ZN319_MOUSE
ID ZN319_MOUSE Reviewed; 581 AA.
AC Q9ERR8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger protein 319;
GN Name=Znf319; Synonyms=Zfp319;
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 [GENOMIC DNA].
RX PubMed=11161788; DOI=10.1006/geno.2000.6420;
RA Laub F., Aldabe R., Ou J., Ramirez F.;
RT "Overexpression of a novel zinc-finger protein induces apoptosis in NIH3T3
RT fibroblasts.";
RL Genomics 70:375-380(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF288403; AAG28743.1; -; Genomic_DNA.
DR EMBL; BC059823; AAH59823.1; -; mRNA.
DR CCDS; CCDS22559.1; -.
DR RefSeq; NP_077787.3; NM_024467.3.
DR AlphaFoldDB; Q9ERR8; -.
DR SMR; Q9ERR8; -.
DR STRING; 10090.ENSMUSP00000053397; -.
DR iPTMnet; Q9ERR8; -.
DR PhosphoSitePlus; Q9ERR8; -.
DR MaxQB; Q9ERR8; -.
DR PaxDb; Q9ERR8; -.
DR PRIDE; Q9ERR8; -.
DR ProteomicsDB; 299575; -.
DR Antibodypedia; 29030; 99 antibodies from 19 providers.
DR DNASU; 79233; -.
DR Ensembl; ENSMUST00000057717; ENSMUSP00000053397; ENSMUSG00000046556.
DR GeneID; 79233; -.
DR KEGG; mmu:79233; -.
DR UCSC; uc009myf.1; mouse.
DR CTD; 79233; -.
DR MGI; MGI:1890618; Zfp319.
DR VEuPathDB; HostDB:ENSMUSG00000046556; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160309; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q9ERR8; -.
DR OMA; QHHSAHT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9ERR8; -.
DR TreeFam; TF332615; -.
DR BioGRID-ORCS; 79233; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp319; mouse.
DR PRO; PR:Q9ERR8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ERR8; protein.
DR Bgee; ENSMUSG00000046556; Expressed in rostral migratory stream and 223 other tissues.
DR Genevisible; Q9ERR8; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..581
FT /note="Zinc finger protein 319"
FT /id="PRO_0000047528"
FT ZN_FING 75..99
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 103..125
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 131..153
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 201..223
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 257..279
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..308
FT /note="C2H2-type 7; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 427..449
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 13; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..535
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 541..563
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2F9"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2F9"
SQ SEQUENCE 581 AA; 65644 MW; C78724098648C84F CRC64;
MSESWQQPPQ TQPQQPQAPQ PQHHAETPPA LAEHTLPPGS AENPLGCAVY GILLQPDPGL
QPPQHAPLQA GEPGPKCGVC GHDLAHLSSP HEHQCLAGHD RSFQCTQCLK IFHQATDLLE
HQCVQAEQKP FVCGVCKMGF SLLTSLAQHH SSHTGMVKCS ICDKTYKPAE AAEPATTTAP
SLPSAPPPAN IAPVEQPEKP YSCPVCQKPF KHLSELSRHE RIHTGEKPYK CTLCDKSFSQ
SSHLVHHKRT HSSERPYKCA VCEKTFKHRS HLVRHMYAHS GEHHLFRCNV CELHFKESSE
LLQHPCTPSG ERPFRCGECQ KAFKRPSDLR QHERTHSAER PFKCDLCPMG FKQQYALMRH
RRTHKTEEPF KCGLCEKGFG QPSHLLYHQH VHTLETLFKC PVCQKGFDQS AELLRHKCLP
TSTERPFKCP VCNKAYKRAS ALQKHQLSHC AAAEKPLRCT LCERRFFSSS EFVQHRCDPA
REKPLKCPDC EKRFKYASDL QRHRRVHTGE KPYKCPSCDK AFKQREHLNK HQGVHAREQQ
FKCVWCGERF LDVALLQEHS AQHSAAAAAA EGAYQVAACL P
