PHB1_MOUSE
ID PHB1_MOUSE Reviewed; 272 AA.
AC P67778; P24142; Q3UB75; Q5SQG4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Prohibitin 1 {ECO:0000305};
DE AltName: Full=B-cell receptor-associated protein 32;
DE Short=BAP 32;
GN Name=Phb1; Synonyms=Phb {ECO:0000312|MGI:MGI:97572};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Lymphoid tissue;
RX PubMed=8070406; DOI=10.1002/j.1460-2075.1994.tb06689.x;
RA Terashima M., Kim K.-M., Adachi T., Nielsen P.J., Reth M., Koehler G.,
RA Lamers M.C.;
RT "The IgM antigen receptor of B lymphocytes is associated with prohibitin
RT and a prohibitin-related protein.";
RL EMBO J. 13:3782-3792(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow, Heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 12-34; 94-105; 158-177; 220-239 AND 241-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH PHB2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11302691; DOI=10.1006/excr.2001.5166;
RA Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H.,
RA Hall P.A., Wright E.G.;
RT "Mammalian prohibitin proteins respond to mitochondrial stress and decrease
RT during cellular senescence.";
RL Exp. Cell Res. 265:262-273(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=20959514; DOI=10.1096/fj.10-167502;
RA Strub G.M., Paillard M., Liang J., Gomez L., Allegood J.C., Hait N.C.,
RA Maceyka M., Price M.M., Chen Q., Simpson D.C., Kordula T., Milstien S.,
RA Lesnefsky E.J., Spiegel S.;
RT "Sphingosine-1-phosphate produced by sphingosine kinase 2 in mitochondria
RT interacts with prohibitin 2 to regulate complex IV assembly and
RT respiration.";
RL FASEB J. 25:600-612(2011).
RN [10]
RP FUNCTION, INTERACTION WITH CD86, AND INDUCTION BY CD40L.
RX PubMed=23241883; DOI=10.4049/jimmunol.1201646;
RA Lucas C.R., Cordero-Nieves H.M., Erbe R.S., McAlees J.W., Bhatia S.,
RA Hodes R.J., Campbell K.S., Sanders V.M.;
RT "Prohibitins and the cytoplasmic domain of CD86 cooperate to mediate CD86
RT signaling in B lymphocytes.";
RL J. Immunol. 190:723-736(2013).
RN [11]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128; LYS-186 AND LYS-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [13]
RP FUNCTION, INTERACTION WITH PHB2, AND SUBCELLULAR LOCATION.
RX PubMed=24856930; DOI=10.1016/j.cmet.2014.04.016;
RA Richter-Dennerlein R., Korwitz A., Haag M., Tatsuta T., Dargazanli S.,
RA Baker M., Decker T., Lamkemeyer T., Rugarli E.I., Langer T.;
RT "DNAJC19, a mitochondrial cochaperone associated with cardiomyopathy, forms
RT a complex with prohibitins to regulate cardiolipin remodeling.";
RL Cell Metab. 20:158-171(2014).
RN [14]
RP FUNCTION.
RX PubMed=24947361; DOI=10.2337/db13-1807;
RA Ande S.R., Nguyen K.H., Padilla-Meier G.P., Wahida W., Nyomba B.L.,
RA Mishra S.;
RT "Prohibitin overexpression in adipocytes induces mitochondrial biogenesis,
RT leads to obesity development, and affects glucose homeostasis in a sex-
RT specific manner.";
RL Diabetes 63:3734-3741(2014).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ENTEROVIRUS 71
RP CAPSID PROTEIN VP0; PROTEIN 3CD AND PROTEASE 3C, SUBCELLULAR LOCATION, AND
RP ACTIVITY REGULATION.
RX PubMed=29324904; DOI=10.1371/journal.ppat.1006778;
RA Too I.H.K., Bonne I., Tan E.L., Chu J.J.H., Alonso S.;
RT "Prohibitin plays a critical role in Enterovirus 71 neuropathogenesis.";
RL PLoS Pathog. 14:e1006778-e1006778(2018).
RN [16]
RP FUNCTION.
RX PubMed=31819158; DOI=10.1038/s41418-019-0469-4;
RA Anderson C.J., Kahl A., Fruitman H., Qian L., Zhou P., Manfredi G.,
RA Iadecola C.;
RT "Prohibitin levels regulate OMA1 activity and turnover in neurons.";
RL Cell Death Differ. 27:1896-1906(2020).
