O43189 (PHF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PHD finger protein 1
Short name=Protein PHF1
Short name=hPHF1

Alternative name(s):
Polycomb-like protein 1
Short name=hPCl1

Gene names

Name:	PHF1
Synonyms:	PCL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (Ref.8 and Ref.16). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (Ref.17). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. Ref.7 Ref.8 Ref.9 Ref.14 Ref.16 Ref.17
Subunit structure	Interacts with CHMP1 By similarity. Associated component of the PRC2 complex. Interacts with p53/TP53. Ref.7 Ref.8 Ref.14
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Note: Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Co-localizes with NEK6 in the centrosome. Ref.8 Ref.9 Ref.11 Ref.14 Ref.16 Ref.17
Tissue specificity	Highest levels in heart, skeletal muscle, and pancreas, lower levels in brain, placenta, lung, liver and kidney.
Domain	The Tudor domain recognizes and binds H3K36me3 (Ref.13, Ref.16 and Ref.17).
Involvement in disease	A chromosomal aberration involving PHF1 may be a cause of endometrial stromal tumors. Translocation t(6;7)(p21;p22) with JAZF1. Translocation t(1;6)(p34;p21) with MEAF6. Ref.6 Ref.12
Sequence similarities	Belongs to the Polycomblike family. Contains 2 PHD-type zinc fingers. Contains 1 Tudor domain.

Ontologies

Keywords
Biological process	DNA damage Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of histone H3-K27 methylation Inferred from mutant phenotype Ref.17. Source: UniProtKB positive regulation of histone H3-K27 methylation Inferred from mutant phenotype Ref.16. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay Ref.17. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.16. Source: UniProtKB site of double-strand break Inferred from direct assay Ref.17. Source: UniProtKB
Molecular_function	methylated histone residue binding Inferred from direct assay Ref.17Ref.16. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc 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 2 (identifier: O43189-1)

Also known as: PHF2;

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 1 (identifier: O43189-2)

Also known as: PHF1;

The sequence of this isoform differs from the canonical sequence as follows:
     350-457: SFPSGQGPGG...IRMFASFHPS → RAGPWGRGLT...QTSLKVPPTR
     458-567: Missing.

Note: Contains a phosphoserine at position 360.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 567

567

PHD finger protein 1

PRO_0000059288

Regions

Domain

29 – 86

58

Tudor

Zinc finger

87 – 142

56

PHD-type 1

Zinc finger

186 – 240

55

PHD-type 2

Natural variations

Alternative sequence

350 – 457

108

SFPSG…SFHPS → RAGPWGRGLTSPGEAPEAGA RAPEEEAEGESGGAGATLSS AQSARAPGAEGAGSSAEGTA AAPSGCLLPSTLLPAPQGPL GTVDPQTGHPWNFTLVSPQT SLKVPPTR in isoform 1.

VSP_004694

Alternative sequence

458 – 567

110

Missing in isoform 1.

VSP_004695

Natural variant

42

1

T → S.
Corresponds to variant rs6934613 [ dbSNP | Ensembl ].

VAR_044500

Natural variant

304

1

R → K. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs3116713 [ dbSNP | Ensembl ].

VAR_034382

Experimental info

Mutagenesis

41

1

W → A: Abolishes histone H3K36me3-binding and localization at double-strand breaks (DSBs). Ref.16 Ref.17

Mutagenesis

47

1

Y → A: Abolishes histone H3K36me3-binding. Ref.16 Ref.17

Mutagenesis

65

1

F → A: Abolishes histone H3K36me3-binding. Ref.16

Mutagenesis

66

1

E → K: Impairs histone H3K36me3-binding. Ref.16

Mutagenesis

71

1

F → A: Abolishes histone H3K36me3-binding. Ref.16

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

567

Helix Strand Turn

Details...

