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P63072 (UBD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin D
Alternative name(s):
Diubiquitin
Ubiquitin-like protein FAT10
Gene names
Name:Ubd
Synonyms:Fat10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 NUB1L-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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Subunit structure

Interact directly with the 26S proteasome. The interaction with NUB1L vie 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 By similarity. Interacts with the spindle checkpoint protein MAD2L1 during mitosis. Present in aggresomes of proteasome inhibited cells. Interacts with HDAC6 under proteasome impairment conditions. Forms a thioester with UBA6 in cells stimulated with tumor necrosis factor-alpha (TNFa) and interferon-gamma (IFNg). Ref.10

Subcellular location

Nucleus. Cytoplasm. Note: Accumulates in aggresomes under proteasome inhibition conditions By similarity. Ref.6

Tissue specificity

Mostly expressed in thymus and intestine. Ref.9

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). Ref.6 Ref.9 Ref.11

Post-translational modification

Can be acetylated By similarity.

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. Ref.9 Ref.12

Sequence similarities

Contains 2 ubiquitin-like domains.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaggresome assembly

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid dendritic cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

protein modification by small protein conjugation

Inferred by curator Ref.6. Source: UniProtKB

protein ubiquitination

Inferred from mutant phenotype Ref.6Ref.10. Source: UniProtKB

response to interferon-gamma

Inferred from expression pattern Ref.9. Source: UniProtKB

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from expression pattern Ref.9. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.6Ref.10. Source: UniProtKB

   Cellular_componentaggresome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionproteasome binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Ubiquitin D
PRO_0000114894

Regions

Domain3 – 7876Ubiquitin-like 1
Domain87 – 16074Ubiquitin-like 2

Sites

Site161 – 1622Activation by thioester intermediate formation with UBA6

Experimental info

Mutagenesis161 – 1622Missing: Impaired conjugation of target proteins. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P63072 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 6107D8604F96455F

FASTA16218,376
        10         20         30         40         50         60 
MASVRTCVVR SDQWRLMTFE TTENDKVKKI NEHIRSQTKV SVQDQILLLD SKILKPHRKL 

        70         80         90        100        110        120 
SSYGIDKETT IHLTLKVVKP SDEELPLFLV ESKNEGQRHL LRVRRSSSVA QVKEMIESVT 

       130        140        150        160 
SVIPKKQVVN CNGKKLEDGK IMADYNIKSG SLLFLTTHCT GG 

« Hide

References

« Hide 'large scale' references
[1]"Disruption of the mouse Fat10 gene by gene targeting in the mouse embryonic stem cells."
Yu X., Liu Y., Weissman S.M.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Small intestine.
[3]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[6]"The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis."
Raasi S., Schmidtke G., Groettrup M.
J. Biol. Chem. 276:35334-35343(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF 161-GLY-GLY-162.
[7]"FAT10, a ubiquitin-independent signal for proteasomal degradation."
Hipp M.S., Kalveram B., Raasi S., Groettrup M., Schmidtke G.
Mol. Cell. Biol. 25:3483-3491(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Role of ubiquitin-like protein FAT10 in epithelial apoptosis in renal disease."
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.
J. Am. Soc. Nephrol. 17:996-1004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"FAT10/diubiquitin-like protein-deficient mice exhibit minimal phenotypic differences."
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.
Mol. Cell. Biol. 26:5180-5189(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY TNFA AND IFNG, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[10]"E1-L2 activates both ubiquitin and FAT10."
Chiu Y.-H., Sun Q., Chen Z.J.
Mol. Cell 27:1014-1023(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBA6.
[11]"Fat10 is an epigenetic marker for liver preneoplasia in a drug-primed mouse model of tumorigenesis."
Oliva J., Bardag-Gorce F., French B.A., Li J., McPhaul L., Amidi F., Dedes J., Habibi A., Nguyen S., French S.W.
Exp. Mol. Pathol. 84:102-112(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY DRUG INJURY.
[12]"The ubiquitin-like protein FAT10 mediates NF-kappa-B activation."
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.
J. Am. Soc. Nephrol. 21:316-326(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF314088 Genomic DNA. Translation: AAG27477.1.
AK008116 mRNA. Translation: BAB25471.1.
AK008552 mRNA. Translation: BAB25738.1.
CT010257 mRNA. Translation: CAJ18465.1.
AL078630 Genomic DNA. No translation available.
BC027627 mRNA. Translation: AAH27627.2.
BC036383 mRNA. Translation: AAH36383.1.
CCDSCCDS28737.1.
RefSeqNP_075626.1. NM_023137.3.
UniGeneMm.140210.

3D structure databases

ProteinModelPortalP63072.
SMRP63072. Positions 9-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204900. 3 interactions.
MINTMINT-1341042.
STRING10090.ENSMUSP00000035808.

PTM databases

PhosphoSiteP63072.

Proteomic databases

PRIDEP63072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038844; ENSMUSP00000035808; ENSMUSG00000035186.
GeneID24108.
KEGGmmu:24108.
UCSCuc008cmi.2. mouse.

Organism-specific databases

CTD10537.
MGIMGI:1344410. Ubd.

Phylogenomic databases

eggNOGNOG259502.
GeneTreeENSGT00750000117776.
HOGENOMHOG000134446.
HOVERGENHBG101094.
InParanoidQ4FJZ5.
KOK12157.
OMATCNGKKL.
OrthoDBEOG75TMDT.
PhylomeDBP63072.

Gene expression databases

BgeeP63072.
CleanExMM_UBD.
GenevestigatorP63072.

Family and domain databases

InterProIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00240. ubiquitin. 2 hits.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMSSF54236. SSF54236. 2 hits.
PROSITEPS50053. UBIQUITIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBD. mouse.
NextBio304123.
PROP63072.
SOURCESearch...

Entry information

Entry nameUBD_MOUSE
AccessionPrimary (citable) accession number: P63072
Secondary accession number(s): Q4FJZ5, Q9WV10
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot