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Reviewed, UniProtKB/Swiss-Prot Q9Y385 (UB2J1_HUMAN)

Last modified November 4, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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=NCUBE1
    Yeast ubiquitin-conjugating enzyme UBC6 homolog E
    HSUBC6e
Gene names
Name: UBE2J1
Synonyms: NCUBE1
ORF Names: CGI-76, HSPC153, HSPC205
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

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.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAF36125.1 differs from that shown. Reason: Frameshift at position 119.

Ontologies

Keywords

   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   Molecular functionLigase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionubiquitin-protein ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Ubiquitin-conjugating enzyme E2 J1
PRO_0000082594

Regions

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

Sites

Active site911Glycyl thioester intermediate

Amino acid modifications

Modified residue2661Phosphoserine
Modified residue2681Phosphoserine

Natural variations

Natural variant551G → V: dbSNP rs8099.
VAR_019689
Natural variant2291L → V: dbSNP rs10502.
VAR_019690

Experimental info

Mutagenesis911C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER
Sequence conflict32 – 332QP → HA in AAD34071. Ref.3
Sequence conflict2761Q → H in AAF21505. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y385-1 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: CFF5FE00C2BBD39E

FASTA31835,199
        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 LPLKSGSDSS QADQEAKELA 

       190        200        210        220        230        240 
RQISFKAEVN SSGKTISESD LNHSFSLTDL QDDIPTTFQG ATASTSYGLQ NSSAASFHQP 

       250        260        270        280        290        300 
TQPVAKNTSM SPRQRRAQQQ SQRRLSTSPD VIQGHQPRDN HTDHGGSAVL IVILTLALAA 

       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: 10708578] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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], VARIANT VAL-55, FUNCTION, MUTAGENESIS OF CYS-91, SUBCELLULAR LOCATION.
[3]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-229.
Tissue: Umbilical cord blood.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANT VAL-229.
Tissue: Muscle.
[7]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND SER-268, MASS SPECTROMETRY.
Tissue: Epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ245898 mRNA. Translation: CAB83212.1.
U93243 mRNA. Translation: AAF21505.1.
AF151039 mRNA. Translation: AAF36125.1. Frameshift.
AF151834 mRNA. Translation: AAD34071.1. Different initiation.
AF161502 mRNA. Translation: AAF29117.1.
AL138717, AL139804 Genomic DNA. Translation: CAH70228.1.
AL139804, AL138717 Genomic DNA. Translation: CAI19635.1.
BC013973 mRNA. Translation: AAH13973.1.
RefSeqNP_057105.2.
UniGeneHs.163776

3D structure databases

HSSPHSSP built from PDB template 1QCQ based on UniProtKB P15731.
ModBaseSearch...

PTM databases

PhosphoSiteQ9Y385.

2-D gel databases

OGPQ9Y385.

Proteomic databases

PeptideAtlasQ9Y385.

Genome annotation databases

EnsemblENSG00000198833. Homo sapiens. [Contig view]
GeneID51465.
KEGGhsa:51465.

Organism-specific databases

H-InvDBHIX0023025.
HGNCHGNC:17598. UBE2J1.
HPAHPA003509.
PharmGKBPA134906541.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ9Y385.

Gene expression databases

ArrayExpressQ9Y385.
CleanExHS_UBE2J1.
GermOnlineENSG00000198833. Homo sapiens.

Family and domain databases

InterProIPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]
Gene3DG3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
PANTHERPTHR11621. UBQ-conjugat_E2. 1 hit.
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
ProDomPD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00212. UBCc. 1 hit.
[Graphical view]
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio55093.

Entry information

Entry nameUB2J1_HUMAN
AccessionPrimary (citable) accession number: Q9Y385
Secondary accession number(s): Q5W0N4 expand/collapse secondary AC list , Q9BZ32, Q9NQL3, Q9NY66, Q9P011, Q9P0S0, Q9UF10
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: November 4, 2008
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents