UBE4A_MOUSE
ID UBE4A_MOUSE Reviewed; 1028 AA.
AC E9Q735;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000305};
DE EC=2.3.2.- {ECO:0000269|PubMed:11435423};
GN Name=Ube4a {ECO:0000312|MGI:MGI:2154580};
GN Synonyms=Ufd2b {ECO:0000312|MGI:MGI:2154580};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11435423; DOI=10.1074/jbc.m102755200;
RA Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
RT "U box proteins as a new family of ubiquitin-protein ligases.";
RL J. Biol. Chem. 276:33111-33120(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:P54860, ECO:0000269|PubMed:11435423}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11435423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11435423}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, heart, brain, kidney and
CC testis. {ECO:0000269|PubMed:11435423}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC061963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23122.2; -.
DR RefSeq; NP_663375.3; NM_145400.3.
DR AlphaFoldDB; E9Q735; -.
DR SMR; E9Q735; -.
DR BioGRID; 228292; 7.
DR STRING; 10090.ENSMUSP00000113346; -.
DR PhosphoSitePlus; E9Q735; -.
DR jPOST; E9Q735; -.
DR MaxQB; E9Q735; -.
DR PaxDb; E9Q735; -.
DR PeptideAtlas; E9Q735; -.
DR PRIDE; E9Q735; -.
DR ProteomicsDB; 298086; -.
DR Antibodypedia; 32453; 247 antibodies from 32 providers.
DR DNASU; 140630; -.
DR Ensembl; ENSMUST00000117506; ENSMUSP00000113346; ENSMUSG00000059890.
DR GeneID; 140630; -.
DR KEGG; mmu:140630; -.
DR UCSC; uc009peu.2; mouse.
DR CTD; 9354; -.
DR MGI; MGI:2154580; Ube4a.
DR VEuPathDB; HostDB:ENSMUSG00000059890; -.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00390000009300; -.
DR TreeFam; TF300802; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140630; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ube4a; mouse.
DR PRO; PR:E9Q735; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; E9Q735; protein.
DR Bgee; ENSMUSG00000059890; Expressed in hindlimb stylopod muscle and 199 other tissues.
DR ExpressionAtlas; E9Q735; baseline and differential.
DR Genevisible; E9Q735; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; 2.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 2.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1028
FT /note="Ubiquitin conjugation factor E4 A"
FT /id="PRO_0000430791"
FT DOMAIN 949..1023
FT /note="U-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01034"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14139"
SQ SEQUENCE 1028 AA; 118198 MW; 00221784ECDD8761 CRC64;
MTDQENNNNI SSNPFAALFG SLADAKQFAA IQKEQLKQQS DELPASPDDS DNSVSESLDE
FDYSVSEISR SFRTHQEMCE QLNINHMIQR IFLITLDNSD PSLKSGNGIP SRCVYLEEMA
VELEDQDWLD MSNVEQAIFA RLLLQDPGNH LISMTSSTTL NLSADRDAGE RHIFCYLYSC
FQRAKEEITK VPENLLPFAV QCRNLTVSNT RTVLLTPEIY VDQNIHEQLV DLMLEAIQGA
HFEDVTEFLE EVIEALLLDE EVRTFPEVMI PVFDILLSRI KDLELCQILL YAYLDILLYF
TRQKDMAKVF LEYIQPKDPS NGQMYQKTLL GVILNISCLL KTPGVVENHG FFLNPSRSSP
QEIKVQEANI HQFMAQFHEK IYQMLKNLLQ LSPETKHCIL FWLGNCLHAN AGRTKIWANQ
MPEIFFQMYA SDAFFLNLGA ALLKLCQPFC KPRSSRLLTF NPTYCVLKDL NDEERKIKSV
HMRGLDKETC LIPAVQEPTF PQSYNLVTEN LALTEYTLYL GFHRLHDQMV KINQNLHRLQ
VAWRDAQQSS SPAADNLREQ FERLMTIYLS TKTAMTEPQM LQNCLNLQVS MAVLLVQLAI
GNEGSQPIEL SFPLPDGYSS LAYVPEFFAD NLGDFLIFLR RFAEDILETS ADSLEHVLHF
ITIFTGSIER MKNPHLRAKL AEVLEAVMPH LDQTPSPLVS SVFHRKRVFC NFPYAPQLAE
ALIKVFVDIE FTGDPHQFEQ KFNYRRPMYP ILRYMWGTDC YRESIKYLSK IKIQQIEKDR
GEWESLTPEA RREKEAGLQM FGQLARFHNI MSNETIGTLS FLTSEIKSLF VHPFLAERII
SMLNYFLQHL VGPKMGALKV KDFSEFDFKP QQLVSDICTI YLNLGDEENF CATVPKDGRS
YSPTLFAQTV RVLKKINKPG NMIVAFSNLA ERIKSLADLQ QQEEETYADA CDEFLDPIMS
TLMSDPVVLP SSRVTVDRST IARHLLSDQT DPFNRSPLTM DQIRPNTELK EKIQRWLAER
KQQKEQPE
