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PHD finger protein 1 (Protein PHF1) (hPHF1) (Polycomb-like protein 1) (hPCl1)

 PHF1_HUMAN              Reviewed;         567 AA.
O43189; B1AZX2; B1AZX3; O60929; Q5SU07; Q5SU08; Q96KM7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
23-MAY-2018, entry version 175.
RecName: Full=PHD finger protein 1;
Short=Protein PHF1;
Short=hPHF1;
AltName: Full=Polycomb-like protein 1;
Short=hPCl1;
Name=PHF1; Synonyms=PCL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-304.
TISSUE=Placenta;
PubMed=9545646; DOI=10.1006/geno.1997.5201;
Coulson M., Robert S., Eyre H.J., Saint R.;
"The identification and localization of a human gene with sequence
similarity to Polycomblike of Drosophila melanogaster.";
Genomics 48:381-383(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LYS-304.
Wang J.H., Du G.W., Zhou Y., Yuan J.G., Qiang B.Q.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-304.
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-304.
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
LYS-304.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH JAZF1.
PubMed=16397222; DOI=10.1158/0008-5472.CAN-05-2485;
Micci F., Panagopoulos I., Bjerkehagen B., Heim S.;
"Consistent rearrangement of chromosomal band 6p21 with generation of
fusion genes JAZF1/PHF1 and EPC1/PHF1 in endometrial stromal
sarcoma.";
Cancer Res. 66:107-112(2006).
[7]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
THE PRC2 COMPLEX.
PubMed=18086877; DOI=10.1128/MCB.01589-07;
Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.;
"Role of hPHF1 in H3K27 methylation and Hox gene silencing.";
Mol. Cell. Biol. 28:1862-1872(2008).
[8]
FUNCTION, INTERACTION WITH THE PRC2 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=18285464; DOI=10.1128/MCB.02017-07;
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.;
"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27
trimethylation in vivo.";
Mol. Cell. Biol. 28:2718-2731(2008).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18385154; DOI=10.1093/nar/gkn146;
Hong Z., Jiang J., Lan L., Nakajima S., Kanno S., Koseki H., Yasui A.;
"A polycomb group protein, PHF1, is involved in the response to DNA
double-strand breaks in human cell.";
Nucleic Acids Res. 36:2939-2947(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 (ISOFORM 1), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
SUBCELLULAR LOCATION.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[12]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH MEAF6.
PubMed=22761769; DOI=10.1371/journal.pone.0039354;
Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M.,
Bjerkehagen B., Davidson B., Heim S.;
"Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial
stromal sarcoma.";
PLoS ONE 7:E39354-E39354(2012).
[13]
H3K36ME3-BINDING.
PubMed=23228662; DOI=10.1016/j.bbrc.2012.11.116;
Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.;
"Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind
to histone H3K36me3.";
Biochem. Biophys. Res. Commun. 430:547-553(2013).
[14]
FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
PubMed=23150668; DOI=10.1074/jbc.M111.338996;
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.;
"Polycomb group protein PHF1 regulates p53-dependent cell growth
arrest and apoptosis.";
J. Biol. Chem. 288:529-539(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
STRUCTURE BY NMR OF 29-85.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the Tudor domain of PHD finger protein 1 (PHF1
protein).";
Submitted (JUN-2007) to the PDB data bank.
[18]
STRUCTURE BY NMR OF 6-83, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF TRP-41; TYR-47; PHE-65; GLU-66 AND
PHE-71.
PubMed=23273982; DOI=10.1016/j.molcel.2012.11.026;
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.;
"An H3K36 methylation-engaging Tudor motif of Polycomb-like proteins
mediates PRC2 complex targeting.";
Mol. Cell 49:571-582(2013).
[19]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION,
H3K36ME3-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-41 AND
TYR-47.
PubMed=23142980; DOI=10.1038/nsmb.2435;
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.;
"Molecular basis for H3K36me3 recognition by the Tudor domain of
PHF1.";
Nat. Struct. Mol. Biol. 19:1266-1272(2012).
