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Q9NPD8

- UBE2T_HUMAN

UniProt

Q9NPD8 - UBE2T_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 T

Gene

UBE2T

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.6 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Glycyl thioester intermediate

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. chromatin binding Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB
    3. protein autoubiquitination Source: UniProtKB
    4. protein K11-linked ubiquitination Source: UniProtKB
    5. protein K27-linked ubiquitination Source: UniProtKB
    6. protein K29-linked ubiquitination Source: UniProtKB
    7. protein K48-linked ubiquitination Source: UniProtKB
    8. protein K63-linked ubiquitination Source: UniProtKB
    9. protein K6-linked ubiquitination Source: UniProtKB
    10. protein monoubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_18410. Fanconi Anemia pathway.
    SignaLinkiQ9NPD8.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 T (EC:6.3.2.19)
    Alternative name(s):
    Cell proliferation-inducing gene 50 protein
    Ubiquitin carrier protein T
    Ubiquitin-protein ligase T
    Gene namesi
    Name:UBE2T
    ORF Names:HSPC150, PIG50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25009. UBE2T.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Accumulates to chromatin.

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631F → A: Decreased binding to FANCL. 1 Publication
    Mutagenesisi86 – 861C → A: Loss of E2 enzyme activity. 5 Publications
    Mutagenesisi91 – 911K → R: Decreased monoubiquitination. 1 Publication
    Mutagenesisi182 – 19110Missing: Decreased monoubiquitination.

    Organism-specific databases

    PharmGKBiPA142670655.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 197197Ubiquitin-conjugating enzyme E2 TPRO_0000082509Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki91 – 91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Auto-ubiquitinated. Effects of auto-monoubiquitination at Lys-91 and Lys-182 are unclear: according to a report, monoubiquitination inactivates E2 enzyme activity (PubMed:16916645). In contrast, according to another report, autoubiquitination does not affect E2 enzyme activity (PubMed:19111657).2 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NPD8.
    PaxDbiQ9NPD8.
    PRIDEiQ9NPD8.

    PTM databases

    PhosphoSiteiQ9NPD8.

    Expressioni

    Inductioni

    Down-regulated following hypoxia. Up-regulated in breast cancers.1 Publication

    Gene expression databases

    BgeeiQ9NPD8.
    CleanExiHS_UBE2T.
    GenevestigatoriQ9NPD8.

    Organism-specific databases

    HPAiHPA002831.

    Interactioni

    Subunit structurei

    Interacts with FANCL and BRCA1.5 Publications

    Protein-protein interaction databases

    BioGridi118858. 22 interactions.
    DIPiDIP-52740N.
    IntActiQ9NPD8. 10 interactions.
    STRINGi9606.ENSP00000356243.

    Structurei

    Secondary structure

    197
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1616
    Beta strandi22 – 298
    Beta strandi33 – 397
    Turni45 – 484
    Beta strandi50 – 567
    Turni59 – 624
    Beta strandi67 – 726
    Helixi88 – 903
    Turni93 – 953
    Helixi104 – 11613
    Helixi126 – 1349
    Helixi136 – 15015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YH2X-ray2.00A1-167[»]
    4CCGX-ray2.40A/B1-197[»]
    ProteinModelPortaliQ9NPD8.
    SMRiQ9NPD8. Positions 1-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPD8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiQ9NPD8.
    KOiK13960.
    OMAiIVPERYP.
    OrthoDBiEOG7BP84K.
    PhylomeDBiQ9NPD8.
    TreeFamiTF354203.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NPD8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRASRLKRE LHMLATEPPP GITCWQDKDQ MDDLRAQILG GANTPYEKGV    50
    FKLEVIIPER YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP 100
    SLNIATVLTS IQLLMSEPNP DDPLMADISS EFKYNKPAFL KNARQWTEKH 150
    ARQKQKADEE EMLDNLPEAG DSRVHNSTQK RKASQLVGIE KKFHPDV 197
    Length:197
    Mass (Da):22,521
    Last modified:October 1, 2000 - v1
    Checksum:i6C02D774A7FA928A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032931 mRNA. Translation: BAA93711.1.
    AF160215 mRNA. Translation: AAF67016.1.
    AF161499 mRNA. Translation: AAF29114.1.
    AK000504 mRNA. Translation: BAA91211.1.
    AY542309 mRNA. Translation: AAT08178.1.
    AL356953 Genomic DNA. Translation: CAI15933.1.
    CH471067 Genomic DNA. Translation: EAW91411.1.
    BC004152 mRNA. Translation: AAH04152.1.
    BC019284 mRNA. Translation: AAH19284.1.
    CCDSiCCDS1425.1.
    RefSeqiNP_054895.1. NM_014176.3.
    UniGeneiHs.5199.

    Genome annotation databases

    EnsembliENST00000367274; ENSP00000356243; ENSG00000077152.
    GeneIDi29089.
    KEGGihsa:29089.
    UCSCiuc001gxx.4. human.

