Reviewed, UniProtKB/Swiss-Prot Q6P073 (UB2J2_MOUSE)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 J2
    EC=6.3.2.19
Alternative name(s):
    Non-canonical ubiquitin-conjugating enzyme 2
      Short name=NCUBE2

Gene names

Name:	Ube2j2
Synonyms:	Ncube2

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	259 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum. Ref.1 Ref.2
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type IV membrane protein Ref.1 Ref.2.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Ref.1 Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 259	259	Ubiquitin-conjugating enzyme E2 J2		PRO_0000082597
Regions
	Topological domain	1 – 226	226	Cytoplasmic Potential
	Transmembrane	227 – 247	21	Anchor for type IV membrane protein Potential
	Topological domain	248 – 259	12	Lumenal Potential
Sites
	Active site	94	1	Glycyl thioester intermediate
Experimental info
	Mutagenesis	94	1	C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER. Ref.1 Ref.2
	Sequence conflict	25	1	K → T in BAC36280. Ref.3
	Sequence conflict	32	1	I → M in BAC36280. Ref.3
	Sequence conflict	49	1	R → G in BAC36280. Ref.3
	Sequence conflict	80	1	M → I in BAB26835. Ref.3
	Sequence conflict	84	1	N → H in BAB26835. Ref.3
	Sequence conflict	87	1	F → I in BAB26835. Ref.3
	Sequence conflict	133	1	E → K in BAB23421. Ref.3
	Sequence conflict	150	1	N → I in BAB26835. Ref.3
	Sequence conflict	157	1	C → G in BAC36280. Ref.3
	Sequence conflict	162	1	E → K in BAB23421. Ref.3
	Sequence conflict	186	1	L → W in BAC36280. Ref.3
	Sequence conflict	217 – 218	2	AG → GW in AAF21504. Ref.2
	Sequence conflict	237	1	F → L in BAC36280. Ref.3
	Sequence conflict	246	1	A → P in AAK52607. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6P073-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 0C539BC0ACEAC7C7	FASTA	259	28,954
	10 20 30 40 50 60 MSNNSNKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY 70 80 90 100 110 120 YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS 130 140 150 160 170 180 FMVEKGPTLG SIETSDFTKK QLAAQSLVFN LKDKVFCELF PEVVEEIKQK QKAQDELSNR 190 200 210 220 230 240 PQNLPLPDVV PDGELHRGQH GIQLLNGHAP AAGPNLAGLP QANRHHGLLG GALANLFVIV 250 GFAAFAYTVK YVLRSIAQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)." Tiwari S., Weissman A.M. J. Biol. Chem. 276:16193-16200(2001) [PubMed: 11278356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-94, SUBCELLULAR LOCATION. Strain: C57BL/6J. Tissue: Fetus.
[2]	"A role for mammalian Ubc6 homologues in ER-associated protein degradation." Lenk U., Yu H., Walter J., Gelman M.S., Hartmann E., Kopito R.R., Sommer T. J. Cell Sci. 115:3007-3014(2002) [PubMed: 12082160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-94, SUBCELLULAR LOCATION.
[3]	"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. Tissue: Lung and Skin.
[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]. Strain: C57BL/6J. Tissue: Thymus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF296656 mRNA. Translation: AAK52607.1. U93242 mRNA. Translation: AAF21504.1. AK004626 mRNA. Translation: BAB23421.1. AK010302 mRNA. Translation: BAB26835.1. AK076265 mRNA. Translation: BAC36280.1. BC065779 mRNA. Translation: AAH65779.1.
IPI	IPI00420213.
RefSeq	NP_001034246.1. NP_001034247.1. NP_001034248.1. NP_067377.4.
UniGene	Mm.371673
3D structure databases
SMR	Q6P073. Positions 11-171.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6P073.
Proteomic databases
PRIDE	Q6P073.
Genome annotation databases
Ensembl	ENSMUST00000024056; ENSMUSP00000024056; ENSMUSG00000023286; Mus musculus. [Genome view] ENSMUST00000103175; ENSMUSP00000099464; ENSMUSG00000023286; Mus musculus. [Genome view] ENSMUST00000105581; ENSMUSP00000101206; ENSMUSG00000023286; Mus musculus. [Genome view] ENSMUST00000105582; ENSMUSP00000101207; ENSMUSG00000023286; Mus musculus. [Genome view] ENSMUST00000105583; ENSMUSP00000101208; ENSMUSG00000023286; Mus musculus. [Genome view]
GeneID	140499.
KEGG	mmu:140499.
UCSC	uc007ubh.1. mouse.
Organism-specific databases
CTD	140499.
MGI	MGI:2153608. Ube2j2.
Phylogenomic databases
eggNOG	roNOG14047.
HOVERGEN	Q6P073.
InParanoid	Q6P073.
OrthoDB	EOG9XPT20.
PhylomeDB	Q6P073.
Enzyme and pathway databases
BRENDA	6.3.2.19. 244.
Gene expression databases
ArrayExpress	Q6P073.
Genevestigator	Q6P073.
GermOnline	ENSMUSG00000023286. Mus musculus.
Family and domain databases
InterPro	IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SMART	SM00212. UBCc. 1 hit. [Graphical view]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	369836.
SOURCE	Search...

Entry information

Entry name

UB2J2_MOUSE

Accession

Primary (citable) accession number: Q6P073
Secondary accession number(s): Q8C6A1 , Q91Y64, Q9CWY5, Q9DC18, Q9QX58

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)