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Q9BVI0 (PHF20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Glioma-expressed antigen 2
Hepatocellular carcinoma-associated antigen 58
Novel zinc finger protein
Transcription factor TZP
Gene names
Name:PHF20
Synonyms:C20orf104, GLEA2, HCA58, NZF, TZP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.17

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, 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. Ref.9 Ref.13 Ref.17

Subcellular location

Nucleus Ref.13.

Tissue specificity

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. Ref.1

Domain

The Tudor domain 2 mediates reading of dimethyl-lysine residues. Ref.16

The Tudor domain 1 doesn't bind dimethyl-lysine residues, due to an atypical and occluded aromatic cage. Ref.16

Miscellaneous

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

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.

Sequence caution

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST1H3DP684316EBI-2560802,EBI-79722
HIST2H4BP628053EBI-2560802,EBI-302023

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BVI0-1)

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: Q9BVI0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10121012PHD finger protein 20
PRO_0000059310

Regions

Domain4 – 6966Tudor 1
Domain83 – 14765Tudor 2
DNA binding257 – 26913A.T hook
Zinc finger452 – 47726C2H2-type
Zinc finger654 – 70047PHD-type
Compositional bias162 – 22160Lys-rich
Compositional bias523 – 55230Lys-rich

Amino acid modifications

Modified residue1591Phosphoserine Ref.15
Modified residue8431N6-acetyllysine Ref.12
Modified residue8781Phosphoserine Ref.10 Ref.11
Modified residue8801Phosphoserine Ref.10 Ref.11
Disulfide bond96Interchain (with C-100) Probable
Disulfide bond100Interchain (with C-96) Probable

Natural variations

Alternative sequence237 – 27337VDKKP…TAVDS → KTRQTPFHSSYCCGFKLSNF ATNNIGTEKKENIKRM in isoform 2.
VSP_007760
Alternative sequence274 – 1012739Missing in isoform 2.
VSP_007761
Natural variant6051V → M. Ref.6
Corresponds to variant rs17431878 [ dbSNP | Ensembl ].
VAR_051600

Experimental info

Mutagenesis961C → S: Abolishes homodimerization. Ref.17
Mutagenesis971W → A: Abolishes interaction with methylated p53. Ref.17
Mutagenesis1001C → S: Abolishes homodimerization. Ref.17
Mutagenesis1031Y → A: Abolishes interaction with methylated p53. Ref.17
Sequence conflict221 – 2222KE → QG in AAG49888. Ref.7
Sequence conflict2261E → G in AAG49888. Ref.7
Sequence conflict3721S → F in AAH80598. Ref.6
Sequence conflict5161S → F in AAG49888. Ref.7
Sequence conflict5321K → E in BAG37103. Ref.3
Sequence conflict6711E → G in BAG37103. Ref.3
Isoform 2:
Sequence conflict237 – 2393KTR → KKTS in AAF34184. Ref.1

Secondary structure

..................... 1012
Helix Strand Turn

Details...

Sequences

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

Last modified July 11, 2003. Version 2.
Checksum: 1CDBADC23D007503

FASTA1,012115,386
        10         20         30         40         50         60 
MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GKVLIHFKRW NHRYDEWFCW 

        70         80         90        100        110        120 
DSPYLRPLEK IQLRKEGLHE EDGSSEFQIN EQVLACWSDC RFYPAKVTAV NKDGTYTVKF 

       130        140        150        160        170        180 
YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE TDHKSLSSSP DKREKFKEQR KATVNVKKDK 

       190        200        210        220        230        240 
EDKPLKTEKR PKQPDKEGKL ICSEKGKVSE KSLPKNEKED KENISENDRE YSGDAQVDKK 

       250        260        270        280        290        300 
PENDIVKSPQ ENLREPKRKR GRPPSIAPTA VDSNSQTLQP ITLELRRRKI SKGCEVPLKR 

       310        320        330        340        350        360 
PRLDKNSSQE KSKNYSENTD KDLSRRRSSR LSTNGTHEIL DPDLVVSDLV DTDPLQDTLS 

       370        380        390        400        410        420 
STKESEEGQL KSALEAGQVS SALTCHSFGD GSGAAGLELN CPSMGENTMK TEPTSPLVEL 

