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Protein

Ubiquitin-conjugating enzyme E2 T

Gene

UBE2T

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.PROSITE-ProRule annotation1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei86Glycyl thioester intermediate1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • ubiquitin conjugating enzyme activity Source: MGI
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB
  • interstrand cross-link repair Source: Reactome
  • protein autoubiquitination Source: UniProtKB
  • protein K11-linked ubiquitination Source: UniProtKB
  • protein K27-linked ubiquitination Source: UniProtKB
  • protein K29-linked ubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein K6-linked ubiquitination Source: UniProtKB
  • protein monoubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01232-MONOMER.
BRENDAi2.3.2.B6. 2681.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.
R-HSA-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
SignaLinkiQ9NPD8.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 T (EC:2.3.2.231 Publication)
Alternative name(s):
Cell proliferation-inducing gene 50 protein
E2 ubiquitin-conjugating enzyme T
Ubiquitin carrier protein T
Ubiquitin-protein ligase T
Gene namesi
Name:UBE2T
ORF Names:HSPC150, PIG50
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25009. UBE2T.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Fanconi anemia complementation group T (FANCT)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.
See also OMIM:616435
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0738612Q → E in FANCT; abolishes FANCD2 monoubiquitination; abolishes interaction with FANCL. 1 PublicationCorresponds to variant rs774357609dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63F → A: Decreased binding to FANCL. 1 Publication1
Mutagenesisi86C → A: Loss of E2 enzyme activity. 5 Publications1
Mutagenesisi91K → R: Decreased monoubiquitination. 1 Publication1
Mutagenesisi182 – 191Missing : Decreased monoubiquitination. 1 Publication10

Keywords - Diseasei

Disease mutation, Fanconi anemia

Organism-specific databases

DisGeNETi29089.
MIMi616435. phenotype.
OpenTargetsiENSG00000077152.
PharmGKBiPA142670655.

Polymorphism and mutation databases

BioMutaiUBE2T.
DMDMi73622065.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000825091 – 197Ubiquitin-conjugating enzyme E2 TAdd BLAST197

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei184PhosphoserineCombined sources1

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, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NPD8.
MaxQBiQ9NPD8.
PaxDbiQ9NPD8.
PeptideAtlasiQ9NPD8.
PRIDEiQ9NPD8.
TopDownProteomicsiQ9NPD8.

PTM databases

iPTMnetiQ9NPD8.
PhosphoSitePlusiQ9NPD8.
SwissPalmiQ9NPD8.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000077152.
CleanExiHS_UBE2T.
ExpressionAtlasiQ9NPD8. baseline and differential.
GenevisibleiQ9NPD8. HS.

Organism-specific databases

HPAiHPA002831.

Interactioni

Subunit structurei

Interacts with FANCL and BRCA1.5 Publications

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118858. 37 interactors.
DIPiDIP-52740N.
IntActiQ9NPD8. 11 interactors.
STRINGi9606.ENSP00000356243.

Structurei

Secondary structure

1197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 16Combined sources16
Beta strandi22 – 29Combined sources8
Beta strandi33 – 39Combined sources7
Turni45 – 48Combined sources4
Beta strandi50 – 56Combined sources7
Turni59 – 62Combined sources4
Beta strandi67 – 72Combined sources6
Helixi88 – 90Combined sources3
Turni93 – 95Combined sources3
Helixi104 – 116Combined sources13
Helixi126 – 134Combined sources9
Helixi136 – 150Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YH2X-ray2.00A1-167[»]
4CCGX-ray2.40A/B1-197[»]
ProteinModelPortaliQ9NPD8.
SMRiQ9NPD8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPD8.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0417. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ9NPD8.
KOiK13960.
OMAiKIPERYP.
OrthoDBiEOG091G0VPD.
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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0738612Q → E in FANCT; abolishes FANCD2 monoubiquitination; abolishes interaction with FANCL. 1 PublicationCorresponds to variant rs774357609dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001297255.1. NM_001310326.1.
NP_054895.1. NM_014176.3.
UniGeneiHs.5199.

Genome annotation databases

EnsembliENST00000367274; ENSP00000356243; ENSG00000077152.
GeneIDi29089.
KEGGihsa:29089.
UCSCiuc001gxx.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001297255.1. NM_001310326.1.
NP_054895.1. NM_014176.3.
UniGeneiHs.5199.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YH2X-ray2.00A1-167[»]
4CCGX-ray2.40A/B1-197[»]
ProteinModelPortaliQ9NPD8.
SMRiQ9NPD8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118858. 37 interactors.
DIPiDIP-52740N.
IntActiQ9NPD8. 11 interactors.
STRINGi9606.ENSP00000356243.

PTM databases

iPTMnetiQ9NPD8.
PhosphoSitePlusiQ9NPD8.
SwissPalmiQ9NPD8.

Polymorphism and mutation databases

BioMutaiUBE2T.
DMDMi73622065.

Proteomic databases

EPDiQ9NPD8.
MaxQBiQ9NPD8.
PaxDbiQ9NPD8.
PeptideAtlasiQ9NPD8.
PRIDEiQ9NPD8.
TopDownProteomicsiQ9NPD8.

Protocols and materials databases

DNASUi29089.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367274; ENSP00000356243; ENSG00000077152.
GeneIDi29089.
KEGGihsa:29089.
UCSCiuc001gxx.5. human.

Organism-specific databases

CTDi29089.
DisGeNETi29089.
GeneCardsiUBE2T.
HGNCiHGNC:25009. UBE2T.
HPAiHPA002831.
MIMi610538. gene.
616435. phenotype.
neXtProtiNX_Q9NPD8.
OpenTargetsiENSG00000077152.
PharmGKBiPA142670655.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0417. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ9NPD8.
KOiK13960.
OMAiKIPERYP.
OrthoDBiEOG091G0VPD.
PhylomeDBiQ9NPD8.
TreeFamiTF354203.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:HS01232-MONOMER.
BRENDAi2.3.2.B6. 2681.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.
R-HSA-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
SignaLinkiQ9NPD8.

Miscellaneous databases

ChiTaRSiUBE2T. human.
EvolutionaryTraceiQ9NPD8.
GenomeRNAii29089.
PROiQ9NPD8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000077152.
CleanExiHS_UBE2T.
ExpressionAtlasiQ9NPD8. baseline and differential.
GenevisibleiQ9NPD8. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 141 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. 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.