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Q9BVI0

- PHF20_HUMAN

UniProt

Q9BVI0 - PHF20_HUMAN

Protein

PHD finger protein 20

Gene

PHF20

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 (11 Jul 2003)
      Previous versions | rss
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    Functioni

    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 By similarity. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.By similarity2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi257 – 26913A.T hookAdd
    BLAST
    Zinc fingeri452 – 47726C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri654 – 70047PHD-typeAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H4-K16 acetylation Source: UniProtKB
    3. histone H4-K5 acetylation Source: UniProtKB
    4. histone H4-K8 acetylation Source: UniProtKB
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. 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_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PHD finger protein 20
    Alternative name(s):
    Glioma-expressed antigen 2
    Hepatocellular carcinoma-associated antigen 58
    Novel zinc finger protein
    Transcription factor TZP
    Gene namesi
    Name:PHF20
    Synonyms:C20orf104, GLEA2, HCA58, NZF, TZP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16098. PHF20.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. histone acetyltransferase complex Source: UniProtKB
    3. MLL1 complex Source: UniProtKB
    4. nuclear membrane Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi96 – 961C → S: Abolishes homodimerization. 1 Publication
    Mutagenesisi97 – 971W → A: Abolishes interaction with methylated p53. 1 Publication
    Mutagenesisi100 – 1001C → S: Abolishes homodimerization. 1 Publication
    Mutagenesisi103 – 1031Y → A: Abolishes interaction with methylated p53. 1 Publication

    Organism-specific databases

    PharmGKBiPA25644.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10121012PHD finger protein 20PRO_0000059310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi96 – 96Interchain (with C-100)1 Publication
    Disulfide bondi100 – 100Interchain (with C-96)1 Publication
    Modified residuei159 – 1591Phosphoserine1 Publication
    Modified residuei843 – 8431N6-acetyllysine1 Publication
    Modified residuei878 – 8781Phosphoserine2 Publications
    Modified residuei880 – 8801Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BVI0.
    PaxDbiQ9BVI0.
    PRIDEiQ9BVI0.

    PTM databases

    PhosphoSiteiQ9BVI0.

    Expressioni

    Tissue specificityi

    Expressed in heart, kidney, liver, lung, pancreas, placenta, spleen and testis. Not expressed in brain, skeletal muscle, colon, ovary, prostate, small intestine and thymus. Expressed in colon and ovary cancer cell lines while it is not expressed in the respective normal tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9BVI0.
    BgeeiQ9BVI0.
    CleanExiHS_PHF20.
    GenevestigatoriQ9BVI0.

    Organism-specific databases

    HPAiHPA029619.
    HPA029620.
    HPA029621.

    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, KAT8/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 HCFC1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST1H3DP684316EBI-2560802,EBI-79722
    HIST2H4BP628053EBI-2560802,EBI-302023

    Protein-protein interaction databases

    BioGridi119393. 10 interactions.
    IntActiQ9BVI0. 6 interactions.
    MINTiMINT-2829252.

    Structurei

    Secondary structure

    1
    1012
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 225
    Beta strandi28 – 3710
    Turni38 – 414
    Beta strandi42 – 476
    Helixi52 – 543
    Beta strandi56 – 594
    Beta strandi92 – 965
    Beta strandi102 – 1109
    Beta strandi114 – 1207
    Beta strandi125 – 1295
    Helixi130 – 1323
    Beta strandi133 – 1353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LDMNMR-A84-147[»]
    3P8DX-ray2.00A/B84-147[»]
    3Q1JX-ray2.35A4-69[»]
    3QIIX-ray2.30A83-150[»]
    3SD4X-ray1.93A/B4-69[»]
    ProteinModelPortaliQ9BVI0.
    SMRiQ9BVI0. Positions 4-68, 85-137, 651-698.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BVI0.

    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 – 22160Lys-richAdd
    BLAST
    Compositional biasi523 – 55230Lys-richAdd
    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.

