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O15205

- UBD_HUMAN

UniProt

O15205 - UBD_HUMAN

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Protein

Ubiquitin D

Gene

UBD

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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MBENMR-A8-82[»]
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.
GeneTreeiENSGT00760000119340.
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

        10         20         30         40         50
MAPNASCLCV HVRSEEWDLM TFDANPYDSV KKIKEHVRSK TKVPVQDQVL
60 70 80 90 100
LLGSKILKPR RSLSSYGIDK EKTIHLTLKV VKPSDEELPL FLVESGDEAK
110 120 130 140 150
RHLLQVRRSS SVAQVKAMIE TKTGIIPETQ IVTCNGKRLE DGKMMADYGI
160
RKGNLLFLAC YCIGG
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

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MBE NMR - A 8-82 [» ]
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.
GeneTreei ENSGT00760000119340.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3