ID   PHB_HUMAN               Reviewed;         272 AA.
AC   P35232; B4DY47; Q4VBQ0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   12-AUG-2020, entry version 200.
DE   RecName: Full=Prohibitin {ECO:0000305};
GN   Name=PHB {ECO:0000312|HGNC:HGNC:8912};
GN   Synonyms=PHB1 {ECO:0000303|PubMed:28017329};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-88 AND HIS-105.
RC   TISSUE=Mammary gland;
RX   PubMed=1540973;
RA   Sato T., Saito H., Swensen J., Olifant A., Wood C., Danner D., Sakamoto T.,
RA   Takita K., Kasumi F., Miki Y., Skolnick M., Nakamura Y.;
RT   "The human prohibitin gene located on chromosome 17q21 is mutated in
RT   sporadic breast cancer.";
RL   Cancer Res. 52:1643-1646(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8244394; DOI=10.1006/geno.1993.1402;
RA   Sato T., Sakamoto T., Takita K., Saito H., Okui K., Nakamura Y.;
RT   "The human prohibitin (PHB) gene family and its somatic mutations in human
RT   tumors.";
RL   Genomics 17:762-764(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Muscle;
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   [7]
RP   PROTEIN SEQUENCE OF 5-11; 84-93; 106-128; 134-143; 178-186 AND 209-219, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (MAR-2005) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 75-83; 94-117; 134-143; 158-177; 220-253 AND 256-272,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   FUNCTION, INTERACTION WITH PHB2, DEVELOPMENTAL STAGE, AND INDUCTION.
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   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14500729; DOI=10.1074/jbc.m305171200;
RA   Fusaro G., Dasgupta P., Rastogi S., Joshi B., Chellappan S.;
RT   "Prohibitin induces the transcriptional activity of p53 and is exported
RT   from the nucleus upon apoptotic signaling.";
RL   J. Biol. Chem. 278:47853-47861(2003).
RN   [11]
RP   INTERACTION WITH SARS-COV NSP2 (MICROBIAL INFECTION).
RX   PubMed=19640993; DOI=10.1128/jvi.00842-09;
RA   Cornillez-Ty C.T., Liao L., Yates J.R., Kuhn P., Buchmeier M.J.;
RT   "Severe acute respiratory syndrome coronavirus nonstructural protein 2
RT   interacts with a host protein complex involved in mitochondrial biogenesis
RT   and intracellular signaling.";
RL   J. Virol. 83:10314-10318(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   INTERACTION WITH HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 ENVELOPE GLYCOPROTEIN
RP   GP160.
RX   PubMed=19906925; DOI=10.1128/jvi.01641-09;
RA   Emerson V., Holtkotte D., Pfeiffer T., Wang I.H., Schnoelzer M., Kempf T.,
RA   Bosch V.;
RT   "Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an
RT   interaction partner of the C-terminal cytoplasmic domain of the HIV-1
RT   glycoprotein.";
RL   J. Virol. 84:1355-1365(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PHB2.
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   [16]
RP   INTERACTION WITH STOML2.
RX   PubMed=21746876; DOI=10.1128/mcb.05393-11;
RA   Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B.,
RA   Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.;
RT   "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial
RT   biogenesis and function.";
RL   Mol. Cell. Biol. 31:3845-3856(2011).
RN   [17]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CHIKUNGUNYA VIRUS SPIKE
RP   GLYCOPROTEIN E2.
RX   PubMed=22997079; DOI=10.1002/jmv.23403;
RA   Wintachai P., Wikan N., Kuadkitkan A., Jaimipuk T., Ubol S.,
RA   Pulmanausahakul R., Auewarakul P., Kasinrerk W., Weng W.Y.,
RA   Panyasrivanit M., Paemanee A., Kittisenachai S., Roytrakul S., Smith D.R.;
RT   "Identification of prohibitin as a Chikungunya virus receptor protein.";
RL   J. Med. Virol. 84:1757-1770(2012).
RN   [18]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24003225; DOI=10.1074/jbc.m113.510826;
RA   Fu P., Yang Z., Bach L.A.;
RT   "Prohibitin-2 binding modulates insulin-like growth factor-binding protein-
RT   6 (IGFBP-6)-induced rhabdomyosarcoma cell migration.";
RL   J. Biol. Chem. 288:29890-29900(2013).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91 AND TYR-249, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [21]
RP   INTERACTION WITH PHB2 AND MAP1LC3B.
