Reviewed, UniProtKB/Swiss-Prot Q9QZU9 (UB2L6_MOUSE)

Names and origin

Protein names

Recommended name:
    Ubiquitin/ISG15-conjugating enzyme E2 L6
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase L6
    Ubiquitin carrier protein L6
    UbcM8

Gene names

Name:	Ube2l6
Synonyms:	Ubce8

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53 By similarity.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with RNF19A, RNF19B and RNF144B By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Ligase
Gene Ontology (GO)
Biological process	ISG15-protein conjugation Inferred from direct assay. Source: MGI modification-dependent protein catabolic process Inferred from direct assay. Source: MGI regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ISG15 ligase activity Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction. Source: MGI ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 153	153	Ubiquitin/ISG15-conjugating enzyme E2 L6		PRO_0000082479
Sites
	Active site	86	1	Glycyl thioester intermediate By similarity
Experimental info
	Sequence conflict	29	1	D → Y in AAD55978. Ref.1
	Sequence conflict	63	1	F → L in AAH08238. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9QZU9-1 [UniParc]. Last modified May 26, 2009. Version 3. Checksum: 71EEFF050CDE57F1	FASTA	153	17,841
	10 20 30 40 50 60 MMASKRVAKE LESLSKELPP YLRQLSSDDA NVLVWHMLLL PDQLPYGLKA FQVRIDFPRE 70 80 90 100 110 120 YPFKPPTLRF TTKIYHPNVR EDGLVCLPLI SNENWKPYTK PYQVLEALNV LVSKPNLEEP 130 140 150 VRLELADLLT QNPEMFRKKA EEFTLKFGVD RPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Progression from mammary hyperplasia to adenocarcinoma in MMTV-FGF8b transgenic mice is associated with altered expression of CD63, IGFBP7/mac25, alpha-synuclein, and UbcM8." Cook G., Lawshe A., MacArthur C.A. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Embryo and Embryonic liver.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF159230 mRNA. Translation: AAD55978.1. Different initiation. AK010942 mRNA. Translation: BAB27282.1. AK013452 mRNA. Translation: BAB28861.1. AK152010 mRNA. Translation: BAE30873.1. AK152113 mRNA. Translation: BAE30957.1. AK168695 mRNA. Translation: BAE40539.1. AK171629 mRNA. Translation: BAE42574.1. CH466519 Genomic DNA. Translation: EDL27303.1. BC008238 mRNA. Translation: AAH08238.1.
IPI	IPI00874750.
RefSeq	NP_064333.2.
UniGene	Mm.38261
3D structure databases
HSSP	HSSP built from PDB template 1C4Z based on UniProtKB P51966.
SMR	Q9QZU9. Positions 2-151.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000027078. Mus musculus. [Contig view]
GeneID	56791.
KEGG	mmu:56791.
NMPDR	fig|10090.3.peg.6261.
Organism-specific databases
MGI	MGI:1914500. Ube2l6.
Phylogenomic databases
HOVERGEN	Q9QZU9.
Enzyme and pathway databases
BRENDA	6.3.2.19. 244.
Gene expression databases
Bgee	Q3U8R0. Q9QZU9.
CleanEx	MM_UBE2L6.
GermOnline	ENSMUSG00000027078. Mus musculus.
Family and domain databases
ProDom	PD000461. UBQ_conjugat. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	313332.
SOURCE	Search...

Entry information

Entry name

UB2L6_MOUSE

Accession

Primary (citable) accession number: Q9QZU9
Secondary accession number(s): Q3U8R0, Q922F1, Q9CQN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	May 26, 2009
Last modified:	June 16, 2009
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)