ID UBD_HUMAN Reviewed; 165 AA. AC O15205; B0UZT6; Q5STL2; Q5SUK2; Q96EC7; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 2. DT 24-JAN-2024, entry version 181. DE RecName: Full=Ubiquitin D; DE AltName: Full=Diubiquitin; DE AltName: Full=Ubiquitin-like protein FAT10; GN Name=UBD; Synonyms=FAT10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-160, AND TISSUE SPECIFICITY. RX PubMed=9368598; DOI=10.1002/eji.1830271002; RA Bates E.E.M., Ravel O., Dieu M.-C., Ho S., Guret C., Bridon J.-M., RA Ait-Yahia S., Briere F., Caux C., Banchereau J., Lebecque S.; RT "Identification and analysis of a novel member of the ubiquitin family RT expressed in dendritic cells and mature B cells."; RL Eur. J. Immunol. 27:2471-2477(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAD2L1, AND VARIANT SER-160. RC TISSUE=Spleen; RX PubMed=10200259; DOI=10.1073/pnas.96.8.4313; RA Liu Y.-C., Pan J., Zhang C., Fan W., Collinge M., Bender J.R., RA Weissman S.M.; RT "A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the RT spindle assembly checkpoint protein MAD2."; RL Proc. Natl. Acad. Sci. U.S.A. 96:4313-4318(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-160. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-160. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION IN HEPATOCELLULAR RP CARCINOMA. RX PubMed=12730673; DOI=10.1038/sj.onc.1206337; RA Lee C.G.L., Ren J., Cheong I.S.Y., Ban K.H.K., Ooi L.L.P.J., Yong Tan S., RA Kan A., Nuchprayoon I., Jin R., Lee K.-H., Choti M., Lee L.A.; RT "Expression of the FAT10 gene is highly upregulated in hepatocellular RT carcinoma and other gastrointestinal and gynecological cancers."; RL Oncogene 22:2592-2603(2003). RN [7] RP INTERACTION WITH NUB1, AND INDUCTION BY NUB1. RX PubMed=14757770; DOI=10.1074/jbc.m310114200; RA Hipp M.S., Raasi S., Groettrup M., Schmidtke G.; RT "NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 RT and accelerates its degradation."; RL J. Biol. Chem. 279:16503-16510(2004). RN [8] RP FUNCTION. RX PubMed=15831455; DOI=10.1128/mcb.25.9.3483-3491.2005; RA Hipp M.S., Kalveram B., Raasi S., Groettrup M., Schmidtke G.; RT "FAT10, a ubiquitin-independent signal for proteasomal degradation."; RL Mol. Cell. Biol. 25:3483-3491(2005). RN [9] RP INDUCTION BY CELL CYCLE. RX PubMed=16959044; DOI=10.1186/1747-1028-1-20; RA Lim C.-B., Zhang D., Lee C.G.; RT "FAT10, a gene up-regulated in various cancers, is cell-cycle regulated."; RL Cell Div. 1:20-20(2006). RN [10] RP FUNCTION, AND INDUCTION IN HIVAN. RX PubMed=16495380; DOI=10.1681/asn.2005070692; RA Ross M.J., Wosnitzer M.S., Ross M.D., Granelli B., Gusella G.L., Husain M., RA Kaufman L., Vasievich M., D'Agati V.D., Wilson P.D., Klotman M.E., RA Klotman P.E.; RT "Role of ubiquitin-like protein FAT10 in epithelial apoptosis in renal RT disease."; RL J. Am. Soc. Nephrol. 17:996-1004(2006). RN [11] RP FUNCTION, AND INTERACTION WITH MAD2L1. RX PubMed=16495226; DOI=10.1074/jbc.m507218200; RA Ren J., Kan A., Leong S.H., Ooi L.L.P.J., Jeang K.-T., Chong S.S., RA Kon O.L., Lee C.G.L.; RT "FAT10 plays a role in the regulation of chromosomal stability."; RL J. Biol. Chem. 281:11413-11421(2006). RN [12] RP INTERACTION WITH NUB1 AND PROTEASOME. RX PubMed=16707496; DOI=10.1074/jbc.m603063200; RA Schmidtke G., Kalveram B., Weber E., Bochtler P., Lukasiak S., Hipp M.S., RA Groettrup M.; RT "The UBA domains of NUB1L are required for binding but not for accelerated RT degradation of the ubiquitin-like modifier FAT10."; RL J. Biol. Chem. 281:20045-20054(2006). RN [13] RP INDUCTION BY TP53. RX PubMed=16501612; DOI=10.1038/sj.onc.1209220; RA Zhang D.W., Jeang K.