PHB1_HUMAN
ID PHB1_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 03-AUG-2022, entry version 209.
DE RecName: Full=Prohibitin 1 {ECO:0000305};
GN Name=PHB1 {ECO:0000303|PubMed:28017329, ECO:0000312|HGNC:HGNC:8912};
GN Synonyms=PHB;
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 pro-inflammatory cytokine IL6
CC (PubMed:31522117). {ECO:0000250|UniProtKB:P67778,
CC ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:28017329,
CC 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 (PHB1 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}.
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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 AlphaFoldDB; P35232; -.
DR SMR; P35232; -.
DR BioGRID; 111264; 1085.
DR ComplexPortal; CPX-5741; Prohibitin complex.
DR CORUM; P35232; -.
DR DIP; DIP-24248N; -.
DR IntAct; P35232; 162.
DR MINT; P35232; -.
DR STRING; 9606.ENSP00000479488; -.
DR ChEMBL; CHEMBL4295750; -.
DR DrugBank; DB15496; Didesmethylrocaglamide.
DR DrugBank; DB15495; Rocaglamide.
DR TCDB; 8.A.21.2.8; the stomatin/podocin/band 7/nephrosis,2/spfh (stomatin) family.
DR GlyGen; P35232; 3 sites, 1 O-linked glycan (3 sites).
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; 752 antibodies from 43 providers.
DR DNASU; 5245; -.
DR Ensembl; ENST00000300408.8; ENSP00000300408.3; ENSG00000167085.13. [P35232-1]
DR Ensembl; ENST00000419140.7; ENSP00000393320.3; ENSG00000167085.13. [P35232-1]
DR Ensembl; ENST00000504124.6; ENSP00000426433.3; ENSG00000167085.13. [P35232-1]
DR Ensembl; ENST00000511832.6; ENSP00000425035.2; ENSG00000167085.13. [P35232-1]
DR Ensembl; ENST00000512041.7; ENSP00000422182.3; ENSG00000167085.13. [P35232-1]
DR Ensembl; ENST00000614445.5; ENSP00000479488.1; ENSG00000167085.13. [P35232-1]
DR Ensembl; ENST00000617874.5; ENSP00000484113.1; ENSG00000167085.13. [P35232-1]
DR GeneID; 5245; -.
DR KEGG; hsa:5245; -.
DR MANE-Select; ENST00000300408.8; ENSP00000300408.3; NM_002634.4; NP_002625.1.
DR UCSC; uc002iox.3; human. [P35232-1]
DR CTD; 5245; -.
DR DisGeNET; 5245; -.
DR GeneCards; PHB; -.
DR HGNC; HGNC:8912; PHB1.
DR HPA; ENSG00000167085; Low tissue specificity.
DR MalaCards; PHB; -.
DR MIM; 176705; gene.
DR neXtProt; NX_P35232; -.
DR OpenTargets; ENSG00000167085; -.
DR PharmGKB; PA33251; -.
DR VEuPathDB; HostDB:ENSG00000167085; -.
DR eggNOG; KOG3083; Eukaryota.
DR GeneTree; ENSGT00950000183070; -.
DR HOGENOM; CLU_047969_0_0_1; -.
DR InParanoid; P35232; -.
DR OMA; QKMQFVL; -.
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 SignaLink; P35232; -.
DR BioGRID-ORCS; 5245; 811 hits in 1088 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 mucosa of transverse colon and 206 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: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:0003714; F:transcription corepressor activity; 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: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:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
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; IDA:ComplexPortal.
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 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; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; DNA synthesis; Host-virus interaction; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..272
FT /note="Prohibitin 1"
FT /id="PRO_0000213878"
FT COILED 177..211
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|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:0007744|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:0007744|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