       430        440        450        460        470        480 
QEISTVEVTN TFKKTDDFGS SNAPAVDLDH KFRCKVVDCL KFFRKAKLLH YHMKYFHGME 

       490        500        510        520        530        540 
KSLEPEESPG KRHVQTRGPS ASDKPSQETL TRKRVSASSP TTKDKEKNKE KKFKEFVRVK 

       550        560        570        580        590        600 
PKKKKKKKKK TKPECPCSEE ISDTSQEPSP PKAFAVTRCG SSHKPGVHMS PQLHGPESGH 

       610        620        630        640        650        660 
HKGKVKALEE DNLSESSSES FLWSDDEYGQ DVDVTTNPDE ELDGDDRYDF EVVRCICEVQ 

       670        680        690        700        710        720 
EENDFMIQCE ECQCWQHGVC MGLLEENVPE KYTCYVCQDP PGQRPGFKYW YDKEWLSRGH 

       730        740        750        760        770        780 
MHGLAFLEEN YSHQNAKKIV ATHQLLGDVQ RVIEVLHGLQ LKMSILQSRE HPDLPLWCQP 

       790        800        810        820        830        840 
WKQHSGEGRS HFRNIPVTDT RSKEEAPSYR TLNGAVEKPR PLALPLPRSV EESYITSEHC 

       850        860        870        880        890        900 
YQKPRAYYPA VEQKLVVETR GSALDDAVNP LHENGDDSLS PRLGWPLDQD RSKGDSDPKP 

       910        920        930        940        950        960 
GSPKVKEYVS KKALPEEAPA RKLLDRGGEG LLSSQHQWQF NLLTHVESLQ DEVTHRMDSI 

       970        980        990       1000       1010 
EKELDVLESW LDYTGELEPP EPLARLPQLK HCIKQLLMDL GKVQQIALCC ST 

« Hide

Isoform 2 [UniParc].

Checksum: 11C579B3C0050A12
Show »

FASTA27231,856

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries."
Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., Asmuss H.-P., Bise K., Mautner J.
Int. J. Cancer 106:244-251(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_057520.2. NM_016436.4.
UniGeneHs.517044.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDMNMR-A84-147[»]
3P8DX-ray2.00A/B84-147[»]
3Q1JX-ray2.35A4-69[»]
3QIIX-ray2.30A83-150[»]
3SD4X-ray1.93A/B4-69[»]
ProteinModelPortalQ9BVI0.
SMRQ9BVI0. Positions 4-137, 651-806.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119393. 10 interactions.
IntActQ9BVI0. 6 interactions.
MINTMINT-2829252.

PTM databases

PhosphoSiteQ9BVI0.

Polymorphism databases

DMDM32699605.

Proteomic databases

PaxDbQ9BVI0.
PRIDEQ9BVI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374012; ENSP00000363124; ENSG00000025293. [Q9BVI0-1]
ENST00000439301; ENSP00000410373; ENSG00000025293. [Q9BVI0-2]
GeneID51230.
KEGGhsa:51230.
UCSCuc002xei.1. human. [Q9BVI0-1]

Organism-specific databases

CTD51230.
GeneCardsGC20P034359.
HGNCHGNC:16098. PHF20.
HPAHPA029619.
HPA029620.
HPA029621.
MIM610335. gene.
neXtProtNX_Q9BVI0.
PharmGKBPA25644.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG053586.
InParanoidQ9BVI0.
OMAENTMKTE.
OrthoDBEOG7RZ5PD.
PhylomeDBQ9BVI0.
TreeFamTF106475.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ9BVI0.
BgeeQ9BVI0.
CleanExHS_PHF20.
GenevestigatorQ9BVI0.

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. human.
EvolutionaryTraceQ9BVI0.
GeneWikiPHF20.
GenomeRNAi51230.
NextBio54328.
PROQ9BVI0.
SOURCESearch...

Entry information

Entry namePHF20_HUMAN
AccessionPrimary (citable) accession number: Q9BVI0
Secondary accession number(s): A7E235 expand/collapse secondary AC list , B2RB56, E1P5S3, Q566Q2, Q5JWY9, Q66K49, Q9BWV4, Q9BXA3, Q9BZW3, Q9H421, Q9H4J6, Q9NZ22
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: July 11, 2003
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM