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Protein

PHD finger protein 19

Gene

PHF19

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471Histone H3K36me3
Binding sitei55 – 551Histone H3K36me3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri96 – 15156PHD-type 1Add
BLAST
Zinc fingeri195 – 24955PHD-type 2Add
BLAST

GO - Molecular functioni

  1. methylated histone binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. negative regulation of gene expression, epigenetic Source: Reactome
  4. positive regulation of histone H3-K27 methylation Source: UniProtKB
  5. regulation of gene expression, epigenetic Source: Reactome
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_264352. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
PHD finger protein 19
Alternative name(s):
Polycomb-like protein 3
Short name:
hPCL3
Gene namesi
Name:PHF19
Synonyms:PCL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:24566. PHF19.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501W → A in muthPhf19; abolishes histone H3K36me3-binding and impaired activity of the PRC2 complex and subsequent H3K27me3 methylation. 2 Publications
Mutagenesisi50 – 501W → C: Abolishes histone H3K36me3-binding and recruitment of the PRC2 complex and NO66; when associated with A-56. 2 Publications
Mutagenesisi56 – 561Y → A: Abolishes histone H3K36me3-binding. Abolishes histone H3K36me3-binding and recruitment of the PRC2 complex and NO66; when associated with C-50. 2 Publications

Organism-specific databases

PharmGKBiPA134911501.

Polymorphism and mutation databases

DMDMi74745265.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580PHD finger protein 19PRO_0000318570Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5T6S3.
PaxDbiQ5T6S3.
PRIDEiQ5T6S3.

PTM databases

PhosphoSiteiQ5T6S3.

Expressioni

Tissue specificityi

Isoform 1 is expressed in thymus, heart, lung and kidney. Isoform 2 is predominantly expressed in placenta, skeletal muscle and kidney, whereas isoform 1 is predominantly expressed in liver and peripheral blood leukocytes. Overexpressed in many types of cancers, including colon, skin, lung, rectal, cervical, uterus, liver cancers, in cell lines derived from different stages of melanoma and in glioma cell lines.1 Publication

Gene expression databases

BgeeiQ5T6S3.
CleanExiHS_PHF19.
ExpressionAtlasiQ5T6S3. baseline and differential.
GenevestigatoriQ5T6S3.

Organism-specific databases

HPAiHPA051458.

Interactioni

Subunit structurei

Associated component of the PRC2 complex. Interacts with EZH2 (via its Tudor domain). Isoform 1 interacts with SUZ12; isoform 2 does not interact with SUZ12. Interacts with NO66.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KDM1AO603412EBI-2339674,EBI-710124
SUV39H1O434632EBI-2339674,EBI-349968
SUV39H2Q9H5I12EBI-2339674,EBI-723127

Protein-protein interaction databases

BioGridi117578. 13 interactions.
IntActiQ5T6S3. 4 interactions.
MINTiMINT-8417713.
STRINGi9606.ENSP00000363003.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 495Combined sources
Beta strandi55 – 606Combined sources
Beta strandi68 – 747Combined sources
Beta strandi79 – 835Combined sources
Helixi84 – 863Combined sources
Beta strandi87 – 893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5QNMR-A40-95[»]
4BD3NMR-A38-95[»]
ProteinModelPortaliQ5T6S3.
SMRiQ5T6S3. Positions 38-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5T6S3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 9354TudorAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 807Histone H3K36me3 binding

Domaini

The Tudor domain recognizes and binds H3K36me3 (PubMed:23273982, PubMed:23160351, PubMed:23104054 and PubMed:23228662). May also bind H3K27me3, with a lower affinity (PubMed:23160351).2 Publications

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri96 – 15156PHD-type 1Add
BLAST
Zinc fingeri195 – 24955PHD-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG244542.
GeneTreeiENSGT00390000009222.
HOGENOMiHOG000010307.
HOVERGENiHBG004755.
InParanoidiQ5T6S3.
KOiK11486.
OMAiDWDSPHR.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ5T6S3.
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.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5T6S3-1) [UniParc]FASTAAdd to basket

