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PRDM4_MOUSE
ID   PRDM4_MOUSE             Reviewed;         803 AA.
AC   Q80V63; B2RTL4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=PR domain zinc finger protein 4;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 4;
GN   Name=Prdm4;
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=Brain, and Mammary tumor;
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: May function as a transcription factor involved in cell
CC       differentiation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC042516; AAH42516.1; ALT_INIT; mRNA.
DR   EMBL; BC139409; AAI39410.1; -; mRNA.
DR   CCDS; CCDS24093.1; -.
DR   RefSeq; NP_857633.2; NM_181650.3.
DR   RefSeq; XP_006514256.1; XM_006514193.3.
DR   RefSeq; XP_006514257.1; XM_006514194.3.
DR   RefSeq; XP_011241884.1; XM_011243582.1.
DR   AlphaFoldDB; Q80V63; -.
DR   SMR; Q80V63; -.
DR   BioGRID; 215601; 32.
DR   STRING; 10090.ENSMUSP00000041942; -.
DR   PhosphoSitePlus; Q80V63; -.
DR   PaxDb; Q80V63; -.
DR   PRIDE; Q80V63; -.
DR   ProteomicsDB; 289839; -.
DR   Antibodypedia; 18264; 292 antibodies from 32 providers.
DR   DNASU; 72843; -.
DR   Ensembl; ENSMUST00000220032; ENSMUSP00000151931; ENSMUSG00000035529.
DR   GeneID; 72843; -.
DR   KEGG; mmu:72843; -.
DR   UCSC; uc011xkq.1; mouse.
DR   CTD; 11108; -.
DR   MGI; MGI:1920093; Prdm4.
DR   VEuPathDB; HostDB:ENSMUSG00000035529; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; KOG2461; Eukaryota.
DR   GeneTree; ENSGT00940000156443; -.
DR   HOGENOM; CLU_019772_0_0_1; -.
DR   InParanoid; Q80V63; -.
DR   OMA; RDYAQQM; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q80V63; -.
DR   TreeFam; TF332513; -.
DR   BioGRID-ORCS; 72843; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Prdm4; mouse.
DR   PRO; PR:Q80V63; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q80V63; protein.
DR   Bgee; ENSMUSG00000035529; Expressed in embryonic post-anal tail and 229 other tissues.
DR   ExpressionAtlas; Q80V63; baseline and differential.
DR   Genevisible; Q80V63; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0035097; C:histone methyltransferase complex; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005123; F:death receptor binding; ISO:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:1990226; F:histone methyltransferase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISO:MGI.
DR   GO; GO:2000736; P:regulation of stem cell differentiation; ISO:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd19189; PR-SET_PRDM4; 1.
DR   Gene3D; 2.170.270.10; -; 1.
DR   InterPro; IPR017124; PRDM4.
DR   InterPro; IPR044404; PRDM4_PR/SET.
DR   InterPro; IPR041493; PRDM4_Znf_knuckle.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   Pfam; PF18445; zf_PR_Knuckle; 1.
DR   PIRSF; PIRSF037161; PRDM4; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..803
FT                   /note="PR domain zinc finger protein 4"
FT                   /id="PRO_0000230792"
FT   DOMAIN          408..532
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   ZN_FING         593..615
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         621..643
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         649..671
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         677..699
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         705..727
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         733..755
FT                   /note="C2H2-type 6; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          757..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..779
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  88145 MW;  99A0DDBEDC54561E CRC64;
     MNDMNLSPVG MEQLSSSSVS NALPVSGSHL GLAASPSHSA IPAPGLPVAI PNLGPSLSSL
     PSALSLMLPV GIGDRGVMCG LPERNYTLPP PPYPHLESSY FRTILPGILS YLADRPPPQY
     IHPNSINVDG NTALSITNNP SALDPYQANG NVGLELGIVS IDSRSVNTHG AQSLHPNDGH
     EVALDTTITM ENVSRVTSPI STDGMAEELT MDGVTGEHPQ IPNGSRSHEP LSVDSVSNSL
     TAEAVGHGGV IPIHGNGLEL PVVMETDHIA NRVNGMSDST LSDSIHTVAM STNSVSVALS
     TSHNLASLES VSLHEVGLSL EPVAVSSITQ EVAMGTGHVD VSSDSLSFVP SSLQMEDSNS
     NKENMATLFT IWCTLCDRAY PSDCPDHGPV TFVPDTPIES RARLSLPKQL VLRQSIVGTD
     VVGVLPLIGV WTAETIPVRT CFGPLIGQQS HSLEVAEWTD KAVNHVWKIY HTGVLEFCII
     TTDENECNWM MFVRKARNRE EQNLVAYPHD GKIYFCTSQD IPPESELLFY YSRNYAQQIG
     VPEHPDVHLC NCGKECSSYS EFKAHLTSHI HNHLPSQGHS SSHGPSHSKE RKWKCSMCPQ
     AFISPSKLHV HFMGHMGMKP HKCDFCSKAF SDPSNLRTHL KIHTGQKNYR CTLCDKSFTQ
     KAHLESHMVI HTGEKNLKCD YCDKLFMRRQ DLKQHVLIHT QERQIKCPKC DKLFLRTNHL
     KKHLNSHEGK RDYVCEKCTK AYLTKYHLTR HLKTCKEPSS SSSAQEEEDD ESEEEDLADS
     MRTEDCRMGS AVYSTDESLS AHK
 
 
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