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Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (Huntingtin-interacting protein 2) (HIP-2) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-25 kDa) (Ubiquitin-conjugating enzyme E2(25K)) (Ubiquitin-conjugating enzyme E2-25K) (Ubiquitin-protein ligase)

 UBE2K_BOVIN             Reviewed;         200 AA.
P61085; A5PK22; O54806; P27924; Q16721; Q9CVV9;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 127.
RecName: Full=Ubiquitin-conjugating enzyme E2 K;
EC=2.3.2.23;
AltName: Full=E2 ubiquitin-conjugating enzyme K;
AltName: Full=Huntingtin-interacting protein 2;
Short=HIP-2;
AltName: Full=Ubiquitin carrier protein;
AltName: Full=Ubiquitin-conjugating enzyme E2-25 kDa;
Short=Ubiquitin-conjugating enzyme E2(25K);
Short=Ubiquitin-conjugating enzyme E2-25K;
AltName: Full=Ubiquitin-protein ligase;
Name=UBE2K; Synonyms=HIP2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=1714895;
Chen Z., Niles E.G., Pickart C.M.;
"Isolation of a cDNA encoding a mammalian multiubiquitinating enzyme
(E225K) and overexpression of the functional enzyme in Escherichia
coli.";
J. Biol. Chem. 266:15698-15704(1991).
[2]
SEQUENCE REVISION TO 23, AND MUTAGENESIS OF SER-86.
PubMed=9657692; DOI=10.1021/bi9800911;
Mastrandrea L.D., Kasperek E.M., Niles E.G., Pickart C.M.;
"Core domain mutation (S86Y) selectively inactivates polyubiquitin
chain synthesis catalyzed by E2-25K.";
Biochemistry 37:9784-9792(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Thymus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION IN UBIQUITINATION OF NF-KAPPA-B.
PubMed=9535861; DOI=10.1074/jbc.273.15.8820;
Coux O., Goldberg A.L.;
"Enzymes catalyzing ubiquitination and proteolytic processing of the
p105 precursor of nuclear factor kappaB1.";
J. Biol. Chem. 273:8820-8828(1998).
[5]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=1322903;
Cook W.J., Jeffrey L.C., Carson M., Chen Z., Pickart C.M.;
"Structure of a diubiquitin conjugate and a model for interaction with
ubiquitin conjugating enzyme (E2).";
J. Biol. Chem. 267:16467-16471(1992).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUMOYLATION AT LYS-14.
PubMed=15723079; DOI=10.1038/nsmb903;
Pichler A., Knipscheer P., Oberhofer E., van Dijk W.J., Koerner R.,
Olsen J.V., Jentsch S., Melchior F., Sixma T.K.;
"SUMO modification of the ubiquitin-conjugating enzyme E2-25K.";
Nat. Struct. Mol. Biol. 12:264-269(2005).
-!- 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. {ECO:0000250|UniProtKB:P61086,
ECO:0000269|PubMed:9535861}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1.
{ECO:0000250|UniProtKB:P61086}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: Sumoylation at Lys-14 impairs catalytic activity.
{ECO:0000269|PubMed:15723079}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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EMBL; S51016; AAB19536.1; -; mRNA.
EMBL; BC142324; AAI42325.1; -; mRNA.
PIR; A40797; A40797.
RefSeq; NP_776505.1; NM_174080.2.
UniGene; Bt.65293; -.
PDB; 2BEP; X-ray; 1.80 A; A=1-155.
PDB; 2BF8; X-ray; 2.30 A; A=2-155.
PDBsum; 2BEP; -.
PDBsum; 2BF8; -.
ProteinModelPortal; P61085; -.
SMR; P61085; -.
STRING; 9913.ENSBTAP00000026871; -.
PaxDb; P61085; -.
PeptideAtlas; P61085; -.
PRIDE; P61085; -.
Ensembl; ENSBTAT00000026871; ENSBTAP00000026871; ENSBTAG00000020175.
GeneID; 281225; -.
KEGG; bta:281225; -.
CTD; 3093; -.
VGNC; VGNC:36587; UBE2K.
eggNOG; KOG0418; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00670000098059; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P61085; -.
KO; K04649; -.
OMA; NKEIADC; -.
OrthoDB; EOG091G0KVW; -.
TreeFam; TF101127; -.
Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
EvolutionaryTrace; P61085; -.
Proteomes; UP000009136; Chromosome 6.
Bgee; ENSBTAG00000020175; Expressed in 10 organ(s), highest expression level in brain.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00627; UBA; 1.
Pfam; PF00179; UQ_con; 1.
SMART; SM00165; UBA; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50030; UBA; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Isopeptide bond; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P61086}.
CHAIN 2 200 Ubiquitin-conjugating enzyme E2 K.
/FTId=PRO_0000082442.
DOMAIN 160 200 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
ACT_SITE 92 92 Glycyl thioester intermediate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P61086}.
MOD_RES 14 14 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61086}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:P61086}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P61086}.
MUTAGEN 86 86 S->Y: Inhibits ubiquitin transfer to
macromolecular acceptors.
{ECO:0000269|PubMed:9657692}.
CONFLICT 23 23 S -> T (in Ref. 1; AAB19536).
{ECO:0000305}.
HELIX 3 18 {ECO:0000244|PDB:2BEP}.
HELIX 20 23 {ECO:0000244|PDB:2BEP}.
STRAND 26 31 {ECO:0000244|PDB:2BEP}.
STRAND 33 44 {ECO:0000244|PDB:2BEP}.
TURN 50 53 {ECO:0000244|PDB:2BEP}.
STRAND 55 61 {ECO:0000244|PDB:2BEP}.
TURN 64 67 {ECO:0000244|PDB:2BEP}.
STRAND 72 77 {ECO:0000244|PDB:2BEP}.
TURN 86 88 {ECO:0000244|PDB:2BEP}.
HELIX 94 96 {ECO:0000244|PDB:2BEP}.
TURN 97 99 {ECO:0000244|PDB:2BEP}.
HELIX 106 118 {ECO:0000244|PDB:2BEP}.
HELIX 128 136 {ECO:0000244|PDB:2BEP}.
HELIX 138 152 {ECO:0000244|PDB:2BEP}.
SEQUENCE 200 AA; 22407 MW; E40668099ED25828 CRC64;
MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI
KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA
EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI
VALSSKSWDV ETATELLLSN


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