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   17-JUN-2020, entry version 199.
DE   RecName: Full=Prohibitin;
GN   Name=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   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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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).
CC   -!- FUNCTION: Regulates mitochondrial respiration activity and in aging
CC       (PubMed:11302691). In neurons, regulates the protein turnover of OMA1
CC       in a cardiolipin-binding manner (By similarity). Inhibits DNA synthesis
CC       (By similarity). {ECO:0000250|UniProtKB:P67778,
CC       ECO:0000250|UniProtKB:P67779, ECO:0000269|PubMed:11302691}.
CC   -!- SUBUNIT: Interacts with PHB2 (PubMed:11302691, PubMed:20959514).
CC       Interacts with STOML2 (PubMed:21746876). {ECO:0000269|PubMed:11302691,
CC       ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:21746876}.
CC   -!- INTERACTION:
CC       P35232; Q496Y0: LONRF3; NbExp=2; IntAct=EBI-354213, EBI-2690768;
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:20959514}. Nucleus {ECO:0000269|PubMed:20959514}.
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. {ECO:0000269|PubMed:11302691}.
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; 939.
DR   CORUM; P35232; -.
DR   DIP; DIP-24248N; -.
DR   IntAct; P35232; 140.
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; 683 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   eggNOG; COG0330; LUCA.
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   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; 744 hits in 792 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 230 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:BHF-UCL.
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: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:0031871; F:proteinase activated receptor binding; IPI:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
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:0006851; P:mitochondrial calcium ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0007005; P:mitochondrion organization; IMP: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: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:0007165; P:signal transduction; TAS: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; Coiled coil;
KW   Direct protein sequencing; DNA synthesis; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleus; Phosphoprotein; Polymorphism;
KW   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
//