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Reviewed, UniProtKB/Swiss-Prot Q8WVN8 (UB2Q2_HUMAN)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin-conjugating enzyme E2 Q2
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase Q2
    Ubiquitin carrier protein Q2
Gene names
Name: UBE2Q2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 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 By similarity.

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasm. Ref.3

Tissue specificity

Detected in hypopharyngeal head and neck squamous cell carcinoma, in tumor masses and invasive epithelium. Ref.3

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processmodification-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 componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WVN8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WVN8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     296-314: YVLGGGALCMELLTKQGWS → LVHPSKGRWLNMLTVVCLD
     315-375: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Ubiquitin-conjugating enzyme E2 Q2
PRO_0000223879

Regions

Compositional bias134 – 17845Glu-rich

Sites

Active site3041Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue3691Phosphothreonine Ref.4

Natural variations

Alternative sequence296 – 31419YVLGG…KQGWS → LVHPSKGRWLNMLTVVCLD in isoform 2.
VSP_017298
Alternative sequence315 – 37561Missing in isoform 2.
VSP_017299

Secondary structure

............................. 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 7DE07315E89178A3

FASTA37542,818
        10         20         30         40         50         60 
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PQQGSPHSLP PPLTLHCNIT 

        70         80         90        100        110        120 
ESYPSSSPIW FVDSEDPNLT SVLERLEDTK NNNLLRQQLK WLICELCSLY NLPKHLDVEM 

       130        140        150        160        170        180 
LDQPLPTGQN GTTEEVTSEE EEEEEEMAED IEDLDHYEMK EEEPISGKKS EDEGIEKENL 

       190        200        210        220        230        240 
AILEKIRKTQ RQDHLNGAVS GSVQASDRLM KELRDIYRSQ SYKTGIYSVE LINDSLYDWH 

       250        260        270        280        290        300 
VKLQKVDPDS PLHSDLQILK EKEGIEYILL NFSFKDNFPF DPPFVRVVLP VLSGGYVLGG 

       310        320        330        340        350        360 
GALCMELLTK QGWSSAYSIE SVIMQINATL VKGKARVQFG ANKNQYNLAR AQQSYNSIVQ 

       370 
IHEKNGWYTP PKEDG 

« Hide

Isoform 2.

Checksum: 2C8943AFD4F6EE8A
Show »

FASTA31436,135

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Melanoma.
[2]"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-375 (ISOFORM 2).
Tissue: Ovary, Placenta and Uterus.
[3]"Analysis of a novel human gene, LOC92912, over-expressed in hypopharyngeal tumours."
Seghatoleslam A., Zambrano A., Millon R., Ganguli G., Argentini M., Cromer A., Abecassis J., Wasylyk B.
Biochem. Biophys. Res. Commun. 339:422-429(2006) [PubMed: 16300736] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369, MASS SPECTROMETRY.
[5]"Structure of human ubiquitin-conjugating enzyme (UBCI) involved in embryo attachment and implantation."
Structural genomics consortium (SGC)
Submitted (JAN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 197-363.
+Additional computationally mapped references.

Cross-references

Sequence databases

AL832429 mRNA. Translation: CAH10654.1.
BC006827 mRNA. Translation: AAH06827.1.
BC017708 mRNA. Translation: AAH17708.1.
BC034342 mRNA. Translation: AAH34342.1. Different initiation.
IPIIPI00103165.
IPI00386815.
RefSeqNP_775740.1.
UniGeneHs.714732

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUOX-ray1.80A/B197-363[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ8WVN8.

Proteomic databases

PRIDEQ8WVN8.

Genome annotation databases

EnsemblENSG00000140367. Homo sapiens. [Contig view]
GeneID92912.
KEGGhsa:92912.

Organism-specific databases

GeneCardsGC15P073923.
H-InvDBHIX0012448.
HIX0038395.
HGNCHGNC:19248. UBE2Q2.
MIM612501. gene.
PharmGKBPA142670652.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ8WVN8.
HOVERGENQ8WVN8.
OMAQ8WVN8. YKAGIYS.

Enzyme and pathway databases

BRENDA6.3.2.19. 247.

Gene expression databases

ArrayExpressQ8WVN8.
BgeeQ8WVN8.
CleanExHS_UBE2Q2.
GermOnlineENSG00000140367. Homo sapiens.

Family and domain databases

InterProIPR006575. RWD.
IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]
Gene3DG3DSA:3.10.110.10. 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]
SMARTSM00591. RWD. 1 hit.
SM00212. UBCc. 1 hit.
[Graphical view]
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio77912.
SOURCESearch...

Entry information

Entry nameUB2Q2_HUMAN
AccessionPrimary (citable) accession number: Q8WVN8
Secondary accession number(s): Q8N4G6, Q96J08
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2002
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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