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http://www.biopax.org/relea...
http://www.biopax.org/relea...
Golgin-45
http://www.biopax.org/relea...
GO45_HUMAN
http://www.biopax.org/relea...
http://www.biopax.org/relea...
Basic leucine zipper nuclear factor 1, JEM-1, p45 basic leucine-zipper nuclear factor
http://www.biopax.org/relea...
FUNCTION: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface. SUBUNIT: Interacts with GORASP2 and with the GTP-bound form of RAB2, but not with other Golgi Rab proteins. GORASP2 and BLZF1 form a RAB2 effector complex on medial Golgi. SUBCELLULAR LOCATION: Golgi apparatus lumen. SUBCELLULAR LOCATION: Isoform 1: Nucleus. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H2G9-1; Sequence=Displayed; Name=2; Synonyms=JEM1s; IsoId=Q9H2G9-2; Sequence=VSP_011186, VSP_011187; TISSUE SPECIFICITY: Ubiquitous. Also found in cell lines derived from several hematopoietic pathologies, such as T-cell leukemia, pro-B, pre-B, myeloma, and plasmacytoma cell lines, but not in Burkitt lymphoma cells. INDUCTION: Up-regulated by retinoids. DOMAIN: The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2. PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP- ribosylated protein is recognized by RNF146, followed by ubiquitination. PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. CAUTION: Because of the presence of a potential basic motif and leucine-zipper domain, PubMed:9129147 and PubMed:11056056 have thought that BLZF1 is a potential transcription factor. They found it localized in the nucleus, except isoform 2, which was cytoplasmic. However, homology at several typical position for basic or hydrophobic residues is missing. GENE SYNONYMS: JEM1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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