-T., Lee C.G.; RT "p53 negatively regulates the expression of FAT10, a gene upregulated in RT various cancers."; RL Oncogene 25:2318-2327(2006). RN [14] RP FUNCTION, INTERACTION WITH UBA6, THIOESTER FORMATION, INDUCTION BY TNF AND RP IFNG, AND MUTAGENESIS OF 164-GLY-GLY-165. RX PubMed=17889673; DOI=10.1016/j.molcel.2007.08.020; RA Chiu Y.-H., Sun Q., Chen Z.J.; RT "E1-L2 activates both ubiquitin and FAT10."; RL Mol. Cell 27:1014-1023(2007). RN [15] RP FUNCTION, INTERACTION WITH HDAC6, SUBCELLULAR LOCATION, AND ACETYLATION. RX PubMed=19033385; DOI=10.1242/jcs.035006; RA Kalveram B., Schmidtke G., Groettrup M.; RT "The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to RT aggresomes under proteasome inhibition."; RL J. Cell Sci. 121:4079-4088(2008). RN [16] RP FUNCTION, AND INDUCTION BY CYTOKINES. RX PubMed=18574467; DOI=10.1038/onc.2008.201; RA Lukasiak S., Schiller C., Oehlschlaeger P., Schmidtke G., Krause P., RA Legler D.F., Autschbach F., Schirmacher P., Breuhahn K., Groettrup M.; RT "Proinflammatory cytokines cause FAT10 upregulation in cancers of liver and RT colon."; RL Oncogene 27:6068-6074(2008). RN [17] RP FUNCTION. RX PubMed=19166848; DOI=10.1016/j.febslet.2009.01.006; RA Schmidtke G., Kalveram B., Groettrup M.; RT "Degradation of FAT10 by the 26S proteasome is independent of RT ubiquitylation but relies on NUB1L."; RL FEBS Lett. 583:591-594(2009). RN [18] RP FUNCTION, AND INDUCTION. RX PubMed=19028597; DOI=10.1016/j.biocel.2008.10.023; RA Ebstein F., Lange N., Urban S., Seifert U., Krueger E., Kloetzel P.-M.; RT "Maturation of human dendritic cells is accompanied by functional RT remodelling of the ubiquitin-proteasome system."; RL Int. J. Biochem. Cell Biol. 41:1205-1215(2009). RN [19] RP FUNCTION, AND INDUCTION. RX PubMed=19726511; DOI=10.1128/jvi.00034-09; RA Snyder A., Alsauskas Z., Gong P., Rosenstiel P.E., Klotman M.E., RA Klotman P.E., Ross M.J.; RT "FAT10: a novel mediator of Vpr-induced apoptosis in human immunodeficiency RT virus-associated nephropathy."; RL J. Virol. 83:11983-11988(2009). RN [20] RP INDUCTION. RX PubMed=19437562; DOI=10.3748/wjg.15.2228; RA Ji F., Jin X., Jiao C.-H., Xu Q.-W., Wang Z.-W., Chen Y.-L.; RT "FAT10 level in human gastric cancer and its relation with mutant p53 RT level, lymph node metastasis and TNM staging."; RL World J. Gastroenterol. 15:2228-2233(2009). RN [21] RP FUNCTION, AND INDUCTION. RX PubMed=19959714; DOI=10.1681/asn.2009050479; RA Gong P., Canaan A., Wang B., Leventhal J., Snyder A., Nair V., Cohen C.D., RA Kretzler M., D'Agati V., Weissman S., Ross M.J.; RT "The ubiquitin-like protein FAT10 mediates NF-kappa-B activation."; RL J. Am. Soc. Nephrol. 21:316-326(2010). RN [22] {ECO:0007744|PDB:2MBE} RP STRUCTURE BY NMR OF 8-82, INTERACTION WITH TP53; MAD2L1; HDAC6; UBA6; NUB1 RP AND SQSTM1, AND MUTAGENESIS OF HIS-11; ARG-13; HIS-75; THR-77; LYS-79 AND RP 164-GLY-GLY-165. RX PubMed=25422469; DOI=10.1073/pnas.1403383111; RA Theng S.S., Wang W., Mah W.C., Chan C., Zhuo J., Gao Y., Qin H., Lim L., RA Chong S.S., Song J., Lee C.G.; RT "Disruption of FAT10-MAD2 binding inhibits tumor progression."; RL Proc. Natl. Acad. Sci. U.S.A. 111:E5282-E5291(2014). CC -!