ID   UBE2N_DICDI             Reviewed;         154 AA.
AC   Q86K32; B0M0P7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 N;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme N;
DE   AltName: Full=Ubiquitin carrier protein N;
DE   AltName: Full=Ubiquitin-protein ligase N;
GN   Name=ube2n; ORFNames=DDB_G0277267;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
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).
CC   -!- FUNCTION: The ube2v/ube2n heterodimer catalyzes the synthesis of non-
CC       canonical poly-ubiquitin chains that are linked through 'Lys-63'. This
CC       type of poly-ubiquitination does not lead to protein degradation by the
CC       proteasome. Mediates transcriptional activation of target genes. Plays
CC       a role in the control of progress through the cell cycle and
CC       differentiation. Plays a role in the error-free DNA repair pathway and
CC       contributes to the survival of cells after DNA damage.
CC       {ECO:0000250|UniProtKB:P61088}.
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   -!- SUBUNIT: Heterodimer with ube2v. {ECO:0000250|UniProtKB:P61088}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AAFI02000019; EAL68819.2; -; Genomic_DNA.
DR   RefSeq; XP_642773.2; XM_637681.2.
DR   AlphaFoldDB; Q86K32; -.
DR   SMR; Q86K32; -.
DR   STRING; 44689.Q86K32; -.
DR   PaxDb; 44689-DDB0237667; -.
DR   EnsemblProtists; EAL68819; EAL68819; DDB_G0277267.
DR   GeneID; 8620964; -.
DR   KEGG; ddi:DDB_G0277267; -.
DR   dictyBase; DDB_G0277267; ube2n.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_13_2_1; -.
DR   InParanoid; Q86K32; -.
DR   OMA; PDDYPME; -.
DR   PhylomeDB; Q86K32; -.
DR   Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-DDI-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-DDI-9020702; Interleukin-1 signaling.
DR   Reactome; R-DDI-9646399; Aggrephagy.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q86K32; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; 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:0006301; P:postreplication repair; IBA:GO_Central.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
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:SF370; UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 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   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..154
FT                   /note="Probable ubiquitin-conjugating enzyme E2 N"
FT                   /id="PRO_0000328343"
FT   DOMAIN          3..149
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,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   154 AA;  17380 MW;  AD66DD66A58CC046 CRC64;
     MATLPKRIIK ETQRLMTEPA PGISATPATD NFRYFKVAIS GPLDSPFEGG VFNLELFLTD
     DYPMSAPKVR FLTKIYHPNI DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP
     LANDVAEHWK TNEKEAMARA REWTRLYAEA PVEN
//