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ZCC17_MOUSE
ID   ZCC17_MOUSE             Reviewed;         241 AA.
AC   Q9ESX4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Zinc finger CCHC domain-containing protein 17;
DE   AltName: Full=Nucleolar protein of 40 kDa {ECO:0000303|PubMed:12893261};
DE            Short=pNO40 {ECO:0000303|PubMed:12893261};
DE   AltName: Full=Putative S1 RNA-binding domain protein;
DE            Short=PS1D protein;
GN   Name=Zcchc17; Synonyms=Ps1d; ORFNames=Ldc4;
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 [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP   IDENTIFICATION IN THE 60 S RIBOSOMAL SUBUNIT, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=12202495; DOI=10.1074/jbc.m208551200;
RA   Gueydan C., Wauquier C., De Mees C., Huez G., Kruys V.;
RT   "Identification of ribosomal proteins specific to higher eukaryotic
RT   organisms.";
RL   J. Biol. Chem. 277:45034-45040(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, and Liver;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=12893261; DOI=10.1016/s0006-291x(03)01208-7;
RA   Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.;
RT   "Molecular characterization of a novel nucleolar protein, pNO40.";
RL   Biochem. Biophys. Res. Commun. 307:569-577(2003).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- SUBUNIT: Interacts with PNN (By similarity). Associates with the 60S
CC       ribosomal subunit. {ECO:0000250, ECO:0000269|PubMed:12202495}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12202495,
CC       ECO:0000269|PubMed:12893261}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ESX4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ESX4-2; Sequence=VSP_015309;
CC   -!- TISSUE SPECIFICITY: Expressed in liver, brain, heart, kidney testis,
CC       stomach, small intestine, skin, thymus, uterus, placenta, spleen, lung
CC       and skeletal muscle. {ECO:0000269|PubMed:12202495,
CC       ECO:0000269|PubMed:12893261}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Less abundant than isoform 1.
CC       {ECO:0000305}.
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DR   EMBL; AJ272345; CAC03718.1; -; mRNA.
DR   EMBL; AY253297; AAO83392.1; -; mRNA.
DR   EMBL; BC018382; AAH18382.1; -; mRNA.
DR   EMBL; BC049231; AAH49231.1; -; mRNA.
DR   CCDS; CCDS38891.1; -. [Q9ESX4-1]
DR   RefSeq; NP_694800.1; NM_153160.4. [Q9ESX4-1]
DR   RefSeq; XP_006503322.1; XM_006503259.1.
DR   RefSeq; XP_006503323.1; XM_006503260.1.
DR   AlphaFoldDB; Q9ESX4; -.
DR   SMR; Q9ESX4; -.
DR   BioGRID; 546920; 5.
DR   IntAct; Q9ESX4; 1.
DR   STRING; 10090.ENSMUSP00000120807; -.
DR   iPTMnet; Q9ESX4; -.
DR   PhosphoSitePlus; Q9ESX4; -.
DR   EPD; Q9ESX4; -.
DR   MaxQB; Q9ESX4; -.
DR   PaxDb; Q9ESX4; -.
DR   PRIDE; Q9ESX4; -.
DR   ProteomicsDB; 252979; -. [Q9ESX4-1]
DR   ProteomicsDB; 252980; -. [Q9ESX4-2]
DR   Antibodypedia; 31100; 196 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000134159; ENSMUSP00000120807; ENSMUSG00000028772. [Q9ESX4-1]
DR   GeneID; 619605; -.
DR   KEGG; mmu:619605; -.
DR   UCSC; uc008uze.1; mouse. [Q9ESX4-1]
DR   CTD; 51538; -.
DR   MGI; MGI:1919955; Zcchc17.
DR   VEuPathDB; HostDB:ENSMUSG00000028772; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   GeneTree; ENSGT00510000047363; -.
DR   HOGENOM; CLU_068074_0_0_1; -.
DR   InParanoid; Q9ESX4; -.
DR   OMA; SEMVDVG; -.
DR   PhylomeDB; Q9ESX4; -.
DR   TreeFam; TF332136; -.
DR   BioGRID-ORCS; 619605; 1 hit in 70 CRISPR screens.
DR   ChiTaRS; Zcchc17; mouse.
DR   PRO; PR:Q9ESX4; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9ESX4; protein.
DR   Bgee; ENSMUSG00000028772; Expressed in undifferentiated genital tubercle and 71 other tissues.
DR   ExpressionAtlas; Q9ESX4; baseline and differential.
DR   Genevisible; Q9ESX4; MM.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043489; P:RNA stabilization; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR037320; pNO40.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR15838:SF1; PTHR15838:SF1; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50126; S1; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Zinc; Zinc-finger.
FT   CHAIN           1..241
FT                   /note="Zinc finger CCHC domain-containing protein 17"
FT                   /id="PRO_0000096904"
FT   DOMAIN          16..88
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   ZN_FING         131..148
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          160..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..241
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP64"
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP64"
FT   VAR_SEQ         1..48
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12202495"
FT                   /id="VSP_015309"
SQ   SEQUENCE   241 AA;  27472 MW;  C6F6B3B420716167 CRC64;
     MNSGRPETME NLPALYTIFQ GEVAMVTDYG AFIKIPGCRK QGLVHRTHMS SCRVDKPSEI
     VDVGDKVWVK LIGREMKNDR IKVSLSMKVV NQGTGKDLDP NNVVIEQEER RRRSFQDYTG
     QKITLEAVLN TTCKKCGCKG HFAKDCFMQP GGTKYSLIPE EEEEKEEAKA EGLEKPDPTK
     NSSRKRKKEK KKKKHRDRKS SDCDSSDSES DTGKKARHSS KDSKATKKKK KKKKHKKKHK
     E
 
 
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