ID   UB2E2_MOUSE             Reviewed;         201 AA.
AC   Q91W82;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 E2;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme E2;
DE   AltName: Full=Ubiquitin carrier protein E2;
DE   AltName: Full=Ubiquitin-protein ligase E2;
GN   Name=Ube2e2;
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 [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
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).
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and
CC       'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the
CC       ISGylation of influenza A virus NS1 protein.
CC       {ECO:0000250|UniProtKB:Q96LR5}.
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:Q96LR5, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q96LR5}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; BC016265; AAH16265.1; -; mRNA.
DR   CCDS; CCDS26838.1; -.
DR   RefSeq; NP_659088.1; NM_144839.1.
DR   RefSeq; XP_006518076.1; XM_006518013.1.
DR   AlphaFoldDB; Q91W82; -.
DR   SMR; Q91W82; -.
DR   BioGRID; 230065; 5.
DR   STRING; 10090.ENSMUSP00000115738; -.
DR   iPTMnet; Q91W82; -.
DR   PhosphoSitePlus; Q91W82; -.
DR   SwissPalm; Q91W82; -.
DR   EPD; Q91W82; -.
DR   jPOST; Q91W82; -.
DR   MaxQB; Q91W82; -.
DR   PaxDb; 10090-ENSMUSP00000115738; -.
DR   ProteomicsDB; 297772; -.
DR   Pumba; Q91W82; -.
DR   Antibodypedia; 11339; 203 antibodies from 31 providers.
DR   DNASU; 218793; -.
DR   Ensembl; ENSMUST00000076133.10; ENSMUSP00000075495.4; ENSMUSG00000058317.13.
DR   Ensembl; ENSMUST00000150727.8; ENSMUSP00000115738.2; ENSMUSG00000058317.13.
DR   GeneID; 218793; -.
DR   KEGG; mmu:218793; -.
DR   UCSC; uc007shv.1; mouse.
DR   AGR; MGI:2384997; -.
DR   CTD; 7325; -.
DR   MGI; MGI:2384997; Ube2e2.
DR   VEuPathDB; HostDB:ENSMUSG00000058317; -.
DR   eggNOG; KOG0417; Eukaryota.
DR   GeneTree; ENSGT00940000155985; -.
DR   InParanoid; Q91W82; -.
DR   OMA; HMNISEQ; -.
DR   OrthoDB; 5478564at2759; -.
DR   PhylomeDB; Q91W82; -.
DR   TreeFam; TF101117; -.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 218793; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Ube2e2; mouse.
DR   PRO; PR:Q91W82; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q91W82; Protein.
DR   Bgee; ENSMUSG00000058317; Expressed in dentate gyrus of hippocampal formation granule cell and 255 other cell types or tissues.
DR   ExpressionAtlas; Q91W82; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042296; F:ISG15 transferase activity; ISO:MGI.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:0006974; P:DNA damage response; ISO:MGI.
DR   GO; GO:0032020; P:ISG15-protein conjugation; ISO:MGI.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISO:MGI.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
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; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF429; UBIQUITIN-CONJUGATING ENZYME E2 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.
DR   Genevisible; Q91W82; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LR5"
FT   CHAIN           2..201
FT                   /note="Ubiquitin-conjugating enzyme E2 E2"
FT                   /id="PRO_0000082473"
FT   DOMAIN          55..201
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LR5"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LR5"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LR5"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LR5"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LR5"
SQ   SEQUENCE   201 AA;  22241 MW;  445D00BECA8CD83F CRC64;
     MSTEAQRVDD SPSTSGGSSD GDQRESVQQE PDREQVQPKK KEGKISSKTA AKLSTSAKRI
     QKELAEITLD PPPNCSAGPK GDNIYEWRST ILGPPGSVYE GGVFFLDITF SPDYPFKPPK
     VTFRTRIYHC NINSQGVICL DILKDNWSPA LTISKVLLSI CSLLTDCNPA DPLVGSIATQ
     YMTNRAEHDR MARQWTKRYA T
//