UB2E2_MOUSE
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 03-AUG-2022, entry version 146.
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}.
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; 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; Q91W82; -.
DR PRIDE; Q91W82; -.
DR ProteomicsDB; 297772; -.
DR Antibodypedia; 11339; 181 antibodies from 31 providers.
DR DNASU; 218793; -.
DR Ensembl; ENSMUST00000076133; ENSMUSP00000075495; ENSMUSG00000058317.
DR Ensembl; ENSMUST00000150727; ENSMUSP00000115738; ENSMUSG00000058317.
DR GeneID; 218793; -.
DR KEGG; mmu:218793; -.
DR UCSC; uc007shv.1; mouse.
DR CTD; 7325; -.
DR MGI; MGI:2384997; Ube2e2.
DR VEuPathDB; HostDB:ENSMUSG00000058317; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000155985; -.
DR InParanoid; Q91W82; -.
DR OMA; PPIVIFR; -.
DR OrthoDB; 1337945at2759; -.
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 74 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 252 other tissues.
DR ExpressionAtlas; Q91W82; baseline and differential.
DR Genevisible; Q91W82; MM.
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:cellular response to DNA damage stimulus; 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 GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 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