- FUNCTION: Ubiquitin-like protein modifier which can be covalently CC attached to target protein and subsequently leads to their degradation CC by the 26S proteasome, in a NUB1-dependent manner. Probably functions CC as a survival factor. Conjugation ability activated by UBA6. Promotes CC the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). CC Regulates TNF-alpha-induced and LPS-mediated activation of the central CC mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated CC proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for CC TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial CC cells (RTECs). May be involved in dendritic cell (DC) maturation, the CC process by which immature dendritic cells differentiate into fully CC competent antigen-presenting cells that initiate T-cell responses. CC Mediates mitotic non-disjunction and chromosome instability, in long- CC term in vitro culture and cancers, by abbreviating mitotic phase and CC impairing the kinetochore localization of MAD2L1 during the CC prometaphase stage of the cell cycle. May be involved in the formation CC of aggresomes when proteasome is saturated or impaired. Mediates CC apoptosis in a caspase-dependent manner, especially in renal epithelium CC and tubular cells during renal diseases such as polycystic kidney CC disease and Human immunodeficiency virus (HIV)-associated nephropathy CC (HIVAN). {ECO:0000269|PubMed:15831455, ECO:0000269|PubMed:16495226, CC ECO:0000269|PubMed:16495380, ECO:0000269|PubMed:17889673, CC ECO:0000269|PubMed:18574467, ECO:0000269|PubMed:19028597, CC ECO:0000269|PubMed:19033385, ECO:0000269|PubMed:19166848, CC ECO:0000269|PubMed:19726511, ECO:0000269|PubMed:19959714}. CC -!- SUBUNIT: Interacts directly with the 26S proteasome. The interaction CC with NUB1 via the N-terminal ubiquitin domain facilitates the linking CC of UBD-conjugated target protein to the proteasome complex and CC accelerates its own degradation and that of its conjugates. Interacts CC (via ubiquitin-like 1 domain) with the spindle checkpoint protein CC MAD2L1 during mitosis. Present in aggresomes of proteasome inhibited CC cells. Interacts with HDAC6 under proteasome impairment conditions. CC Forms a thioester with UBA6 in cells stimulated with tumor necrosis CC factor-alpha (TNFa) and interferon-gamma (IFNg). Interacts with SQSTM1 CC and TP53/p53 (PubMed:25422469). {ECO:0000269|PubMed:10200259, CC ECO:0000269|PubMed:14757770, ECO:0000269|PubMed:16495226, CC ECO:0000269|PubMed:16707496, ECO:0000269|PubMed:17889673, CC ECO:0000269|PubMed:19033385, ECO:0000269|PubMed:25422469}. CC -!- INTERACTION: CC O15205; Q13387: MAPK8IP2; NbExp=3; IntAct=EBI-6657186, EBI-722813; CC O15205; O76083-2: PDE9A; NbExp=3; IntAct=EBI-6657186, EBI-11524542; CC O15205; O60260-5: PRKN; NbExp=3; IntAct=EBI-6657186, EBI-21251460; CC O15205; P37840: SNCA; NbExp=3; IntAct=EBI-6657186, EBI-985879; CC O15205; Q9H832: UBE2Z; NbExp=2; IntAct=EBI-6657186, EBI-720977; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730673, CC ECO:0000269|PubMed:19033385}. Cytoplasm {ECO:0000250}. Note=Accumulates CC in aggresomes under proteasome inhibition conditions. CC -!- TISSUE SPECIFICITY: Constitutively expressed in mature dendritic cells CC and B-cells. Mostly expressed in the reticuloendothelial system (e.g. CC thymus, spleen), the gastrointestinal system, kidney, lung and prostate CC gland. {ECO:0000269|PubMed:12730673, ECO:0000269|PubMed:9368598}. CC -!