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Q5T6S3

- PHF19_HUMAN

UniProt

Q5T6S3 - PHF19_HUMAN

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Protein
PHD finger protein 19
Gene
PHF19, PCL3
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. 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 1
Add
BLAST
Zinc fingeri195 – 24955PHD-type 2
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of histone H3-K27 methylation Source: UniProtKB
  4. stem cell maintenance Source: Ensembl
  5. 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_200808. 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: Chromosome 9

Organism-specific databases

HGNCiHGNC:24566. PHF19.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. ESC/E(Z) complex Source: Ensembl
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.

PTM / Processingi

Molecule processing

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

ArrayExpressiQ5T6S3.
BgeeiQ5T6S3.
CleanExiHS_PHF19.
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. 8 interactions.
IntActiQ5T6S3. 4 interactions.
MINTiMINT-8417713.
STRINGi9606.ENSP00000363003.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5QNMR-A40-95[»]
4BD3NMR-A38-95[»]
ProteinModelPortaliQ5T6S3.
SMRiQ5T6S3. Positions 38-156, 195-249.

Miscellaneous databases

EvolutionaryTraceiQ5T6S3.

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

The Tudor domain recognizes and binds H3K36me3 (1 Publication, 1 Publication, 1 Publication and 1 Publication). May also bind H3K27me3, with a lower affinity (1 Publication).2 Publications

Sequence similaritiesi

Belongs to the Polycomblike family.
Contains 1 Tudor domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG244542.
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. Align

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

MENRALDPGT RDSYGATSHL PNKGALAKVK NNFKDLMSKL TEGQYVLCRW    50
TDGLYYLGKI KRVSSSKQSC LVTFEDNSKY WVLWKDIQHA GVPGEEPKCN 100
ICLGKTSGPL NEILICGKCG LGYHQQCHIP IAGSADQPLL TPWFCRRCIF 150
ALAVRKGGAL KKGAIARTLQ AVKMVLSYQP EELEWDSPHR TNQQQCYCYC 200
GGPGEWYLRM LQCYRCRQWF HEACTQCLNE PMMFGDRFYL FFCSVCNQGP 250
EYIERLPLRW VDVVHLALYN LGVQSKKKYF DFEEILAFVN HHWELLQLGK 300
LTSTPVTDRG PHLLNALNSY KSRFLCGKEI KKKKCIFRLR IRVPPNPPGK 350
LLPDKGLLPN ENSASSELRK RGKSKPGLLP HEFQQQKRRV YRRKRSKFLL 400
EDAIPSSDFT SAWSTNHHLA SIFDFTLDEI QSLKSASSGQ TFFSDVDSTD 450
AASTSGSAST SLSYDSRWTV GSRKRKLAAK AYMPLRAKRW AAELDGRCPS 500
DSSAEGASVP ERPDEGIDSH TFESISEDDS SLSHLKSSIT NYFGAAGRLA 550
CGEKYQVLAR RVTPEGKVQY LVEWEGTTPY 580
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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei122 – 1309GYHQQCHIP → VPHPHSGQC in isoform 3.
VSP_031222
Alternative sequencei131 – 580450Missing in isoform 3.
VSP_031223Add
BLAST
Alternative sequencei155 – 20753RKGGA…PGEWY → RVSLPSSPVPASPASSSGAD QRLPSQSLSSKQKGHTWALE TDSASATVLGQDL in isoform 2.
VSP_031224Add
BLAST
Alternative sequencei208 – 580373Missing in isoform 2.
VSP_031225Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811E → G in CAE45832. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
XP_006717108.1. XM_006717045.1. [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]

Polymorphism databases

DMDMi74745265.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS35116.1. [Q5T6S3-1 ]
CCDS35117.1. [Q5T6S3-2 ]
PIRi T17260.
RefSeqi NP_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 ]
XP_006717108.1. XM_006717045.1. [Q5T6S3-1 ]
UniGenei Hs.460124.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E5Q NMR - A 40-95 [» ]
4BD3 NMR - A 38-95 [» ]
ProteinModelPortali Q5T6S3.
SMRi Q5T6S3. Positions 38-156, 195-249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117578. 8 interactions.
IntActi Q5T6S3. 4 interactions.
MINTi MINT-8417713.
STRINGi 9606.ENSP00000363003.

PTM databases

PhosphoSitei Q5T6S3.

Polymorphism databases

DMDMi 74745265.

Proteomic databases

MaxQBi Q5T6S3.
PaxDbi Q5T6S3.
PRIDEi Q5T6S3.

Protocols and materials databases

DNASUi 26147.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312189 ; ENSP00000310372 ; ENSG00000119403 . [Q5T6S3-2 ]
ENST00000373896 ; ENSP00000363003 ; ENSG00000119403 . [Q5T6S3-1 ]
GeneIDi 26147.
KEGGi hsa:26147.
UCSCi uc004bks.1. human. [Q5T6S3-1 ]
uc004bkt.3. human. [Q5T6S3-2 ]

Organism-specific databases

CTDi 26147.
GeneCardsi GC09M123617.
HGNCi HGNC:24566. PHF19.
HPAi HPA051458.
MIMi 609740. gene.
neXtProti NX_Q5T6S3.
PharmGKBi PA134911501.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG244542.
HOGENOMi HOG000010307.
HOVERGENi HBG004755.
InParanoidi Q5T6S3.
KOi K11486.
OMAi DWDSPHR.
OrthoDBi EOG73V6JJ.
PhylomeDBi Q5T6S3.
TreeFami TF106420.

Enzyme and pathway databases

Reactomei REACT_200808. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSi PHF19. human.
EvolutionaryTracei Q5T6S3.
GenomeRNAii 26147.
NextBioi 48205.
PROi Q5T6S3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q5T6S3.
Bgeei Q5T6S3.
CleanExi HS_PHF19.
Genevestigatori Q5T6S3.

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.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 97 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 (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

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