位置:首页 > 蛋白库 > CNBP_PONAB
CNBP_PONAB
ID   CNBP_PONAB              Reviewed;         177 AA.
AC   Q5R5R5;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=CCHC-type zinc finger nucleic acid binding protein {ECO:0000305};
DE   AltName: Full=Cellular nucleic acid-binding protein {ECO:0000305};
DE            Short=CNBP {ECO:0000305};
DE   AltName: Full=Zinc finger protein 9;
GN   Name=CNBP; Synonyms=ZNF9;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Single-stranded DNA-binding protein that preferentially binds
CC       to the sterol regulatory element (SRE) sequence 5'-GTGCGGTG-3', and
CC       thereby mediates transcriptional repression (By similarity). Has a role
CC       as transactivator of the Myc promoter (By similarity). Binds single-
CC       stranded RNA in a sequence-specific manner (By similarity). Binds G-
CC       rich elements in target mRNA coding sequences (By similarity). Prevents
CC       G-quadruplex structure formation in vitro, suggesting a role in
CC       supporting translation by resolving stable structures on mRNAs (By
CC       similarity). {ECO:0000250|UniProtKB:P53996,
CC       ECO:0000250|UniProtKB:P62633, ECO:0000250|UniProtKB:P62634}.
CC   -!- SUBUNIT: Associates with the 40S ribosomal subunit, the 80S ribosome
CC       and with polysomes. {ECO:0000250|UniProtKB:P62633}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53996}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P62633}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P53996}.
CC   -!- PTM: Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes
CC       RNA binding. {ECO:0000250|UniProtKB:P62633}.
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; CR860791; CAH92901.1; -; mRNA.
DR   RefSeq; NP_001126703.1; NM_001133231.1.
DR   AlphaFoldDB; Q5R5R5; -.
DR   STRING; 9601.ENSPPYP00000015013; -.
DR   Ensembl; ENSPPYT00000015613; ENSPPYP00000015013; ENSPPYG00000013423.
DR   GeneID; 100173703; -.
DR   KEGG; pon:100173703; -.
DR   CTD; 7555; -.
DR   eggNOG; KOG4400; Eukaryota.
DR   GeneTree; ENSGT00950000183041; -.
DR   HOGENOM; CLU_058879_4_0_1; -.
DR   InParanoid; Q5R5R5; -.
DR   OMA; SHQARDC; -.
DR   OrthoDB; 1535084at2759; -.
DR   TreeFam; TF316974; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF00098; zf-CCHC; 7.
DR   SMART; SM00343; ZnF_C2HC; 7.
DR   SUPFAM; SSF57756; SSF57756; 4.
DR   PROSITE; PS50158; ZF_CCHC; 7.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; DNA-binding; Endoplasmic reticulum; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62633"
FT   CHAIN           2..177
FT                   /note="CCHC-type zinc finger nucleic acid binding protein"
FT                   /id="PRO_0000089967"
FT   ZN_FING         4..21
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         52..69
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         72..89
FT                   /note="CCHC-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         96..113
FT                   /note="CCHC-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         117..134
FT                   /note="CCHC-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         135..152
FT                   /note="CCHC-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         156..173
FT                   /note="CCHC-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          25..38
FT                   /note="RNA-binding Arg/Gly-rich region (RGG-box)"
FT                   /evidence="ECO:0000250|UniProtKB:P62633"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62633"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P53996"
FT   MOD_RES         25
FT                   /note="Omega-N-methylarginine; by PRMT1"
FT                   /evidence="ECO:0000250|UniProtKB:P62633"
FT   MOD_RES         27
FT                   /note="Omega-N-methylarginine; by PRMT1"
FT                   /evidence="ECO:0000250|UniProtKB:P62633"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53996"
FT   MOD_RES         79
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P62633"
SQ   SEQUENCE   177 AA;  19463 MW;  996F398285F52618 CRC64;
     MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGGFTSD RGFQFVSSSL PDICYRCGES
     GHLAKDCDLQ EDACYNCGRG GHIAKDCKEP KREREQCCYN CGKPGHLARD CDHADEQKCY
     SCGEFGHIQK DCTKVKCYRC GETGHVAINC SKTSEVNCYR CGESGHLARE CTIEATA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024