- INDUCTION: Rapidly degraded by the proteasome. Cell-cycle regulation CC with highest expression during the S-phase (at protein level). Induced CC during dendritic cell maturation. Negatively regulated by p53/TP53. CC High levels in various gastrointestinal and gynecological cancer cells. CC Induced in RTECs in common renal diseases including diabetic CC nephropathy (DN), IgA nephropathy (IgAN), and hypertensive CC nephrosclerosis (HN), as well as in hepatocellular carcinoma (HCC) and CC during HIVAN. Inducible by the pro-inflammatory cytokines IFNG/IFN- CC gamma and TNF in cancers of liver and colon. Repressed by NUB1 (at CC protein level). {ECO:0000269|PubMed:12730673, CC ECO:0000269|PubMed:14757770, ECO:0000269|PubMed:16495380, CC ECO:0000269|PubMed:16501612, ECO:0000269|PubMed:16959044, CC ECO:0000269|PubMed:17889673, ECO:0000269|PubMed:18574467, CC ECO:0000269|PubMed:19028597, ECO:0000269|PubMed:19437562, CC ECO:0000269|PubMed:19726511, ECO:0000269|PubMed:19959714}. CC -!- PTM: Can be acetylated. {ECO:0000269|PubMed:19033385}. CC -!- MISCELLANEOUS: Common types of chronic kidney disease are associated CC with tubulointerstitial up-regulation of FAT10. FAT10 may mediate NF- CC kappa-B activation and may promote tubulointerstitial inflammation in CC chronic kidney diseases. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43742/UBD"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y12653; CAA73200.1; -; mRNA. DR EMBL; AF123050; AAD52982.1; -; mRNA. DR EMBL; AL031983; CAA21458.1; -; Genomic_DNA. DR EMBL; AL662826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645936; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759766; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759770; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR942274; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03201.1; -; Genomic_DNA. DR EMBL; BC012472; AAH12472.1; -; mRNA. DR CCDS; CCDS4662.1; -. DR RefSeq; NP_006389.2; NM_006398.3. DR PDB; 2MBE; NMR; -; A=8-82. DR PDB; 6GF1; X-ray; 1.93 A; A/B/C=10-86. DR PDB; 6GF2; NMR; -; A=85-165. DR PDB; 7PYV; X-ray; 3.27 A; C=7-165. DR PDBsum; 2MBE; -. DR PDBsum; 6GF1; -. DR PDBsum; 6GF2; -. DR PDBsum; 7PYV; -. DR AlphaFoldDB; O15205; -. DR BMRB; O15205; -. DR SMR; O15205; -. DR BioGRID; 115791; 35. DR IntAct; O15205; 8. DR MINT; O15205; -. DR STRING; 9606.ENSP00000366249; -. DR iPTMnet; O15205; -. DR PhosphoSitePlus; O15205; -. DR BioMuta; UBD; -. DR MassIVE; O15205; -. DR MaxQB; O15205; -. DR PaxDb; 9606-ENSP00000366249; -. DR PeptideAtlas; O15205; -. DR ProteomicsDB; 48509; -. DR Antibodypedia; 25984; 352 antibodies from 37 providers. DR DNASU; 10537; -. DR Ensembl; ENST00000377050.5; ENSP00000366249.4; ENSG00000213886.4. DR Ensembl; ENST00000383547.3; ENSP00000373039.3; ENSG00000206468.3. DR Ensembl; ENST00000421519.2; ENSP00000396152.2; ENSG00000231968.2. DR Ensembl; ENST00000432676.2; ENSP00000410416.2; ENSG00000228913.2. DR GeneID; 10537; -. DR KEGG; hsa:10537; -. DR MANE-Select; ENST00000377050.5; ENSP00000366249.4; NM_006398.4; NP_006389.2. DR UCSC; uc003nmo.4; human. DR AGR; HGNC:18795; -. DR CTD; 10537; -. DR DisGeNET; 10537; -. DR GeneCards; UBD; -. DR HGNC; HGNC:18795; UBD. DR HPA; ENSG00000213886; Tissue enriched (lymphoid). DR MIM; 606050; gene. DR neXtProt; NX_O15205; -. DR OpenTargets; ENSG00000213886; -. DR PharmGKB; PA38682; -. DR VEuPathDB; HostDB:ENSG00000213886; -. DR eggNOG; KOG0001; Eukaryota. DR GeneTree; ENSGT00910000144359; -. DR HOGENOM; CLU_139252_0_0_1; -. DR InParanoid; O15205; -. DR OMA; MMADYGI; -. DR OrthoDB; 5315604at2759; -. DR PhylomeDB; O15205; -. DR PathwayCommons; O15205; -. