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Database: UniProt
Entry: Q3MHP1
LinkDB: Q3MHP1
Original site: Q3MHP1 
ID   UB2L3_BOVIN             Reviewed;         154 AA.
AC   Q3MHP1; Q1JPH3;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   19-FEB-2014, entry version 70.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 L3;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin carrier protein L3;
DE   AltName: Full=Ubiquitin-protein ligase L3;
GN   Name=UBE2L3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-154.
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Ubiquitin-conjugating enzyme E2 that specifically acts
CC       with HECT-type and RBR family E3 ubiquitin-protein ligases. Does
CC       not function with most RING-containing E3 ubiquitin-protein
CC       ligases because it lacks intrinsic E3-independent reactivity with
CC       lysine: in contrast, it has activity with the RBR family E3
CC       enzymes, such as PARK2 and ARIH1, that function like function like
CC       RING-HECT hybrids. Accepts ubiquitin from the E1 complex and
CC       catalyzes its covalent attachment to other proteins. In vitro
CC       catalyzes 'Lys-11'-linked polyubiquitination. Involved in the
CC       selective degradation of short-lived and abnormal proteins. Down-
CC       regulated during the S-phase it is involved in progression through
CC       the cell cycle. Regulates nuclear hormone receptors
CC       transcriptional activity. May play a role in myelopoiesis (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 PARK2; involved in ubiquitination and
CC       degradation of misfolded proteins. Interacts with UBE3A. Interacts
CC       with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts
CC       with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with
CC       NCOA1; they functionally interact to regulate progesterone
CC       receptor transcriptional activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- DOMAIN: In contrast to other ubiquitin-conjugating enzymes E2,
CC       residues essential for lysine reactivity are absent: Pro and a His
CC       residues are present instead of an Asp and an Asp residues in
CC       positions 88 and 119,respectively (By similarity).
CC   -!- PTM: Ubiquitinated. The alteration of UBE2L3 protein levels during
CC       the S-phase of the cell cycle is due to ubiquitin-dependent
CC       proteasomal degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; BC105164; AAI05165.1; -; mRNA.
DR   EMBL; BT025380; ABF57336.1; -; mRNA.
DR   RefSeq; NP_001071562.1; NM_001078094.1.
DR   UniGene; Bt.34832; -.
DR   ProteinModelPortal; Q3MHP1; -.
DR   SMR; Q3MHP1; 4-147.
DR   PRIDE; Q3MHP1; -.
DR   GeneID; 767894; -.
DR   KEGG; bta:767894; -.
DR   CTD; 7332; -.
DR   eggNOG; COG5078; -.
DR   HOGENOM; HOG000233455; -.
DR   HOVERGEN; HBG063308; -.
DR   InParanoid; Q3MHP1; -.
DR   KO; K04552; -.
DR   UniPathway; UPA00143; -.
DR   NextBio; 20918251; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Ligase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    154       Ubiquitin-conjugating enzyme E2 L3.
FT                                /FTId=PRO_0000245037.
FT   ACT_SITE     86     86       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES       9      9       N6-acetyllysine (By similarity).
FT   MOD_RES     131    131       N6-acetyllysine (By similarity).
FT   MOD_RES     138    138       N6-acetyllysine (By similarity).
SQ   SEQUENCE   154 AA;  17862 MW;  F5A30243BE3C9985 CRC64;
     MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE
     YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP
     LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD
//
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