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Q8BLG0

- PHF20_MOUSE

UniProt

Q8BLG0 - PHF20_MOUSE

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Protein

PHD finger protein 20

Gene

Phf20

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. cytoplasm Source: Ensembl
  2. histone acetyltransferase complex Source: UniProtKB
  3. MLL1 complex Source: UniProtKB
  4. nuclear membrane Source: Ensembl
Complete GO annotation...

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

MaxQBiQ8BLG0.
PRIDEiQ8BLG0.

PTM databases

PhosphoSiteiQ8BLG0.

Expressioni

Gene expression databases

BgeeiQ8BLG0.
CleanExiMM_PHF20.
ExpressionAtlasiQ8BLG0. baseline and differential.
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.
InParanoidiQ8BLG0.
KOiK18402.
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

        10         20         30         40         50
MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GRVLIHFKRW
60 70 80 90 100
NHRYDEWFCW DSPYLRPLEK IQLRKEGLHD EDGSSEFQIN QQVLACWSDC
110 120 130 140 150
RFYPARVTAV NKDGTYTVKF YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE
160 170 180 190 200
TDHKSLSSSP EKREKFKEQR KVTVNVKKDK VEKALKTEKR PKQPDKEGKL
210 220 230 240 250
ICSEKGKVSE KSLPKNEKED KENISENERE YSGDAQVEKK PEKDLVKNPQ
260 270 280 290 300
ENLKEPKRKR GRPPSITPTA VDSNSQTLQP ITLELRRRKI SKRSDTPLKR
310 320 330 340 350
PRLDKNSPQE QSKKRSENSD KDLSRRRSSR LSTNGTREIL DPDSIVPDLV
360 370 380 390 400
HTVDTNPLPD KSPSAKDSAE GQLKSPLEAG QVSSALTCHP IGDGLGAADL
410 420 430 440 450
ELNCKSMGEN TMKTEPVSPL AEVQEVSTVE VPNTLKKVDD SVTLNVPAVD
460 470 480 490 500
LDHKFRCKVL DCLKFFRKAK LLHYHMKYFH GMEKSPEPEE GPGKTHVQTR
510 520 530 540 550
GSAVPDKTSQ ESLTRKRVSA SSPTAKEKEK TKEKKFKELV RVKPKKKKKK
560 570 580 590 600
KKKTKPECPC SEDISDTSQE PSPPKTFAVT RCGSSHKPGV HMSPQLHGSD
610 620 630 640 650
NGNHKGKLKT CEEDNLSESS SESFLWSDEE YGQDVDVTTN PDEELEGDDR
660 670 680 690 700
YDFEVVRCIC EVQEENDFMI QCEECQCWQH GVCMGLLEEN VPEKYTCYVC
710 720 730 740 750
QDPPGQRPGF KYWYDKEWLS RGHMHGLAFL DQNYSHQNAR KIVATHQLLG
760 770 780 790 800
DVQRVIQVLH GLQLKMSILQ SREHPDLQLW CQPWKQHSGE GRAHPRHIHI
810 820 830 840 850
TDARSEESPS YRTLNGAVEK PSPLPRSVEE SYITSEHCYQ KPRAYYPAVE
860 870 880 890 900
QRLVVETRGS ALDAAVSPLC ENGDDSLSPR LGWPIDQDRS RGDIDPKPSS
910 920 930 940 950
PKVREYISKN VLPEETPARK LLDRGGEGLV SSQHQWQFNL LTHVESLQDE
960 970 980 990 1000
VTHRMDSIEK ELDVLESWLD YTGELEPPEP LARLPQLKHC IKQLLTDLGK
1010
VQQIALCCST
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

MaxQBi Q8BLG0.
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.
InParanoidi Q8BLG0.
KOi K18402.
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

Bgeei Q8BLG0.
CleanExi MM_PHF20.
ExpressionAtlasi Q8BLG0. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 107 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