Prohibitin

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• complement component C3a binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Prohibitin binds to C3 and enhances complement activation."
    Mishra S., Moulik S., Murphy L.J.
    Mol Immunol 44:1897-1902(2007) [PubMed] [Europe PMC] [Abstract]
• complement component C3b binding Source: UniProtKBInferred from direct assayⁱ
  • "Prohibitin binds to C3 and enhances complement activation."
    Mishra S., Moulik S., Murphy L.J.
    Mol Immunol 44:1897-1902(2007) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
• histone deacetylase binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Prohibitin, a protein downregulated by androgens, represses androgen receptor activity."
    Gamble S.C., Chotai D., Odontiadis M., Dart D.A., Brooke G.N., Powell S.M., Reebye V., Varela-Carver A., Kawano Y., Waxman J., Bevan C.L.
    Oncogene 26:1757-1768(2007) [PubMed] [Europe PMC] [Abstract]
• proteinase activated receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Prohibitin is involved in the activated internalization and degradation of protease-activated receptor 1."
    Wang Y.J., Guo X.L., Li S.A., Zhao Y.Q., Liu Z.C., Lee W.H., Xiang Y., Zhang Y.
    Biochim Biophys Acta 1843:1393-1401(2014) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.13

    "Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein."
    Emerson V., Holtkotte D., Pfeiffer T., Wang I.H., Schnoelzer M., Kempf T., Bosch V.
    J. Virol. 84:1355-1365(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 ENVELOPE GLYCOPROTEIN GP160.
• protein heterodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.21

    "Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor."
    Wei Y., Chiang W.C., Sumpter R. Jr., Mishra P., Levine B.
    Cell 168:224.e10-238.e10(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH PHB2 AND MAP1LC3B.
• transcription corepressor activity Source: BHF-UCLInferred from direct assayⁱ
  • "Prohibitin and the SWI/SNF ATPase subunit BRG1 are required for effective androgen antagonist-mediated transcriptional repression of androgen receptor-regulated genes."
    Dai Y., Ngo D., Jacob J., Forman L.W., Faller D.V.
    Carcinogenesis 29:1725-1733(2008) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• activation of phospholipase C activity Source: UniProtKB
• activation of protein kinase C activity Source: UniProtKB
• animal organ regeneration Source: Ensembl
• antiviral innate immune response Source: UniProtKBInferred from direct assayⁱ
  • Ref.22

