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Q99623

- PHB2_HUMAN

UniProt

Q99623 - PHB2_HUMAN

Protein

Prohibitin-2

Gene

PHB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases By similarity. Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity. Probably involved in regulating mitochondrial respiration activity and in aging.By similarity1 Publication1 Publication

    GO - Molecular functioni

    1. estrogen receptor binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. mammary gland alveolus development Source: Ensembl
    2. mammary gland branching involved in thelarche Source: Ensembl
    3. negative regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
    4. negative regulation of mammary gland epithelial cell proliferation Source: Ensembl
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of branching involved in mammary gland duct morphogenesis Source: Ensembl
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prohibitin-2
    Alternative name(s):
    B-cell receptor-associated protein BAP37
    D-prohibitin
    Repressor of estrogen receptor activity
    Gene namesi
    Name:PHB2Imported
    Synonyms:BAPImported, REAImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30306. PHB2.

    Subcellular locationi

    Mitochondrion inner membrane By similarity. Cytoplasm By similarity. Nucleus By similarity
    Note: Also cytoplasmic and nuclear.By similarity

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: UniProtKB
    3. mitochondrion Source: UniProt
    4. nuclear matrix Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 299298Prohibitin-2PRO_0000213884Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei128 – 1281Phosphotyrosine1 Publication
    Modified residuei147 – 1471N6-acetyllysineBy similarity
    Modified residuei200 – 2001N6-acetyllysineBy similarity
    Modified residuei236 – 2361N6-acetyllysineBy similarity
    Modified residuei250 – 2501N6-acetyllysine1 Publication
    Modified residuei262 – 2621N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99623.
    PaxDbiQ99623.
    PeptideAtlasiQ99623.
    PRIDEiQ99623.

    2D gel databases

    OGPiQ99623.

    PTM databases

    PhosphoSiteiQ99623.

    Expressioni

    Developmental stagei

    Levels of expression in fibroblasts decrease heterogeneously during cellular aging.1 Publication

    Inductioni

    Expression increases approximately 3-fold upon entry into G1 phase compared to other phases of the cell cycle. Also induced following inhibition of mitochondrial protein synthesis by thiamphenicol.1 Publication

    Gene expression databases

    ArrayExpressiQ99623.
    BgeeiQ99623.
    CleanExiHS_PHB2.
    GenevestigatoriQ99623.

    Organism-specific databases

    HPAiCAB014889.
    CAB026335.
    HPA039874.

    Interactioni

    Subunit structurei

    Interacts with PHB, ESR1, HDAC1 and HDAC5 By similarity. Interacts with ZNF703. Interacts with STOML2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESR1P033724EBI-358348,EBI-78473

    Protein-protein interaction databases

    BioGridi116459. 72 interactions.
    IntActiQ99623. 23 interactions.
    MINTiMINT-142400.
    STRINGi9606.ENSP00000382362.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99623.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 4931Necessary for transcriptional repression1 PublicationAdd
    BLAST
    Regioni150 – 17425Necessary for transcriptional repression1 PublicationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili190 – 23849Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the prohibitin family.Sequence Analysis

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0330.
    HOGENOMiHOG000205692.
    HOVERGENiHBG004457.
    InParanoidiQ99623.
    KOiK17081.
    OMAiIGGVKKE.
    PhylomeDBiQ99623.
    TreeFamiTF354230.

    Family and domain databases

    InterProiIPR001107. Band_7.
    IPR000163. Prohibitin.
    [Graphical view]
    PANTHERiPTHR23222. PTHR23222. 1 hit.
    PfamiPF01145. Band_7. 1 hit.
    [Graphical view]
    PRINTSiPR00679. PROHIBITIN.
    SMARTiSM00244. PHB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99623-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAQNLKDLAG RLPAGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI    50
    FFNRIGGVQQ DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ 100
    MVNISLRVLS RPNAQELPSM YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA 150
    SQLITQRAQV SLLIRRELTE RAKDFSLILD DVAITELSFS REYTAAVEAK 200
    QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE ALSKNPGYIK 250
    LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK 299
    Length:299
    Mass (Da):33,296
    Last modified:July 1, 1997 - v2
    Checksum:iA887CC982BF85C80
    GO
    Isoform 2 (identifier: Q99623-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         203-240: Missing.

    Show »
    Length:261
    Mass (Da):29,044
    Checksum:iF698CB300517B30A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei203 – 24038Missing in isoform 2. 1 PublicationVSP_045311Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72511 mRNA. Translation: AAC51639.1.
    AF150962 mRNA. Translation: AAD38042.1.
    AF178980 mRNA. Translation: AAF44345.1.
    AF126021 mRNA. Translation: AAF17231.1.
    AK298217 mRNA. Translation: BAG60487.1.
    U47924 Genomic DNA. Translation: AAB51324.1.
    BC014766 mRNA. Translation: AAH14766.1.
    BC110322 mRNA. Translation: AAI10323.1.
    CCDSiCCDS53741.1. [Q99623-1]
    CCDS58207.1. [Q99623-2]
    RefSeqiNP_001138303.1. NM_001144831.1. [Q99623-1]
    NP_001254629.1. NM_001267700.1. [Q99623-2]
    UniGeneiHs.504620.

