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Q9JJZ4 (UB2J1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 J1
EC=6.3.2.19
Alternative name(s):
Non-canonical ubiquitin-conjugating enzyme 1
Short name=NCUBE-1
Gene names
Name:Ube2j1
Synonyms:Ncube1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Ubiquitin-conjugating enzyme E2 J1
PRO_0000082595

Regions

Topological domain1 – 282282Cytoplasmic Potential
Transmembrane283 – 30321Helical; Anchor for type IV membrane protein; Potential
Topological domain304 – 31815Lumenal Potential

Sites

Active site911Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue2661Phosphoserine Ref.4 Ref.5
Modified residue2681Phosphoserine By similarity

Experimental info

Sequence conflict2861G → V in CAB83217. Ref.1
Sequence conflict2891M → V in CAB83217. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JJZ4 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: 61A409ADF397EA36

FASTA31834,990
        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

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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.
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ245899 mRNA. Translation: CAB83217.1.
AK003050 mRNA. Translation: BAB22532.1.
AK031669 mRNA. Translation: BAC27502.1.
BC024623 mRNA. Translation: AAH24623.1.
IPIIPI00321895.
RefSeqNP_062532.2. NM_019586.3.
UniGeneMm.259095.

3D structure databases

ProteinModelPortalQ9JJZ4.
SMRQ9JJZ4. Positions 9-147.
ModBaseSearch...

PTM databases

PhosphoSiteQ9JJZ4.

Proteomic databases

PaxDbQ9JJZ4.
PRIDEQ9JJZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000124992; ENSMUSP00000118333; ENSMUSG00000028277.
GeneID56228.
KEGGmmu:56228.

Organism-specific databases

CTD51465.
MGIMGI:1926245. Ube2j1.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00530000063379.
HOGENOMHOG000167871.
HOVERGENHBG058959.
InParanoidQ9JJZ4.
KOK10578.
OMACCEGCGC.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9JJZ4.
BgeeQ9JJZ4.
CleanExMM_UBE2J1.
GenevestigatorQ9JJZ4.
GermOnlineENSMUSG00000028277. Mus musculus.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312128.
SOURCESearch...

Entry information

Entry nameUB2J1_MOUSE
AccessionPrimary (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: May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents