Reviewed, UniProtKB/Swiss-Prot Q9JJZ4 (UB2J1_MOUSE)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 J1
    EC=6.3.2.19
Alternative name(s):
    Non-canonical ubiquitin-conjugating enzyme 1
      Short name=NCUBE1

Gene names

Name:	Ube2j1
Synonyms:	Ncube1

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	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
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 By similarity.
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
PTM	Phosphoprotein
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 Inferred from electronic annotation. Source: UniProtKB-KW 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 – 318	318	Ubiquitin-conjugating enzyme E2 J1		PRO_0000082595
Regions
	Topological domain	1 – 282	282	Cytoplasmic Potential
	Transmembrane	283 – 303	21	Anchor for type IV membrane protein Potential
	Topological domain	304 – 318	15	Lumenal Potential
Sites
	Active site	91	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	266	1	Phosphoserine Ref.4 Ref.5
	Modified residue	268	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	286	1	G → V in CAB83217. Ref.1
	Sequence conflict	289	1	M → V in CAB83217. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9JJZ4-1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: 61A409ADF397EA36	FASTA	318	34,990
	10 20 30 40 50 60 METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD SDFDGGVYHG 70 80 90 100 110 120 RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE TWQPSWSIRT ALLAIIGFMP 130 140 150 160 170 180 TKGEGAIGSL DYTPEERRAL AKKSQDFCCE GCGSAMKDVL LPLKSGSGSS QADQEAKELA 190 200 210 220 230 240 RQISFKAEVN SSGKTIAESD LNQCFSLNDS QDDLPTTFQG ATASTSYGAQ NPSGAPLPQP 250 260 270 280 290 300 TQPAPKNTSM SPRQRRAQQQ SQRRPSTSPD VLQGQPPRAH HTEHGGSAML IIILTLALAA 310 LIFRRIYLAN EYIFDFEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a family of non-canonical ubiquitin-conjugating enzymes structurally related to yeast UBC6." Lester D.H., Farquharson C., Russell G.C., Houston B. Biochem. Biophys. Res. Commun. 269:474-480(2000) [PubMed: 10708578] [Abstract] 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. Tissue: Brain and Testis.
[3]	"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: FVB/N. Tissue: Colon.
[4]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ245899 mRNA. Translation: CAB83217.1. AK003050 mRNA. Translation: BAB22532.1. AK031669 mRNA. Translation: BAC27502.1. BC024623 mRNA. Translation: AAH24623.1.
IPI	IPI00321895.
RefSeq	NP_062532.2.
UniGene	Mm.259095
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JJZ4.
PTM databases
PhosphoSite	Q9JJZ4.
Proteomic databases
PRIDE	Q9JJZ4.
Genome annotation databases
Ensembl	ENSMUST00000029944; ENSMUSP00000029944; ENSMUSG00000028277; Mus musculus. [Genome view]
GeneID	56228.
KEGG	mmu:56228.
UCSC	uc008sfp.1. mouse.
Organism-specific databases
CTD	56228.
MGI	MGI:1926245. Ube2j1.
Phylogenomic databases
HOGENOM	Q9JJZ4.
HOVERGEN	Q9JJZ4.
OMA	CGSTMKD
Enzyme and pathway databases
BRENDA	6.3.2.19. 244.
Gene expression databases
ArrayExpress	Q9JJZ4.
Bgee	Q9JJZ4.
CleanEx	MM_UBE2J1.
Genevestigator	Q9JJZ4.
GermOnline	ENSMUSG00000028277. 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	312128.
SOURCE	Search...

Entry information

Entry name

UB2J1_MOUSE

Accession

Primary (citable) accession number: Q9JJZ4
Secondary accession number(s): Q9DC92

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	November 24, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)