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; O15205; -. DR BioGRID-ORCS; 10537; 10 hits in 1146 CRISPR screens. DR ChiTaRS; UBD; human. DR GeneWiki; Ubiquitin_D; -. DR GenomeRNAi; 10537; -. DR Pharos; O15205; Tbio. DR PRO; PR:O15205; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O15205; Protein. DR Bgee; ENSG00000213886; Expressed in vermiform appendix and 99 other cell types or tissues. DR ExpressionAtlas; O15205; baseline and differential. DR GO; GO:0016235; C:aggresome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB. DR GO; GO:0070842; P:aggresome assembly; IDA:UniProtKB. DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB. DR GO; GO:0032446; P:protein modification by small protein conjugation; NAS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB. DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB. DR GO; GO:0034612; P:response to tumor necrosis factor; IEP:UniProtKB. DR GO; GO:0034341; P:response to type II interferon; IEP:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR CDD; cd17052; Ubl1_FAT10; 1. DR CDD; cd17053; Ubl2_FAT10; 1. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR042969; Ubiquitin_D. DR InterPro; IPR019956; Ubiquitin_dom. DR PANTHER; PTHR47731; UBIQUITIN D; 1. DR PANTHER; PTHR47731:SF1; UBIQUITIN D; 1. DR Pfam; PF00240; ubiquitin; 2. DR PRINTS; PR00348; UBIQUITIN. DR SMART; SM00213; UBQ; 2. DR SUPFAM; SSF54236; Ubiquitin-like; 2. DR PROSITE; PS50053; UBIQUITIN_2; 2. DR Genevisible; O15205; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Reference proteome; Repeat; KW Ubl conjugation pathway. FT CHAIN 1..165 FT /note="Ubiquitin D" FT /id="PRO_0000114893" FT DOMAIN 6..81 FT /note="Ubiquitin-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT DOMAIN 90..163 FT /note="Ubiquitin-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT SITE 164..165 FT /note="Activation by thioester intermediate formation with FT UBA6" FT VARIANT 51 FT /note="L -> S (in dbSNP:rs2076484)" FT /id="VAR_024273" FT VARIANT 68 FT /note="I -> T (in dbSNP:rs2076485)" FT /id="VAR_024274" FT VARIANT 95 FT /note="S -> P (in dbSNP:rs2076486)" FT /id="VAR_024275" FT VARIANT 99 FT /note="A -> G (in dbSNP:rs2076487)" FT /id="VAR_025401" FT VARIANT 120 FT /note="E -> K (in dbSNP:rs17184290)" FT /id="VAR_052693" FT VARIANT 160 FT /note="C -> S (in dbSNP:rs8337)" FT /evidence="ECO:0000269|PubMed:10200259, FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:9368598, FT ECO:0000269|Ref.4" FT /id="VAR_025402" FT VARIANT 162 FT /note="C -> F (in dbSNP:rs7757931)" FT /id="VAR_024276" FT MUTAGEN 11 FT /note="H->D: Decreases interaction with MAD2L1, no effect FT on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and FT moderately attenuates UBD-induced tumor formation in vivo; FT when associated with Q-13. Complete loss of interaction FT with MAD2L1, no effect on the interaction with TP53/p53, FT HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates FT UBD-induced tumor formation in vivo; when associated with FT Q-13; D-75; D-77 and Q-79." FT /evidence="ECO:0000269|PubMed:25422469" FT MUTAGEN 13 FT /note="R->Q: Decreases interaction with