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Q9Z1B8 (PHF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PHD finger protein 1

Short name=Protein PHF1
Alternative name(s):
Polycomb-like protein 1
Short name=mPCl1
T-complex testis-expressed 3
Gene names
Name:Phf1
Synonyms:Plc1, Tctex-3, Tctex3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence 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.4). According to other reports, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2. Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. Ref.4

Subunit structure

Associated component of the PRC2 complex. Interacts with p53/TP53 By similarity. Interacts with CHMP1. Ref.3

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Colocalizes with NEK6 in the centrosome By similarity. Ref.4

Tissue specificity

Testis-specific.

Domain

The Tudor domain recognizes and binds H3K36me3 (Ref.5).

Sequence similarities

Belongs to the Polycomblike family.

Contains 2 PHD-type zinc fingers.

Contains 1 Tudor domain.

Ontologies

Keywords
   Biological processDNA damage
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of histone H3-K27 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of histone H3-K27 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

site of double-strand break

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmethylated histone binding

Inferred from direct assay Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559PHD finger protein 1
PRO_0000059289

Regions

Domain29 – 8658Tudor
Zinc finger87 – 14256PHD-type 1
Zinc finger186 – 24055PHD-type 2

Experimental info

Sequence conflict2491L → F in AAD00518. Ref.2
Sequence conflict3441G → E in BAA25074. Ref.1
Sequence conflict3771R → S in BAA25074. Ref.1
Sequence conflict5551G → R in BAA25074. Ref.1
Sequence conflict558 – 5592IF → HLPDSLLLLPSPFTHWHFHA LDL in BAA25074. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z1B8 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 6D2EE5F53D6164C2

FASTA55961,140
        10         20         30         40         50         60 
MAQLPRLSRL GAPSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV 

        70         80         90        100        110        120 
CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV 

       130        140        150        160        170        180 
PRAPAPGEGE GASWVCRQCV 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 
RSSQLLSALN SHKDRFISGR EIKKRKCLFG LHARTPPPVE LLTGDGAPTS FPSGQGPGGG 

       370        380        390        400        410        420 
VSRPLGKRWR SEPEPLRRRQ KGKVEELGPP TAAHSRHGSR EQRALQASVS PPPPSPNQSY 

       430        440        450        460        470        480 
EGSSGYNFRP TDARCLPSSP IRMFASFHPS ASTAGTSGDS EPPDRSPLGL HIGFPTDTPK 

       490        500        510        520        530        540 
SSPHSVTASS SSVPALTPGF SRHSPPSPLC RSLSPGTGGG VRGGVSYLSR GDPVRVLARR 

       550 
VRPDGSVQYL VEWGGGGIF 

« Hide

References

[1]"Tctex3, related to Drosophila polycomblike, is expressed in male germ cells and mapped to the mouse T-complex."
Kawakami S., Mitsunaga K., Kikuti Y.Y., Ando A., Inoko H., Yamamura K., Abe K.
Mamm. Genome 9:874-880(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Misexpression of Polycomb-group proteins in Xenopus alters anterior neural development and represses neural target genes."
Yoshitake Y., Howard T.L., Christian J.L., Hollenberg S.M.
Dev. Biol. 215:375-387(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NIH Swiss.
[3]"CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1.
[4]"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, SUBCELLULAR LOCATION.
[5]"Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity."
Ballare C., Lange M., Lapinaite A., Martin G.M., Morey L., Pascual G., Liefke R., Simon B., Shi Y., Gozani O., Carlomagno T., Benitah S.A., Di Croce L.
Nat. Struct. Mol. Biol. 19:1257-1265(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: H3K36ME3-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011550 mRNA. Translation: BAA25074.1.
U81490 mRNA. Translation: AAD00518.1.
CCDSCCDS37518.1.
RefSeqNP_033369.2. NM_009343.2.
UniGeneMm.258953.

3D structure databases

ProteinModelPortalQ9Z1B8.
SMRQ9Z1B8. Positions 28-147, 186-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204083. 2 interactions.
IntActQ9Z1B8. 1 interaction.
MINTMINT-4107427.

PTM databases

PhosphoSiteQ9Z1B8.

Proteomic databases

PaxDbQ9Z1B8.
PRIDEQ9Z1B8.

Protocols and materials databases

DNASU21652.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073724; ENSMUSP00000073402; ENSMUSG00000024193.
GeneID21652.
KEGGmmu:21652.
UCSCuc008bes.1. mouse.

Organism-specific databases

CTD5252.
MGIMGI:98647. Phf1.

Phylogenomic databases

eggNOGNOG244542.
GeneTreeENSGT00390000009222.
HOGENOMHOG000010307.
HOVERGENHBG004755.
InParanoidQ9Z1B8.
KOK11467.
OMAGEPPDRS.
OrthoDBEOG73V6JJ.
PhylomeDBQ9Z1B8.
TreeFamTF106420.

Gene expression databases

BgeeQ9Z1B8.
CleanExMM_PHF1.
GenevestigatorQ9Z1B8.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR025894. 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]
PfamPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 2 hits.
PROSITEPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio300920.
PROQ9Z1B8.
SOURCESearch...

Entry information

Entry namePHF1_MOUSE
AccessionPrimary (citable) accession number: Q9Z1B8
Secondary accession number(s): O54808
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot