PRDM2

PRDM2
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2JV0, 2QPW
Identifiers
Aliases	PRDM2, HUMHOXY1, KMT8, MTB-ZF, RIZ, RIZ1, RIZ2, PR domain 2, PR/SET domain 2, KMT8A
External IDs	OMIM: 601196; MGI: 107628; HomoloGene: 40822; GeneCards: PRDM2; OMA:PRDM2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p36.21 Start 13,700,188 bp End 13,825,079 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 E1|4 76.84 cM Start 143,107,391 bp End 143,212,995 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve secondary oocyte buccal mucosa cell middle temporal gyrus epithelium of colon Brodmann area 46 Brodmann area 10 frontal pole bone marrow cells Brodmann area 23 Top expressed in interventricular septum spermatocyte spermatid granulocyte zygote tail of embryo genital tubercle otic vesicle muscle of thigh visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity methyltransferase activity transferase activity DNA binding zinc ion binding histone-lysine N-methyltransferase activity metal ion binding nucleic acid binding RNA polymerase II transcription regulatory region sequence-specific DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity, RNA polymerase II-specific chromatin DNA binding sequence-specific DNA binding Cellular component nucleus Golgi apparatus Biological process histone lysine methylation methylation regulation of transcription, DNA-templated determination of adult lifespan transcription, DNA-templated transcription by RNA polymerase II positive regulation of transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7799 110593 Ensembl ENSG00000116731 ENSMUSG00000057637 UniProt Q13029 n/a RefSeq (mRNA) NM_001007257 NM_001135610 NM_012231 NM_015866 NM_001393986 NM_001393987 NM_001393988 NM_001081355 NM_001256380 RefSeq (protein) NP_001007258 NP_001129082 NP_036363 NP_056950 n/a Location (UCSC) Chr 1: 13.7 – 13.83 Mb Chr 4: 143.11 – 143.21 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

PR domain zinc finger protein 2 is a protein that in humans is encoded by the PRDM2 gene.

Function

This tumor suppressor gene is a member of a nuclear histone/protein methyltransferase superfamily. It encodes a zinc finger protein that can bind to retinoblastoma protein, estrogen receptor, and the TPA-responsive element (MTE) of the heme-oxygenase-1 gene. Although the functions of this protein have not been fully characterized, it may (1) play a role in transcriptional regulation during neuronal differentiation and pathogenesis of retinoblastoma, (2) act as a transcriptional activator of the heme-oxygenase-1 gene, and (3) be a specific effector of estrogen action. Three transcript variants encoding different isoforms have been found for this gene.

Interactions

PRDM2 has been shown to interact with Estrogen receptor alpha and Retinoblastoma protein.

