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P61085 (UBE2K_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. 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

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 K

EC=6.3.2.19
Alternative name(s):
Huntingtin-interacting protein 2
Short name=HIP-2
Ubiquitin carrier protein
Ubiquitin-conjugating enzyme E2-25 kDa
Short name=Ubiquitin-conjugating enzyme E2(25K)
Short name=Ubiquitin-conjugating enzyme E2-25K
Ubiquitin-protein ligase
Gene names
Name:UBE2K
Synonyms:HIP2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53 By similarity. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. Ref.4

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with RNF138/NARF. Interacts with BRCA1 By similarity.

Subcellular location

Cytoplasm.

Post-translational modification

Sumoylation at Lys-14 impairs catalytic activity. Ref.6

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Contains 1 UBA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 200199Ubiquitin-conjugating enzyme E2 K
PRO_0000082442

Regions

Domain160 – 20041UBA

Sites

Active site921Glycyl thioester intermediate

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue141N6-acetyllysine; alternate By similarity
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.6

Experimental info

Mutagenesis861S → Y: Inhibits ubiquitin transfer to macromolecular acceptors. Ref.2
Sequence conflict231S → T in AAB19536. Ref.1

Secondary structure

............................ 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61085 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E40668099ED25828

FASTA20022,407
        10         20         30         40         50         60 
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI 

        70         80         90        100        110        120 
KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA 

       130        140        150        160        170        180 
EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI 

       190        200 
VALSSKSWDV ETATELLLSN 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding a mammalian multiubiquitinating enzyme (E225K) and overexpression of the functional enzyme in Escherichia coli."
Chen Z., Niles E.G., Pickart C.M.
J. Biol. Chem. 266:15698-15704(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thymus.
[2]"Core domain mutation (S86Y) selectively inactivates polyubiquitin chain synthesis catalyzed by E2-25K."
Mastrandrea L.D., Kasperek E.M., Niles E.G., Pickart C.M.
Biochemistry 37:9784-9792(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 23, MUTAGENESIS OF SER-86.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.
[4]"Enzymes catalyzing ubiquitination and proteolytic processing of the p105 precursor of nuclear factor kappaB1."
Coux O., Goldberg A.L.
J. Biol. Chem. 273:8820-8828(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF NF-KAPPA-B.
[5]"Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2)."
Cook W.J., Jeffrey L.C., Carson M., Chen Z., Pickart C.M.
J. Biol. Chem. 267:16467-16471(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[6]"SUMO modification of the ubiquitin-conjugating enzyme E2-25K."
Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R., Olsen J.V., Jentsch S., Melchior F., Sixma T.K.
Nat. Struct. Mol. Biol. 12:264-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUMOYLATION AT LYS-14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S51016 mRNA. Translation: AAB19536.1.
BC142324 mRNA. Translation: AAI42325.1.
PIRA40797.
RefSeqNP_776505.1. NM_174080.2.
UniGeneBt.65293.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BEPX-ray1.80A1-155[»]
2BF8X-ray2.30A1-155[»]
ProteinModelPortalP61085.
SMRP61085. Positions 3-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1537679.
STRING9913.ENSBTAP00000026871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000026871; ENSBTAP00000026871; ENSBTAG00000020175.
GeneID281225.
KEGGbta:281225.

Organism-specific databases

CTD3093.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00670000098059.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidP61085.
KOK04649.
OMAARQFKEN.
OrthoDBEOG7F513F.
TreeFamTF101127.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61085.
NextBio20805272.

Entry information

Entry nameUBE2K_BOVIN
AccessionPrimary (citable) accession number: P61085
Secondary accession number(s): A5PK22 expand/collapse secondary AC list , O54806, P27924, Q16721, Q9CVV9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways