ID UBE2B_RABIT Reviewed; 152 AA. AC P63148; P23567; Q9D0J6; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Ubiquitin-conjugating enzyme E2 B {ECO:0000305}; DE EC=2.3.2.23 {ECO:0000250|UniProtKB:P63146}; DE AltName: Full=E2 ubiquitin-conjugating enzyme B; DE AltName: Full=RAD6 homolog B; DE Short=HR6B; DE AltName: Full=Ubiquitin carrier protein B; DE AltName: Full=Ubiquitin-conjugating enzyme E2(14k); DE AltName: Full=Ubiquitin-protein ligase B; GN Name=UBE2B; Synonyms=RAD6B; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1313008; DOI=10.1016/s0021-9258(19)50455-0; RA Wing S.S., Dumas F., Banville D.; RT "A rabbit reticulocyte ubiquitin carrier protein that supports ubiquitin- RT dependent proteolysis (E214k) is homologous to the yeast DNA repair gene RT RAD6."; RL J. Biol. Chem. 267:6495-6501(1992). CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its CC covalent attachment to other proteins. In association with the E3 CC enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription CC regulation by catalyzing the monoubiquitination of histone H2B at 'Lys- CC 120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic CC transcriptional activation, elongation by RNA polymerase II, telomeric CC silencing, and is also a prerequisite for H3K4me and H3K79me formation. CC In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked CC polyubiquitination. Required for postreplication repair of UV-damaged CC DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 CC ubiquitin ligase complex involved in mono-ubiquitination of DNA- CC associated PCNA on 'Lys-164'. May be involved in neurite outgrowth. May CC play a role in DNA repair (By similarity). CC {ECO:0000250|UniProtKB:P63146}. 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:0000250|UniProtKB:P63146, ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000250|UniProtKB:P63146, ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBUNIT: Interacts with RAD18, UBR2 and WAC. CC {ECO:0000250|UniProtKB:P63146}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63149}. CC Nucleus {ECO:0000250|UniProtKB:P63149}. Note=In peripheral neurons, CC expressed both at the plasma membrane and in nuclei. CC {ECO:0000250|UniProtKB:P63149}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. 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; M62387; AAA31492.1; -; mRNA. DR PIR; A42416; A42416. DR RefSeq; NP_001075765.1; NM_001082296.1. DR AlphaFoldDB; P63148; -. DR BMRB; P63148; -. DR SMR; P63148; -. DR BioGRID; 1172155; 1. DR IntAct; P63148; 2. DR STRING; 9986.ENSOCUP00000014382; -. DR PaxDb; 9986-ENSOCUP00000013548; -. DR Ensembl; ENSOCUT00000015769.2; ENSOCUP00000013548.2; ENSOCUG00000015774.3. DR GeneID; 100009132; -. DR KEGG; ocu:100009132; -. DR CTD; 7320; -. DR eggNOG; KOG0419; Eukaryota. DR GeneTree; ENSGT00940000156580; -. DR HOGENOM; CLU_030988_10_2_1; -. DR InParanoid; P63148; -. DR OMA; DNIMCCH; -. DR OrthoDB; 5478564at2759; -. DR TreeFam; TF101128; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000001811; Chromosome 3. DR Bgee; ENSOCUG00000015774; Expressed in blood and 15 other cell types or tissues. DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. 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:SF246; UBIQUITIN-CONJUGATING ENZYME E2 B; 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. PE 2: Evidence at transcript level; KW ATP-binding; Cell membrane; DNA damage; DNA repair; Membrane; KW Nucleotide-binding; Nucleus; Reference proteome; Transferase; KW Ubl conjugation pathway. FT CHAIN 1..152 FT /note="Ubiquitin-conjugating enzyme E2 B" FT /id="PRO_0000082449" FT DOMAIN 4..150 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT ACT_SITE 88 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133" SQ SEQUENCE 152 AA; 17312 MW; CFDEEEE7E06840BE CRC64; MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED GTFKLVIEFS EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWN DS //