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Q9NPD8

- UBE2T_HUMAN

UniProt

Q9NPD8 - UBE2T_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication

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. 29 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.
GeneTreeiENSGT00540000070023.
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

        10         20         30         40         50
MQRASRLKRE LHMLATEPPP GITCWQDKDQ MDDLRAQILG GANTPYEKGV
60 70 80 90 100
FKLEVIIPER YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP
110 120 130 140 150
SLNIATVLTS IQLLMSEPNP DDPLMADISS EFKYNKPAFL KNARQWTEKH
160 170 180 190
ARQKQKADEE EMLDNLPEAG DSRVHNSTQK RKASQLVGIE KKFHPDV
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. 29 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.
GeneTreei ENSGT00540000070023.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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