MAD2L1, no effect FT on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and FT moderately attenuates UBD-induced tumor formation in vivo; FT when associated with D-11. Complete loss of interaction FT with MAD2L1, no effect on the interaction with TP53/p53, FT HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates FT UBD-induced tumor formation in vivo; when associated with FT D-11; D-75; D-77 and Q-79." FT /evidence="ECO:0000269|PubMed:25422469" FT MUTAGEN 75 FT /note="H->D: Decreases interaction with MAD2L1, no effect FT on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and FT moderately attenuates UBD-induced tumor formation in vivo; FT when associated with D-77 and Q-79. Complete loss of FT interaction with MAD2L1, no effect on the interaction with FT TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly FT attenuates UBD-induced tumor formation in vivo; when FT associated with D-11; Q-13; D-77 and Q-79." FT /evidence="ECO:0000269|PubMed:25422469" FT MUTAGEN 77 FT /note="T->D: Decreases interaction with MAD2L1, no effect FT on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and FT moderately attenuates UBD-induced tumor formation in vivo; FT when associated with D-75 and Q-79. Complete loss of FT interaction with MAD2L1, no effect on the interaction with FT TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly FT attenuates UBD-induced tumor formation in vivo; when FT associated with D-11; Q-13; D-75 and Q-79." FT /evidence="ECO:0000269|PubMed:25422469" FT MUTAGEN 79 FT /note="K->Q: Decreases interaction with MAD2L1, no effect FT on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and FT moderately attenuates UBD-induced tumor formation in vivo; FT when associated with D-75 and D-77. Complete loss of FT interaction with MAD2L1, no effect on the interaction with FT TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly FT attenuates UBD-induced tumor formation in vivo; when FT associated with D-11; Q-13; D-75 and D-77." FT /evidence="ECO:0000269|PubMed:25422469" FT MUTAGEN 164..165 FT /note="GG->AA: Impaired thioester formation-mediated FT activation by UBA6. Loss of interaction with UBA6 and FT SQSTM1. No effect on its interaction with MAD2L1, HDAC6 and FT NUB1." FT /evidence="ECO:0000269|PubMed:17889673, FT ECO:0000269|PubMed:25422469" FT STRAND 10..17 FT /evidence="ECO:0007829|PDB:6GF1" FT STRAND 20..24 FT /evidence="ECO:0007829|PDB:6GF1" FT HELIX 30..41 FT /evidence="ECO:0007829|PDB:6GF1" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:6GF1" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:6GF1" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:6GF1" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:6GF1" FT STRAND 72..80 FT /evidence="ECO:0007829|PDB:6GF1" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:7PYV" FT STRAND 102..109 FT /evidence="ECO:0007829|PDB:7PYV" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:7PYV" FT TURN 127..129 FT /evidence="ECO:0007829|PDB:7PYV" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:7PYV" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:7PYV" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:7PYV" SQ SEQUENCE 165 AA; 18473 MW; 40BE415049920CC6 CRC64; MAPNASCLCV HVRSEEWDLM TFDANPYDSV KKIKEHVRSK TKVPVQDQVL LLGSKILKPR RSLSSYGIDK EKTIHLTLKV VKPSDEELPL FLVESGDEAK RHLLQVRRSS SVAQVKAMIE TKTGIIPETQ IVTCNGKRLE DGKMMADYGI RKGNLLFLAC YCIGG //