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O43189

- PHF1_HUMAN

UniProt

O43189 - PHF1_HUMAN

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Protein

PHD finger protein 1

Gene

PHF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (PubMed:18285464 and PubMed:23273982). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri87 – 14256PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri186 – 24055PHD-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. methylated histone binding Source: UniProtKB
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. chromatin modification Source: UniProtKB-KW
  3. negative regulation of histone H3-K27 methylation Source: UniProtKB
  4. positive regulation of histone H3-K27 methylation Source: UniProtKB
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200808. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
PHD finger protein 1
Short name:
Protein PHF1
Short name:
hPHF1
Alternative name(s):
Polycomb-like protein 1
Short name:
hPCl1
Gene namesi
Name:PHF1
Synonyms:PCL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:8919. PHF1.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
  4. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

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 MEAF6.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411W → A: Abolishes histone H3K36me3-binding and localization at double-strand breaks (DSBs). 2 Publications
Mutagenesisi47 – 471Y → A: Abolishes histone H3K36me3-binding. 2 Publications
Mutagenesisi65 – 651F → A: Abolishes histone H3K36me3-binding. 1 Publication
Mutagenesisi66 – 661E → K: Impairs histone H3K36me3-binding. 1 Publication
Mutagenesisi71 – 711F → A: Abolishes histone H3K36me3-binding. 1 Publication

Organism-specific databases

PharmGKBiPA33259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567PHD finger protein 1PRO_0000059288Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43189.
PaxDbiO43189.
PRIDEiO43189.

PTM databases

PhosphoSiteiO43189.

Expressioni

Tissue specificityi

Highest levels in heart, skeletal muscle, and pancreas, lower levels in brain, placenta, lung, liver and kidney.

Gene expression databases

BgeeiO43189.
CleanExiHS_PHF1.
ExpressionAtlasiO43189. baseline and differential.
GenevestigatoriO43189.

Organism-specific databases

HPAiHPA031038.

Interactioni

Subunit structurei

Interacts with CHMP1 (By similarity). Associated component of the PRC2 complex. Interacts with p53/TP53.By similarity3 Publications

Protein-protein interaction databases

BioGridi111271. 27 interactions.
DIPiDIP-34001N.
IntActiO43189. 10 interactions.
MINTiMINT-1437706.

Structurei

Secondary structure

1
567
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 405Combined sources
Beta strandi46 – 5510Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 656Combined sources
Turni66 – 683Combined sources
Beta strandi70 – 745Combined sources
Helixi75 – 773Combined sources
Beta strandi78 – 803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5PNMR-A29-83[»]
2M0ONMR-A6-83[»]
4HCZX-ray1.85A/B28-85[»]
ProteinModelPortaliO43189.
SMRiO43189. Positions 6-82, 85-147, 188-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43189.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 8658TudorAdd
BLAST

Domaini

The Tudor domain recognizes and binds H3K36me3 (PubMed:23228662, PubMed:23273982 and PubMed:23142980).

Sequence similaritiesi

Belongs to the Polycomblike family.Curated
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 Tudor domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri87 – 14256PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri186 – 24055PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG244542.
GeneTreeiENSGT00390000009222.
HOVERGENiHBG004755.
InParanoidiO43189.
KOiK11467.
PhylomeDBiO43189.
TreeFamiTF106420.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025894. 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]
PfamiPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: O43189-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT
60 70 80 90 100
IKKVDSAREV CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP
110 120 130 140 150
GNRLVSCEKC RHAYHQDCHV PRAPAPGEGE GTSWVCRQCV FAIATKRGGA
160 170 180 190 200
LKKGPYARAM LGMKLSLPYG LKGLDWDAGH LSNRQQSYCY CGGPGEWNLK
210 220 230 240 250
MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG PEKVRRLQLR
260 270 280 290 300
WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE
310 320 330 340 350
RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS
360 370 380 390 400
FPSGQGPGGG VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ
410 420 430 440 450
EQRERAHLQR ALQASVSPPS PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM
460 470 480 490 500
FASFHPSAST AGTSGDSGPP DRSPLELHIG FPTDIPKSAP HSMTASSSSV
510 520 530 540 550
SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD PVRVLARRVR
560
PDGSVQYLVE WGGGGIF
Length:567
Mass (Da):62,106
Last modified:January 11, 2011 - v3
Checksum:iE81BA9475565957C
GO
Isoform 1 (identifier: O43189-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:457
Mass (Da):49,643
Checksum:i611EF2B5A416841C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421T → S.
Corresponds to variant rs6934613 [ dbSNP | Ensembl ].
VAR_044500
Natural varianti304 – 3041R → K.5 Publications
Corresponds to variant rs3116713 [ dbSNP | Ensembl ].
VAR_034382