    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 fingeri452 – 47726C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri654 – 70047PHD-typeAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOVERGENiHBG053586.
    InParanoidiQ9BVI0.
    OMAiENTMKTE.
    OrthoDBiEOG7RZ5PD.
    PhylomeDBiQ9BVI0.
    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: Q9BVI0-1) [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 GKVLIHFKRW     50
    NHRYDEWFCW DSPYLRPLEK IQLRKEGLHE EDGSSEFQIN EQVLACWSDC 100
    RFYPAKVTAV NKDGTYTVKF YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE 150
    TDHKSLSSSP DKREKFKEQR KATVNVKKDK EDKPLKTEKR PKQPDKEGKL 200
    ICSEKGKVSE KSLPKNEKED KENISENDRE YSGDAQVDKK PENDIVKSPQ 250
    ENLREPKRKR GRPPSIAPTA VDSNSQTLQP ITLELRRRKI SKGCEVPLKR 300
    PRLDKNSSQE KSKNYSENTD KDLSRRRSSR LSTNGTHEIL DPDLVVSDLV 350
    DTDPLQDTLS STKESEEGQL KSALEAGQVS SALTCHSFGD GSGAAGLELN 400
    CPSMGENTMK TEPTSPLVEL QEISTVEVTN TFKKTDDFGS SNAPAVDLDH 450
    KFRCKVVDCL KFFRKAKLLH YHMKYFHGME KSLEPEESPG KRHVQTRGPS 500
    ASDKPSQETL TRKRVSASSP TTKDKEKNKE KKFKEFVRVK PKKKKKKKKK 550
    TKPECPCSEE ISDTSQEPSP PKAFAVTRCG SSHKPGVHMS PQLHGPESGH 600
    HKGKVKALEE DNLSESSSES FLWSDDEYGQ DVDVTTNPDE ELDGDDRYDF 650
    EVVRCICEVQ EENDFMIQCE ECQCWQHGVC MGLLEENVPE KYTCYVCQDP 700
    PGQRPGFKYW YDKEWLSRGH MHGLAFLEEN YSHQNAKKIV ATHQLLGDVQ 750
    RVIEVLHGLQ LKMSILQSRE HPDLPLWCQP WKQHSGEGRS HFRNIPVTDT 800
    RSKEEAPSYR TLNGAVEKPR PLALPLPRSV EESYITSEHC YQKPRAYYPA 850
    VEQKLVVETR GSALDDAVNP LHENGDDSLS PRLGWPLDQD RSKGDSDPKP 900
    GSPKVKEYVS KKALPEEAPA RKLLDRGGEG LLSSQHQWQF NLLTHVESLQ 950
    DEVTHRMDSI EKELDVLESW LDYTGELEPP EPLARLPQLK HCIKQLLMDL 1000
    GKVQQIALCC ST 1012
    Length:1,012
    Mass (Da):115,386
    Last modified:July 11, 2003 - v2
    Checksum:i1CDBADC23D007503
    GO
    Isoform 2 (identifier: Q9BVI0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         237-273: VDKKPENDIVKSPQENLREPKRKRGRPPSIAPTAVDS → KTRQTPFHSSYCCGFKLSNFATNNIGTEKKENIKRM
         274-1012: Missing.

    Show »
    Length:272
    Mass (Da):31,856
    Checksum:i11C579B3C0050A12
    GO

    Sequence cautioni

    The sequence AAF34184.1 differs from that shown. Reason: Frameshift at position 260.
    The sequence AAK19748.1 differs from that shown. Reason: Frameshift at positions 635, 653 and 655.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2222KE → QG in AAG49888. (PubMed:11703362)Curated
    Sequence conflicti226 – 2261E → G in AAG49888. (PubMed:11703362)Curated
    Sequence conflicti372 – 3721S → F in AAH80598. (PubMed:15489334)Curated
    Sequence conflicti516 – 5161S → F in AAG49888. (PubMed:11703362)Curated
    Sequence conflicti532 – 5321K → E in BAG37103. (PubMed:14702039)Curated
    Sequence conflicti671 – 6711E → G in BAG37103. (PubMed:14702039)Curated
    Isoform 2 (identifier: Q9BVI0-2)
    Sequence conflicti237 – 2393KTR → KKTS in AAF34184. (PubMed:12097419)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti605 – 6051V → M.1 Publication
    Corresponds to variant rs17431878 [ dbSNP | Ensembl ].
    VAR_051600

