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Q8BLG0

- PHF20_MOUSE

UniProt

Q8BLG0 - PHF20_MOUSE

Protein

PHD finger protein 20

Gene

Phf20

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (11 Jul 2003)
      Previous versions | rss
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    Functioni

    Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage By similarity. Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi257 – 26913A.T hookAdd
    BLAST
    Zinc fingeri455 – 48531C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri657 – 70347PHD-typeAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone acetyltransferase activity (H4-K16 specific) Source: Ensembl
    3. histone acetyltransferase activity (H4-K5 specific) Source: Ensembl
    4. histone acetyltransferase activity (H4-K8 specific) Source: Ensembl
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H4-K16 acetylation Source: UniProtKB
    2. histone H4-K5 acetylation Source: UniProtKB
    3. histone H4-K8 acetylation Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PHD finger protein 20
    Alternative name(s):
    Hepatocellular carcinoma-associated antigen 58 homolog
    Gene namesi
    Name:Phf20
    Synonyms:Hca58
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2444148. Phf20.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. histone acetyltransferase complex Source: UniProtKB
    2. MLL1 complex Source: UniProtKB
    3. nuclear membrane Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice die shortly after birth and display a wide variety of phenotypes within the skeletal and hematopoietic systems.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi97 – 971W → A: Abolishes Methyllysine-binding. 1 Publication
    Mutagenesisi103 – 1031Y → A: Abolishes Methyllysine-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10101010PHD finger protein 20PRO_0000059311Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi96 – 96Interchain (with C-100)By similarity
    Disulfide bondi100 – 100Interchain (with C-96)By similarity
    Modified residuei159 – 1591PhosphoserineBy similarity
    Modified residuei841 – 8411N6-acetyllysineBy similarity
    Modified residuei876 – 8761PhosphoserineBy similarity
    Modified residuei878 – 8781PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    PRIDEiQ8BLG0.

    PTM databases

    PhosphoSiteiQ8BLG0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BLG0.
    BgeeiQ8BLG0.
    CleanExiMM_PHF20.
    GenevestigatoriQ8BLG0.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi230779. 7 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BLG0.
    SMRiQ8BLG0. Positions 4-68, 85-137, 654-701.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 6966Tudor 1Add
    BLAST
    Domaini83 – 14765Tudor 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi162 – 25998Lys-richAdd
    BLAST
    Compositional biasi526 – 55530Lys-richAdd
    BLAST
    Compositional biasi543 – 55513Poly-LysAdd
    BLAST

    Domaini

    The Tudor domain 2 mediates reading of dimethyl-lysine residues.
    The Tudor domain 1 doesn't bind dimethyl-lysine residues, due to an atypical and occluded aromatic cage.By similarity

    Sequence similaritiesi

    Contains 1 A.T hook DNA-binding domain.Curated
    Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.Curated
    Contains 2 Tudor domains.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri455 – 48531C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri657 – 70347PHD-typeAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00390000006451.
    HOGENOMiHOG000231997.
    HOVERGENiHBG053586.
    OMAiENTMKTE.
    OrthoDBiEOG7RZ5PD.
    PhylomeDBiQ8BLG0.
    TreeFamiTF106475.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR022255. DUF3776.
    IPR002999. Tudor.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF12618. DUF3776. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00384. AT_hook. 1 hit.
    SM00249. PHD. 1 hit.
    SM00333. TUDOR. 2 hits.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS01359. ZF_PHD_1. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BLG0-1) [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

    MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GRVLIHFKRW     50
    NHRYDEWFCW DSPYLRPLEK IQLRKEGLHD EDGSSEFQIN QQVLACWSDC 100
    RFYPARVTAV NKDGTYTVKF YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE 150
    TDHKSLSSSP EKREKFKEQR KVTVNVKKDK VEKALKTEKR PKQPDKEGKL 200
    ICSEKGKVSE KSLPKNEKED KENISENERE YSGDAQVEKK PEKDLVKNPQ 250
    ENLKEPKRKR GRPPSITPTA VDSNSQTLQP ITLELRRRKI SKRSDTPLKR 300
    PRLDKNSPQE QSKKRSENSD KDLSRRRSSR LSTNGTREIL DPDSIVPDLV 350
    HTVDTNPLPD KSPSAKDSAE GQLKSPLEAG QVSSALTCHP IGDGLGAADL 400
    ELNCKSMGEN TMKTEPVSPL AEVQEVSTVE VPNTLKKVDD SVTLNVPAVD 450
    LDHKFRCKVL DCLKFFRKAK LLHYHMKYFH GMEKSPEPEE GPGKTHVQTR 500
    GSAVPDKTSQ ESLTRKRVSA SSPTAKEKEK TKEKKFKELV RVKPKKKKKK 550
    KKKTKPECPC SEDISDTSQE PSPPKTFAVT RCGSSHKPGV HMSPQLHGSD 600
    NGNHKGKLKT CEEDNLSESS SESFLWSDEE YGQDVDVTTN PDEELEGDDR 650
    YDFEVVRCIC EVQEENDFMI QCEECQCWQH GVCMGLLEEN VPEKYTCYVC 700
    QDPPGQRPGF KYWYDKEWLS RGHMHGLAFL DQNYSHQNAR KIVATHQLLG 750
    DVQRVIQVLH GLQLKMSILQ SREHPDLQLW CQPWKQHSGE GRAHPRHIHI 800
    TDARSEESPS YRTLNGAVEK PSPLPRSVEE SYITSEHCYQ KPRAYYPAVE 850
    QRLVVETRGS ALDAAVSPLC ENGDDSLSPR LGWPIDQDRS RGDIDPKPSS 900
    PKVREYISKN VLPEETPARK LLDRGGEGLV SSQHQWQFNL LTHVESLQDE 950
    VTHRMDSIEK ELDVLESWLD YTGELEPPEP LARLPQLKHC IKQLLTDLGK 1000
    VQQIALCCST 1010
    Length:1,010
    Mass (Da):115,280
    Last modified:July 11, 2003 - v2
    Checksum:i2BC32811A520342D
    GO
    Isoform 2 (identifier: Q8BLG0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-28: MTKHPPNRRGISFEVGAQLEARDRLKNW → GAARTVLLSVGLERRSRSGAVR

