PRAM1

PRAM1
Identifiers
Aliases	PRAM1 , PML-RAR, PRAM-1, PML-RARA regulated adaptor molecule 1
External IDs	OMIM: 606466; MGI: 3576625; HomoloGene: 12963; GeneCards: PRAM1; OMA:PRAM1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19p13.2 Start 8,490,056 bp [1] End 8,502,640 bp [1]
Gene location (Mouse) Chr. Chromosome 17 (mouse) [2] Band 17|17 B1 Start 33,857,030 bp [2] End 33,864,680 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte blood bone marrow cells trabecular bone spleen C1 segment upper lobe of left lung right lung appendix Top expressed in granulocyte bone marrow neural layer of retina cerebellar cortex morula primary oocyte embryo hypothalamus spermatocyte blastocyst More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding lipid binding protein kinase binding Cellular component protein-containing complex plasma membrane Biological process signal transduction integrin-mediated signaling pathway regulation of neutrophil degranulation T cell receptor signaling pathway protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84106 378460 Ensembl ENSG00000133246 ENSMUSG00000032739 UniProt Q96QH2 Q6BCL1 RefSeq (mRNA) NM_032152 NM_001002842 RefSeq (protein) NP_115528 NP_001002842 Location (UCSC) Chr 19: 8.49 – 8.5 Mb Chr 17: 33.86 – 33.86 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

PML-RARA-regulated adapter molecule 1 is a protein that in humans is encoded by the PRAM1 gene. ^{[5] [6] [7]}

Function

The protein encoded by this gene is similar to FYN binding protein (FYB/SLAP-130), which is an adaptor protein involved in T cell receptor mediated signaling. This gene is expressed and regulated during normal myelopoiesis. The expression of this gene is induced by retinoic acid and is inhibited by the expression of PML-RARalpha, a fusion protein of promyelocytic leukemia (PML) and the retinoic acid receptor-alpha (RARalpha). ^[7]

Interactions

PRAM1 has been shown to interact with TRIM27. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000133246 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032739 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Moog-Lutz C, Peterson EJ, Lutz PG, Eliason S, Cavé-Riant F, Singer A, Di Gioia Y, Dmowski S, Kamens J, Cayre YE, Koretzky G (Jun 2001). "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells". J Biol Chem. 276 (25): 22375–81. doi: 10.1074/jbc.M011683200 . PMID   11301322.
6. Clemens RA, Newbrough SA, Chung EY, Gheith S, Singer AL, Koretzky GA, Peterson EJ (Dec 2004). "PRAM-1 Is Required for Optimal Integrin-Dependent Neutrophil Function". Mol Cell Biol. 24 (24): 10923–32. doi:10.1128/MCB.24.24.10923-10932.2004. PMC   533979 . PMID   15572693.
7. "Entrez Gene: PRAM1 PML-RARA regulated adaptor molecule 1".
8. Cao T, Duprez E, Borden KL, Freemont PS, Etkin LD (May 1998). "Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML". J. Cell Sci. 111 (10): 1319–29. doi:10.1242/jcs.111.10.1319. PMID   9570750.

Further reading

• Boddy MN, Howe K, Etkin LD, Solomon E, Freemont PS (1996). "PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia". Oncogene. 13 (5): 971–82. PMID   8806687.
• Cao T, Duprez E, Borden KL, Freemont PS, Etkin LD (1998). "Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML". J. Cell Sci. 111 (10): 1319–29. doi:10.1242/jcs.111.10.1319. PMID   9570750.
• Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S (2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Mol. Cell. 7 (6): 1233–43. doi: 10.1016/S1097-2765(01)00257-X . PMID   11430826.
• Denis FM, Benecke A, Di Gioia Y, Touw IP, Cayre YE, Lutz PG (2005). "PRAM-1 potentiates arsenic trioxide-induced JNK activation" (PDF). J. Biol. Chem. 280 (10): 9043–8. doi: 10.1074/jbc.M413564200 . PMID   15637062. Archived from the original (PDF) on August 6, 2024.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Rossi V, Levati L, Biondi A (2006). "Diagnosis and monitoring of PML-RARA-positive acute promyelocytic leukemia by qualitative RT-PCR". Methods Mol. Med. 125: 115–26. doi:10.1385/1-59745-017-0:115. ISBN   1-59745-017-0. PMID   16502581.
• Mokany E, Todd AV, Fuery CJ, Applegate TL (2006). "Diagnosis and monitoring of PML-RARalpha-positive acute promyelocytic leukemia by quantitative RT-PCR". Methods Mol. Med. 125: 127–47. doi:10.1385/1-59745-017-0:127. ISBN   1-59745-017-0. PMID   16502582.
• Heuer K, Sylvester M, Kliche S, Pusch R, Thiemke K, Schraven B, Freund C (2006). "Lipid-binding hSH3 domains in immune cell adapter proteins". J. Mol. Biol. 361 (1): 94–104. doi:10.1016/j.jmb.2006.06.004. PMID   16831444.