    "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region."
    Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O., Tamada T., Koshiba T.
    IScience 19:1065-1078(2019) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH PHB2 AND CLPB, FUNCTION.
• B cell activation Source: UniProtKB
• CD40 signaling pathway Source: UniProtKB
• cellular response to interleukin-6 Source: BHF-UCLInferred from direct assayⁱ
  • "Interleukin-6 transcriptionally regulates prohibitin expression in intestinal epithelial cells."
    Theiss A.L., Obertone T.S., Merlin D., Sitaraman S.V.
    J Biol Chem 282:12804-12812(2007) [PubMed] [Europe PMC] [Abstract]
• DNA biosynthetic process Source: UniProtKB-KW
• histone deacetylation Source: UniProtKBInferred from direct assayⁱ
  • "Prohibitin co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression."
    Wang S., Fusaro G., Padmanabhan J., Chellappan S.P.
    Oncogene 21:8388-8396(2002) [PubMed] [Europe PMC] [Abstract]
• mitochondrial calcium ion transmembrane transport Source: Reactome
• mitochondrion organization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Mitochondrial functions and estrogen receptor-dependent nuclear translocation of pleiotropic human prohibitin 2."
    Kasashima K., Ohta E., Kagawa Y., Endo H.
    J Biol Chem 281:36401-36410(2006) [PubMed] [Europe PMC] [Abstract]
• modulation by host of viral RNA genome replication Source: UniProtKB
• negative regulation of androgen receptor signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Prohibitin, a protein downregulated by androgens, represses androgen receptor activity."
    Gamble S.C., Chotai D., Odontiadis M., Dart D.A., Brooke G.N., Powell S.M., Reebye V., Varela-Carver A., Kawano Y., Waxman J., Bevan C.L.
    Oncogene 26:1757-1768(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: Ensembl
• negative regulation of cell growth Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth."
    Wang S., Zhang B., Faller D.V.
    EMBO J 21:3019-3028(2002) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell population proliferation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Prohibitin and the SWI/SNF ATPase subunit BRG1 are required for effective androgen antagonist-mediated transcriptional repression of androgen receptor-regulated genes."
    Dai Y., Ngo D., Jacob J., Forman L.W., Faller D.V.
    Carcinogenesis 29:1725-1733(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of ERK1 and ERK2 cascade Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Prohibitin is involved in the activated internalization and degradation of protease-activated receptor 1."
    Wang Y.J., Guo X.L., Li S.A., Zhao Y.Q., Liu Z.C., Lee W.H., Xiang Y., Zhang Y.
    Biochim Biophys Acta 1843:1393-1401(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of glucocorticoid receptor signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Prohibitin, a protein downregulated by androgens, represses androgen receptor activity."
    Gamble S.C., Chotai D., Odontiadis M., Dart D.A., Brooke G.N., Powell S.M., Reebye V., Varela-Carver A., Kawano Y., Waxman J., Bevan C.L.
    Oncogene 26:1757-1768(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein catabolic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Prohibitin is involved in the activated internalization and degradation of protease-activated receptor 1."
    Wang Y.J., Guo X.L., Li S.A., Zhao Y.Q., Liu Z.C., Lee W.H., Xiang Y., Zhang Y.
    Biochim Biophys Acta 1843:1393-1401(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • "Radon: a possible risk factor in multiple sclerosis."
    Bolviken B., Celius E.G., Nilsen R., Strand T.
    Neuroepidemiology 22:87-94(2003) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by competitive promoter binding Source: BHF-UCLInferred from direct assayⁱ
  • "Prohibitin and the SWI/SNF ATPase subunit BRG1 are required for effective androgen antagonist-mediated transcriptional repression of androgen receptor-regulated genes."
    Dai Y., Ngo D., Jacob J., Forman L.W., Faller D.V.
    Carcinogenesis 29:1725-1733(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by RNA polymerase II Source: BHF-UCLInferred from direct assayⁱ
  • "Prohibitin, a protein downregulated by androgens, represses androgen receptor activity."
    Gamble S.C., Chotai D., Odontiadis M., Dart D.A., Brooke G.N., Powell S.M., Reebye V., Varela-Carver A., Kawano Y., Waxman J., Bevan C.L.
    Oncogene 26:1757-1768(2007) [PubMed] [Europe PMC] [Abstract]
• osteoblast differentiation Source: UniProtKBInferred from high throughput direct assayⁱ
  • "Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation."
    Foster L.J., Zeemann P.A., Li C., Mann M., Jensen O.N., Kassem M.
    Stem Cells 23:1367-1377(2005) [PubMed] [Europe PMC] [Abstract]
• ovarian follicle atresia Source: Ensembl
• ovarian follicle development Source: Ensembl
• positive regulation of cell death Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy."
    Zhou Z.D., Xie S.P., Sathiyamoorthy S., Saw W.T., Sing T.Y., Ng S.H., Chua H.P., Tang A.M., Shaffra F., Li Z., Wang H., Ho P.G., Lai M.K., Angeles D.C., Lim T.M., Tan E.K.
    Hum Mol Genet 24:6314-6330(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of complement activation Source: UniProtKBInferred from direct assayⁱ
  • "Prohibitin binds to C3 and enhances complement activation."
    Mishra S., Moulik S., Murphy L.J.
    Mol Immunol 44:1897-1902(2007) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ERK1 and ERK2 cascade Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Expression of prohibitins on the surface of activated T cells."
    Yurugi H., Tanida S., Ishida A., Akita K., Toda M., Inoue M., Nakada H.
    Biochem Biophys Res Commun 420:275-280(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of gene expression Source: ParkinsonsUK-UCLInferred from genetic interactionⁱ
  • "F-box protein 7 mutations promote protein aggregation in mitochondria and inhibit mitophagy."
    Zhou Z.D., Xie S.P., Sathiyamoorthy S., Saw W.T., Sing T.Y., Ng S.H., Chua H.P., Tang A.M., Shaffra F., Li Z., Wang H., Ho P.G., Lai M.K., Angeles D.C., Lim T.M., Tan E.K.
    Hum Mol Genet 24:6314-6330(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of G protein-coupled receptor signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Prohibitin is involved in the activated internalization and degradation of protease-activated receptor 1."
    Wang Y.J., Guo X.L., Li S.A., Zhao Y.Q., Liu Z.C., Lee W.H., Xiang Y., Zhang Y.
    Biochim Biophys Acta 1843:1393-1401(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of immunoglobulin production Source: UniProtKB
• positive regulation of interleukin-17 production Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.23