-!- 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
(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.
{ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464,
ECO:0000269|PubMed:18385154, ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23150668, ECO:0000269|PubMed:23273982}.
-!- SUBUNIT: Interacts with CHMP1 (By similarity). Associated
component of the PRC2 complex. Interacts with p53/TP53.
{ECO:0000250, ECO:0000269|PubMed:18086877,
ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:23150668}.
-!- INTERACTION:
Q96B67:ARRDC3; NbExp=4; IntAct=EBI-530034, EBI-2875665;
Q9ULK2:ATXN7L1; NbExp=3; IntAct=EBI-530034, EBI-310660;
Q96CA5:BIRC7; NbExp=3; IntAct=EBI-530034, EBI-517623;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-530034, EBI-739580;
Q15910:EZH2; NbExp=5; IntAct=EBI-530034, EBI-530054;
Q9BPX1:HSD17B14; NbExp=5; IntAct=EBI-530034, EBI-742664;
Q15742:NAB2; NbExp=5; IntAct=EBI-530034, EBI-8641936;
Q9NR12:PDLIM7; NbExp=3; IntAct=EBI-530034, EBI-350517;
Q93062:RBPMS; NbExp=4; IntAct=EBI-530034, EBI-740322;
Q12800:TFCP2; NbExp=4; IntAct=EBI-530034, EBI-717422;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-530034, EBI-741515;
Q05BL1:TP53BP2; NbExp=4; IntAct=EBI-530034, EBI-11952721;
P36406:TRIM23; NbExp=3; IntAct=EBI-530034, EBI-740098;
Q70EL1-9:USP54; NbExp=4; IntAct=EBI-530034, EBI-11975223;
Q08AM6:VAC14; NbExp=3; IntAct=EBI-530034, EBI-2107455;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=PHF2;
IsoId=O43189-1; Sequence=Displayed;
Name=1; Synonyms=PHF1;
IsoId=O43189-2; Sequence=VSP_004694, VSP_004695;
Note=Contains a phosphoserine at position 360.
{ECO:0000244|PubMed:18669648};
-!- 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
(PubMed:23228662, PubMed:23273982 and PubMed:23142980).
-!- DISEASE: Note=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.
{ECO:0000269|PubMed:16397222, ECO:0000269|PubMed:22761769}.
-!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
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EMBL; AF029678; AAC52062.1; -; mRNA.
EMBL; AF052205; AAC13273.1; -; mRNA.
EMBL; AL662799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL021366; CAA16158.1; -; Genomic_DNA.
EMBL; AL021366; CAA16159.1; -; Genomic_DNA.
EMBL; AL050332; CAC38366.1; -; Genomic_DNA.
EMBL; AL050332; CAC38367.1; -; Genomic_DNA.
EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03729.1; -; Genomic_DNA.
EMBL; CH471081; EAX03730.1; -; Genomic_DNA.
EMBL; BC008834; AAH08834.1; -; mRNA.
CCDS; CCDS4777.1; -. [O43189-1]
CCDS; CCDS4778.1; -. [O43189-2]
RefSeq; NP_002627.1; NM_002636.4.
RefSeq; NP_077084.1; NM_024165.2.
RefSeq; XP_011512964.1; XM_011514662.1. [O43189-1]
UniGene; Hs.166204; -.
PDB; 2E5P; NMR; -; A=29-83.
PDB; 2M0O; NMR; -; A=6-83.
PDB; 4HCZ; X-ray; 1.85 A; A/B=28-85.
PDB; 5XFN; X-ray; 1.90 A; A=25-340.
PDB; 5XFO; X-ray; 1.90 A; A=25-340.
PDB; 5XFP; X-ray; 2.30 A; A/B/E=25-360.
PDBsum; 2E5P; -.
PDBsum; 2M0O; -.
