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Q9CQ37

- UBE2T_MOUSE

UniProt

Q9CQ37 - UBE2T_MOUSE

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Protein

Ubiquitin-conjugating enzyme E2 T

Gene

Ube2t

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

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 intermediatePROSITE-ProRule annotation

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 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_232842. Fanconi Anemia pathway.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 T (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein T
Ubiquitin-protein ligase T
Gene namesi
Name:Ube2t
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1914446. Ube2t.

Subcellular locationi

Nucleus By similarity
Note: Accumulates to chromatin.By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Ubiquitin-conjugating enzyme E2 TPRO_0000082510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki91 – 91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki181 – 181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Auto-ubiquitinated. Effects of auto-monoubiquitination at Lys-91 and Lys-181 are unclear (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9CQ37.
PaxDbiQ9CQ37.
PRIDEiQ9CQ37.

PTM databases

PhosphoSiteiQ9CQ37.

Expressioni

Gene expression databases

BgeeiQ9CQ37.
CleanExiMM_UBE2T.
GenevestigatoriQ9CQ37.

Interactioni

Subunit structurei

Interacts with FANCL and BRCA1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027687.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ37.
SMRiQ9CQ37. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ9CQ37.
KOiK13960.
OMAiIVPERYP.
OrthoDBiEOG7BP84K.
PhylomeDBiQ9CQ37.
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.

Q9CQ37-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQRASRLKKE LHMLAIEPPP GITCWQEKDQ VADLRAQILG GANTPYEKGV
60 70 80 90 100
FTLEVIIPER YPFEPPQVRF LTPIYHPNID SSGRICLDIL KLPPKGAWRP
110 120 130 140 150
SLNIATVLTS IQLLMAEPNP DDPLMADISS EFKYNKIAFL KKAKQWTEAH
160 170 180 190 200
ARQKQKADEE ELGTSSEVGD SEESHSTQKR KARPLGGMEK KFSPDVQRVY

PGPS
Length:204
Mass (Da):22,975
Last modified:June 1, 2001 - v1
Checksum:iCD47378F090FD0C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012565 mRNA. Translation: BAB28320.1.
AK021213 mRNA. Translation: BAB32332.1.
BC029213 mRNA. Translation: AAH29213.1.
CCDSiCCDS15313.1.
RefSeqiNP_001265044.1. NM_001278115.1.
NP_080300.1. NM_026024.3.
UniGeneiMm.284587.

Genome annotation databases

EnsembliENSMUST00000027687; ENSMUSP00000027687; ENSMUSG00000026429.
GeneIDi67196.
KEGGimmu:67196.
UCSCiuc007csp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012565 mRNA. Translation: BAB28320.1 .
AK021213 mRNA. Translation: BAB32332.1 .
BC029213 mRNA. Translation: AAH29213.1 .
CCDSi CCDS15313.1.
RefSeqi NP_001265044.1. NM_001278115.1.
NP_080300.1. NM_026024.3.
UniGenei Mm.284587.

3D structure databases

ProteinModelPortali Q9CQ37.
SMRi Q9CQ37. Positions 1-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000027687.

PTM databases

PhosphoSitei Q9CQ37.

Proteomic databases

MaxQBi Q9CQ37.
PaxDbi Q9CQ37.
PRIDEi Q9CQ37.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027687 ; ENSMUSP00000027687 ; ENSMUSG00000026429 .
GeneIDi 67196.
KEGGi mmu:67196.
UCSCi uc007csp.1. mouse.

Organism-specific databases

CTDi 29089.
MGIi MGI:1914446. Ube2t.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00540000070023.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi Q9CQ37.
KOi K13960.
OMAi IVPERYP.
OrthoDBi EOG7BP84K.
PhylomeDBi Q9CQ37.
TreeFami TF354203.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_232842. Fanconi Anemia pathway.

Miscellaneous databases

NextBioi 323844.
PROi Q9CQ37.
SOURCEi Search...

Gene expression databases

Bgeei Q9CQ37.
CleanExi MM_UBE2T.
Genevestigatori Q9CQ37.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiUBE2T_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3