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei237 – 27337VDKKP…TAVDS → KTRQTPFHSSYCCGFKLSNF ATNNIGTEKKENIKRM in isoform 2. 1 PublicationVSP_007760Add
    BLAST
    Alternative sequencei274 – 1012739Missing in isoform 2. 1 PublicationVSP_007761Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220416 mRNA. Translation: AAF34184.1. Frameshift.
    AF348207 mRNA. Translation: AAK19748.1. Frameshift.
    AY027523 mRNA. Translation: AAK13046.1.
    AK314503 mRNA. Translation: BAG37103.1.
    AL109965, AL078461 Genomic DNA. Translation: CAI19247.1.
    AL078461, AL109965 Genomic DNA. Translation: CAI43145.1.
    CH471077 Genomic DNA. Translation: EAW76153.1.
    CH471077 Genomic DNA. Translation: EAW76155.1.
    CH471077 Genomic DNA. Translation: EAW76156.1.
    CH471077 Genomic DNA. Translation: EAW76157.1.
    BC048210 mRNA. Translation: AAH48210.1.
    BC080598 mRNA. Translation: AAH80598.1.
    BC093405 mRNA. Translation: AAH93405.1.
    BC150178 mRNA. Translation: AAI50179.1.
    AF258787 mRNA. Translation: AAG49888.1.
    CCDSiCCDS13268.1. [Q9BVI0-1]
    RefSeqiNP_057520.2. NM_016436.4. [Q9BVI0-1]
    UniGeneiHs.517044.

    Genome annotation databases

    EnsembliENST00000374012; ENSP00000363124; ENSG00000025293. [Q9BVI0-1]
    ENST00000439301; ENSP00000410373; ENSG00000025293. [Q9BVI0-2]
    GeneIDi51230.
    KEGGihsa:51230.
    UCSCiuc002xei.1. human. [Q9BVI0-1]

    Polymorphism databases

    DMDMi32699605.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220416 mRNA. Translation: AAF34184.1 . Frameshift.
    AF348207 mRNA. Translation: AAK19748.1 . Frameshift.
    AY027523 mRNA. Translation: AAK13046.1 .
    AK314503 mRNA. Translation: BAG37103.1 .
    AL109965 , AL078461 Genomic DNA. Translation: CAI19247.1 .
    AL078461 , AL109965 Genomic DNA. Translation: CAI43145.1 .
    CH471077 Genomic DNA. Translation: EAW76153.1 .
    CH471077 Genomic DNA. Translation: EAW76155.1 .
    CH471077 Genomic DNA. Translation: EAW76156.1 .
    CH471077 Genomic DNA. Translation: EAW76157.1 .
    BC048210 mRNA. Translation: AAH48210.1 .
    BC080598 mRNA. Translation: AAH80598.1 .
    BC093405 mRNA. Translation: AAH93405.1 .
    BC150178 mRNA. Translation: AAI50179.1 .
    AF258787 mRNA. Translation: AAG49888.1 .
    CCDSi CCDS13268.1. [Q9BVI0-1 ]
    RefSeqi NP_057520.2. NM_016436.4. [Q9BVI0-1 ]
    UniGenei Hs.517044.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LDM NMR - A 84-147 [» ]
    3P8D X-ray 2.00 A/B 84-147 [» ]
    3Q1J X-ray 2.35 A 4-69 [» ]
    3QII X-ray 2.30 A 83-150 [» ]
    3SD4 X-ray 1.93 A/B 4-69 [» ]
    ProteinModelPortali Q9BVI0.
    SMRi Q9BVI0. Positions 4-68, 85-137, 651-698.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119393. 10 interactions.
    IntActi Q9BVI0. 6 interactions.
    MINTi MINT-2829252.

