Ubiquitin-conjugating enzyme E2 K

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P61085 (UBE2K_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein K48-linked ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin protein ligase binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-ubiquitin ligase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 200

199

Ubiquitin-conjugating enzyme E2 K

PRO_0000082442

Regions

Domain

160 – 200

UBA

Sites

Active site

Glycyl thioester intermediate

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

N6-acetyllysine By similarity

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6

Experimental info

Mutagenesis

S → Y: Inhibits ubiquitin transfer to macromolecular acceptors. Ref.2

Sequence conflict

S → T in AAB19536. Ref.1

Secondary structure

200

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P61085 [UniParc].

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

FASTA

200

22,407

        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' referencesShow '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.

IPI

IPI00695690.

PIR

A40797.

RefSeq

NP_776505.1. NM_174080.2.

UniGene

Bt.65293.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BEP	X-ray	1.80	A	1-155	[»]
2BF8	X-ray	2.30	A	1-155	[»]

ProteinModelPortal

P61085.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1537679.

STRING

9913.ENSBTAP00000026871.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000026871; ENSBTAP00000026871; ENSBTAG00000020175.

GeneID

281225.

KEGG

bta:281225.

Organism-specific databases

CTD

3093.

Phylogenomic databases

eggNOG

COG5078.

GeneTree

ENSGT00670000098059.

HOGENOM

HOG000233455.

HOVERGEN

HBG063308.

InParanoid

P61085.

K04649.

OMA

MAVSRIK.

OrthoDB

EOG4CC42C.

Enzyme and pathway databases

BioCyc

CATTLE:281225-MONOMER.

UniPathway

UPA00143.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]

SMART

SM00165. UBA. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.
SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P61085.

NextBio

20805272.

Entry information

Entry name

UBE2K_BOVIN

Accession

Primary (citable) accession number: P61085
Secondary accession number(s): A5PK22

Q9CVV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents