UBD_HUMAN
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 03-AUG-2022, entry version 173.
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="http://atlasgeneticsoncology.org/Genes/UBDID43742ch6p22.html";
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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 PDBsum; 2MBE; -.
DR PDBsum; 6GF1; -.
DR PDBsum; 6GF2; -.
DR AlphaFoldDB; O15205; -.
DR BMRB; O15205; -.
DR SMR; O15205; -.
DR BioGRID; 115791; 31.
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; O15205; -.
DR PeptideAtlas; O15205; -.
DR PRIDE; O15205; -.
DR ProteomicsDB; 48509; -.
DR Antibodypedia; 25984; 318 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 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; ETQIVTC; -.
DR OrthoDB; 1377739at2759; -.
DR PhylomeDB; O15205; -.
DR PathwayCommons; O15205; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; O15205; -.
DR BioGRID-ORCS; 10537; 10 hits in 1075 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 98 other tissues.
DR ExpressionAtlas; O15205; baseline and differential.
DR Genevisible; O15205; HS.
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 I-kappaB kinase/NF-kappaB signaling; 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:0034341; P:response to interferon-gamma; IEP:UniProtKB.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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; PTHR47731; 1.
DR Pfam; PF00240; ubiquitin; 2.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
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 90..96
FT /evidence="ECO:0007829|PDB:6GF2"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6GF2"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:6GF2"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6GF2"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6GF2"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6GF2"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6GF2"
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
