.6.3384-3393.2003. PMC 149504. PMID 12610113.
• Lee CG, Ren J, Cheong IS, Ban KH, Ooi LL, Yong Tan S, Kan A, Nuchprayoon I, Jin R, Lee KH, Choti M, Lee LA (May 2003). "Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers". Oncogene. 22 (17): 2592–603. doi:10.1038/sj.onc.1206337. PMID 12730673.
• Brès V, Kiernan RE, Linares LK, Chable-Bessia C, Plechakova O, Tréand C, Emiliani S, Peloponese JM, Jeang KT, Coux O, Scheffner M, Benkirane M (Aug 2003). "A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter". Nature Cell Biology. 5 (8): 754–61. doi:10.1038/ncb1023. PMID 12883554.
• Hipp MS, Raasi S, Groettrup M, Schmidtke G (Apr 2004). "NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation". The Journal of Biological Chemistry. 279 (16): 16503–10. doi:10.1074/jbc.M310114200. PMID 14757770.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (Mar 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
• Hipp MS, Kalveram B, Raasi S, Groettrup M, Schmidtke G (May 2005). "FAT10, a ubiquitin-independent signal for proteasomal degradation". Molecular and Cellular Biology. 25 (9): 3483–91. doi:10.1128/MCB.25.9.3483-3491.2005. PMC 1084302. PMID 15831455.
• Gottwein E, Kräusslich HG (Jul 2005). "Analysis of human immunodeficiency virus type 1 Gag ubiquitination". Journal of Virology. 79 (14): 9134–44. doi:10.1128/JVI.79.14.9134-9144.2005. PMC 1168789. PMID 15994808.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.