Beta strand

36 – 40

5

Beta strand

46 – 55

10

Turn

56 – 59

4

Beta strand

60 – 65

6

Turn

66 – 68

3

Beta strand

70 – 74

5

Helix

75 – 77

3

Beta strand

78 – 80

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (PHF2) [UniParc]. Last modified January 11, 2011. Version 3. Checksum: E81BA9475565957C	FASTA	567	62,106
	10 20 30 40 50 60 MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV 70 80 90 100 110 120 CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV 130 140 150 160 170 180 PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH 190 200 210 220 230 240 LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG 250 260 270 280 290 300 PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE 310 320 330 340 350 360 RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS FPSGQGPGGG 370 380 390 400 410 420 VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ EQRERAHLQR ALQASVSPPS 430 440 450 460 470 480 PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM FASFHPSAST AGTSGDSGPP DRSPLELHIG 490 500 510 520 530 540 FPTDIPKSAP HSMTASSSSV SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD 550 560 PVRVLARRVR PDGSVQYLVE WGGGGIF
	Isoform 1 (PHF1) [UniParc]. Checksum: 611EF2B5A416841C	FASTA	457	49,643
	10 20 30 40 50 60 MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV 70 80 90 100 110 120 CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV 130 140 150 160 170 180 PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH 190 200 210 220 230 240 LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG 250 260 270 280 290 300 PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE 310 320 330 340 350 360 RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTR AGPWGRGLTS 370 380 390 400 410 420 PGEAPEAGAR APEEEAEGES GGAGATLSSA QSARAPGAEG AGSSAEGTAA APSGCLLPST 430 440 450 LLPAPQGPLG TVDPQTGHPW NFTLVSPQTS LKVPPTR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The identification and localization of a human gene with sequence similarity to Polycomblike of Drosophila melanogaster." Coulson M., Robert S., Eyre H.J., Saint R. Genomics 48:381-383(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-304. Tissue: Placenta.
[2]	Wang J.H., Du G.W., Zhou Y., Yuan J.G., Qiang B.Q. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LYS-304.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-304.
[4]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-304.
[5]	"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 2), VARIANT LYS-304. Tissue: Uterus.
[6]	"Consistent rearrangement of chromosomal band 6p21 with generation of fusion genes JAZF1/PHF1 and EPC1/PHF1 in endometrial stromal sarcoma." Micci F., Panagopoulos I., Bjerkehagen B., Heim S. Cancer Res. 66:107-112(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH JAZF1.
[7]	"Role of hPHF1 in H3K27 methylation and Hox gene silencing." Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y. Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE PRC2 COMPLEX.
[8]	"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo." Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D. Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH THE PRC2 COMPLEX, SUBCELLULAR LOCATION.
[9]	"A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell." Hong Z., Jiang J., Lan L., Nakajima S., Kanno S., Koseki H., Yasui A. Nucleic Acids Res. 36:2939-2947(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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-360 (ISOFORM 1), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome." Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J. J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial stromal sarcoma." Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M., Bjerkehagen B., Davidson B., Heim S. PLoS ONE 7:E39354-E39354(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH MEAF6.
[13]	"Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3." Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J. Biochem. Biophys. Res. Commun. 430:547-553(2013) [PubMed] [Europe PMC] [Abstract] Cited for: H3K36ME3-BINDING.
[14]	"Polycomb group protein PHF1 regulates p53-dependent cell growth arrest and apoptosis." Yang Y., Wang C., Zhang P., Gao K., Wang D., Yu H., Zhang T., Jiang S., Hexige S., Hong Z., Yasui A., Liu J.O., Huang H., Yu L. J. Biol. Chem. 288:529-539(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
[15]	"Solution structure of the Tudor domain of PHD finger protein 1 (PHF1 protein)." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 29-85.
[16]	"An H3K36 methylation-engaging Tudor motif of Polycomb-like proteins mediates PRC2 complex targeting." Cai L., Rothbart S.B., Lu R., Xu B., Chen W.Y., Tripathy A., Rockowitz S., Zheng D., Patel D.J., Allis C.D., Strahl B.D., Song J., Wang G.G. Mol. Cell 49:571-582(2013) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 6-83, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41; TYR-47; PHE-65; GLU-66 AND PHE-71.
[17]	"Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1." Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E., Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A., Yasui A., Cote J., Kutateladze T.G. Nat. Struct. Mol. Biol. 19:1266-1272(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41 AND TYR-47.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF029678 mRNA. Translation: AAC52062.1.
AF052205 mRNA. Translation: AAC13273.1.
AL662799 Genomic DNA. Translation: CAI18271.1.
AL662799 Genomic DNA. Translation: CAI18272.1.
AL021366 Genomic DNA. Translation: CAA16158.1.
AL021366 Genomic DNA. Translation: CAA16159.1.
AL050332 Genomic DNA. Translation: CAC38366.1.
AL050332 Genomic DNA. Translation: CAC38367.1.
BX088650 Genomic DNA. Translation: CAM26298.1.
BX088650 Genomic DNA. Translation: CAM26299.1.
CH471081 Genomic DNA. Translation: EAX03729.1.
CH471081 Genomic DNA. Translation: EAX03730.1.
BC008834 mRNA. Translation: AAH08834.1.

IPI

IPI00011231.
IPI00064665.

RefSeq

NP_002627.1. NM_002636.4.
NP_077084.1. NM_024165.2.

UniGene

Hs.166204.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E5P	NMR	-	A	29-83	[»]
2M0O	NMR	-	A	6-83	[»]
4HCZ	X-ray	1.85	A/B	28-85	[»]

ProteinModelPortal

O43189.

SMR

O43189. Positions 28-147, 189-238.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43189. 9 interactions.

MINT

MINT-1437706.

PTM databases

PhosphoSite

O43189.

Proteomic databases

PaxDb

O43189.

PRIDE

O43189.

Protocols and materials databases

DNASU

5252.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374512; ENSP00000363636; ENSG00000112511.
ENST00000374516; ENSP00000363640; ENSG00000112511.
ENST00000427869; ENSP00000391901; ENSG00000225553.
ENST00000454914; ENSP00000407295; ENSG00000225553.

GeneID

5252.

KEGG

hsa:5252.

UCSC

uc003oeh.3. human.
uc003oei.3. human.

Organism-specific databases

CTD

5252.

GeneCards

GC06P033379.

HGNC

HGNC:8919. PHF1.

HPA

HPA031038.

MIM

602881. gene.

neXtProt

NX_O43189.

PharmGKB

PA33259.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG244542.

HOVERGEN

HBG004755.

InParanoid

O43189.

KO

K11467.

OMA

SPIRMFA.

OrthoDB

EOG4SBDXN.

PhylomeDB

O43189.

Gene expression databases

ArrayExpress

O43189.

Bgee

O43189.

CleanEx

HS_PHF1.

Genevestigator

O43189.

GermOnline

ENSG00000112511. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 2 hits.

InterPro

IPR025894. Mtf2_C_dom.
IPR002999. Tudor.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]

SMART

SM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 2 hits.

PROSITE

PS50304. TUDOR. False negative.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O43189.

GenomeRNAi

5252.

NextBio

20290.

SOURCE

Search...

Entry information

Entry name

PHF1_HUMAN

Accession

Primary (citable) accession number: O43189
Secondary accession number(s): B1AZX2 , B1AZX3, O60929, Q5SU07, Q5SU08, Q96KM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.