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei350 – 457108SFPSG…SFHPS → RAGPWGRGLTSPGEAPEAGA RAPEEEAEGESGGAGATLSS AQSARAPGAEGAGSSAEGTA AAPSGCLLPSTLLPAPQGPL GTVDPQTGHPWNFTLVSPQT SLKVPPTR in isoform 1. 1 PublicationVSP_004694Add
BLAST
Alternative sequencei458 – 567110Missing in isoform 1. 1 PublicationVSP_004695Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4777.1. [O43189-1]
CCDS4778.1. [O43189-2]
RefSeqiNP_002627.1. NM_002636.4.
NP_077084.1. NM_024165.2.
UniGeneiHs.166204.

Genome annotation databases

EnsembliENST00000374512; ENSP00000363636; ENSG00000112511. [O43189-2]
ENST00000374516; ENSP00000363640; ENSG00000112511. [O43189-1]
ENST00000427869; ENSP00000391901; ENSG00000225553.
ENST00000454914; ENSP00000407295; ENSG00000225553.
GeneIDi5252.
KEGGihsa:5252.
UCSCiuc003oeh.3. human. [O43189-1]
uc003oei.3. human. [O43189-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4777.1. [O43189-1 ]
CCDS4778.1. [O43189-2 ]
RefSeqi NP_002627.1. NM_002636.4.
NP_077084.1. NM_024165.2.
UniGenei Hs.166204.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali O43189.
SMRi O43189. Positions 6-82, 85-147, 188-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111271. 27 interactions.
DIPi DIP-34001N.
IntActi O43189. 10 interactions.
MINTi MINT-1437706.

PTM databases

PhosphoSitei O43189.

Proteomic databases

MaxQBi O43189.
PaxDbi O43189.
PRIDEi O43189.

Protocols and materials databases

DNASUi 5252.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374512 ; ENSP00000363636 ; ENSG00000112511 . [O43189-2 ]
ENST00000374516 ; ENSP00000363640 ; ENSG00000112511 . [O43189-1 ]
ENST00000427869 ; ENSP00000391901 ; ENSG00000225553 .
ENST00000454914 ; ENSP00000407295 ; ENSG00000225553 .
GeneIDi 5252.
KEGGi hsa:5252.
UCSCi uc003oeh.3. human. [O43189-1 ]
uc003oei.3. human. [O43189-2 ]

Organism-specific databases

CTDi 5252.
GeneCardsi GC06P033379.
GC06Po33517.
HGNCi HGNC:8919. PHF1.
HPAi HPA031038.
MIMi 602881. gene.
neXtProti NX_O43189.
PharmGKBi PA33259.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG244542.
GeneTreei ENSGT00390000009222.
HOVERGENi HBG004755.
InParanoidi O43189.
KOi K11467.
PhylomeDBi O43189.
TreeFami TF106420.

Enzyme and pathway databases

Reactomei REACT_200808. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSi PHF1. human.
EvolutionaryTracei O43189.
GeneWikii PHF1.
GenomeRNAii 5252.
NextBioi 20290.
PROi O43189.
SOURCEi Search...

Gene expression databases

Bgeei O43189.
CleanExi HS_PHF1.
ExpressionAtlasi O43189. baseline and differential.
Genevestigatori O43189.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi 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 ]
Pfami PF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 2 hits.
PROSITEi PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41 AND TYR-47.

Entry informationi

Entry nameiPHF1_HUMAN
AccessioniPrimary (citable) accession number: O43189
Secondary accession number(s): B1AZX2
, B1AZX3, O60929, Q5SU07, Q5SU08, Q96KM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: November 26, 2014
This is version 141 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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