ID   UB2R1_MOUSE             Reviewed;         235 AA.
AC   Q8CFI2; Q505K8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 R1;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase R1;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-32 kDa complementing;
DE   AltName: Full=E2-CDC34;
GN   Name=Cdc34; Synonyms=Ube2r1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129, and C57BL/6J; TISSUE=Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. May be involved in degradation of katenin (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC       ligase complex. When phosphorylated, interacts with beta-TrCP
CC       (BTRC) (By similarity).
CC   -!- INTERACTION:
CC       P62137:Ppp1ca; NbExp=1; IntAct=EBI-1202331, EBI-357187;
CC       P63087-1:Ppp1cc; NbExp=1; IntAct=EBI-1202331, EBI-450267;
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC039160; AAH39160.1; -; mRNA.
DR   EMBL; BC094502; AAH94502.1; -; mRNA.
DR   RefSeq; NP_808281.1; -.
DR   RefSeq; XP_001478177.1; -.
DR   UniGene; Mm.21981; -.
DR   HSSP; P34477; 1PZV.
DR   SMR; Q8CFI2; 9-181.
DR   IntAct; Q8CFI2; -.
DR   Ensembl; ENSMUSG00000020307; Mus musculus.
DR   GeneID; 100046898; -.
DR   GeneID; 216150; -.
DR   KEGG; mmu:100046898; -.
DR   KEGG; mmu:216150; -.
DR   MGI; MGI:102657; Cdc34.
DR   HOGENOM; Q8CFI2; -.
DR   HOVERGEN; Q8CFI2; -.
DR   NextBio; 460338; -.
DR   ArrayExpress; Q8CFI2; -.
DR   CleanEx; MM_CDC34; -.
DR   GermOnline; ENSMUSG00000020307; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   PANTHER; PTHR11621; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   Ligase; Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1    235       Ubiquitin-conjugating enzyme E2 R1.
FT                                /FTId=PRO_0000082452.
FT   COMPBIAS    200    235       Asp/Glu-rich (acidic).
FT   ACT_SITE     93     93       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     230    230       Phosphoserine; by CK2 (By similarity).
SQ   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
//