Also known as: PCL3L, hPCL3L

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
MENRALDPGT RDSYGATSHL PNKGALAKVK NNFKDLMSKL TEGQYVLCRW
60 70 80 90 100
TDGLYYLGKI KRVSSSKQSC LVTFEDNSKY WVLWKDIQHA GVPGEEPKCN
110 120 130 140 150
ICLGKTSGPL NEILICGKCG LGYHQQCHIP IAGSADQPLL TPWFCRRCIF
160 170 180 190 200
ALAVRKGGAL KKGAIARTLQ AVKMVLSYQP EELEWDSPHR TNQQQCYCYC
210 220 230 240 250
GGPGEWYLRM LQCYRCRQWF HEACTQCLNE PMMFGDRFYL FFCSVCNQGP
260 270 280 290 300
EYIERLPLRW VDVVHLALYN LGVQSKKKYF DFEEILAFVN HHWELLQLGK
310 320 330 340 350
LTSTPVTDRG PHLLNALNSY KSRFLCGKEI KKKKCIFRLR IRVPPNPPGK
360 370 380 390 400
LLPDKGLLPN ENSASSELRK RGKSKPGLLP HEFQQQKRRV YRRKRSKFLL
410 420 430 440 450
EDAIPSSDFT SAWSTNHHLA SIFDFTLDEI QSLKSASSGQ TFFSDVDSTD
460 470 480 490 500
AASTSGSAST SLSYDSRWTV GSRKRKLAAK AYMPLRAKRW AAELDGRCPS
510 520 530 540 550
DSSAEGASVP ERPDEGIDSH TFESISEDDS SLSHLKSSIT NYFGAAGRLA
560 570 580
CGEKYQVLAR RVTPEGKVQY LVEWEGTTPY
Length:580
Mass (Da):65,591
Last modified:December 21, 2004 - v1
Checksum:i17CCF21BA2827826
GO
Isoform 2 (identifier: Q5T6S3-2) [UniParc]FASTAAdd to basket

Also known as: PCL3S, hPCL3S

The sequence of this isoform differs from the canonical sequence as follows:
     155-207: RKGGALKKGA...CYCGGPGEWY → RVSLPSSPVP...ASATVLGQDL
     208-580: Missing.

Note: Contains a phosphoserine at position 166.1 Publication

Show »
Length:207
Mass (Da):22,512
Checksum:i34F3EF834B17FAF0
GO
Isoform 3 (identifier: Q5T6S3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-130: GYHQQCHIP → VPHPHSGQC
     131-580: Missing.

Show »
Length:130
Mass (Da):14,386
Checksum:iE10645A3F782774C
GO

Sequence cautioni

The sequence CAE45832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811E → G in CAE45832 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei122 – 1309GYHQQCHIP → VPHPHSGQC in isoform 3. 1 PublicationVSP_031222
Alternative sequencei131 – 580450Missing in isoform 3. 1 PublicationVSP_031223Add
BLAST
Alternative sequencei155 – 20753RKGGA…PGEWY → RVSLPSSPVPASPASSSGAD QRLPSQSLSSKQKGHTWALE TDSASATVLGQDL in isoform 2. 1 PublicationVSP_031224Add
BLAST
Alternative sequencei208 – 580373Missing in isoform 2. 1 PublicationVSP_031225Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL117477 mRNA. Translation: CAB55950.1.
BX640713 mRNA. Translation: CAE45832.1. Different initiation.
AL354792 Genomic DNA. Translation: CAI15690.1.
AL354792 Genomic DNA. Translation: CAI15691.1.
AL354792, AL161911 Genomic DNA. Translation: CAI15692.1.
AL161911, AL354792 Genomic DNA. Translation: CAI95112.1.
BC022374 mRNA. Translation: AAH22374.1.
BC108663 mRNA. Translation: AAI08664.1.
BC125076 mRNA. Translation: AAI25077.1.
BC125077 mRNA. Translation: AAI25078.1.
CCDSiCCDS35116.1. [Q5T6S3-1]
CCDS35117.1. [Q5T6S3-2]
PIRiT17260.
RefSeqiNP_001009936.1. NM_001009936.2. [Q5T6S3-2]
NP_001273769.1. NM_001286840.1.
NP_001273772.1. NM_001286843.1. [Q5T6S3-3]
NP_056466.1. NM_015651.2. [Q5T6S3-1]
XP_005251963.1. XM_005251906.1. [Q5T6S3-1]
UniGeneiHs.460124.

Genome annotation databases

EnsembliENST00000312189; ENSP00000310372; ENSG00000119403. [Q5T6S3-2]
ENST00000373896; ENSP00000363003; ENSG00000119403. [Q5T6S3-1]
GeneIDi26147.
KEGGihsa:26147.
UCSCiuc004bks.1. human. [Q5T6S3-1]
uc004bkt.3. human. [Q5T6S3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL117477 mRNA. Translation: CAB55950.1.
BX640713 mRNA. Translation: CAE45832.1. Different initiation.
AL354792 Genomic DNA. Translation: CAI15690.1.
AL354792 Genomic DNA. Translation: CAI15691.1.
AL354792, AL161911 Genomic DNA. Translation: CAI15692.1.
AL161911, AL354792 Genomic DNA. Translation: CAI95112.1.
BC022374 mRNA. Translation: AAH22374.1.
BC108663 mRNA. Translation: AAI08664.1.
BC125076 mRNA. Translation: AAI25077.1.
BC125077 mRNA. Translation: AAI25078.1.
CCDSiCCDS35116.1. [Q5T6S3-1]
CCDS35117.1. [Q5T6S3-2]
PIRiT17260.
RefSeqiNP_001009936.1. NM_001009936.2. [Q5T6S3-2]
NP_001273769.1. NM_001286840.1.
NP_001273772.1. NM_001286843.1. [Q5T6S3-3]
NP_056466.1. NM_015651.2. [Q5T6S3-1]
XP_005251963.1. XM_005251906.1. [Q5T6S3-1]
UniGeneiHs.460124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5QNMR-A40-95[»]
4BD3NMR-A38-95[»]
ProteinModelPortaliQ5T6S3.
SMRiQ5T6S3. Positions 38-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117578. 13 interactions.
IntActiQ5T6S3. 4 interactions.
MINTiMINT-8417713.
STRINGi9606.ENSP00000363003.

