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P61085

- UBE2K_BOVIN

UniProt

P61085 - UBE2K_BOVIN

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Protein

Ubiquitin-conjugating enzyme E2 K

Gene

UBE2K

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Glycyl thioester intermediate

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin protein ligase binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. ubiquitin-ubiquitin ligase activity Source: Ensembl

GO - Biological processi

  1. protein K48-linked ubiquitination Source: UniProtKB
  2. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:UBE2K
Synonyms:HIP2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 6

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861S → Y: Inhibits ubiquitin transfer to macromolecular acceptors. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 200199Ubiquitin-conjugating enzyme E2 KPRO_0000082442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei14 – 141N6-acetyllysine; alternateBy similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate

Post-translational modificationi

Sumoylation at Lys-14 impairs catalytic activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

MINTiMINT-1537679.
STRINGi9913.ENSBTAP00000026871.

Structurei

Secondary structure

1
200
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi20 – 234Combined sources
Beta strandi26 – 316Combined sources
Beta strandi33 – 4412Combined sources
Turni50 – 534Combined sources
Beta strandi55 – 617Combined sources
Turni64 – 674Combined sources
Beta strandi72 – 776Combined sources
Turni86 – 883Combined sources
Helixi94 – 963Combined sources
Turni97 – 993Combined sources
Helixi106 – 11813Combined sources
Helixi128 – 1369Combined sources
Helixi138 – 15215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BEPX-ray1.80A1-155[»]
2BF8X-ray2.30A2-155[»]
ProteinModelPortaliP61085.
SMRiP61085. Positions 3-200.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61085.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 20041UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00670000098059.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP61085.
KOiK04649.
OMAiNKEIADC.
OrthoDBiEOG7F513F.
TreeFamiTF101127.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR009060. 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]
PfamiPF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SMARTiSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61085-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP
60 70 80 90 100
YEGGRYQLEI KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW
110 120 130 140 150
AAAMTLRTVL LSLQALLAAA EPDDPQDAVV ANQYKQNPEM FKQTARLWAH
160 170 180 190 200
VYAGAPVSSP EYTKKIENLC AMGFDRNAVI VALSSKSWDV ETATELLLSN
Length:200
Mass (Da):22,407
Last modified:January 23, 2007 - v3
Checksum:iE40668099ED25828
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231S → T in AAB19536. (PubMed:1714895)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S51016 mRNA. Translation: AAB19536.1.
BC142324 mRNA. Translation: AAI42325.1.
PIRiA40797.
RefSeqiNP_776505.1. NM_174080.2.
UniGeneiBt.65293.

Genome annotation databases

EnsembliENSBTAT00000026871; ENSBTAP00000026871; ENSBTAG00000020175.
GeneIDi281225.
KEGGibta:281225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S51016 mRNA. Translation: AAB19536.1 .
BC142324 mRNA. Translation: AAI42325.1 .
PIRi A40797.
RefSeqi NP_776505.1. NM_174080.2.
UniGenei Bt.65293.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BEP X-ray 1.80 A 1-155 [» ]
2BF8 X-ray 2.30 A 2-155 [» ]
ProteinModelPortali P61085.
SMRi P61085. Positions 3-200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1537679.
STRINGi 9913.ENSBTAP00000026871.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000026871 ; ENSBTAP00000026871 ; ENSBTAG00000020175 .
GeneIDi 281225.
KEGGi bta:281225.

Organism-specific databases

CTDi 3093.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00670000098059.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi P61085.
KOi K04649.
OMAi NKEIADC.
OrthoDBi EOG7F513F.
TreeFami TF101127.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei P61085.
NextBioi 20805272.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR009060. 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 ]
Pfami PF00627. UBA. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view ]
SMARTi SM00165. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEi PS50030. UBA. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUMOYLATION AT LYS-14.

Entry informationi

Entry nameiUBE2K_BOVIN
AccessioniPrimary (citable) accession number: P61085
Secondary accession number(s): A5PK22
, O54806, P27924, Q16721, Q9CVV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3