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Ubiquitin D (Diubiquitin) (Ubiquitin-like protein FAT10)

 UBD_MOUSE               Reviewed;         162 AA.
P63072; Q4FJZ5; Q9WV10;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
12-SEP-2018, entry version 117.
RecName: Full=Ubiquitin D;
AltName: Full=Diubiquitin;
AltName: Full=Ubiquitin-like protein FAT10;
Name=Ubd; Synonyms=Fat10;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Yu X., Liu Y., Weissman S.M.;
"Disruption of the mouse Fat10 gene by gene targeting in the mouse
embryonic stem cells.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Small intestine;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF
161-GLY-GLY-162.
PubMed=11445583; DOI=10.1074/jbc.M105139200;
Raasi S., Schmidtke G., Groettrup M.;
"The ubiquitin-like protein FAT10 forms covalent conjugates and
induces apoptosis.";
J. Biol. Chem. 276:35334-35343(2001).
[7]
FUNCTION.
PubMed=15831455; DOI=10.1128/MCB.25.9.3483-3491.2005;
Hipp M.S., Kalveram B., Raasi S., Groettrup M., Schmidtke G.;
"FAT10, a ubiquitin-independent signal for proteasomal degradation.";
Mol. Cell. Biol. 25:3483-3491(2005).
[8]
FUNCTION.
PubMed=16495380; DOI=10.1681/ASN.2005070692;
Ross M.J., Wosnitzer M.S., Ross M.D., Granelli B., Gusella G.L.,
Husain M., Kaufman L., Vasievich M., D'Agati V.D., Wilson P.D.,
Klotman M.E., Klotman P.E.;
"Role of ubiquitin-like protein FAT10 in epithelial apoptosis in renal
disease.";
J. Am. Soc. Nephrol. 17:996-1004(2006).
[9]
FUNCTION, INDUCTION BY TNFA AND IFNG, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=16782901; DOI=10.1128/MCB.00966-05;
Canaan A., Yu X., Booth C.J., Lian J., Lazar I., Gamfi S.L.,
Castille K., Kohya N., Nakayama Y., Liu Y.-C., Eynon E., Flavell R.,
Weissman S.M.;
"FAT10/diubiquitin-like protein-deficient mice exhibit minimal
phenotypic differences.";
Mol. Cell. Biol. 26:5180-5189(2006).
[10]
FUNCTION, AND INTERACTION WITH UBA6.
PubMed=17889673; DOI=10.1016/j.molcel.2007.08.020;
Chiu Y.-H., Sun Q., Chen Z.J.;
"E1-L2 activates both ubiquitin and FAT10.";
Mol. Cell 27:1014-1023(2007).
[11]
INDUCTION BY DRUG INJURY.
PubMed=18280469; DOI=10.1016/j.yexmp.2007.12.003;
Oliva J., Bardag-Gorce F., French B.A., Li J., McPhaul L., Amidi F.,
Dedes J., Habibi A., Nguyen S., French S.W.;
"Fat10 is an epigenetic marker for liver preneoplasia in a drug-primed
mouse model of tumorigenesis.";
Exp. Mol. Pathol. 84:102-112(2008).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19959714; DOI=10.1681/ASN.2009050479;
Gong P., Canaan A., Wang B., Leventhal J., Snyder A., Nair V.,
Cohen C.D., Kretzler M., D'Agati V., Weissman S., Ross M.J.;
"The ubiquitin-like protein FAT10 mediates NF-kappa-B activation.";
J. Am. Soc. Nephrol. 21:316-326(2010).
-!- FUNCTION: Ubiquitin-like protein modifier which can be covalently
attached to target protein and subsequently leads to their
degradation by the 26S proteasome, in a NUB1-dependent manner.
Probably functions as a survival factor. Promotes the expression
of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-
alpha-induced and LPS-mediated activation of the central mediator
of innate immunity NF-kappa-B by promoting TNF-alpha-mediated
proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required
for TNF-alpha-induced p65 nuclear translocation in renal tubular
epithelial cells (RTECs). May be involved in dendritic cell (DC)
maturation, the process by which immature dendritic cells
differentiate into fully competent antigen-presenting cells that
initiate T-cell responses. Mediates mitotic non-disjunction and
chromosome instability, in long-term in vitro culture and cancers,
by abbreviating mitotic phase and impairing the kinetochore
localization of MAD2L1 during the prometaphase stage of the cell
cycle. May be involved in the formation of aggresomes when
proteasome is saturated or impaired. Mediates apoptosis in a
caspase-dependent manner, especially in renal epithelium and
tubular cells during renal diseases. {ECO:0000269|PubMed:11445583,
ECO:0000269|PubMed:15831455, ECO:0000269|PubMed:16495380,
ECO:0000269|PubMed:16782901, ECO:0000269|PubMed:17889673,
ECO:0000269|PubMed:19959714}.
