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Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1)

 UB2R1_MOUSE             Reviewed;         235 AA.
Q8CFI2; Q505K8;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 130.
RecName: Full=Ubiquitin-conjugating enzyme E2 R1;
EC=2.3.2.23;
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme R1;
EC=2.3.2.24;
AltName: Full=E2 ubiquitin-conjugating enzyme R1;
AltName: Full=Ubiquitin-conjugating enzyme E2-32 kDa complementing;
AltName: Full=Ubiquitin-conjugating enzyme E2-CDC34;
AltName: Full=Ubiquitin-protein ligase R1;
Name=Cdc34; Synonyms=Ubch3, Ube2r1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129, and C57BL/6J; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
INTERACTION WITH SCF COMPLEX, AND FUNCTION.
PubMed=10230406; DOI=10.1016/S1097-2765(00)80481-5;
Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.;
"Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to
catalyze the ubiquitination of I kappa B alpha.";
Mol. Cell 3:527-533(1999).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro catalyzes 'Lys-
48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and
the SCF(FBXW11) E3 ligase complex for the polyubiquitination of
NFKBIA leading to its subsequent proteasomal degradation. Performs
ubiquitin chain elongation building ubiquitin chains from the
UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator
E2, priming the phosphorylated NFKBIA target at positions 'Lys-21'
and/or 'Lys-22' with a monoubiquitin. Cooperates with the
SCF(SKP2) E3 ligase complex to regulate cell proliferation through
ubiquitination and degradation of MYBL2 and KIP1. Involved in
ubiquitin conjugation and degradation of CREM isoform ICERIIgamma
and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-
mediated repression of cAMP-induced transcription during both
meiotic and mitotic cell cycles. Involved in the regulation of the
cell cycle G2/M phase through its targeting of the WEE1 kinase for
ubiquitination and degradation. Also involved in the degradation
of beta-catenin. {ECO:0000250|UniProtKB:P49427,
ECO:0000269|PubMed:10230406}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine.
{ECO:0000250|UniProtKB:P49427, ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-
activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:P49427}.
-!- ENZYME REGULATION: CDC34-catalyzed polyubiquitin chain assembly
activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF
E3 ligase complex subunit. {ECO:0000250|UniProtKB:P49427}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3
ubiquitin ligase complex together with HINT1 and RBX1. When cullin
is neddylated, the interaction between the E2 and the SCF complex
is strengthened (By similarity). When phosphorylated, interacts
with beta-TrCP (BTRC) (By similarity). Interacts with casein
kinase subunit CSNK2B. {ECO:0000250|UniProtKB:P49427}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49427}.
Nucleus {ECO:0000250|UniProtKB:P49427}. Note=The phosphorylation
of the C-terminal tail plays an important role in mediating
nuclear localization. Colocalizes with beta-tubulin on mitotic
spindles in anaphase. {ECO:0000250|UniProtKB:P49427}.
-!- DOMAIN: The C-terminal acidic tail is required for nuclear
localization and is involved in the binding to SCF E3 ligase
complexes, and more specifically with the CUL1 subunit.
{ECO:0000250|UniProtKB:P49427}.
-!- PTM: Phosphorylated by CK2. Phosphorylation of the C-terminal tail
by CK2 controles the nuclear localization.
{ECO:0000250|UniProtKB:P49427}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; BC039160; AAH39160.1; -; mRNA.
EMBL; BC094502; AAH94502.1; -; mRNA.
CCDS; CCDS23983.1; -.
RefSeq; NP_808281.1; NM_177613.2.
RefSeq; XP_017169376.1; XM_017313887.1.
RefSeq; XP_017169377.1; XM_017313888.1.
UniGene; Mm.21981; -.
ProteinModelPortal; Q8CFI2; -.
SMR; Q8CFI2; -.
BioGrid; 229706; 4.
IntAct; Q8CFI2; 3.
STRING; 10090.ENSMUSP00000020550; -.
iPTMnet; Q8CFI2; -.
PhosphoSitePlus; Q8CFI2; -.
EPD; Q8CFI2; -.
MaxQB; Q8CFI2; -.
PaxDb; Q8CFI2; -.
PeptideAtlas; Q8CFI2; -.
PRIDE; Q8CFI2; -.
DNASU; 216150; -.
Ensembl; ENSMUST00000020550; ENSMUSP00000020550; ENSMUSG00000020307.
Ensembl; ENSMUST00000166603; ENSMUSP00000128806; ENSMUSG00000020307.
GeneID; 216150; -.
KEGG; mmu:216150; -.
UCSC; uc007fzi.1; mouse.
CTD; 997; -.
MGI; MGI:102657; Cdc34.
eggNOG; KOG0425; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00730000110436; -.
HOGENOM; HOG000233454; -.
HOVERGEN; HBG063308; -.
InParanoid; Q8CFI2; -.
KO; K02207; -.
OMA; CVKTKTP; -.
OrthoDB; EOG091G0O9F; -.
PhylomeDB; Q8CFI2; -.
TreeFam; TF101107; -.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Cdc34; mouse.
PRO; PR:Q8CFI2; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020307; -.
CleanEx; MM_CDC34; -.
ExpressionAtlas; Q8CFI2; baseline and differential.
Genevisible; Q8CFI2; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISO:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Complete proteome; Cytoplasm;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation pathway.
CHAIN 1 235 Ubiquitin-conjugating enzyme E2 R1.
/FTId=PRO_0000082452.
REGION 190 235 SCF-binding.
{ECO:0000250|UniProtKB:P49427}.
COMPBIAS 200 235 Asp/Glu-rich (acidic).
ACT_SITE 93 93 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
MOD_RES 203 203 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P49427}.
MOD_RES 221 221 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P49427}.
MOD_RES 230 230 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P49427}.
MOD_RES 232 232 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:P49427}.
MOD_RES 235 235 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P49427}.
SEQUENCE 235 AA; 26622 MW; 3259FA0CD407E1E3 CRC64;
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA
RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV
RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG
VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEAD SCFGDEEDDS GTEES


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