RX   PubMed=28017329; DOI=10.1016/j.cell.2016.11.042;
RA   Wei Y., Chiang W.C., Sumpter R. Jr., Mishra P., Levine B.;
RT   "Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor.";
RL   Cell 168:224.e10-238.e10(2017).
RN   [22]
RP   INTERACTION WITH PHB2 AND CLPB, AND FUNCTION.
RX   PubMed=31522117; DOI=10.1016/j.isci.2019.08.056;
RA   Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O.,
RA   Tamada T., Koshiba T.;
RT   "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes:
RT   Insight into a Role of the Coiled-Coil Region.";
RL   IScience 19:1065-1078(2019).
RN   [23]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=31899195; DOI=10.1016/j.imlet.2019.12.008;
RA   Zhang J., Sun Z., Wu Q., Shen J.;
RT   "Prohibitin 1 interacts with signal transducer and activator of
RT   transcription 3 in T-helper 17 cells.";
RL   Immunol. Lett. 219:8-14(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:28017329,
CC       PubMed:31522117). Plays a role in adipose tissue and glucose
CC       Homeostasis in a sex-specific manner (By similarity). Contributes to
CC       pulmonary vascular remodeling by accelerating proliferation of
CC       pulmonary arterial smooth muscle cells (By similarity).
CC       {ECO:0000250|UniProtKB:P67778, ECO:0000250|UniProtKB:P67779,
CC       ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514,
CC       ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117}.
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 (By similarity). 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:28017329). Involved in mitochondrial-mediated antiviral innate
CC       immunity, activates DDX58/RIG-I-mediated signal transduction and
CC       production of IFNB1 and proinflammatory cytokine IL6 (PubMed:31522117).
CC       {ECO:0000250|UniProtKB:P67778, ECO:0000269|PubMed:11302691,
CC       ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117, 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 (PubMed:14500729). Interacts with STAT3 to affect IL17
CC       secretion in T-helper Th17 cells (PubMed:31899195).
CC       {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:31899195}.
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 (By
CC       similarity). Upon CD40 engagement, required to activate NF-kappa-B
CC       signaling pathway via phospholipase C and protein kinase C activation
CC       (By similarity). {ECO:0000250|UniProtKB:P67778}.
CC   -!- SUBUNIT: The mitochondrial prohibitin complex consists of two subunits
CC       (PHB and PHB2), assembled into a membrane-associated ring-shaped
CC       supercomplex of approximately 1 mDa (PubMed:11302691, PubMed:20959514,
CC       PubMed:28017329, PubMed:31522117). Interacts with STOML2
CC       (PubMed:21746876). Interacts with MAP1LC3B (membrane-bound form LC3-
CC       II); the interaction requires PHB2 and takes place upon Parkin-mediated
CC       mitochondrial damage (PubMed:28017329). Interacts with STAT3
CC       (unphosphorylated or phosphorylated at 'Ser-727') (PubMed:31899195).
CC       Interacts with CLPB (PubMed:31522117). Interacts with CD86 (via
CC       cytoplasmic domain); the interactions increases after priming with CD40
CC       (By similarity). {ECO:0000250|UniProtKB:P67778,
CC       ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514,
CC       ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:28017329,
CC       ECO:0000269|PubMed:31522117, ECO:0000269|PubMed:31899195}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus/SARS-CoV
CC       nsp2 protein. {ECO:0000269|PubMed:19640993}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with chikungunya virus spike
CC       glycoprotein E2. {ECO:0000269|PubMed:22997079}.
CC   -!- SUBUNIT: (Microbial infection) Interaction with human immunodeficiency
CC       virus type 1/HIV-1 envelope glycoprotein GP160.
CC       {ECO:0000269|PubMed:19906925}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human enterovirus 71/EV-
CC       71 capsid protein VP0, protein 3CD and protease 3C.
CC       {ECO:0000250|UniProtKB:P67778}.
