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O15205

- UBD_HUMAN

UniProt

O15205 - UBD_HUMAN

Protein

Ubiquitin D

Gene

UBD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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. Conjugation ability activated by UBA6. 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 such as polycystic kidney disease and Human immunodeficiency virus (HIV)-associated nephropathy (HIVAN).10 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei164 – 1652Activation by thioester intermediate formation with UBA6

    GO - Molecular functioni

    1. proteasome binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. aggresome assembly Source: UniProtKB
    2. myeloid dendritic cell differentiation Source: UniProtKB
    3. positive regulation of apoptotic process Source: UniProtKB
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. protein modification by small protein conjugation Source: UniProtKB
    6. protein ubiquitination Source: UniProtKB
    7. proteolysis Source: UniProtKB
    8. response to interferon-gamma Source: UniProtKB
    9. response to organonitrogen compound Source: Ensembl
    10. response to tumor necrosis factor Source: UniProtKB
    11. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin D
    Alternative name(s):
    Diubiquitin
    Ubiquitin-like protein FAT10
    Gene namesi
    Name:UBD
    Synonyms:FAT10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:18795. UBD.

    Subcellular locationi

    Nucleus 2 Publications. Cytoplasm By similarity
    Note: Accumulates in aggresomes under proteasome inhibition conditions.

    GO - Cellular componenti

    1. aggresome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1652GG → AA: Impaired thioester formation-mediated activation by UBA6. 1 Publication

    Organism-specific databases

    PharmGKBiPA38682.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 165165Ubiquitin DPRO_0000114893Add
    BLAST

    Post-translational modificationi

    Can be acetylated.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO15205.
    PaxDbiO15205.
    PRIDEiO15205.

    PTM databases

    PhosphoSiteiO15205.

    Expressioni

    Tissue specificityi

    Constitutively expressed in mature dendritic cells and B-cells. Mostly expressed in the reticuloendothelial system (e.g. thymus, spleen), the gastrointestinal system, kidney, lung and prostate gland.2 Publications

    Inductioni

    Rapidly degraded by the proteasome. Cell-cycle regulation with highest expression during the S-phase (at protein level). Induced during dendritic cell maturation. Negatively regulated by p53/TP53. High levels in various gastrointestinal and gynecological cancer cells. Induced in RTECs in common renal diseases including diabetic nephropathy (DN), IgA nephropathy (IgAN), and hypertensive nephrosclerosis (HN), as well as in hepatocellular carcinoma (HCC) and during HIVAN. Inducible by the proinflammatory cytokines IFNG/IFN-gamma and TNF in cancers of liver and colon. Repressed by NUB1L (at protein level).11 Publications

    Gene expression databases

    BgeeiO15205.
    CleanExiHS_UBD.
    GenevestigatoriO15205.

    Organism-specific databases

    HPAiHPA043710.

    Interactioni

    Subunit structurei

    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. 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).6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBE2ZQ9H8322EBI-6657186,EBI-720977

    Protein-protein interaction databases

    BioGridi115791. 667 interactions.
    IntActiO15205. 4 interactions.
    STRINGi9606.ENSP00000366249.

    Structurei

    3D structure databases

    ProteinModelPortaliO15205.
    SMRiO15205. Positions 10-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 8176Ubiquitin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini90 – 16374Ubiquitin-like 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 ubiquitin-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5272.
    HOVERGENiHBG101094.
    InParanoidiO15205.
    KOiK12157.
    OMAiEINIFFL.
    OrthoDBiEOG75TMDT.
    PhylomeDBiO15205.

    Family and domain databases

    InterProiIPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00240. ubiquitin. 2 hits.
    [Graphical view]
    PRINTSiPR00348. UBIQUITIN.
    SMARTiSM00213. UBQ. 2 hits.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 2 hits.
    PROSITEiPS50053. UBIQUITIN_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O15205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPNASCLCV HVRSEEWDLM TFDANPYDSV KKIKEHVRSK TKVPVQDQVL    50
    LLGSKILKPR RSLSSYGIDK EKTIHLTLKV VKPSDEELPL FLVESGDEAK 100
    RHLLQVRRSS SVAQVKAMIE TKTGIIPETQ IVTCNGKRLE DGKMMADYGI 150
    RKGNLLFLAC YCIGG 165
    Length:165
    Mass (Da):18,473
    Last modified:November 24, 2009 - v2
    Checksum:i40BE415049920CC6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511L → S.
    Corresponds to variant rs2076484 [ dbSNP | Ensembl ].
    VAR_024273
    Natural varianti68 – 681I → T.
    Corresponds to variant rs2076485 [ dbSNP | Ensembl ].
    VAR_024274
    Natural varianti95 – 951S → P.
    Corresponds to variant rs2076486 [ dbSNP | Ensembl ].
    VAR_024275
    Natural varianti99 – 991A → G.
    Corresponds to variant rs2076487 [ dbSNP | Ensembl ].
    VAR_025401
    Natural varianti120 – 1201E → K.
    Corresponds to variant rs17184290 [ dbSNP | Ensembl ].
    VAR_052693
    Natural varianti160 – 1601C → S.4 Publications
    Corresponds to variant rs8337 [ dbSNP | Ensembl ].
    VAR_025402
    Natural varianti162 – 1621C → F.
    Corresponds to variant rs7757931 [ dbSNP | Ensembl ].
    VAR_024276

