Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);FUNCTION;TISSUE SPECIFICITY
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2);FUNCTION;TISSUE SPECIFICITY;INDUCTION
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2);FUNCTION;TISSUE SPECIFICITY;INDUCTION
4.
"Full-length cDNA libraries and normalization." Li W.B.
,
Gruber C.
,
Jessee J.
,
Polayes D.
Submitted (2003-04) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: PROTEIN SEQUENCE OF 2-10; 62-72; 79-97 AND 166-186;FUNCTION;IDENTIFICATION BY MASS SPECTROMETRY;INTERACTION WITH RNF138
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Cited for: PROTEIN SEQUENCE OF 2-8; 56-72 AND 177-186;CLEAVAGE OF INITIATOR METHIONINE;ACETYLATION AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: FUNCTION IN DEGRADATION OF MHC CLASS I HEAVY CHAINS
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Cited for: FUNCTION IN POLYUBIQUITINATION;INTERACTION WITH BRCA1
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS)
22.
"A novel and unexpected complex between the SUMO-1-conjugating enzyme UBC9 and the ubiquitin-conjugating enzyme E2-25 kDA." Structural genomics consortium (SGC)
Submitted (2009-02) to the PDB data bank
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Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE2I
23.
"Ubiquitin-conjugating enzyme E2-25 kDA (Huntington-interacting protein 2)." Structural genomics consortium (SGC)
Submitted (2009-02) to the PDB data bank
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Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Vaild Sequence:
