GenomeNet

Database: UniProt
Entry: ZN319_MOUSE
LinkDB: ZN319_MOUSE
Original site: 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   27-MAR-2024, entry version 167.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 10090-ENSMUSP00000053397; -.
DR   ProteomicsDB; 299575; -.
DR   Antibodypedia; 29030; 106 antibodies from 20 providers.
DR   DNASU; 79233; -.
DR   Ensembl; ENSMUST00000057717.8; ENSMUSP00000053397.7; ENSMUSG00000046556.8.
DR   GeneID; 79233; -.
DR   KEGG; mmu:79233; -.
DR   UCSC; uc009myf.1; mouse.
DR   AGR; MGI:1890618; -.
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; 4044100at2759; -.
DR   PhylomeDB; Q9ERR8; -.
DR   TreeFam; TF332615; -.
DR   BioGRID-ORCS; 79233; 3 hits in 77 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 225 other cell types or 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   Gene3D; 3.30.160.60; Classic Zinc Finger; 11.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24379; KRAB AND ZINC FINGER DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR24379:SF124; ZINC FINGER PROTEIN 319-LIKE; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   Pfam; PF13465; zf-H2C2_2; 2.
DR   SMART; SM00355; ZnF_C2H2; 14.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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
//
DBGET integrated database retrieval system