Q9CQ37 (UBE2T_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 T
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein T
Ubiquitin-protein ligase T

Gene names

Name:

Ube2t

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with FANCL and BRCA1 By similarity.
Subcellular location	Nucleus By similarity. Note: Accumulates to chromatin By similarity.
Post-translational modification	Auto-ubiquitinated. Effects of auto-monoubiquitination at Lys-91 and Lys-181 are unclear By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from sequence or structural similarity. Source: UniProtKB protein K11-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K27-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K29-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K48-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K6-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K63-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein autoubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein monoubiquitination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	Ubiquitin-conjugating enzyme E2 T		PRO_0000082510
Sites
	Active site	86	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Cross-link	91		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	181		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CQ37 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: CD47378F090FD0C5	FASTA	204	22,975
	10 20 30 40 50 60 MQRASRLKKE LHMLAIEPPP GITCWQEKDQ VADLRAQILG GANTPYEKGV FTLEVIIPER 70 80 90 100 110 120 YPFEPPQVRF LTPIYHPNID SSGRICLDIL KLPPKGAWRP SLNIATVLTS IQLLMAEPNP 130 140 150 160 170 180 DDPLMADISS EFKYNKIAFL KKAKQWTEAH ARQKQKADEE ELGTSSEVGD SEESHSTQKR 190 200 KARPLGGMEK KFSPDVQRVY PGPS

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK012565 mRNA. Translation: BAB28320.1. AK021213 mRNA. Translation: BAB32332.1. BC029213 mRNA. Translation: AAH29213.1.
IPI	IPI00131962.
RefSeq	NP_080300.1. NM_026024.2.
UniGene	Mm.284587.
3D structure databases
ProteinModelPortal	Q9CQ37.
SMR	Q9CQ37. Positions 1-154.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000027687.
PTM databases
PhosphoSite	Q9CQ37.
Proteomic databases
PaxDb	Q9CQ37.
PRIDE	Q9CQ37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027687; ENSMUSP00000027687; ENSMUSG00000026429.
GeneID	67196.
KEGG	mmu:67196.
UCSC	uc007csp.1. mouse.
Organism-specific databases
CTD	29089.
MGI	MGI:1914446. Ube2t.
Phylogenomic databases
eggNOG	COG5078.
GeneTree	ENSGT00540000070023.
HOGENOM	HOG000233455.
HOVERGEN	HBG063308.
InParanoid	Q9CQ37.
KO	K13960.
OMA	GITCWQE.
OrthoDB	EOG40GCRT.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	Q9CQ37.
CleanEx	MM_UBE2T.
Genevestigator	Q9CQ37.
GermOnline	ENSMUSG00000026429. Mus musculus.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	323844.
SOURCE	Search...

Entry information

Entry name

UBE2T_MOUSE

Accession

Primary (citable) accession number: Q9CQ37

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program