ID   PHB2_HUMAN              Reviewed;         299 AA.
AC   Q99623; B4DP75; Q2YDA4; Q7KYU3; Q92978;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   17-JUN-2020, entry version 187.
DE   RecName: Full=Prohibitin-2;
DE   AltName: Full=B-cell receptor-associated protein BAP37;
DE   AltName: Full=D-prohibitin;
DE   AltName: Full=Repressor of estrogen receptor activity;
GN   Name=PHB2 {ECO:0000312|EMBL:AAH14766.1, ECO:0000312|HGNC:HGNC:30306};
GN   Synonyms=BAP {ECO:0000312|EMBL:AAB51324.1},
GN   REA {ECO:0000312|EMBL:AAD38042.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC51639.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=9074930; DOI=10.1101/gr.7.3.268;
RA   Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT   "Large-scale sequencing in human chromosome 12p13: experimental and
RT   computational gene structure determination.";
RL   Genome Res. 7:268-280(1997).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAD38042.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP   ESR1.
RC   TISSUE=Mammary cancer {ECO:0000312|EMBL:AAD38042.1};
RX   PubMed=10359819; DOI=10.1073/pnas.96.12.6947;
RA   Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P.,
RA   Katzenellenbogen B.S.;
RT   "An estrogen receptor-selective coregulator that potentiates the
RT   effectiveness of antiestrogens and represses the activity of estrogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999).
RN   [3] {ECO:0000312|EMBL:AAF44345.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Dendritic cell;
RA   Zhang W., Wan T., Chen T., Cao X.;
RT   "Identification of a novel D-prohibitin from dendritic cells.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAF17231.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hypothalamus {ECO:0000312|EMBL:AAF17231.1};
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [7] {ECO:0000312|EMBL:AAH14766.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta {ECO:0000312|EMBL:AAH14766.1}, and Skin;
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   [8] {ECO:0000312|EMBL:AAF44345.1}
RP   PROTEIN SEQUENCE OF 2-11; 108-131; 148-157; 172-191; 210-216; 225-236 AND
RP   271-289, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma;
RA   Bienvenut W.V., Lilla S., Zebisch A., Kolch W.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [9] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH PHB, 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   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [13]
RP   INTERACTION WITH ARFGEF3, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19496786; DOI=10.1111/j.1349-7006.2009.01209.x;
RA   Kim J.W., Akiyama M., Park J.H., Lin M.L., Shimo A., Ueki T., Daigo Y.,
RA   Tsunoda T., Nishidate T., Nakamura Y., Katagiri T.;
RT   "Activation of an estrogen/estrogen receptor signaling by BIG3 through its
RT   inhibitory effect on nuclear transport of PHB2/REA in breast cancer.";
RL   Cancer Sci. 100:1468-1478(2009).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-250, 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   [15]
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   [16]
RP   INTERACTION WITH ZNF703, AND SUBCELLULAR LOCATION.
RX   PubMed=21328542; DOI=10.1002/emmm.201100121;
RA   Sircoulomb F., Nicolas N., Ferrari A., Finetti P., Bekhouche I.,
RA   Rousselet E., Lonigro A., Adelaide J., Baudelet E., Esteyries S.,
RA   Wicinski J., Audebert S., Charafe-Jauffret E., Jacquemier J., Lopez M.,
RA   Borg J.P., Sotiriou C., Popovici C., Bertucci F., Birnbaum D.,
RA   Chaffanet M., Ginestier C.;
RT   "ZNF703 gene amplification at 8p12 specifies luminal B breast cancer.";
RL   EMBO Mol. Med. 3:153-166(2011).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PHB.