    "Prohibitin 1 interacts with signal transducer and activator of transcription 3 in T-helper 17 cells."
    Zhang J., Sun Z., Wu Q., Shen J.
    Immunol. Lett. 219:8-14(2020) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3, DEVELOPMENTAL STAGE.
• positive regulation of NIK/NF-kappaB signaling Source: UniProtKB
• positive regulation of protein kinase B signaling Source: UniProtKB
• positive regulation of smooth muscle cell proliferation Source: UniProtKB
• positive regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling."
    Fusaro G., Dasgupta P., Rastogi S., Joshi B., Chellappan S.
    J. Biol. Chem. 278:47853-47861(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• progesterone receptor signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Prohibitin, a protein downregulated by androgens, represses androgen receptor activity."
    Gamble S.C., Chotai D., Odontiadis M., Dart D.A., Brooke G.N., Powell S.M., Reebye V., Varela-Carver A., Kawano Y., Waxman J., Bevan C.L.
    Oncogene 26:1757-1768(2007) [PubMed] [Europe PMC] [Abstract]
• protein stabilization Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Mitochondrial functions and estrogen receptor-dependent nuclear translocation of pleiotropic human prohibitin 2."
    Kasashima K., Ohta E., Kagawa Y., Endo H.
    J Biol Chem 281:36401-36410(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of apoptotic process Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis."
    Bruneel A., Labas V., Mailloux A., Sharma S., Royer N., Vinh J., Pernet P., Vaubourdolle M., Baudin B.
    Proteomics 5:3876-3884(2005) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling."
    Fusaro G., Dasgupta P., Rastogi S., Joshi B., Chellappan S.
    J. Biol. Chem. 278:47853-47861(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• response to drug Source: Ensembl
• response to ethanol Source: Ensembl
• response to immobilization stress Source: Ensembl
• response to peptide hormone Source: Ensembl
• RIG-I signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • Ref.22

    "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region."
    Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O., Tamada T., Koshiba T.
    IScience 19:1065-1078(2019) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH PHB2 AND CLPB, FUNCTION.
• signal transduction Source: UniProtKBTraceable author statementⁱ
  • "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis."
    Bruneel A., Labas V., Mailloux A., Sharma S., Royer N., Vinh J., Pernet P., Vaubourdolle M., Baudin B.
    Proteomics 5:3876-3884(2005) [PubMed] [Europe PMC] [Abstract]
• T-helper 17 type immune response Source: UniProtKBInferred from direct assayⁱ
  • Ref.23

    "Prohibitin 1 interacts with signal transducer and activator of transcription 3 in T-helper 17 cells."
    Zhang J., Sun Z., Wu Q., Shen J.
    Immunol. Lett. 219:8-14(2020) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3, DEVELOPMENTAL STAGE.
• viral entry into host cell Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• complement component C3a binding Source: UniProtKBInferred from direct assayⁱ
  • "Prohibitin binds to C3 and enhances complement activation."
    Mishra S., Moulik S., Murphy L.J.
    Mol Immunol 44:1897-1902(2007) [PubMed] [Europe PMC] [Abstract]
• complement component C3b binding Source: UniProtKBInferred from direct assayⁱ
  • "Prohibitin binds to C3 and enhances complement activation."
    Mishra S., Moulik S., Murphy L.J.
    Mol Immunol 44:1897-1902(2007) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
• histone deacetylase binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Prohibitin, a protein downregulated by androgens, represses androgen receptor activity."
    Gamble S.C., Chotai D., Odontiadis M., Dart D.A., Brooke G.N., Powell S.M., Reebye V., Varela-Carver A., Kawano Y., Waxman J., Bevan C.L.
    Oncogene 26:1757-1768(2007) [PubMed] [Europe PMC] [Abstract]
• proteinase activated receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Prohibitin is involved in the activated internalization and degradation of protease-activated receptor 1."
    Wang Y.J., Guo X.L., Li S.A., Zhao Y.Q., Liu Z.C., Lee W.H., Xiang Y., Zhang Y.
    Biochim Biophys Acta 1843:1393-1401(2014) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.13

    "Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein."
    Emerson V., Holtkotte D., Pfeiffer T., Wang I.H., Schnoelzer M., Kempf T., Bosch V.
    J. Virol. 84:1355-1365(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 ENVELOPE GLYCOPROTEIN GP160.
• protein heterodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.21

    "Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor."
    Wei Y., Chiang W.C., Sumpter R. Jr., Mishra P., Levine B.
    Cell 168:224.e10-238.e10(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH PHB2 AND MAP1LC3B.

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Coiled coil

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV 
        60         70         80         90        100
GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA 
       110        120        130        140        150
SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV 
       160        170        180        190        200
SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV 
       210        220        230        240        250
EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ 
       260        270 
LSRSRNITYL PAGQSVLLQL PQ                               

        10         20         30         40         50
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV 
        60         70         80         90        100
GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA 
       110        120        130        140        150
SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TYLPAGQSVL 

LQLPQ                                                  

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human chromosome 17
   Human chromosome 17: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
6. SIMILARITY comments
   Index of protein domains and families