UBE2B_MOUSE
ID UBE2B_MOUSE Reviewed; 152 AA.
AC P63147; P23567; Q3UGS2; Q9D0J6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 B;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme B;
DE AltName: Full=E214K;
DE AltName: Full=RAD6 homolog B;
DE Short=HR6B;
DE Short=mHR6B;
DE AltName: Full=Ubiquitin carrier protein B;
DE AltName: Full=Ubiquitin-protein ligase B;
GN Name=Ube2b; Synonyms=Rad6b;
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 [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Testis;
RX PubMed=8797826; DOI=10.1016/s0092-8674(00)80154-3;
RA Roest H.P., van Klaveren J., de Wit J., van Gurp C.G., Koken M.H.M.,
RA Vermey M., van Roijen J.H., Vreeburg J.T.M., Baarends W.M., Bootsma D.,
RA Grootegoed J.A., Hoeijmakers J.H.J.;
RT "Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice
RT causes male sterility associated with chromatin modification.";
RL Cell 86:799-810(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Varshavsky A., Grigoryev S., Stewart A.E., Kwon Y.T., Arfin S.M.,
RA Bradshaw R.A., Jenkins N.A., Copeland N.G.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP INTERACTION WITH UBR2.
RX PubMed=14585983; DOI=10.1128/mcb.23.22.8255-8271.2003;
RA Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W., Sheng J.,
RA Xie Y., Varshavsky A.;
RT "Female lethality and apoptosis of spermatocytes in mice lacking the UBR2
RT ubiquitin ligase of the N-end rule pathway.";
RL Mol. Cell. Biol. 23:8255-8271(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, 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: 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.
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:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with RAD18, UBR2 and WAC.
CC {ECO:0000269|PubMed:14585983}.
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}.
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DR EMBL; X96859; CAA65602.1; -; mRNA.
DR EMBL; U57690; AAC52884.1; -; mRNA.
DR EMBL; AK010432; BAB26934.1; -; mRNA.
DR EMBL; AK011363; BAB27570.1; -; mRNA.
DR EMBL; AK147785; BAE28135.1; -; mRNA.
DR EMBL; AK169229; BAE40998.1; -; mRNA.
DR CCDS; CCDS24664.1; -.
DR RefSeq; NP_033484.3; NM_009458.4.
DR RefSeq; XP_006533223.1; XM_006533160.2.
DR RefSeq; XP_011247269.1; XM_011248967.1.
DR AlphaFoldDB; P63147; -.
DR BMRB; P63147; -.
DR SMR; P63147; -.
DR BioGRID; 204415; 7.
DR STRING; 10090.ENSMUSP00000020657; -.
DR PhosphoSitePlus; P63147; -.
DR EPD; P63147; -.
DR MaxQB; P63147; -.
DR PaxDb; P63147; -.
DR PRIDE; P63147; -.
DR ProteomicsDB; 298446; -.
DR Antibodypedia; 26297; 272 antibodies from 33 providers.
DR DNASU; 22210; -.
DR Ensembl; ENSMUST00000020657; ENSMUSP00000020657; ENSMUSG00000020390.
DR Ensembl; ENSMUST00000109086; ENSMUSP00000104714; ENSMUSG00000020390.
DR GeneID; 22210; -.
DR KEGG; mmu:22210; -.
DR UCSC; uc007iut.2; mouse.
DR CTD; 7320; -.
DR MGI; MGI:102944; Ube2b.
DR VEuPathDB; HostDB:ENSMUSG00000020390; -.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000156580; -.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P63147; -.
DR OMA; EDTIWEC; -.
DR OrthoDB; 1292821at2759; -.
DR PhylomeDB; P63147; -.
DR TreeFam; TF101128; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22210; 8 hits in 114 CRISPR screens.
DR ChiTaRS; Ube2b; mouse.
DR PRO; PR:P63147; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63147; protein.
DR Bgee; ENSMUSG00000020390; Expressed in intercostal muscle and 257 other tissues.
DR ExpressionAtlas; P63147; baseline and differential.
DR Genevisible; P63147; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; ISO:MGI.
DR GO; GO:0001741; C:XY body; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IGI:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0051026; P:chiasma assembly; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0033522; P:histone H2A ubiquitination; ISO:MGI.
DR GO; GO:0070076; P:histone lysine demethylation; IMP:MGI.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI.
DR GO; GO:1901874; P:negative regulation of post-translational protein modification; IMP:MGI.
DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:MGI.
DR GO; GO:0006301; P:postreplication repair; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
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 GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0031056; P:regulation of histone modification; IMP:MGI.
DR GO; GO:0009411; P:response to UV; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; TAS:MGI.
DR GO; GO:0070193; P:synaptonemal complex organization; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
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 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_0000082448"
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"
FT CONFLICT 7
FT /note="R -> E (in Ref. 3; BAB27570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17312 MW; CFDEEEE7E06840BE CRC64;
MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED GTFKLVIEFS
EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS
PANSQAAQLY QENKREYEKR VSAIVEQSWN DS