    Genome annotation databases

    EnsembliENST00000440277; ENSP00000412856; ENSG00000215021. [Q99623-2]
    ENST00000535923; ENSP00000441875; ENSG00000215021. [Q99623-1]
    GeneIDi11331.
    KEGGihsa:11331.
    UCSCiuc010sft.2. human.
    uc021quf.1. human. [Q99623-1]

    Polymorphism databases

    DMDMi74752151.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72511 mRNA. Translation: AAC51639.1 .
    AF150962 mRNA. Translation: AAD38042.1 .
    AF178980 mRNA. Translation: AAF44345.1 .
    AF126021 mRNA. Translation: AAF17231.1 .
    AK298217 mRNA. Translation: BAG60487.1 .
    U47924 Genomic DNA. Translation: AAB51324.1 .
    BC014766 mRNA. Translation: AAH14766.1 .
    BC110322 mRNA. Translation: AAI10323.1 .
    CCDSi CCDS53741.1. [Q99623-1 ]
    CCDS58207.1. [Q99623-2 ]
    RefSeqi NP_001138303.1. NM_001144831.1. [Q99623-1 ]
    NP_001254629.1. NM_001267700.1. [Q99623-2 ]
    UniGenei Hs.504620.

    3D structure databases

    ProteinModelPortali Q99623.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116459. 72 interactions.
    IntActi Q99623. 23 interactions.
    MINTi MINT-142400.
    STRINGi 9606.ENSP00000382362.

    PTM databases

    PhosphoSitei Q99623.

    Polymorphism databases

    DMDMi 74752151.

    2D gel databases

    OGPi Q99623.

    Proteomic databases

    MaxQBi Q99623.
    PaxDbi Q99623.
    PeptideAtlasi Q99623.
    PRIDEi Q99623.

    Protocols and materials databases

    DNASUi 11331.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000440277 ; ENSP00000412856 ; ENSG00000215021 . [Q99623-2 ]
    ENST00000535923 ; ENSP00000441875 ; ENSG00000215021 . [Q99623-1 ]
    GeneIDi 11331.
    KEGGi hsa:11331.
    UCSCi uc010sft.2. human.
    uc021quf.1. human. [Q99623-1 ]

    Organism-specific databases

    CTDi 11331.
    GeneCardsi GC12M007074.
    HGNCi HGNC:30306. PHB2.
    HPAi CAB014889.
    CAB026335.
    HPA039874.
    MIMi 610704. gene.
    neXtProti NX_Q99623.
    PharmGKBi PA142671181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0330.
    HOGENOMi HOG000205692.
    HOVERGENi HBG004457.
    InParanoidi Q99623.
    KOi K17081.
    OMAi IGGVKKE.
    PhylomeDBi Q99623.
    TreeFami TF354230.

    Miscellaneous databases

    ChiTaRSi PHB2. human.
    GeneWikii PHB2.
    GenomeRNAii 11331.
    NextBioi 43043.
    PROi Q99623.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99623.
    Bgeei Q99623.
    CleanExi HS_PHB2.
    Genevestigatori Q99623.

    Family and domain databases

    InterProi IPR001107. Band_7.
    IPR000163. Prohibitin.
    [Graphical view ]
    PANTHERi PTHR23222. PTHR23222. 1 hit.
    Pfami PF01145. Band_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00679. PROHIBITIN.
    SMARTi SM00244. PHB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
      Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
      Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. "An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens."
      Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P., Katzenellenbogen B.S.
      Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESR1.
      Tissue: Mammary cancerImported.
    3. "Identification of a novel D-prohibitin from dendritic cells."
      Zhang W., Wan T., Chen T., Cao X.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Dendritic cell.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: HypothalamusImported.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: PlacentaImported and Skin.
    8. Bienvenut W.V., Lilla S., Zebisch A., Kolch W.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 108-131; 148-157; 172-191; 210-216; 225-236 AND 271-289, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    9. "Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence."
      Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H., Hall P.A., Wright E.G.
      Exp. Cell Res. 265:262-273(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PHB, DEVELOPMENTAL STAGE, INDUCTION.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: INTERACTION WITH ZNF703, SUBCELLULAR LOCATION.
    15. "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
      Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.
      Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STOML2.
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPHB2_HUMAN
    AccessioniPrimary (citable) accession number: Q99623
    Secondary accession number(s): B4DP75
    , Q2YDA4, Q7KYU3, Q92978
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3