Further reading

• Shapiro VS, Lee P, Winoto A (Oct 1995). "Identification and cloning of the G3B cDNA encoding a 3' segment of a protein binding to GATA-3". Gene. 163 (2): 329–30. doi:10.1016/0378-1119(95)00420-B. PMID 7590293.
• Muraosa Y, Takahashi K, Yoshizawa M, Shibahara S (Feb 1996). "cDNA cloning of a novel protein containing two zinc-finger domains that may function as a transcription factor for the human heme-oxygenase-1 gene". European Journal of Biochemistry. 235 (3): 471–9. doi:10.1111/j.1432-1033.1996.00471.x. PMID 8654390.
• Buyse IM, Takahashi EI, Huang S (May 1996). "Physical mapping of the retinoblastoma interacting zinc finger gene RIZ to D1S228 on chromosome 1p36". Genomics. 34 (1): 119–21. doi:10.1006/geno.1996.0249. PMID 8661032.
• Liu L, Shao G, Steele-Perkins G, Huang S (Jan 1997). "The retinoblastoma interacting zinc finger gene RIZ produces a PR domain-lacking product through an internal promoter". The Journal of Biological Chemistry. 272 (5): 2984–91. doi:10.1074/jbc.272.5.2984. PMID 9006946.
• Xie M, Shao G, Buyse IM, Huang S (Oct 1997). "Transcriptional repression mediated by the PR domain zinc finger gene RIZ". The Journal of Biological Chemistry. 272 (42): 26360–6. doi:10.1074/jbc.272.42.26360. PMID 9334209.
• He L, Yu JX, Liu L, Buyse IM, Wang MS, Yang QC, Nakagawara A, Brodeur GM, Shi YE, Huang S (Oct 1998). "RIZ1, but not the alternative RIZ2 product of the same gene, is underexpressed in breast cancer, and forced RIZ1 expression causes G2-M cell cycle arrest and/or apoptosis". Cancer Research. 58 (19): 4238–44. PMID 9766644.
• Abbondanza C, Medici N, Nigro V, Rossi V, Gallo L, Piluso G, Belsito A, Roscigno A, Bontempo P, Puca AA, Molinari AM, Moncharmont B, Puca GA (Mar 2000). "The retinoblastoma-interacting zinc-finger protein RIZ is a downstream effector of estrogen action". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3130–5. doi:10.1073/pnas.050015697. PMC 16204. PMID 10706618.
• Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (Mar 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
• Du Y, Carling T, Fang W, Piao Z, Sheu JC, Huang S (Nov 2001). "Hypermethylation in human cancers of the RIZ1 tumor suppressor gene, a member of a histone/protein methyltransferase superfamily". Cancer Research. 61 (22): 8094–9. PMID 11719434.
• Sasaki O, Meguro K, Tohmiya Y, Funato T, Shibahara S, Sasaki T (Mar 2002). "Nucleotide alteration of retinoblastoma protein-interacting zinc finger gene, RIZ, in human leukemia". The Tohoku Journal of Experimental Medicine. 196 (3): 193–201. doi:10.1620/tjem.196.193. PMID 12002276.
• Poetsch M, Dittberner T, Woenckhaus C (May 2002). "Frameshift mutations of RIZ, but no point mutations in RIZ1 exons in malignant melanomas with deletions in 1p36". Oncogene. 21 (19): 3038–42. doi:10.1038/sj.onc.1205457. PMID 12082534. S2CID 37956595.
• Sasaki O, Meguro K, Tohmiya Y, Funato T, Shibahara S, Sasaki T (Dec 2002). "Altered expression of retinoblastoma protein-interacting zinc finger gene, RIZ, in human leukaemia". British Journal of Haematology. 119 (4): 940–8. doi:10.1046/j.1365-2141.2002.03972.x. PMID 12472571. S2CID 21560813.
• Tokumaru Y, Nomoto S, Jerónimo C, Henrique R, Harden S, Trink B, Sidransky D (Oct 2003). "Biallelic inactivation of the RIZ1 gene in human gastric cancer". Oncogene. 22 (44): 6954–8. doi:10.1038/sj.onc.1206403. PMID 14534544. S2CID 20152972.
• Kim KC, Geng L, Huang S (Nov 2003). "Inactivation of a histone methyltransferase by mutations in human cancers". Cancer Research. 63 (22): 7619–23. PMID 14633678.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Pan KF, Lu YY, Liu WG, Zhang L, You WC (Sep 2004). "Detection of frameshift mutations of RIZ in gastric cancers with microsatellite instability". World Journal of Gastroenterology. 10 (18): 2719–22. doi:10.3748/wjg.v10.i18.2719. PMC 4572200. PMID 15309726.
• Rossi M, Abbondanza C, D'Arcangelo A, Gazzerro P, Medici N, Moncharmont B, Puca GA (Nov 2004). "The Zn-finger domain of RIZ protein promotes MCF-7 cell proliferation". Cancer Letters. 215 (2): 229–37. doi:10.1016/j.canlet.2004.05.014. PMID 15488642.
• Grundberg E, Carling T, Brändström H, Huang S, Ribom EL, Ljunggren O, Mallmin H, Kindmark A (Dec 2004). "A deletion polymorphism in the RIZ gene, a female sex steroid hormone receptor coactivator, exhibits decreased response to estrogen in vitro and associates with low bone mineral density in young Swedish women". The Journal of Clinical Endocrinology and Metabolism. 89 (12): 6173–8. doi:10.1210/jc.2004-0403. PMID 15579774.

External links

• PRDM2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.