    PTM databases

    PhosphoSitei Q9BVI0.

    Polymorphism databases

    DMDMi 32699605.

    Proteomic databases

    MaxQBi Q9BVI0.
    PaxDbi Q9BVI0.
    PRIDEi Q9BVI0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374012 ; ENSP00000363124 ; ENSG00000025293 . [Q9BVI0-1 ]
    ENST00000439301 ; ENSP00000410373 ; ENSG00000025293 . [Q9BVI0-2 ]
    GeneIDi 51230.
    KEGGi hsa:51230.
    UCSCi uc002xei.1. human. [Q9BVI0-1 ]

    Organism-specific databases

    CTDi 51230.
    GeneCardsi GC20P034359.
    HGNCi HGNC:16098. PHF20.
    HPAi HPA029619.
    HPA029620.
    HPA029621.
    MIMi 610335. gene.
    neXtProti NX_Q9BVI0.
    PharmGKBi PA25644.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG053586.
    InParanoidi Q9BVI0.
    OMAi ENTMKTE.
    OrthoDBi EOG7RZ5PD.
    PhylomeDBi Q9BVI0.
    TreeFami TF106475.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi PHF20. human.
    EvolutionaryTracei Q9BVI0.
    GeneWikii PHF20.
    GenomeRNAii 51230.
    NextBioi 54328.
    PROi Q9BVI0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BVI0.
    Bgeei Q9BVI0.
    CleanExi HS_PHF20.
    Genevestigatori Q9BVI0.

    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. "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
      Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
      J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, IDENTIFICATION AS ANTIGEN IN HEPATOCELLULAR CARCINOMA.
      Tissue: Hepatoma.
    2. "Cloning and characterization of a novel transcription factor (TZP)."
      Cheng J.Q., Kaneko S., Dan H.C., Testa J.R.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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].
      Tissue: Trachea.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), VARIANT MET-605.
      Tissue: Brain, Eye and Lymph.
    7. "Glioma-expressed antigen 2 (GLEA2): a novel protein that can elicit immune responses in glioblastoma patients and some controls."
      Fischer U., Struss A.-K., Hemmer D., Pallasch C.P., Steudel W.-I., Meese E.
      Clin. Exp. Immunol. 126:206-213(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-543 (ISOFORM 1), IDENTIFICATION AS ANTIGEN IN GLIOBLASTOMA.
      Tissue: Glioblastoma.
    8. Cited for: IDENTIFICATION AS ANTIGEN IN CHILDHOOD MEDULLOBLASTOMA.
    9. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-843, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
      Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins."
      Adams-Cioaba M.A., Li Z., Tempel W., Guo Y., Bian C., Li Y., Lam R., Min J.
      FEBS Lett. 586:859-865(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 4-69 AND 84-147 AND TUDOR DOMAINS.
    17. "PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53."
      Cui G., Park S., Badeaux A.I., Kim D., Lee J., Thompson J.R., Yan F., Kaneko S., Yuan Z., Botuyan M.V., Bedford M.T., Cheng J.Q., Mer G.
      Nat. Struct. Mol. Biol. 19:916-924(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-69 AND 84-147, STRUCTURE BY NMR OF 84-147 IN COMPLEX WITH DIMETHYLATED P53 PEPTIDE, FUNCTION, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-96; TRP-97; CYS-100 AND TYR-103.

    Entry informationi

    Entry nameiPHF20_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVI0
    Secondary accession number(s): A7E235
    , B2RB56, E1P5S3, Q566Q2, Q5JWY9, Q66K49, Q9BWV4, Q9BXA3, Q9BZW3, Q9H421, Q9H4J6, Q9NZ22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: July 11, 2003
    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

    Miscellaneous

    Antibodies against PHF20 are present in sera from patients with hepatocellular carcinoma, glioblastoma and childhood medulloblastula.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3