PHB2

Prohibitin-2 is a protein that in humans is encoded by the PHB2 gene.[5][6][7]

PHB2
Identifiers
Aliases	PHB2, BAP, BCAP37, Bap37, PNAS-141, REA, p22, hBAP, prohibitin 2, Prohibitin-2
External IDs	OMIM: 610704 MGI: 102520 HomoloGene: 5263 GeneCards: PHB2
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12p13.31 Start 6,965,327 bp[1] End 6,970,753 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 F2|6 59.17 cM Start 124,712,336 bp[2] End 124,716,950 bp[2]
Gene ontology Molecular function • protein N-terminus binding • amide binding • protein C-terminus binding • GO:0001948 protein binding • estrogen receptor binding • sphingolipid binding Cellular component • cytoplasm • membrane • nuclear matrix • cell surface • mitochondrial outer membrane • mitochondrion • extracellular exosome • cell nucleus • cell periphery • mitochondrial inner membrane • axon • GO:0097483, GO:0097481 postsynaptic density • macromolecular complex • presynaptic active zone • glutamatergic synapse • GABA-ergic synapse Biological process • regulation of transcription, DNA-templated • mammary gland branching involved in thelarche • protein stabilization • regulation of branching involved in mammary gland duct morphogenesis • mitochondrion organization • negative regulation of mammary gland epithelial cell proliferation • positive regulation of sequence-specific DNA binding transcription factor activity • positive regulation of exit from mitosis • mammary gland alveolus development • negative regulation of sequence-specific DNA binding transcription factor activity • transcription, DNA-templated • sister chromatid cohesion • positive regulation of cell cycle G1/S phase transition • positive regulation of ERK1 and ERK2 cascade • negative regulation of transcription, DNA-templated • negative regulation of intracellular estrogen receptor signaling pathway • regulation of complement activation • mitochondrial calcium ion transmembrane transport • response to wounding • negative regulation of apoptotic process • cellular response to retinoic acid • cellular response to hypoxia • protein import into nucleus • regulation of cytochrome-c oxidase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11331	12034
Ensembl	ENSG00000215021	ENSMUSG00000004264
UniProt	Q99623	O35129
RefSeq (mRNA)	NM_001144831 NM_001267700	NM_007531
RefSeq (protein)	NP_001138303 NP_001254629	NP_031557
Location (UCSC)	Chr 12: 6.97 – 6.97 Mb	Chr 6: 124.71 – 124.72 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

PHB2 has been shown to interact with PTMA.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000215021 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004264 - 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. Coates PJ, Nenutil R, McGregor A, Picksley SM, Crouch DH, Hall PA, Wright EG (Apr 2001). "Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence". Exp Cell Res. 265 (2): 262–73. doi:10.1006/excr.2001.5166. PMID 11302691.
6. Coates PJ, Jamieson DJ, Smart K, Prescott AR, Hall PA (Oct 1997). "The prohibitin family of mitochondrial proteins regulate replicative lifespan". Curr Biol. 7 (8): 607–10. doi:10.1016/S0960-9822(06)00261-2. PMID 9259555.
7. "Entrez Gene: PHB2 prohibitin 2".
8. Martini, Paolo G V; Katzenellenbogen Benita S (Jun 2003). "Modulation of estrogen receptor activity by selective coregulators". J. Steroid Biochem. Mol. Biol. 85 (2–5): 117–22. doi:10.1016/S0960-0760(03)00207-3. ISSN 0960-0760. PMID 12943695.

Further reading

• Martini PG, Katzenellenbogen BS (2003). "Modulation of estrogen receptor activity by selective coregulators". J. Steroid Biochem. Mol. Biol. 85 (2–5): 117–22. doi:10.1016/S0960-0760(03)00207-3. PMID 12943695.
• Ansari-Lari MA, Muzny DM, Lu J, et al. (1996). "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13". Genome Res. 6 (4): 314–26. doi:10.1101/gr.6.4.314. PMID 8723724.
• Ansari-Lari MA, Shen Y, Muzny DM, et al. (1997). "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination". Genome Res. 7 (3): 268–80. doi:10.1101/gr.7.3.268. PMID 9074930.
• Montano MM, Ekena K, Delage-Mourroux R, et al. (1999). "An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens". Proc. Natl. Acad. Sci. U.S.A. 96 (12): 6947–52. Bibcode:1999PNAS...96.6947M. doi:10.1073/pnas.96.12.6947. PMC 22022. PMID 10359819.
• Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
• Martini PG, Delage-Mourroux R, Kraichely DM, Katzenellenbogen BS (2000). "Prothymosin Alpha Selectively Enhances Estrogen Receptor Transcriptional Activity by Interacting with a Repressor of Estrogen Receptor Activity". Mol. Cell. Biol. 20 (17): 6224–32. doi:10.1128/MCB.20.17.6224-6232.2000. PMC 86097. PMID 10938099.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
• Kurtev V, Margueron R, Kroboth K, et al. (2004). "Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases". J. Biol. Chem. 279 (23): 24834–43. doi:10.1074/jbc.M312300200. PMID 15140878.
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Rual JF, Venkatesan K, Hao T, et al. (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.
• Scherer SE, Muzny DM, Buhay CJ, et al. (2006). "The finished DNA sequence of human chromosome 12". Nature. 440 (7082): 346–51. Bibcode:2006Natur.440..346S. doi:10.1038/nature04569. PMID 16541075.
• Kasashima K, Ohta E, Kagawa Y, Endo H (2007). "Mitochondrial functions and estrogen receptor-dependent nuclear translocation of pleiotropic human prohibitin 2". J. Biol. Chem. 281 (47): 36401–10. doi:10.1074/jbc.M605260200. PMID 17008324.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Takata H, Matsunaga S, Morimoto A, et al. (2007). "PHB2 protects sister-chromatid cohesion in mitosis". Curr. Biol. 17 (15): 1356–61. doi:10.1016/j.cub.2007.07.009. PMID 17656096.