CC   -!- INTERACTION:
CC       P35232; Q496Y0: LONRF3; NbExp=2; IntAct=EBI-354213, EBI-2690768;
CC       P35232; Q99623: PHB2; NbExp=3; IntAct=EBI-354213, EBI-358348;
CC       P35232; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-354213, EBI-8652744;
CC       P35232; Q13309-2: SKP2; NbExp=2; IntAct=EBI-354213, EBI-7791408;
CC       P35232; Q9NS68: TNFRSF19; NbExp=3; IntAct=EBI-354213, EBI-530381;
CC       P35232; P04637: TP53; NbExp=6; IntAct=EBI-354213, EBI-366083;
CC       P35232; O14980: XPO1; NbExp=2; IntAct=EBI-354213, EBI-355867;
CC       P35232; Q9JLL3: Tnfrsf19; Xeno; NbExp=3; IntAct=EBI-354213, EBI-20800437;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:20959514}. Nucleus
CC       {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:20959514,
CC       ECO:0000269|PubMed:31899195}. Cytoplasm {ECO:0000269|PubMed:14500729,
CC       ECO:0000269|PubMed:31899195}. Cell membrane
CC       {ECO:0000269|PubMed:22997079, ECO:0000269|PubMed:24003225}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P35232-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35232-2; Sequence=VSP_054922;
CC   -!- TISSUE SPECIFICITY: Widely expressed in different tissues.
CC   -!- DEVELOPMENTAL STAGE: Levels of expression in fibroblasts decrease
CC       heterogeneously during cellular aging (PubMed:11302691). In CD4(+) T
CC       cells, expression increases during polarization towards T-helper Th17,
CC       Th1 and Th2 (PubMed:31899195). {ECO:0000269|PubMed:11302691,
CC       ECO:0000269|PubMed:31899195}.
CC   -!- INDUCTION: Expression increases approximately 3-fold upon entry into G1
CC       phase compared with other phases of the cell cycle. Also induced
CC       following inhibition of mitochondrial protein synthesis by
CC       thiamphenicol. {ECO:0000269|PubMed:11302691}.
CC   -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
DR   EMBL; S85655; AAB21614.1; -; mRNA.
DR   EMBL; L14272; AAO18340.1; -; Genomic_DNA.
DR   EMBL; BT007411; AAP36079.1; -; mRNA.
DR   EMBL; AK302258; BAG63609.1; -; mRNA.
DR   EMBL; AC091180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013401; AAH13401.1; -; mRNA.
DR   EMBL; BC095460; AAH95460.1; -; mRNA.
DR   CCDS; CCDS11548.1; -. [P35232-1]
DR   CCDS; CCDS62244.1; -. [P35232-2]
DR   PIR; I52690; I52690.
DR   RefSeq; NP_001268425.1; NM_001281496.1. [P35232-1]
DR   RefSeq; NP_001268426.1; NM_001281497.1. [P35232-2]
DR   RefSeq; NP_001268644.1; NM_001281715.1. [P35232-1]
DR   RefSeq; NP_002625.1; NM_002634.3. [P35232-1]
DR   RefSeq; XP_016880252.1; XM_017024763.1. [P35232-1]
DR   PDB; 1LU7; Model; -; A=1-272.
DR   PDBsum; 1LU7; -.
DR   SMR; P35232; -.
DR   BioGRID; 111264; 947.
DR   ComplexPortal; CPX-5741; Prohibitin complex.
DR   CORUM; P35232; -.
DR   DIP; DIP-24248N; -.
DR   IntAct; P35232; 141.
DR   MINT; P35232; -.
DR   STRING; 9606.ENSP00000479488; -.
DR   ChEMBL; CHEMBL4295750; -.
DR   DrugBank; DB15496; Didesmethylrocaglamide.
DR   DrugBank; DB15495; Rocaglamide.
DR   iPTMnet; P35232; -.
DR   PhosphoSitePlus; P35232; -.
DR   SwissPalm; P35232; -.
DR   BioMuta; PHB; -.
DR   DMDM; 464371; -.
DR   DOSAC-COBS-2DPAGE; P35232; -.
DR   OGP; P35232; -.
DR   REPRODUCTION-2DPAGE; IPI00017334; -.
DR   REPRODUCTION-2DPAGE; P35232; -.
DR   SWISS-2DPAGE; P35232; -.
DR   UCD-2DPAGE; P35232; -.
DR   EPD; P35232; -.
DR   jPOST; P35232; -.
DR   MassIVE; P35232; -.
DR   MaxQB; P35232; -.
DR   PaxDb; P35232; -.
DR   PeptideAtlas; P35232; -.
DR   PRIDE; P35232; -.
DR   ProteomicsDB; 5497; -.
DR   ProteomicsDB; 54995; -. [P35232-1]
DR   TopDownProteomics; P35232-1; -. [P35232-1]
DR   Antibodypedia; 1078; 696 antibodies.
DR   DNASU; 5245; -.