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12653 mRNA. Translation: CAA73200.1.
    AF123050 mRNA. Translation: AAD52982.1.
    AL031983 Genomic DNA. Translation: CAA21458.1.
    AL662826 Genomic DNA. Translation: CAI17384.1.
    AL645936 Genomic DNA. Translation: CAI18010.1.
    CR759766, CR942274 Genomic DNA. Translation: CAQ06603.1.
    CR759770 Genomic DNA. Translation: CAQ10041.1.
    CR942274, CR759766 Genomic DNA. Translation: CAQ10316.1.
    CH471081 Genomic DNA. Translation: EAX03201.1.
    BC012472 mRNA. Translation: AAH12472.1.
    CCDSiCCDS4662.1.
    RefSeqiNP_006389.2. NM_006398.3.
    UniGeneiHs.44532.

    Genome annotation databases

    EnsembliENST00000377050; ENSP00000366249; ENSG00000213886.
    ENST00000383547; ENSP00000373039; ENSG00000206468.
    ENST00000421519; ENSP00000396152; ENSG00000231968.
    ENST00000432676; ENSP00000410416; ENSG00000228913.
    GeneIDi10537.
    KEGGihsa:10537.
    UCSCiuc003nmo.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12653 mRNA. Translation: CAA73200.1 .
    AF123050 mRNA. Translation: AAD52982.1 .
    AL031983 Genomic DNA. Translation: CAA21458.1 .
    AL662826 Genomic DNA. Translation: CAI17384.1 .
    AL645936 Genomic DNA. Translation: CAI18010.1 .
    CR759766 , CR942274 Genomic DNA. Translation: CAQ06603.1 .
    CR759770 Genomic DNA. Translation: CAQ10041.1 .
    CR942274 , CR759766 Genomic DNA. Translation: CAQ10316.1 .
    CH471081 Genomic DNA. Translation: EAX03201.1 .
    BC012472 mRNA. Translation: AAH12472.1 .
    CCDSi CCDS4662.1.
    RefSeqi NP_006389.2. NM_006398.3.
    UniGenei Hs.44532.

    3D structure databases

    ProteinModelPortali O15205.
    SMRi O15205. Positions 10-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115791. 667 interactions.
    IntActi O15205. 4 interactions.
    STRINGi 9606.ENSP00000366249.

    PTM databases

    PhosphoSitei O15205.

    Proteomic databases

    MaxQBi O15205.
    PaxDbi O15205.
    PRIDEi O15205.

    Protocols and materials databases

    DNASUi 10537.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377050 ; ENSP00000366249 ; ENSG00000213886 .
    ENST00000383547 ; ENSP00000373039 ; ENSG00000206468 .
    ENST00000421519 ; ENSP00000396152 ; ENSG00000231968 .
    ENST00000432676 ; ENSP00000410416 ; ENSG00000228913 .
    GeneIDi 10537.
    KEGGi hsa:10537.
    UCSCi uc003nmo.3. human.

    Organism-specific databases

    CTDi 10537.
    GeneCardsi GC06M029525.
    GC06Mj29519.
    GC06Mk29523.
    GC06Mm29523.
    HGNCi HGNC:18795. UBD.
    HPAi HPA043710.
    MIMi 606050. gene.
    neXtProti NX_O15205.
    PharmGKBi PA38682.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5272.
    HOVERGENi HBG101094.
    InParanoidi O15205.
    KOi K12157.
    OMAi EINIFFL.
    OrthoDBi EOG75TMDT.
    PhylomeDBi O15205.

