ID   PHF13_MOUSE             Reviewed;         296 AA.
AC   Q8K2W6;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=PHD finger protein 13;
GN   Name=Phf13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Modulates chromatin structure. Required for normal chromosome
CC       condensation during the early stages of mitosis. Required for normal
CC       chromosome separation during mitosis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with histone H3 that is trimethylated at 'Lys-4'
CC       (H3K4me3). Interacts with GSK3B (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm
CC       {ECO:0000250}. Note=Predominantly bound to chromatin, but a minor
CC       proportion is also detected in the nucleoplasm. {ECO:0000250}.
CC   -!- PTM: Subject to proteasomal degradation. Stable when bound to
CC       chromatin. The soluble form is rapidly degraded (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; BC029632; AAH29632.2; -; mRNA.
DR   EMBL; BC059282; AAH59282.1; -; mRNA.
DR   CCDS; CCDS51388.1; -.
DR   RefSeq; NP_766293.2; NM_172705.2.
DR   AlphaFoldDB; Q8K2W6; -.
DR   SMR; Q8K2W6; -.
DR   STRING; 10090.ENSMUSP00000062590; -.
DR   iPTMnet; Q8K2W6; -.
DR   PhosphoSitePlus; Q8K2W6; -.
DR   PaxDb; Q8K2W6; -.
DR   PRIDE; Q8K2W6; -.
DR   ProteomicsDB; 289493; -.
DR   Antibodypedia; 13124; 142 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000055688; ENSMUSP00000062590; ENSMUSG00000047777.
DR   GeneID; 230936; -.
DR   KEGG; mmu:230936; -.
DR   UCSC; uc008vyx.2; mouse.
DR   CTD; 148479; -.
DR   MGI; MGI:2446217; Phf13.
DR   VEuPathDB; HostDB:ENSMUSG00000047777; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   GeneTree; ENSGT00530000063882; -.
DR   HOGENOM; CLU_047981_0_0_1; -.
DR   InParanoid; Q8K2W6; -.
DR   OMA; HAFQSEG; -.
DR   OrthoDB; 982722at2759; -.
DR   PhylomeDB; Q8K2W6; -.
DR   TreeFam; TF331373; -.
DR   BioGRID-ORCS; 230936; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Phf13; mouse.
DR   PRO; PR:Q8K2W6; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8K2W6; protein.
DR   Bgee; ENSMUSG00000047777; Expressed in secondary oocyte and 248 other tissues.
DR   ExpressionAtlas; Q8K2W6; baseline and differential.
DR   Genevisible; Q8K2W6; MM.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR   CDD; cd15632; PHD_PHF13; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR041947; PHD_PHF13.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Chromatin regulator; DNA condensation;
KW   Metal-binding; Mitosis; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..296
FT                   /note="PHD finger protein 13"
FT                   /id="PRO_0000059305"
FT   ZN_FING         230..276
FT                   /note="PHD-type"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..244
FT                   /note="Interaction with trimethylated histone H3 (H3K4)"
FT                   /evidence="ECO:0000250"
FT   MOTIF           106..123
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        53..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  33424 MW;  FE89C6ABFB6D57C8 CRC64;
     MDSDSCAAAF HPEEYSPTCK RRRTVEDFNK FCTFVLAYAG YIPYPKEELP LRSSPSPANS
     TAGTIDSDGW DTGFSDITPS VPDRCFSHLQ PSLLQRAKPS NYLLDRKTTD KLKKKKRRKR
     RDSDIPVKEG FRESLLKLEA ADPYVETPSS PTMQDIPQAS ADPCSGWDSD TPSSGSCATV
     SPDQVTEIKT EGKRTIVRQG KQVVFRDEDS TGNDEDIMVD SDDDSWDLVT CFCMKPFAGR
     PMIECNECHT WIHLSCAKIR KSNVPEVFVC QKCRDSKFDI RRSNRSRMGS RKLFLD