PDBsum; 4HCZ; -.
PDBsum; 5XFN; -.
PDBsum; 5XFO; -.
PDBsum; 5XFP; -.
ProteinModelPortal; O43189; -.
SMR; O43189; -.
BioGrid; 111271; 57.
DIP; DIP-34001N; -.
IntAct; O43189; 76.
MINT; O43189; -.
STRING; 9606.ENSP00000363640; -.
BindingDB; O43189; -.
iPTMnet; O43189; -.
PhosphoSitePlus; O43189; -.
BioMuta; PHF1; -.
EPD; O43189; -.
MaxQB; O43189; -.
PaxDb; O43189; -.
PeptideAtlas; O43189; -.
PRIDE; O43189; -.
DNASU; 5252; -.
Ensembl; ENST00000374512; ENSP00000363636; ENSG00000112511. [O43189-2]
Ensembl; ENST00000374516; ENSP00000363640; ENSG00000112511. [O43189-1]
Ensembl; ENST00000427869; ENSP00000391901; ENSG00000225553.
Ensembl; ENST00000454914; ENSP00000407295; ENSG00000225553.
GeneID; 5252; -.
KEGG; hsa:5252; -.
UCSC; uc003oeh.4; human. [O43189-1]
CTD; 5252; -.
DisGeNET; 5252; -.
EuPathDB; HostDB:ENSG00000112511.17; -.
GeneCards; PHF1; -.
HGNC; HGNC:8919; PHF1.
HPA; HPA031038; -.
MIM; 602881; gene.
neXtProt; NX_O43189; -.
OpenTargets; ENSG00000112511; -.
PharmGKB; PA33259; -.
eggNOG; KOG4323; Eukaryota.
eggNOG; ENOG410XQ6E; LUCA.
GeneTree; ENSGT00390000009222; -.
HOVERGEN; HBG004755; -.
InParanoid; O43189; -.
KO; K11467; -.
OMA; FGLHART; -.
OrthoDB; EOG091G01JL; -.
PhylomeDB; O43189; -.
TreeFam; TF106420; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
ChiTaRS; PHF1; human.
EvolutionaryTrace; O43189; -.
GeneWiki; PHF1; -.
GenomeRNAi; 5252; -.
PRO; PR:O43189; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112511; -.
CleanEx; HS_PHF1; -.
ExpressionAtlas; O43189; baseline and differential.
Genevisible; O43189; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR025894; Mtf2_C_dom.
InterPro; IPR031202; PHF1.
InterPro; IPR002999; Tudor.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR12628:SF11; PTHR12628:SF11; 1.
Pfam; PF14061; Mtf2_C; 1.
Pfam; PF00628; PHD; 1.
SMART; SM00249; PHD; 2.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 567 PHD finger protein 1.
/FTId=PRO_0000059288.
DOMAIN 29 86 Tudor.
ZN_FING 87 142 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 186 240 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 350 457 SFPSGQGPGGGVSRPLGKRRRPEPEPLRRRQKGKVEELGPP
SAVRNQPEPQEQRERAHLQRALQASVSPPSPSPNQSYQGSS
GYNFRPTDARCLPSSPIRMFASFHPS -> RAGPWGRGLTS
PGEAPEAGARAPEEEAEGESGGAGATLSSAQSARAPGAEGA
GSSAEGTAAAPSGCLLPSTLLPAPQGPLGTVDPQTGHPWNF
TLVSPQTSLKVPPTR (in isoform 1).
{ECO:0000303|PubMed:9545646}.
/FTId=VSP_004694.
VAR_SEQ 458 567 Missing (in isoform 1).
{ECO:0000303|PubMed:9545646}.
/FTId=VSP_004695.
VARIANT 42 42 T -> S (in dbSNP:rs6934613).
/FTId=VAR_044500.
VARIANT 304 304 R -> K (in dbSNP:rs3116713).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9545646,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_034382.
