UBE2U_HUMAN
ID UBE2U_HUMAN Reviewed; 321 AA.
AC Q5VVX9; Q8N1D4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 U;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme U;
DE AltName: Full=Ubiquitin carrier protein U;
DE AltName: Full=Ubiquitin-protein ligase U;
GN Name=UBE2U;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1-150.
RA Avvakumov G.V., Walker J.R., Choe J., Newman E.M., MacKenzie F.,
RA Bochkarev A., Dhe-Paganon S.;
RT "Novel ubiquitin-conjugating enzyme.";
RL Submitted (FEB-2005) to the PDB data bank.
RN [4] {ECO:0007744|PDB:1YRV}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1-150, FUNCTION, AND
RP AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. {ECO:0000269|PubMed:22496338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- INTERACTION:
CC Q5VVX9; Q08379: GOLGA2; NbExp=4; IntAct=EBI-2130181, EBI-618309;
CC Q5VVX9; Q13049: TRIM32; NbExp=4; IntAct=EBI-2130181, EBI-742790;
CC Q5VVX9-2; P62879: GNB2; NbExp=3; IntAct=EBI-21897992, EBI-356942;
CC Q5VVX9-2; P40337-2: VHL; NbExp=3; IntAct=EBI-21897992, EBI-12157263;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VVX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VVX9-2; Sequence=VSP_016003;
CC -!- PTM: Autoubiquitinated in vitro in the presence of UBR5.
CC {ECO:0000269|PubMed:22496338}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AL445205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029895; AAH29895.1; -; mRNA.
DR CCDS; CCDS627.1; -. [Q5VVX9-2]
DR RefSeq; NP_689702.1; NM_152489.2. [Q5VVX9-2]
DR PDB; 1YRV; X-ray; 2.18 A; A=1-150.
DR PDBsum; 1YRV; -.
DR AlphaFoldDB; Q5VVX9; -.
DR SMR; Q5VVX9; -.
DR BioGRID; 127156; 141.
DR IntAct; Q5VVX9; 71.
DR MINT; Q5VVX9; -.
DR STRING; 9606.ENSP00000360116; -.
DR MoonDB; Q5VVX9; Predicted.
DR iPTMnet; Q5VVX9; -.
DR PhosphoSitePlus; Q5VVX9; -.
DR BioMuta; UBE2U; -.
DR DMDM; 74747311; -.
DR jPOST; Q5VVX9; -.
DR PaxDb; Q5VVX9; -.
DR PeptideAtlas; Q5VVX9; -.
DR PRIDE; Q5VVX9; -.
DR Antibodypedia; 19528; 161 antibodies from 26 providers.
DR DNASU; 148581; -.
DR Ensembl; ENST00000371076.7; ENSP00000360116.3; ENSG00000177414.14. [Q5VVX9-2]
DR Ensembl; ENST00000611228.4; ENSP00000481174.1; ENSG00000177414.14. [Q5VVX9-1]
DR GeneID; 148581; -.
DR KEGG; hsa:148581; -.
DR UCSC; uc001dbn.1; human. [Q5VVX9-1]
DR CTD; 148581; -.
DR DisGeNET; 148581; -.
DR GeneCards; UBE2U; -.
DR HGNC; HGNC:28559; UBE2U.
DR HPA; ENSG00000177414; Tissue enriched (testis).
DR neXtProt; NX_Q5VVX9; -.
DR OpenTargets; ENSG00000177414; -.
DR PharmGKB; PA142670656; -.
DR VEuPathDB; HostDB:ENSG00000177414; -.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000162256; -.
DR HOGENOM; CLU_076373_0_0_1; -.
DR InParanoid; Q5VVX9; -.
DR OMA; NNYEGIT; -.
DR OrthoDB; 1538096at2759; -.
DR PhylomeDB; Q5VVX9; -.
DR TreeFam; TF329302; -.
DR BRENDA; 2.3.2.23; 2681.
DR PathwayCommons; Q5VVX9; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q5VVX9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 148581; 7 hits in 1041 CRISPR screens.
DR EvolutionaryTrace; Q5VVX9; -.
DR GenomeRNAi; 148581; -.
DR Pharos; Q5VVX9; Tdark.
DR PRO; PR:Q5VVX9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VVX9; protein.
DR Bgee; ENSG00000177414; Expressed in sperm and 85 other tissues.
DR ExpressionAtlas; Q5VVX9; baseline and differential.
DR Genevisible; Q5VVX9; HS.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR IDEAL; IID00638; -.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..321
FT /note="Ubiquitin-conjugating enzyme E2 U"
FT /id="PRO_0000082512"
FT DOMAIN 4..153
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 285..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 89
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT VAR_SEQ 227..321
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016003"
FT VARIANT 90
FT /note="I -> T (in dbSNP:rs7532933)"
FT /id="VAR_057323"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:1YRV"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1YRV"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1YRV"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:1YRV"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1YRV"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1YRV"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1YRV"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1YRV"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1YRV"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:1YRV"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:1YRV"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1YRV"
SQ SEQUENCE 321 AA; 37741 MW; 8104FE91620417BB CRC64;
MHGRAYLLLH RDFCDLKENN YKGITAKPVS EDMMEWEVEI EGLQNSVWQG LVFQLTIHFT
SEYNYAPPVV KFITIPFHPN VDPHTGQPCI DFLDNPEKWN TNYTLSSILL ALQVMLSNPV
LENPVNLEAA RILVKDESLY RTILRLFNRP LQMKDDSQEL PKDPRKCIRP IKTTSFSDYY
QTWSRIATSK ATEYYRTPLL KVPNFIGQYY KWKKMDLQHQ KEWNLKYSVI KCWLARKRMP
HEVTHSMEEI KLCPTLIPTT DEIFLESPTA INSITDIYET EEEGWKSDTS LYENDTDEPR
EEEVEDLISW TNTLNTNTSE D