PTM databases

PhosphoSiteiQ5T6S3.

Polymorphism and mutation databases

DMDMi74745265.

Proteomic databases

MaxQBiQ5T6S3.
PaxDbiQ5T6S3.
PRIDEiQ5T6S3.

Protocols and materials databases

DNASUi26147.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312189; ENSP00000310372; ENSG00000119403. [Q5T6S3-2]
ENST00000373896; ENSP00000363003; ENSG00000119403. [Q5T6S3-1]
GeneIDi26147.
KEGGihsa:26147.
UCSCiuc004bks.1. human. [Q5T6S3-1]
uc004bkt.3. human. [Q5T6S3-2]

Organism-specific databases

CTDi26147.
GeneCardsiGC09M123617.
HGNCiHGNC:24566. PHF19.
HPAiHPA051458.
MIMi609740. gene.
neXtProtiNX_Q5T6S3.
PharmGKBiPA134911501.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244542.
GeneTreeiENSGT00390000009222.
HOGENOMiHOG000010307.
HOVERGENiHBG004755.
InParanoidiQ5T6S3.
KOiK11486.
OMAiDWDSPHR.
OrthoDBiEOG73V6JJ.
PhylomeDBiQ5T6S3.
TreeFamiTF106420.

Enzyme and pathway databases

ReactomeiREACT_264352. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSiPHF19. human.
EvolutionaryTraceiQ5T6S3.
GenomeRNAii26147.
NextBioi48205.
PROiQ5T6S3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T6S3.
CleanExiHS_PHF19.
ExpressionAtlasiQ5T6S3. baseline and differential.
GenevestigatoriQ5T6S3.

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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Esophageal carcinoma and Mammary cancer.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Prostate and Skin.
  4. "A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers."
    Wang S., Robertson G.P., Zhu J.
    Gene 343:69-78(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Functional characterization of human Polycomb-like 3 isoforms identifies them as components of distinct EZH2 protein complexes."
    Boulay G., Rosnoblet C., Guerardel C., Angrand P.O., Leprince D.
    Biochem. J. 434:333-342(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH EZH2.
  7. "PHF19 and Akt control the switch between proliferative and invasive states in melanoma."
    Ghislin S., Deshayes F., Middendorp S., Boggetto N., Alcaide-Loridan C.
    Cell Cycle 11:1634-1645(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION IN SPHEROID MELANOMA CELLS.
  8. "Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation."
    Brien G.L., Gambero G., O'Connell D.J., Jerman E., Turner S.A., Egan C.M., Dunne E.J., Jurgens M.C., Wynne K., Piao L., Lohan A.J., Ferguson N., Shi X., Sinha K.M., Loftus B.J., Cagney G., Bracken A.P.
    Nat. Struct. Mol. Biol. 19:1273-1281(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, H3K36ME3-BINDING, DOMAIN, INTERACTION WITH NO66, MUTAGENESIS OF TRP-50 AND TYR-56.
  9. "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.
  10. "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: H3K36ME3-BINDING, MUTAGENESIS OF TYR-56.
  11. "Solution structure of the tudor domain of PHD finger protein 19, isoform B [Homo sapiens]."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 40-95.
  12. Cited for: STRUCTURE BY NMR OF 38-95, FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, H3K36ME3-BINDING, DOMAIN, INTERACTION WITH SUZ12, MUTAGENESIS OF TRP-50.

Entry informationi

Entry nameiPHF19_HUMAN
AccessioniPrimary (citable) accession number: Q5T6S3
Secondary accession number(s): Q32NF2
, Q5T6S4, Q6N038, Q8TBL6, Q9UFS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: April 29, 2015
This is version 104 of the entry and version 1 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

Miscellaneous

Down-regulated in spheroid melanoma cells that display an invasive phenotype, characterized by a higher motility, a poor proliferation rate and a gain of pluripotency gene expression. PHF19 favors the proliferation and reduces the transmigration capacity of melanoma cell lines, 2 properties of invasive cells, suggesting that down-regulation may participate in the switch from proliferative to invasive states in melanoma cells (PubMed:22487681).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.