MUTAGEN 41 41 W->A: Abolishes histone H3K36me3-binding
and localization at double-strand breaks
(DSBs). {ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23273982}.
MUTAGEN 47 47 Y->A: Abolishes histone H3K36me3-binding.
{ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23273982}.
MUTAGEN 65 65 F->A: Abolishes histone H3K36me3-binding.
{ECO:0000269|PubMed:23273982}.
MUTAGEN 66 66 E->K: Impairs histone H3K36me3-binding.
{ECO:0000269|PubMed:23273982}.
MUTAGEN 71 71 F->A: Abolishes histone H3K36me3-binding.
{ECO:0000269|PubMed:23273982}.
STRAND 36 40 {ECO:0000244|PDB:4HCZ}.
STRAND 46 55 {ECO:0000244|PDB:4HCZ}.
TURN 56 59 {ECO:0000244|PDB:4HCZ}.
STRAND 60 65 {ECO:0000244|PDB:4HCZ}.
TURN 66 68 {ECO:0000244|PDB:2E5P}.
STRAND 70 74 {ECO:0000244|PDB:4HCZ}.
HELIX 75 77 {ECO:0000244|PDB:4HCZ}.
STRAND 78 80 {ECO:0000244|PDB:4HCZ}.
STRAND 87 90 {ECO:0000244|PDB:5XFO}.
TURN 91 93 {ECO:0000244|PDB:5XFN}.
STRAND 104 106 {ECO:0000244|PDB:5XFN}.
TURN 108 110 {ECO:0000244|PDB:5XFN}.
STRAND 113 115 {ECO:0000244|PDB:5XFN}.
HELIX 116 118 {ECO:0000244|PDB:5XFN}.
STRAND 119 121 {ECO:0000244|PDB:5XFN}.
STRAND 129 133 {ECO:0000244|PDB:5XFO}.
HELIX 137 144 {ECO:0000244|PDB:5XFN}.
HELIX 155 163 {ECO:0000244|PDB:5XFN}.
HELIX 171 173 {ECO:0000244|PDB:5XFO}.
TURN 189 191 {ECO:0000244|PDB:5XFN}.
TURN 197 200 {ECO:0000244|PDB:5XFN}.
STRAND 201 203 {ECO:0000244|PDB:5XFN}.
TURN 205 207 {ECO:0000244|PDB:5XFN}.
STRAND 210 212 {ECO:0000244|PDB:5XFN}.
HELIX 213 215 {ECO:0000244|PDB:5XFN}.
STRAND 230 233 {ECO:0000244|PDB:5XFN}.
HELIX 235 238 {ECO:0000244|PDB:5XFN}.
STRAND 243 246 {ECO:0000244|PDB:5XFN}.
HELIX 251 266 {ECO:0000244|PDB:5XFN}.
TURN 273 276 {ECO:0000244|PDB:5XFN}.
HELIX 277 283 {ECO:0000244|PDB:5XFN}.
HELIX 285 288 {ECO:0000244|PDB:5XFN}.
HELIX 291 295 {ECO:0000244|PDB:5XFN}.
TURN 298 300 {ECO:0000244|PDB:5XFN}.
HELIX 301 311 {ECO:0000244|PDB:5XFN}.
TURN 313 315 {ECO:0000244|PDB:5XFN}.
STRAND 316 318 {ECO:0000244|PDB:5XFN}.
HELIX 322 324 {ECO:0000244|PDB:5XFO}.
STRAND 328 332 {ECO:0000244|PDB:5XFN}.
SEQUENCE 567 AA; 62106 MW; E81BA9475565957C CRC64;
MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV
CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV
PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH
LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG
PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE
RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS FPSGQGPGGG
VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ EQRERAHLQR ALQASVSPPS
PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM FASFHPSAST AGTSGDSGPP DRSPLELHIG
FPTDIPKSAP HSMTASSSSV SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD
PVRVLARRVR PDGSVQYLVE WGGGGIF


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