DR   Ensembl; ENST00000300408; ENSP00000300408; ENSG00000167085. [P35232-1]
DR   Ensembl; ENST00000511832; ENSP00000425035; ENSG00000167085. [P35232-2]
DR   Ensembl; ENST00000614445; ENSP00000479488; ENSG00000167085. [P35232-1]
DR   Ensembl; ENST00000617874; ENSP00000484113; ENSG00000167085. [P35232-1]
DR   GeneID; 5245; -.
DR   KEGG; hsa:5245; -.
DR   UCSC; uc002iox.3; human. [P35232-1]
DR   CTD; 5245; -.
DR   DisGeNET; 5245; -.
DR   EuPathDB; HostDB:ENSG00000167085.11; -.
DR   GeneCards; PHB; -.
DR   HGNC; HGNC:8912; PHB.
DR   HPA; ENSG00000167085; Low tissue specificity.
DR   MalaCards; PHB; -.
DR   MIM; 176705; gene.
DR   neXtProt; NX_P35232; -.
DR   OpenTargets; ENSG00000167085; -.
DR   PharmGKB; PA33251; -.
DR   eggNOG; KOG3083; Eukaryota.
DR   GeneTree; ENSGT00950000183070; -.
DR   HOGENOM; CLU_047969_0_0_1; -.
DR   InParanoid; P35232; -.
DR   KO; K17080; -.
DR   OMA; RTRIRDN; -.
DR   PhylomeDB; P35232; -.
DR   TreeFam; TF300095; -.
DR   PathwayCommons; P35232; -.
DR   Reactome; R-HSA-5673000; RAF activation.
DR   Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR   Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR   Reactome; R-HSA-8949664; Processing of SMDT1.
DR   Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR   BioGRID-ORCS; 5245; 763 hits in 883 CRISPR screens.
DR   ChiTaRS; PHB; human.
DR   GeneWiki; Prohibitin; -.
DR   GenomeRNAi; 5245; -.
DR   Pharos; P35232; Tbio.
DR   PRO; PR:P35232; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P35232; protein.
DR   Bgee; ENSG00000167085; Expressed in adult mammalian kidney and 245 other tissues.
DR   ExpressionAtlas; P35232; baseline and differential.
DR   Genevisible; P35232; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:HGNC-UCL.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0035632; C:mitochondrial prohibitin complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0001850; F:complement component C3a binding; IDA:UniProtKB.
DR   GO; GO:0001851; F:complement component C3b binding; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0031871; F:proteinase activated receptor binding; IPI:UniProtKB.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
DR   GO; GO:0140374; P:antiviral innate immune response; IDA:UniProtKB.
DR   GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR   GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB.
DR   GO; GO:0071354; P:cellular response to interleukin-6; IDA:BHF-UCL.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR   GO; GO:0002377; P:immunoglobulin production; ISS:UniProtKB.
DR   GO; GO:0072615; P:interleukin-17 secretion; IMP:UniProtKB.
DR   GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0044830; P:modulation by host of viral RNA genome replication; ISS:UniProtKB.
DR   GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR   GO; GO:0010942; P:positive regulation of cell death; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0045917; P:positive regulation of complement activation; IDA:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:ParkinsonsUK-UCL.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS: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; IDA:UniProtKB.
DR   GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0039529; P:RIG-I signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   GO; GO:0072538; P:T-helper 17 type immune response; IDA:UniProtKB.
DR   GO; GO:0046718; P:viral entry into host cell; ISS:UniProtKB.
DR   CDD; cd03401; SPFH_prohibitin; 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   3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW   Coiled coil; Cytoplasm; Direct protein sequencing; DNA synthesis; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleus; Phosphoprotein;
KW   Polymorphism; Proto-oncogene; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:25944712"
FT   CHAIN           2..272
FT                   /note="Prohibitin"
FT                   /id="PRO_0000213878"
FT   COILED          177..211
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:25944712"
FT   MOD_RES         91
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         128
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P67778"
FT   MOD_RES         186
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P67778"
FT   MOD_RES         202
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         202
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P67778"
FT   MOD_RES         249
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   VAR_SEQ         140..256
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054922"
FT   VARIANT         88
FT                   /note="V -> A (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs121918373)"
FT                   /evidence="ECO:0000269|PubMed:1540973"
FT                   /id="VAR_006479"
FT   VARIANT         105
FT                   /note="R -> H (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs121918372)"
FT                   /evidence="ECO:0000269|PubMed:1540973"
FT                   /id="VAR_006480"
SQ   SEQUENCE   272 AA;  29804 MW;  915494273E342C76 CRC64;
     MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW
     VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP
     SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT
     EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK
     LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ
//