CC -!- FUNCTION: Protein with pleiotropic attributes mediated in a cell-
CC compartment- and tissue-specific manner, which include the plasma
CC membrane-associated cell signaling functions, mitochondrial chaperone,
CC and transcriptional co-regulator of transcription factors in the
CC nucleus (PubMed:11302691, PubMed:20959514, PubMed:23241883,
CC PubMed:24856930, PubMed:29324904). Plays a role in adipose tissue and
CC glucose homeostasis in a sex-specific manner (PubMed:24947361).
CC Contributes to pulmonary vascular remodeling by accelerating
CC proliferation of pulmonary arterial smooth muscle cells (By
CC similarity). {ECO:0000250|UniProtKB:P67779,
CC ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514,
CC ECO:0000269|PubMed:23241883, ECO:0000269|PubMed:24856930,
CC ECO:0000269|PubMed:24947361, ECO:0000269|PubMed:29324904}.
CC -!- FUNCTION: In the mitochondria, together with PHB2, forms large ring
CC complexes (prohibitin complexes) in the inner mitochondrial membrane
CC (IMM) and functions as chaperone protein that stabilizes mitochondrial
CC respiratory enzymes and maintains mitochondrial integrity in the IMM,
CC which is required for mitochondrial morphogenesis, neuronal survival,
CC and normal lifespan (Probable). The prohibitin complex, with DNAJC19,
CC regulates cardiolipin remodeling and the protein turnover of OMA1 in a
CC cardiolipin-binding manner (PubMed:24856930). Regulates mitochondrial
CC respiration activity playing a role in cellular aging
CC (PubMed:11302691). The prohibitin complex plays a role of mitophagy
CC receptor involved in targeting mitochondria for autophagic degradation
CC (PubMed:31819158). Involved in mitochondrial-mediated antiviral innate
CC immunity, activates DDX58/RIG-I-mediated signal transduction and
CC production of IFNB1 and pro-inflammatory cytokine IL6 (By similarity).
CC {ECO:0000250|UniProtKB:P35232, ECO:0000269|PubMed:11302691,
CC ECO:0000269|PubMed:24856930, ECO:0000269|PubMed:31819158, ECO:0000305}.
CC -!- FUNCTION: In the nucleus, acts as a transcription coregulator, enhances
CC promoter binding by TP53, a transcription factor it activates, but
CC reduces the promoter binding by E2F1, a transcription factor it
CC represses (By similarity). Interacts with STAT3 to affect IL17
CC secretion in T-helper Th17 cells (By similarity).
CC {ECO:0000250|UniProtKB:P35232}.
CC -!- FUNCTION: In the plasma membrane, cooperates with CD86 to mediate CD86-
CC signaling in B lymphocytes that regulates the level of IgG1 produced
CC through the activation of distal signaling intermediates
CC (PubMed:23241883). Upon CD40 engagement, required to activate NF-kappa-
CC B signaling pathway via phospholipase C and protein kinase C activation
CC (PubMed:23241883). {ECO:0000269|PubMed:23241883}.
CC -!- FUNCTION: (Microbial infection) In neuronal cells, cell surface-
CC expressed PHB1 is involved in human enterovirus 71/EV-71 entry into
CC neuronal cells specifically, while membrane-bound mitochondrial PHB1
CC associates with the virus replication complex and facilitates viral
CC replication (PubMed:29324904). May serve as a receptor for EV71
CC (PubMed:29324904). {ECO:0000269|PubMed:29324904}.
CC -!- ACTIVITY REGULATION: Target of the anti-cancer drug Rocaglamide (Roc-
CC A). {ECO:0000269|PubMed:29324904}.
CC -!- SUBUNIT: Interacts with PHB2. Interacts with STOML2. Interacts with
CC CD86 (via cytoplasmic domain); the interactions increases after priming
CC with CD40 (PubMed:23241883). {ECO:0000250|UniProtKB:P35232,
CC ECO:0000269|PubMed:23241883}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human enterovirus 71/EV-
CC 71 capsid protein VP0, protein 3CD and protease 3C.
CC {ECO:0000269|PubMed:29324904}.
CC -!- INTERACTION:
CC P67778; O35129: Phb2; NbExp=3; IntAct=EBI-298507, EBI-445002;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514,
CC ECO:0000269|PubMed:29324904}. Nucleus {ECO:0000269|PubMed:20959514}.
CC Cell membrane {ECO:0000305|PubMed:29324904}. Cytoplasm
CC {ECO:0000269|PubMed:29324904}.
CC -!- TISSUE SPECIFICITY: Widely expressed in different tissues.
CC {ECO:0000269|PubMed:8070406}.
CC -!- DEVELOPMENTAL STAGE: Throughout gestation, highly expressed in brown
CC fat, heart, liver, developing renal tubules and neurons, and detected
CC at lower levels in tissues such as lung and exocrine pancreas.
