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   24-JAN-2024, entry version 161.
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; 70.
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   MassIVE; Q5VVX9; -.
DR   PaxDb; 9606-ENSP00000360116; -.
DR   PeptideAtlas; Q5VVX9; -.
DR   ProteomicsDB; 65500; -. [Q5VVX9-1]
DR   Antibodypedia; 19528; 175 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   AGR; HGNC:28559; -.
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; 1327944at2759; -.
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   SIGNOR; Q5VVX9; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 148581; 9 hits in 1119 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 87 other cell types or tissues.
DR   ExpressionAtlas; Q5VVX9; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   IDEAL; IID00638; -.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF252; UBIQUITIN-CONJUGATING ENZYME E2 U; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q5VVX9; HS.
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
//