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   [18]
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   [19]
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=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [21]
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   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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: Acts as a mediator of transcriptional repression by nuclear
CC       hormone receptors via recruitment of histone deacetylases
CC       (PubMed:10359819). Functions as an estrogen receptor (ER)-selective
CC       coregulator that potentiates the inhibitory activities of antiestrogens
CC       and represses the activity of estrogens (PubMed:10359819). Competes
CC       with NCOA1 for modulation of ER transcriptional activity
CC       (PubMed:10359819). In mitochondria, regulates cytochrome-c oxidase
CC       assembly (COX) and mitochondrial respiration (PubMed:20959514,
CC       PubMed:11302691). Binding to sphingoid 1-phosphate (SPP) modulates its
CC       regulator activity (PubMed:20959514, PubMed:11302691). In neurons,
CC       regulates the protein turnover of OMA1 in a cardiolipin-binding manner
CC       (By similarity). {ECO:0000250|UniProtKB:O35129,
CC       ECO:0000269|PubMed:10359819, ECO:0000269|PubMed:11302691,
CC       ECO:0000269|PubMed:20959514}.
CC   -!- SUBUNIT: Interacts with PHB (PubMed:20959514). Interacts with ESR1,
CC       HDAC1 and HDAC5 (By similarity). Interacts with ZNF703
CC       (PubMed:21328542). Interacts with STOML2 (PubMed:21746876). Interacts
CC       with ARFGEF3 (PubMed:19496786). Interacts with SPHK2. Interacts with
CC       COX4I1; the interaction associates PHB2 with COX (By similarity).
CC       {ECO:0000250|UniProtKB:O35129, ECO:0000269|PubMed:10359819,
CC       ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:19496786,
CC       ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:21328542,
CC       ECO:0000269|PubMed:21746876}.
CC   -!- INTERACTION:
CC       Q99623; P03372: ESR1; NbExp=4; IntAct=EBI-358348, EBI-78473;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:20959514}. Cytoplasm {ECO:0000269|PubMed:19496786}.
CC       Nucleus {ECO:0000269|PubMed:19496786, ECO:0000269|PubMed:20959514}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99623-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99623-2; Sequence=VSP_045311;
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 to 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:0000255}.
DR   EMBL; U72511; AAC51639.1; -; mRNA.
DR   EMBL; AF150962; AAD38042.1; -; mRNA.
DR   EMBL; AF178980; AAF44345.1; -; mRNA.
DR   EMBL; AF126021; AAF17231.1; -; mRNA.
DR   EMBL; AK298217; BAG60487.1; -; mRNA.
DR   EMBL; U47924; AAB51324.1; -; Genomic_DNA.
DR   EMBL; BC014766; AAH14766.1; -; mRNA.
DR   EMBL; BC110322; AAI10323.1; -; mRNA.
DR   CCDS; CCDS53741.1; -. [Q99623-1]
DR   CCDS; CCDS58207.1; -. [Q99623-2]
DR   RefSeq; NP_001138303.1; NM_001144831.1. [Q99623-1]
DR   RefSeq; NP_001254629.1; NM_001267700.1. [Q99623-2]
DR   PDB; 6IQE; X-ray; 1.70 A; A=188-265.
DR   PDBsum; 6IQE; -.
DR   SMR; Q99623; -.
DR   BioGRID; 116459; 300.
DR   CORUM; Q99623; -.
DR   IntAct; Q99623; 119.
DR   MINT; Q99623; -.
DR   STRING; 9606.ENSP00000441875; -.
DR   ChEMBL; CHEMBL4295931; -.
DR   DrugBank; DB06774; Capsaicin.
DR   DrugBank; DB15496; Didesmethylrocaglamide.
DR   DrugBank; DB15495; Rocaglamide.
DR   CarbonylDB; Q99623; -.
DR   iPTMnet; Q99623; -.
DR   MetOSite; Q99623; -.
DR   PhosphoSitePlus; Q99623; -.
DR   SwissPalm; Q99623; -.
DR   BioMuta; PHB2; -.
DR   DMDM; 74752151; -.
DR   OGP; Q99623; -.
DR   EPD; Q99623; -.
DR   jPOST; Q99623; -.
DR   MassIVE; Q99623; -.
DR   MaxQB; Q99623; -.
DR   PaxDb; Q99623; -.