CC {ECO:0000269|PubMed:11302691}.
CC -!- INDUCTION: In B cells, expression is increased by CD40 engagement (at
CC protein level). {ECO:0000269|PubMed:23241883}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR EMBL; X78682; CAA55349.1; -; mRNA.
DR EMBL; AK002714; BAB22305.1; -; mRNA.
DR EMBL; AK010619; BAB27067.1; -; mRNA.
DR EMBL; AK150956; BAE29988.1; -; mRNA.
DR EMBL; AK151073; BAE30089.1; -; mRNA.
DR EMBL; AK168248; BAE40198.1; -; mRNA.
DR EMBL; AK168656; BAE40512.1; -; mRNA.
DR EMBL; AL732490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083354; AAH83354.1; -; mRNA.
DR EMBL; BC089034; AAH89034.1; -; mRNA.
DR CCDS; CCDS25280.1; -.
DR RefSeq; NP_032857.1; NM_008831.4.
DR AlphaFoldDB; P67778; -.
DR SMR; P67778; -.
DR BioGRID; 202141; 16.
DR ComplexPortal; CPX-5743; Prohibitin complex.
DR CORUM; P67778; -.
DR IntAct; P67778; 16.
DR MINT; P67778; -.
DR STRING; 10090.ENSMUSP00000119603; -.
DR ChEMBL; CHEMBL3751656; -.
DR iPTMnet; P67778; -.
DR PhosphoSitePlus; P67778; -.
DR SwissPalm; P67778; -.
DR REPRODUCTION-2DPAGE; IPI00133440; -.
DR REPRODUCTION-2DPAGE; P67778; -.
DR SWISS-2DPAGE; P67778; -.
DR EPD; P67778; -.
DR jPOST; P67778; -.
DR MaxQB; P67778; -.
DR PaxDb; P67778; -.
DR PeptideAtlas; P67778; -.
DR PRIDE; P67778; -.
DR ProteomicsDB; 301808; -.
DR TopDownProteomics; P67778; -.
DR Antibodypedia; 1078; 752 antibodies from 43 providers.
DR DNASU; 18673; -.
DR Ensembl; ENSMUST00000125172; ENSMUSP00000119603; ENSMUSG00000038845.
DR GeneID; 18673; -.
DR KEGG; mmu:18673; -.
DR UCSC; uc007lan.2; mouse.
DR CTD; 18673; -.
DR MGI; MGI:97572; Phb.
DR VEuPathDB; HostDB:ENSMUSG00000038845; -.
DR eggNOG; KOG3083; Eukaryota.
DR GeneTree; ENSGT00950000183070; -.
DR HOGENOM; CLU_047969_0_0_1; -.
DR InParanoid; P67778; -.
DR OMA; QKMQFVL; -.
DR OrthoDB; 1089994at2759; -.
DR PhylomeDB; P67778; -.
DR TreeFam; TF300095; -.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 18673; 32 hits in 75 CRISPR screens.
DR ChiTaRS; Phb; mouse.
DR PRO; PR:P67778; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P67778; protein.
DR Bgee; ENSMUSG00000038845; Expressed in yolk sac and 258 other tissues.
DR ExpressionAtlas; P67778; baseline and differential.
DR Genevisible; P67778; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0098891; C:extrinsic component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0035632; C:mitochondrial prohibitin complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0001850; F:complement component C3a binding; ISO:MGI.
DR GO; GO:0001851; F:complement component C3b binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0031871; F:proteinase activated receptor binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; IDA:UniProtKB.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR GO; GO:0042113; P:B cell activation; IDA:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; IDA:UniProtKB.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR GO; GO:0071897; P:DNA biosynthetic process; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; IDA:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; ISO:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0001552; P:ovarian follicle atresia; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0045917; P:positive regulation of complement activation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0039529; P:RIG-I signaling pathway; ISO:MGI.
DR GO; GO:0072538; P:T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
DR CDD; cd03401; SPFH_prohibitin; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR000163; Prohibitin.
DR PANTHER; PTHR23222; PTHR23222; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00679; PROHIBITIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; DNA synthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT CHAIN 2..272
FT /note="Prohibitin 1"
FT /id="PRO_0000213879"
FT COILED 177..211
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35232"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 202
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 249
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CONFLICT 255
FT /note="R -> W (in Ref. 2; BAE29988/BAE30089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 29820 MW; 6B26073E169C2FFC CRC64;
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW
VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIYTSI GEDYDERVLP
SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT
EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK
LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ
