Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P61085

- UBE2K_BOVIN

UniProt

P61085 - UBE2K_BOVIN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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 – 1816
    Helixi20 – 234
    Beta strandi26 – 316
    Beta strandi33 – 4412
    Turni50 – 534
    Beta strandi55 – 617
    Turni64 – 674
    Beta strandi72 – 776
    Turni86 – 883
    Helixi94 – 963
    Turni97 – 993
    Helixi106 – 11813
    Helixi128 – 1369
    Helixi138 – 15215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP    50
    YEGGRYQLEI KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW 100
    AAAMTLRTVL LSLQALLAAA EPDDPQDAVV ANQYKQNPEM FKQTARLWAH 150
    VYAGAPVSSP EYTKKIENLC AMGFDRNAVI VALSSKSWDV ETATELLLSN 200
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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 1, 2014
    This is version 99 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