    Polymorphism databases

    DMDMi73622065.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032931 mRNA. Translation: BAA93711.1 .
    AF160215 mRNA. Translation: AAF67016.1 .
    AF161499 mRNA. Translation: AAF29114.1 .
    AK000504 mRNA. Translation: BAA91211.1 .
    AY542309 mRNA. Translation: AAT08178.1 .
    AL356953 Genomic DNA. Translation: CAI15933.1 .
    CH471067 Genomic DNA. Translation: EAW91411.1 .
    BC004152 mRNA. Translation: AAH04152.1 .
    BC019284 mRNA. Translation: AAH19284.1 .
    CCDSi CCDS1425.1.
    RefSeqi NP_054895.1. NM_014176.3.
    UniGenei Hs.5199.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YH2 X-ray 2.00 A 1-167 [» ]
    4CCG X-ray 2.40 A/B 1-197 [» ]
    ProteinModelPortali Q9NPD8.
    SMRi Q9NPD8. Positions 1-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118858. 22 interactions.
    DIPi DIP-52740N.
    IntActi Q9NPD8. 10 interactions.
    STRINGi 9606.ENSP00000356243.

    PTM databases

    PhosphoSitei Q9NPD8.

    Polymorphism databases

    DMDMi 73622065.

    Proteomic databases

    MaxQBi Q9NPD8.
    PaxDbi Q9NPD8.
    PRIDEi Q9NPD8.

    Protocols and materials databases

    DNASUi 29089.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367274 ; ENSP00000356243 ; ENSG00000077152 .
    GeneIDi 29089.
    KEGGi hsa:29089.
    UCSCi uc001gxx.4. human.

    Organism-specific databases

    CTDi 29089.
    GeneCardsi GC01M202300.
    HGNCi HGNC:25009. UBE2T.
    HPAi HPA002831.
    MIMi 610538. gene.
    neXtProti NX_Q9NPD8.
    PharmGKBi PA142670655.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi Q9NPD8.
    KOi K13960.
    OMAi IVPERYP.
    OrthoDBi EOG7BP84K.
    PhylomeDBi Q9NPD8.
    TreeFami TF354203.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_18410. Fanconi Anemia pathway.
    SignaLinki Q9NPD8.

    Miscellaneous databases

    ChiTaRSi UBE2T. human.
    EvolutionaryTracei Q9NPD8.
    GenomeRNAii 29089.
    NextBioi 52094.
    PROi Q9NPD8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NPD8.
    CleanExi HS_UBE2T.
    Genevestigatori Q9NPD8.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ubiquitin-conjugating enzyme isolog."
      Okaze H., Hayashi A., Kozuma S., Saito T.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adrenal gland.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Blood.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Carcinoma.
    5. "Identification of a human cell proliferation inducing gene."
      Kim J.W.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lung.
    9. "UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation."
      Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M., D'Andrea A.D., Dutta A.
      Mol. Cell 23:589-596(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91, MUTAGENESIS OF CYS-86.
    10. "UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited independently to chromatin: a basis for the regulation of FANCD2 monoubiquitination."
      Alpi A., Langevin F., Mosedale G., Machida Y.J., Dutta A., Patel K.J.
      Mol. Cell. Biol. 27:8421-8430(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FANCL, MUTAGENESIS OF CYS-86.
    11. "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
      Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
      Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FANCL, UBIQUITINATION AT LYS-91 AND LYS-182, MUTAGENESIS OF CYS-86; LYS-91 AND 182-LYS--LYS-191.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Ubiquitination and downregulation of BRCA1 by ubiquitin-conjugating enzyme E2T overexpression in human breast cancer cells."
      Ueki T., Park J.H., Nishidate T., Kijima K., Hirata K., Nakamura Y., Katagiri T.
      Cancer Res. 69:8752-8760(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-86, INTERACTION WITH BRCA1.
    14. "FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL."
      Longerich S., San Filippo J., Liu D., Sung P.
      J. Biol. Chem. 284:23182-23186(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-86.
    15. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
      David Y., Ziv T., Admon A., Navon A.
      J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structural analysis of human FANCL, the E3 ligase in the Fanconi anemia pathway."
      Hodson C., Cole A.R., Lewis L.P., Miles J.A., Purkiss A., Walden H.
      J. Biol. Chem. 286:32628-32637(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FANCL, MUTAGENESIS OF PHE-63.
    18. "Hypoxia disrupts the Fanconi anemia pathway and sensitizes cells to chemotherapy through regulation of UBE2T."
      Ramaekers C.H., van den Beucken T., Meng A., Kassam S., Thoms J., Bristow R.G., Wouters B.G.
      Radiother. Oncol. 101:190-197(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    19. "Ubiquitin-conjugating enzyme HSPC150."
      Walker J.R., Avvakumov G.V., Newman E.M., Mackenzie F., Kozieradzki I., Sundstrom M., Arrowsmith C., Edwards A., Bochkarev A., Dhe-Paganon S.
      Submitted (FEB-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-167.

    Entry informationi

    Entry nameiUBE2T_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPD8
    Secondary accession number(s): Q2TU36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3