UBE4A_BOVIN
ID UBE4A_BOVIN Reviewed; 1067 AA.
AC A5PKG6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:E9Q735};
DE AltName: Full=RING-type E3 ubiquitin transferase E4 A;
GN Name=UBE4A {ECO:0000305};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases. May also
CC function as an E4 ligase mediating the assembly of polyubiquitin chains
CC on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates
CC 'Lys-48'-linked polyubiquitination of substrates.
CC {ECO:0000250|UniProtKB:E9Q735, ECO:0000250|UniProtKB:P54860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:E9Q735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:E9Q735}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000305}.
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DR EMBL; BC142480; AAI42481.1; -; mRNA.
DR RefSeq; NP_001092469.1; NM_001098999.1.
DR AlphaFoldDB; A5PKG6; -.
DR SMR; A5PKG6; -.
DR STRING; 9913.ENSBTAP00000026289; -.
DR PaxDb; A5PKG6; -.
DR PRIDE; A5PKG6; -.
DR Ensembl; ENSBTAT00000026289; ENSBTAP00000026289; ENSBTAG00000019725.
DR Ensembl; ENSBTAT00000075080; ENSBTAP00000065403; ENSBTAG00000019725.
DR GeneID; 517544; -.
DR KEGG; bta:517544; -.
DR CTD; 9354; -.
DR VEuPathDB; HostDB:ENSBTAG00000019725; -.
DR VGNC; VGNC:36603; UBE4A.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00390000009300; -.
DR HOGENOM; CLU_003224_1_0_1; -.
DR InParanoid; A5PKG6; -.
DR OMA; EHDTSTQ; -.
DR OrthoDB; 194967at2759; -.
DR TreeFam; TF300802; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000019725; Expressed in neutrophil and 108 other tissues.
DR ExpressionAtlas; A5PKG6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931; PTHR13931; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1067
FT /note="Ubiquitin conjugation factor E4 A"
FT /id="PRO_0000324758"
FT DOMAIN 987..1061
FT /note="U-box"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14139"
SQ SEQUENCE 1067 AA; 122593 MW; F0A9C34D28748A45 CRC64;
MTDQENNNNI SSNPFAALFG SLADAKQFAA IQKEQLKQQS DELPASPDDS DNSVSESLDE
FDYSVAEISR SFRSQQEICE QLNINHMIQR IFLITLDNSD PSLKSGNGIP SRCVYLEEMA
VDLEDQDWLD MNNVEQAVFT RLLLQDPGNH LINMTSSTTL NLSADRDAGE KHIFCYLYSC
FQRAKEEITK VPENLLPFAV QCRNLTVSNT RTVLLTPEIY VDQNIHEQLV DLMVEAILGG
HFESVAEFLD EVIEALILDE EVRTFPEVMI PVFDILSSRI KDLELCQILL YAYLDILLYF
TKQKDMAKVF VDYIQPKDPS NGQMYQKTLL GVILNISCLL KTPGVIENHG YFLNPSRSSP
QEIKVQEANI HQFMARYHEK IYQMLKNLLQ LSPETKHCIL SWLGNCLHAN AGRTKIWANQ
MPEIFFQMYA SDAFFLNLGA ALLKLCQPFC KPRSSRLLTF NPTYCALKEL NDEERKIKNV
HMRGLDKETC LIPAVQEPKF PQNYNLVTEN LVLTEYTLYL GFHRLHDQMV KINQNLHRLQ
VAWRDAQQSS SPAADNLREQ FERLMTVYLS TKTAMTEPQM LQNCLNLQVS MAVLLVQLAI
GNEGSQLMEL TFPLPDGYSS LAYVPEFFAD NLGDFLIFLR RFADDILETS ADSLEHVLHF
ITIFTGSIER MKNPHLRAKL AEVLEAVMPH MDQTPNPLVS SVFHRKRVFC NFPYASHLAE
ALIKVFVDIE FTGDPHQFEQ KFNYRRPMYP ILKYMWGTDT YRESIKDLAD YASKNLEAMN
PPLFLRFLNL LMNDAIFLLD EAIQYLSKIK IQQIEKDRGE WDNLTPEARR EKEAGLQMFG
QLARFHNIMS NETIGTLAFL TSEIKSLFVH PFLAERIISM LNYFLQHLVG PKMGALKVKD
FSEFDFKPQQ LVSDICTIYL NLGDEENFCA TVPKDGRSYS PTLFAQTVRV LKKINKPGNM
IVAFSNLAER IKSLADLQQQ EEETYADACD EFLDPIMSTL MSDPVVLPSS RVTVDRSTIA
RHLLSDQTDP FNRSPLTMDQ IRPNTELKEK IQRWLAERKQ QQKEQLE
