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| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Lysine-specific demethylase 5B
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| http://www.biopax.org/relea... |
KDM5B_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
1.14.11.-,
CT31,
Cancer/testis antigen 31,
Histone demethylase JARID1B,
Jumonji/ARID domain-containing protein 1B,
PLU-1,
RBP2-H1,
Retinoblastoma-binding protein 2 homolog 1
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| http://www.biopax.org/relea... |
FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). SUBUNIT: Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7 (By similarity). SUBCELLULAR LOCATION: Nucleus. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UGL1-1; Sequence=Displayed; Name=2; IsoId=Q9UGL1-2; Sequence=VSP_026408; TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level). DOMAIN: Both the JmjC domain and the JmjN domain are required for enzymatic activity. DOMAIN: The 2 first PHD-type zinc finger domains are required for transcription repression activity. SIMILARITY: Belongs to the JARID1 histone demethylase family. SIMILARITY: Contains 1 ARID domain. SIMILARITY: Contains 1 JmjC domain. SIMILARITY: Contains 1 JmjN domain. SIMILARITY: Contains 3 PHD-type zinc fingers. SEQUENCE CAUTION: Sequence=CAB63108.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; GENE SYNONYMS: JARID1B PLU1 RBBP2H1. 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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