-!- SUBUNIT: Interact directly with the 26S proteasome. The
interaction with NUB1 via the N-terminal ubiquitin domain
facilitates the linking of UBD-conjugated target protein to the
proteasome complex and accelerates its own degradation and that of
its conjugates. Interacts (via ubiquitin-like 1 domain) with the
spindle checkpoint protein MAD2L1 during mitosis. Present in
aggresomes of proteasome inhibited cells. Interacts with HDAC6
under proteasome impairment conditions (By similarity). Forms a
thioester with UBA6 in cells stimulated with tumor necrosis
factor-alpha (TNFa) and interferon-gamma (IFNg) (PubMed:17889673).
Interacts with SQSTM1 and TP53/p53 (By similarity).
{ECO:0000250|UniProtKB:O15205, ECO:0000269|PubMed:17889673}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11445583}.
Cytoplasm {ECO:0000269|PubMed:11445583}. Note=Accumulates in
aggresomes under proteasome inhibition conditions. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Mostly expressed in thymus and intestine.
{ECO:0000269|PubMed:16782901}.
-!- INDUCTION: Rapidly degraded by the proteasome. Cell-cycle
regulation with highest expression during the S-phase (at protein
level). Over expressed in hepatocytes by drug injury (e.g. DDC;
diethyl 1,4-dihydro-2,4,6-trimethyl-3,5-pyridinedicarboxylate).
Inducible by the proinflammatory cytokines tumor necrosis factor-
alpha (TNFa) and interferon-gamma (IFNg).
{ECO:0000269|PubMed:11445583, ECO:0000269|PubMed:16782901,
ECO:0000269|PubMed:18280469}.
-!- PTM: Can be acetylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Spontaneous sporadic apoptotic death. Higher
sensitivity toward endotoxin challenge. Abrogated TNF-alpha-
induced NF-kappa-B activation and reduced induction of NF-kappa-B-
regulated genes. Impaired TNF-alpha-induced I-kappa-B-alpha
degradation and nuclear translocation of p65 in RTECs. Reduced
expression of LMP2. {ECO:0000269|PubMed:16782901,
ECO:0000269|PubMed:19959714}.
-----------------------------------------------------------------------
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EMBL; AF314088; AAG27477.1; -; Genomic_DNA.
EMBL; AK008116; BAB25471.1; -; mRNA.
EMBL; AK008552; BAB25738.1; -; mRNA.
EMBL; CT010257; CAJ18465.1; -; mRNA.
EMBL; AL078630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027627; AAH27627.2; -; mRNA.
EMBL; BC036383; AAH36383.1; -; mRNA.
CCDS; CCDS28737.1; -.
RefSeq; NP_075626.1; NM_023137.3.
UniGene; Mm.140210; -.
ProteinModelPortal; P63072; -.
SMR; P63072; -.
BioGrid; 204900; 1.
MINT; P63072; -.
STRING; 10090.ENSMUSP00000035808; -.
iPTMnet; P63072; -.
PhosphoSitePlus; P63072; -.
PaxDb; P63072; -.
PRIDE; P63072; -.
Ensembl; ENSMUST00000038844; ENSMUSP00000035808; ENSMUSG00000035186.
GeneID; 24108; -.
KEGG; mmu:24108; -.
UCSC; uc008cmi.2; mouse.
CTD; 10537; -.
MGI; MGI:1344410; Ubd.
eggNOG; KOG0001; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00910000144359; -.
HOGENOM; HOG000134446; -.
HOVERGEN; HBG101094; -.
InParanoid; P63072; -.
KO; K12157; -.
OMA; ETQIVTC; -.
OrthoDB; EOG091G178I; -.
PhylomeDB; P63072; -.
Reactome; R-MMU-8951664; Neddylation.
ChiTaRS; Ubd; mouse.
PRO; PR:P63072; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000035186; Expressed in 55 organ(s), highest expression level in thymus.
CleanEx; MM_UBD; -.
Genevisible; P63072; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
GO; GO:0070842; P:aggresome assembly; ISS:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032446; P:protein modification by small protein conjugation; IC:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
GO; GO:0034341; P:response to interferon-gamma; IEP:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF00240; ubiquitin; 2.
PRINTS; PR00348; UBIQUITIN.
SMART; SM00213; UBQ; 2.
SUPFAM; SSF54236; SSF54236; 2.
PROSITE; PS50053; UBIQUITIN_2; 2.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Nucleus;
Reference proteome; Repeat; Ubl conjugation pathway.
CHAIN 1 162 Ubiquitin D.
/FTId=PRO_0000114894.
DOMAIN 3 78 Ubiquitin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 87 160 Ubiquitin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
SITE 161 162 Activation by thioester intermediate
formation with UBA6.
MUTAGEN 161 162 Missing: Impaired conjugation of target
proteins. {ECO:0000269|PubMed:11445583}.
SEQUENCE 162 AA; 18376 MW; 6107D8604F96455F CRC64;
MASVRTCVVR SDQWRLMTFE TTENDKVKKI NEHIRSQTKV SVQDQILLLD SKILKPHRKL
SSYGIDKETT IHLTLKVVKP SDEELPLFLV ESKNEGQRHL LRVRRSSSVA QVKEMIESVT
SVIPKKQVVN CNGKKLEDGK IMADYNIKSG SLLFLTTHCT GG


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