    Miscellaneous databases

    ChiTaRSi UBD. human.
    GeneWikii Ubiquitin_D.
    GenomeRNAii 10537.
    NextBioi 39977.
    PROi O15205.
    SOURCEi Search...

    Gene expression databases

    Bgeei O15205.
    CleanExi HS_UBD.
    Genevestigatori O15205.

    Family and domain databases

    InterProi IPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00240. ubiquitin. 2 hits.
    [Graphical view ]
    PRINTSi PR00348. UBIQUITIN.
    SMARTi SM00213. UBQ. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 2 hits.
    PROSITEi PS50053. UBIQUITIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells."
      Bates E.E.M., Ravel O., Dieu M.-C., Ho S., Guret C., Bridon J.-M., Ait-Yahia S., Briere F., Caux C., Banchereau J., Lebecque S.
      Eur. J. Immunol. 27:2471-2477(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-160, TISSUE SPECIFICITY.
    2. "A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2."
      Liu Y.-C., Pan J., Zhang C., Fan W., Collinge M., Bender J.R., Weissman S.M.
      Proc. Natl. Acad. Sci. U.S.A. 96:4313-4318(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAD2L1, VARIANT SER-160.
      Tissue: Spleen.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-160.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-160.
    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].
      Tissue: Urinary bladder.
    6. "Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers."
      Lee C.G.L., Ren J., Cheong I.S.Y., Ban K.H.K., Ooi L.L.P.J., Yong Tan S., Kan A., Nuchprayoon I., Jin R., Lee K.-H., Choti M., Lee L.A.
      Oncogene 22:2592-2603(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION IN HEPATOCELLULAR CARCINOMA.
    7. "NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation."
      Hipp M.S., Raasi S., Groettrup M., Schmidtke G.
      J. Biol. Chem. 279:16503-16510(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUB1L, INDUCTION BY NUB1L.
    8. "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.
    9. "FAT10, a gene up-regulated in various cancers, is cell-cycle regulated."
      Lim C.-B., Zhang D., Lee C.G.
      Cell Div. 1:20-20(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY CELL CYCLE.
    10. Cited for: FUNCTION, INDUCTION IN HIVAN.
    11. Cited for: FUNCTION, INTERACTION WITH MAD2L1.
    12. "The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10."
      Schmidtke G., Kalveram B., Weber E., Bochtler P., Lukasiak S., Hipp M.S., Groettrup M.
      J. Biol. Chem. 281:20045-20054(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUB1L AND PROTEASOME.
    13. "p53 negatively regulates the expression of FAT10, a gene upregulated in various cancers."
      Zhang D.W., Jeang K.-T., Lee C.G.
      Oncogene 25:2318-2327(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY TP53.
    14. "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, THIOESTER FORMATION, INDUCTION BY TNF AND IFNG, MUTAGENESIS OF 164-GLY-GLY-165.
    15. "The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition."
      Kalveram B., Schmidtke G., Groettrup M.
      J. Cell Sci. 121:4079-4088(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC6, SUBCELLULAR LOCATION, ACETYLATION.
    16. Cited for: FUNCTION, INDUCTION BY CYTOKINES.
    17. "Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L."
      Schmidtke G., Kalveram B., Groettrup M.
      FEBS Lett. 583:591-594(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Maturation of human dendritic cells is accompanied by functional remodelling of the ubiquitin-proteasome system."
      Ebstein F., Lange N., Urban S., Seifert U., Krueger E., Kloetzel P.-M.
      Int. J. Biochem. Cell Biol. 41:1205-1215(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    19. "FAT10: a novel mediator of Vpr-induced apoptosis in human immunodeficiency virus-associated nephropathy."
      Snyder A., Alsauskas Z., Gong P., Rosenstiel P.E., Klotman M.E., Klotman P.E., Ross M.J.
      J. Virol. 83:11983-11988(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    20. "FAT10 level in human gastric cancer and its relation with mutant p53 level, lymph node metastasis and TNM staging."
      Ji F., Jin X., Jiao C.-H., Xu Q.-W., Wang Z.-W., Chen Y.-L.
      World J. Gastroenterol. 15:2228-2233(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    21. Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiUBD_HUMAN
    AccessioniPrimary (citable) accession number: O15205
    Secondary accession number(s): B0UZT6
    , Q5STL2, Q5SUK2, Q96EC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Common types of chronic kidney disease are associated with tubulointerstitial up-regulation of FAT10. FAT10 may mediate NF-kappa-B activation and may promote tubulointerstitial inflammation in chronic kidney diseases.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3