ZN827_MOUSE
ID ZN827_MOUSE Reviewed; 1078 AA.
AC Q505G8; B2RXD8; Q5M7B0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc finger protein 827;
GN Name=Znf827; Synonyms=Zfp827;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Kidney;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: As part of a ribonucleoprotein complex composed at least of
CC HNRNPK, HNRNPL and the circular RNA circZNF827 that nucleates the
CC complex on chromatin, may negatively regulate the transcription of
CC genes involved in neuronal differentiation. Could also recruit the
CC nucleosome remodeling and histone deacetylase/NuRD complex to telomeric
CC regions of chromosomes to regulate chromatin remodeling as part of
CC telomere maintenance. {ECO:0000250|UniProtKB:Q17R98}.
CC -!- SUBUNIT: Part of a transcription inhibitory ribonucleoprotein complex
CC composed at least of the circular RNA circZNF827, HNRNPK and HNRNPL.
CC Interacts with the nucleosome remodeling and histone deacetylase/NuRD
CC complex. Interacts with RBBP4; the interaction is direct and recruits
CC RBBP4, a component of the NuRD complex, to telomeres.
CC {ECO:0000250|UniProtKB:Q17R98}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q17R98}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q17R98}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q505G8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q505G8-2; Sequence=VSP_032466, VSP_032467;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH88739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC101790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088739; AAH88739.1; ALT_INIT; mRNA.
DR EMBL; BC094552; AAH94552.1; -; mRNA.
DR EMBL; BC151183; AAI51184.1; -; mRNA.
DR CCDS; CCDS52604.1; -. [Q505G8-1]
DR RefSeq; NP_001281208.1; NM_001294279.1.
DR RefSeq; NP_839998.2; NM_178267.3. [Q505G8-1]
DR AlphaFoldDB; Q505G8; -.
DR STRING; 10090.ENSMUSP00000096214; -.
DR iPTMnet; Q505G8; -.
DR PhosphoSitePlus; Q505G8; -.
DR MaxQB; Q505G8; -.
DR PaxDb; Q505G8; -.
DR PRIDE; Q505G8; -.
DR Antibodypedia; 56760; 26 antibodies from 11 providers.
DR Ensembl; ENSMUST00000087927; ENSMUSP00000085238; ENSMUSG00000071064. [Q505G8-2]
DR Ensembl; ENSMUST00000098614; ENSMUSP00000096214; ENSMUSG00000071064. [Q505G8-1]
DR GeneID; 622675; -.
DR KEGG; mmu:622675; -.
DR UCSC; uc009mig.1; mouse. [Q505G8-2]
DR UCSC; uc009mii.1; mouse. [Q505G8-1]
DR CTD; 622675; -.
DR MGI; MGI:2444807; Zfp827.
DR VEuPathDB; HostDB:ENSMUSG00000071064; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156063; -.
DR HOGENOM; CLU_595746_0_0_1; -.
DR InParanoid; Q505G8; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q505G8; -.
DR TreeFam; TF333046; -.
DR BioGRID-ORCS; 622675; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp827; mouse.
DR PRO; PR:Q505G8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q505G8; protein.
DR Bgee; ENSMUSG00000071064; Expressed in humerus cartilage element and 204 other tissues.
DR ExpressionAtlas; Q505G8; baseline and differential.
DR Genevisible; Q505G8; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120325; F:NuRD complex binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISS:UniProtKB.
DR GO; GO:1904791; P:negative regulation of shelterin complex assembly; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Telomere;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1078
FT /note="Zinc finger protein 827"
FT /id="PRO_0000325891"
FT ZN_FING 371..393
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..421
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 814..836
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 842..864
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 894..916
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 926..949
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1016..1038
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1044..1066
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..14
FT /note="Mediates direct interaction with RBBP4"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT REGION 307..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..5
FT /note="RRK motif; mediates NuRD recruitment to telomeres"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 463
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 520
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 636
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 655
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 707
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 739
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 775
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 795
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 867
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 888
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 955
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT CROSSLNK 1011
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q17R98"
FT VAR_SEQ 421..509
FT /note="HQHQDRGETFQCQLCPFTSSRHFSLKLHMRCHQHFLRTEAKVKEEIPDPDVK
FT GSPHLSDSGCLGQQREGGGTELVGTVMTSNTPERTGQ -> SHLPRRGRGFVLFSTAGG
FT FLADREHCGGAGLRKLTLGCE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032466"
FT VAR_SEQ 510..1078
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032467"
SQ SEQUENCE 1078 AA; 118536 MW; EA0EC74DB64BEB51 CRC64;
MPRRKQEQPK RLPSHVSRQD EAEGDFSEGE QWYGNSSETP SEASYGEVQE NYKLSLEDRI
QEQSTSPDTS LGSATPSSHT LELVALDGEV LRDSLQCQGH LSPGVSSVCD DDPPSSNKPL
SSNLRRLLEA GSLKLDGTAN GRVESPVNVG PSLSFSPPSH HAQQLSVLAR KLAEKQDQSD
QFTPSNRFIW NQGKWLPNST TTCGLSPDSA ILKLKAAANA VLQDKSLSRT EESLRFESFS
SPFSSQSASS TLAALSKKVS ERSLTPGQEH PPPASSFLSL ASMTSSAALL KEVAARAAGS
LLAEKSSLLP DDPLPLPSSE KKPEKVTPPP PPPPPTAQPP QSLELLLLPV SKGRASKPSN
SAPEEESGKP FQCPICGLVI KRKSYWKRHM VIHTGLKSHQ CPLCPFRCAR KDNLKSHMKV
HQHQDRGETF QCQLCPFTSS RHFSLKLHMR CHQHFLRTEA KVKEEIPDPD VKGSPHLSDS
GCLGQQREGG GTELVGTVMT SNTPERTGQG GAGVAPLLVK EEPKEDNGLP TSFTLNAADR
PANHTKLKDP SEYVSNSAAV LFSQDISVKM ASDFLMKLSA ANQKEPMNLN FKVKEEPKEE
ESLSMPLPRS SYVFSPEPEV STPSVSEDPL TPQEGKGSVL RRDMSAKAAS ELLMKLSAES
YKETQAVTVK EEPMEVDIQD SPASISPSRN IGYSTLMGRE KTEPLQKLPE GRVPPERNLF
SQDISVKMAS ELLFQLSEKV SKEHNHTKEN AMRTTTSPFF SEDTFRQSPF TSNSKDLLPG
ESVLHGRVSA PETEKIVLEA GNGLPSWKFN DQLFPCDVCG KVFGRQQTLS RHLSLHTEER
KYKCHLCPYA AKCRANLNQH LTVHSVKLVS TDTEDIVSAV TSEGSDGKKH PYYYSCHVCG
FETELNVQFV SHMSLHVDKE QWMFSICCTA CDFVTMEEAE IKTHIGTKHT GDDRKTPSES
NSPSSSSLST LSDSANGKDD SDSSQKNKGG NNLLVISVVP GSQPSLNNEE KPEKGFECVF
CNFVCKTKNM FERHLQIHLI TRMFECDVCH KFMKTPEQLL EHKKCHTVPT GGLNSGQW
