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ZN512_BOVIN
ID   ZN512_BOVIN             Reviewed;         567 AA.
AC   A4FV61;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Zinc finger protein 512;
GN   Name=ZNF512;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
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; BC123776; AAI23777.1; -; mRNA.
DR   RefSeq; NP_001076941.1; NM_001083472.1.
DR   AlphaFoldDB; A4FV61; -.
DR   STRING; 9913.ENSBTAP00000032885; -.
DR   PaxDb; A4FV61; -.
DR   PRIDE; A4FV61; -.
DR   Ensembl; ENSBTAT00000032958; ENSBTAP00000032885; ENSBTAG00000003902.
DR   GeneID; 533884; -.
DR   KEGG; bta:533884; -.
DR   CTD; 84450; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003902; -.
DR   VGNC; VGNC:37290; ZNF512.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158595; -.
DR   HOGENOM; CLU_481412_0_0_1; -.
DR   InParanoid; A4FV61; -.
DR   OMA; PFFPESG; -.
DR   OrthoDB; 222563at2759; -.
DR   TreeFam; TF331185; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000003902; Expressed in thymus and 108 other tissues.
DR   ExpressionAtlas; A4FV61; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..567
FT                   /note="Zinc finger protein 512"
FT                   /id="PRO_0000333736"
FT   ZN_FING         197..220
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         287..310
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         406..430
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         440..463
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT   CROSSLNK        84
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT   CROSSLNK        227
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96ME7"
FT   CROSSLNK        333
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96ME7"
SQ   SEQUENCE   567 AA;  64684 MW;  0A78A259D38140D1 CRC64;
     MSSRLGAVPA TPGPTPFKQQ RSTRIVGAKN SRTQCSIKDN SFQYTIPHDD SLSGSSSASS
     CEPVSDFPAS FRKSTYWMKM RRIKSAAASH VEGPGGVSTK GKRKPRQEED EDYREFPQKK
     HKLYGRKQRP KAQPNPKAQT RRIRKEPPAY AAGSLEEQWY LEIVDKGSVS CPTCQAVGRK
     TIEGLKKHME NCKQEMFTCH HCGKQLRSLA GMKYHVMANH NSLPILKAGD EIDEPSERER
     LRTVLKRLGK LRCMRESCSS SFTSIMGYLY HVRKCGKGAA ELEKMTLKCH HCGKPYRSKA
     GLAYHLRSEH GPISFFPESG QPECLKDMSL ESKSGGRVQR RSAKIAVYHL QELASAELAK
     EWPKRKVLQD LVPDDRKLKY TRPGLPTFSQ EVLHKWKSDI KKYHRIQCPN QGCEAVYSSV
     SGLKAHLGSC TLGTFVAGKY KCLLCQKEFV SESGVKYHIN SVHAEDWFVV NPTTTKSFEK
     LMKIKQRQQE EEKRRQQHRS RRSLRRRQQP GIELPETEPS LRVGKDQRRN HEELLVATSR
     KEPEQEPVPT QFQKVRSPKT NHKRGKK
 
 
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