UBCB_DICDI
ID UBCB_DICDI Reviewed; 148 AA.
AC Q94490; Q54P16;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=UBC1;
GN Name=ubcB; ORFNames=DDB_G0284865;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3;
RX PubMed=9348538; DOI=10.1091/mbc.8.10.1989;
RA Clark A., Nomura A., Mohanty S., Firtel R.A.;
RT "A ubiquitin-conjugating enzyme is essential for developmental transitions
RT in Dictyostelium.";
RL Mol. Biol. Cell 8:1989-2002(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, INTERACTION WITH MKKA, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3;
RX PubMed=9832508; DOI=10.1101/gad.12.22.3564;
RA Chung C.Y., Reddy T.B.K., Zhou K., Firtel R.A.;
RT "A novel, putative MEK kinase controls developmental timing and spatial
RT patterning in Dictyostelium and is regulated by ubiquitin-mediated protein
RT degradation.";
RL Genes Dev. 12:3564-3578(1998).
CC -!- FUNCTION: Involved in protein ubiquitination and degradation during
CC development. Mediates protein ubiquitination at the mound and finger
CC stage required for subsequent development and may be an essential
CC component of the developmental transition between the induction of
CC postaggregative gene expression and subsequent cell-type
CC differentiation and morphogenesis. ubcB and ubpB differentially control
CC ubiquitination/deubiquitination and degradation of mkkA protein in a
CC cell-type-specific and temporally regulated manner.
CC {ECO:0000269|PubMed:9348538, ECO:0000269|PubMed:9832508}.
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with mkkA (via F-box/WD40 repeat domains).
CC {ECO:0000269|PubMed:9832508}.
CC -!- DISRUPTION PHENOTYPE: The developmental pattern of protein
CC ubiquitination is altered in null cells. Null cells are blocked in the
CC ability to properly execute the developmental transition that occurs
CC between the induction of postaggregative gene expression during mound
CC formation and the induction of cell-type differentiation and subsequent
CC morphogenesis. Null cells plated on agar form mounds with normal
CC kinetics; however, they remain at this stage for 10 hours before
CC forming multiple tips and fingers that then arrest. Postaggregative
CC gene transcripts accumulate to very high levels and do not decrease
CC significantly with time as they do in wild-type cells. Expression of
CC cell-type-specific genes is very delayed, with the level of prespore-
CC specific gene expression being significantly reduced compared with that
CC in wild-type cells. Defect in the ability of null cells to participate
CC in normal development in chimeras containing wild-type cells. Increased
CC stablity of mkkA and similar phenotype (significant delay at the mound
CC stage and arrest at the first finger stage) of cells that overexpress
CC mkkA. {ECO:0000269|PubMed:9348538, ECO:0000269|PubMed:9832508}.
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; U67838; AAB08700.1; -; Genomic_DNA.
DR EMBL; AAFI02000073; EAL64896.1; -; Genomic_DNA.
DR RefSeq; XP_639901.1; XM_634809.1.
DR AlphaFoldDB; Q94490; -.
DR SMR; Q94490; -.
DR STRING; 44689.DDB0201564; -.
DR PaxDb; Q94490; -.
DR EnsemblProtists; EAL64896; EAL64896; DDB_G0284865.
DR GeneID; 8624813; -.
DR KEGG; ddi:DDB_G0284865; -.
DR dictyBase; DDB_G0284865; ubcB.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q94490; -.
DR OMA; HPNITND; -.
DR PhylomeDB; Q94490; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-DDI-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DDI-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-DDI-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DDI-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-DDI-176412; Phosphorylation of the APC/C.
DR Reactome; R-DDI-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DDI-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR Reactome; R-DDI-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94490; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:dictyBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:dictyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:dictyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..148
FT /note="Ubiquitin conjugating enzyme E2 B"
FT /id="PRO_0000389022"
FT DOMAIN 2..148
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 148 AA; 16809 MW; AAFF04D0C973C166 CRC64;
MAAHKRLQKE ITDMLKTPPS WCSAHLVDDN LQKWKATVQG PEGSPFEKGV FSMDIDIPAD
YPFKPPTLKF TTKIYHPNIK TSDGAICAEV FSTWSPQLKI LDVLTTIRSI LTDPNPDNPL
ETEIAQQFKT DRNAFNKTAK EWTKKYAK