    Note: Incomplete sequence. No experimental confirmation available.

    Show »
    Length:1,004
    Mass (Da):114,284
    Checksum:iF5D70ABE4C5CC87B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti817 – 8171A → T in AAH11337. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828MTKHP…RLKNW → GAARTVLLSVGLERRSRSGA VR in isoform 2. CuratedVSP_007762Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033017 mRNA. Translation: BAC28129.1.
    AK038573 mRNA. Translation: BAC30050.2.
    AK045309 mRNA. Translation: BAC32304.1.
    BC011337 mRNA. Translation: AAH11337.1.
    CCDSiCCDS38297.1. [Q8BLG0-1]
    RefSeqiNP_766262.2. NM_172674.2. [Q8BLG0-1]
    UniGeneiMm.427078.

    Genome annotation databases

    EnsembliENSMUST00000037401; ENSMUSP00000043138; ENSMUSG00000038116. [Q8BLG0-1]
    GeneIDi228829.
    KEGGimmu:228829.
    UCSCiuc008nmy.1. mouse. [Q8BLG0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033017 mRNA. Translation: BAC28129.1 .
    AK038573 mRNA. Translation: BAC30050.2 .
    AK045309 mRNA. Translation: BAC32304.1 .
    BC011337 mRNA. Translation: AAH11337.1 .
    CCDSi CCDS38297.1. [Q8BLG0-1 ]
    RefSeqi NP_766262.2. NM_172674.2. [Q8BLG0-1 ]
    UniGenei Mm.427078.

    3D structure databases

    ProteinModelPortali Q8BLG0.
    SMRi Q8BLG0. Positions 4-68, 85-137, 654-701.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230779. 7 interactions.

    PTM databases

    PhosphoSitei Q8BLG0.

    Proteomic databases

    PRIDEi Q8BLG0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000037401 ; ENSMUSP00000043138 ; ENSMUSG00000038116 . [Q8BLG0-1 ]
    GeneIDi 228829.
    KEGGi mmu:228829.
    UCSCi uc008nmy.1. mouse. [Q8BLG0-1 ]

    Organism-specific databases

    CTDi 51230.
    MGIi MGI:2444148. Phf20.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00390000006451.
    HOGENOMi HOG000231997.
    HOVERGENi HBG053586.
    OMAi ENTMKTE.
    OrthoDBi EOG7RZ5PD.
    PhylomeDBi Q8BLG0.
    TreeFami TF106475.

    Enzyme and pathway databases

    Reactomei REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi PHF20. mouse.
    NextBioi 379182.
    PROi Q8BLG0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BLG0.
    Bgeei Q8BLG0.
    CleanExi MM_PHF20.
    Genevestigatori Q8BLG0.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR022255. DUF3776.
    IPR002999. Tudor.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF12618. DUF3776. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00384. AT_hook. 1 hit.
    SM00249. PHD. 1 hit.
    SM00333. TUDOR. 2 hits.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS01359. ZF_PHD_1. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Embryo and Hypothalamus.
    2. "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] OF 621-1010.
      Tissue: Mammary gland.
    3. "Loss of the methyl-lysine effector molecule PHF20 impacts the expression of genes regulated by the lysine acetyltransferase MOF."
      Badeaux A.I., Yang Y., Cardenas K., Vemulapalli V., Chen K., Kusewitt D., Richie E., Li W., Bedford M.T.
      J. Biol. Chem. 287:429-437(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TUDOR DOMAINS, MUTAGENESIS OF TRP-97 AND TYR-103, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPHF20_MOUSE
    AccessioniPrimary (citable) accession number: Q8BLG0
    Secondary accession number(s): Q8BMA2, Q8BYR4, Q921N1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: July 11, 2003
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3