DR   PeptideAtlas; Q99623; -.
DR   PRIDE; Q99623; -.
DR   ProteomicsDB; 4765; -.
DR   ProteomicsDB; 78364; -. [Q99623-1]
DR   TopDownProteomics; Q99623-1; -. [Q99623-1]
DR   TopDownProteomics; Q99623-2; -. [Q99623-2]
DR   Antibodypedia; 4444; 444 antibodies.
DR   DNASU; 11331; -.
DR   Ensembl; ENST00000440277; ENSP00000412856; ENSG00000215021. [Q99623-2]
DR   Ensembl; ENST00000535923; ENSP00000441875; ENSG00000215021. [Q99623-1]
DR   GeneID; 11331; -.
DR   KEGG; hsa:11331; -.
DR   UCSC; uc058kpb.1; human. [Q99623-1]
DR   CTD; 11331; -.
DR   DisGeNET; 11331; -.
DR   EuPathDB; HostDB:ENSG00000215021.8; -.
DR   GeneCards; PHB2; -.
DR   HGNC; HGNC:30306; PHB2.
DR   HPA; ENSG00000215021; Low tissue specificity.
DR   MIM; 610704; gene.
DR   neXtProt; NX_Q99623; -.
DR   OpenTargets; ENSG00000215021; -.
DR   PharmGKB; PA142671181; -.
DR   eggNOG; KOG3090; Eukaryota.
DR   eggNOG; COG0330; LUCA.
DR   GeneTree; ENSGT00950000183070; -.
DR   InParanoid; Q99623; -.
DR   KO; K17081; -.
DR   OMA; RASRFNI; -.
DR   OrthoDB; 1089994at2759; -.
DR   PhylomeDB; Q99623; -.
DR   TreeFam; TF354230; -.
DR   Reactome; R-HSA-8949664; Processing of SMDT1.
DR   SIGNOR; Q99623; -.
DR   BioGRID-ORCS; 11331; 741 hits in 792 CRISPR screens.
DR   ChiTaRS; PHB2; human.
DR   GeneWiki; PHB2; -.
DR   GenomeRNAi; 11331; -.
DR   Pharos; Q99623; Tbio.
DR   PRO; PR:Q99623; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q99623; protein.
DR   Bgee; ENSG00000215021; Expressed in caecum and 233 other tissues.
DR   ExpressionAtlas; Q99623; baseline and differential.
DR   Genevisible; Q99623; HS.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0033218; F:amide binding; IPI:UniProtKB.
DR   GO; GO:0030331; F:estrogen receptor binding; NAS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0046625; F:sphingolipid binding; IDA:UniProtKB.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
DR   GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR   GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; IMP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   GO; GO:0007062; P:sister chromatid cohesion; IDA: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; Cytoplasm;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:22814378, ECO:0000269|Ref.8"
FT   CHAIN           2..299
FT                   /note="Prohibitin-2"
FT                   /id="PRO_0000213884"
FT   REGION          19..49
FT                   /note="Necessary for transcriptional repression"
FT                   /evidence="ECO:0000269|PubMed:10359819"
FT   REGION          150..174
FT                   /note="Necessary for transcriptional repression"
FT                   /evidence="ECO:0000269|PubMed:10359819"
FT   COILED          190..238
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:22814378, ECO:0000269|Ref.8"
FT   MOD_RES         128
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:15592455"
FT   MOD_RES         147
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35129"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         200
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35129"
FT   MOD_RES         236
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35129"
FT   MOD_RES         250
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         262
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35129"
FT   VAR_SEQ         203..240
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045311"
FT   HELIX           188..244
FT                   /evidence="ECO:0000244|PDB:6IQE"
SQ   SEQUENCE   299 AA;  33296 MW;  A887CC982BF85C80 CRC64;
     MAQNLKDLAG RLPAGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI FFNRIGGVQQ
     DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLS RPNAQELPSM
     YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD
     DVAITELSFS REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE
     ALSKNPGYIK LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK
//