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Q8BLG0 (PHF20_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PHD finger protein 20
Alternative name(s):
Hepatocellular carcinoma-associated antigen 58 homolog
Gene names
Name:Phf20
Synonyms:Hca58
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1010 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

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.

Subcellular location

Nucleus Ref.3.

Domain

The Tudor domain 2 mediates reading of dimethyl-lysine residues. Ref.3

The Tudor domain 1 doesn't bind dimethyl-lysine residues, due to an atypical and occluded aromatic cage By similarity. Ref.3

Disruption phenotype

Mice die shortly after birth and display a wide variety of phenotypes within the skeletal and hematopoietic systems. Ref.3

Sequence similarities

Contains 1 A.T hook DNA-binding domain.

Contains 1 C2H2-type zinc finger.

Contains 1 PHD-type zinc finger.

Contains 2 Tudor domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H4-K16 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K5 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K8 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone acetyltransferase activity (H4-K16 specific)

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity (H4-K5 specific)

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity (H4-K8 specific)

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BLG0-1)

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.
Isoform 2 (identifier: Q8BLG0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MTKHPPNRRGISFEVGAQLEARDRLKNW → GAARTVLLSVGLERRSRSGAVR
Note: Incomplete sequence. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10101010PHD finger protein 20
PRO_0000059311

Regions

Domain4 – 6966Tudor 1
Domain83 – 14765Tudor 2
DNA binding257 – 26913A.T hook
Zinc finger455 – 48531C2H2-type
Zinc finger657 – 70347PHD-type
Compositional bias162 – 25998Lys-rich
Compositional bias526 – 55530Lys-rich
Compositional bias543 – 55513Poly-Lys

Amino acid modifications

Modified residue1591Phosphoserine By similarity
Modified residue8411N6-acetyllysine By similarity
Modified residue8761Phosphoserine By similarity
Modified residue8781Phosphoserine By similarity
Disulfide bond96Interchain (with C-100) By similarity
Disulfide bond100Interchain (with C-96) By similarity

Natural variations

Alternative sequence1 – 2828MTKHP…RLKNW → GAARTVLLSVGLERRSRSGA VR in isoform 2.
VSP_007762

Experimental info

Mutagenesis971W → A: Abolishes Methyllysine-binding. Ref.3
Mutagenesis1031Y → A: Abolishes Methyllysine-binding. Ref.3
Sequence conflict8171A → T in AAH11337. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 11, 2003. Version 2.
Checksum: 2BC32811A520342D

FASTA1,010115,280
        10         20         30         40         50         60 
MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GRVLIHFKRW NHRYDEWFCW 

        70         80         90        100        110        120 
DSPYLRPLEK IQLRKEGLHD EDGSSEFQIN QQVLACWSDC RFYPARVTAV NKDGTYTVKF 

       130        140        150        160        170        180 
YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE TDHKSLSSSP EKREKFKEQR KVTVNVKKDK 

       190        200        210        220        230        240 
VEKALKTEKR PKQPDKEGKL ICSEKGKVSE KSLPKNEKED KENISENERE YSGDAQVEKK 

       250        260        270        280        290        300 
PEKDLVKNPQ ENLKEPKRKR GRPPSITPTA VDSNSQTLQP ITLELRRRKI SKRSDTPLKR 

       310        320        330        340        350        360 
PRLDKNSPQE QSKKRSENSD KDLSRRRSSR LSTNGTREIL DPDSIVPDLV HTVDTNPLPD 

       370        380        390        400        410        420 
KSPSAKDSAE GQLKSPLEAG QVSSALTCHP IGDGLGAADL ELNCKSMGEN TMKTEPVSPL 

       430        440        450        460        470        480 
AEVQEVSTVE VPNTLKKVDD SVTLNVPAVD LDHKFRCKVL DCLKFFRKAK LLHYHMKYFH 

       490        500        510        520        530        540 
GMEKSPEPEE GPGKTHVQTR GSAVPDKTSQ ESLTRKRVSA SSPTAKEKEK TKEKKFKELV 

       550        560        570        580        590        600 
RVKPKKKKKK KKKTKPECPC SEDISDTSQE PSPPKTFAVT RCGSSHKPGV HMSPQLHGSD 

       610        620        630        640        650        660 
NGNHKGKLKT CEEDNLSESS SESFLWSDEE YGQDVDVTTN PDEELEGDDR YDFEVVRCIC 

       670        680        690        700        710        720 
EVQEENDFMI QCEECQCWQH GVCMGLLEEN VPEKYTCYVC QDPPGQRPGF KYWYDKEWLS 

       730        740        750        760        770        780 
RGHMHGLAFL DQNYSHQNAR KIVATHQLLG DVQRVIQVLH GLQLKMSILQ SREHPDLQLW 

       790        800        810        820        830        840 
CQPWKQHSGE GRAHPRHIHI TDARSEESPS YRTLNGAVEK PSPLPRSVEE SYITSEHCYQ 

       850        860        870        880        890        900 
KPRAYYPAVE QRLVVETRGS ALDAAVSPLC ENGDDSLSPR LGWPIDQDRS RGDIDPKPSS 

       910        920        930        940        950        960 
PKVREYISKN VLPEETPARK LLDRGGEGLV SSQHQWQFNL LTHVESLQDE VTHRMDSIEK 

       970        980        990       1000       1010 
ELDVLESWLD YTGELEPPEP LARLPQLKHC IKQLLTDLGK VQQIALCCST 

« Hide

Isoform 2 [UniParc].

Checksum: F5D70ABE4C5CC87B
Show »

FASTA1,004114,284

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK033017 mRNA. Translation: BAC28129.1.
AK038573 mRNA. Translation: BAC30050.2.
AK045309 mRNA. Translation: BAC32304.1.
BC011337 mRNA. Translation: AAH11337.1.
CCDSCCDS38297.1. [Q8BLG0-1]
RefSeqNP_766262.2. NM_172674.2. [Q8BLG0-1]
UniGeneMm.427078.

3D structure databases

ProteinModelPortalQ8BLG0.
SMRQ8BLG0. Positions 4-68, 85-137, 654-701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230779. 7 interactions.

PTM databases

PhosphoSiteQ8BLG0.

Proteomic databases

PRIDEQ8BLG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037401; ENSMUSP00000043138; ENSMUSG00000038116. [Q8BLG0-1]
GeneID228829.
KEGGmmu:228829.
UCSCuc008nmy.1. mouse. [Q8BLG0-1]

Organism-specific databases

CTD51230.
MGIMGI:2444148. Phf20.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00390000006451.
HOGENOMHOG000231997.
HOVERGENHBG053586.
OMAENTMKTE.
OrthoDBEOG7RZ5PD.
PhylomeDBQ8BLG0.
TreeFamTF106475.

Gene expression databases

ArrayExpressQ8BLG0.
BgeeQ8BLG0.
CleanExMM_PHF20.
GenevestigatorQ8BLG0.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR017956. 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]
PfamPF12618. DUF3776. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00384. AT_hook. 1 hit.
SM00249. PHD. 1 hit.
SM00333. TUDOR. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS01359. ZF_PHD_1. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHF20. mouse.
NextBio379182.
PROQ8BLG0.
SOURCESearch...

Entry information

Entry namePHF20_MOUSE
AccessionPrimary (citable) accession number: Q8BLG0
Secondary accession number(s): Q8BMA2, Q8BYR4, Q921N1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: July 11, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot