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FIP1_DANRE
ID   FIP1_DANRE              Reviewed;         570 AA.
AC   Q5XJD3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Pre-mRNA 3'-end-processing factor FIP1;
DE   AltName: Full=FIP1-like 1 protein;
GN   Name=fip1l1; ORFNames=zgc:103421;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125 AND SER-247, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Involved in mRNA processing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
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DR   EMBL; BC083370; AAH83370.1; -; mRNA.
DR   RefSeq; NP_001006042.1; NM_001006042.1.
DR   AlphaFoldDB; Q5XJD3; -.
DR   SMR; Q5XJD3; -.
DR   STRING; 7955.ENSDARP00000094123; -.
DR   iPTMnet; Q5XJD3; -.
DR   PaxDb; Q5XJD3; -.
DR   PRIDE; Q5XJD3; -.
DR   GeneID; 450021; -.
DR   KEGG; dre:450021; -.
DR   CTD; 450021; -.
DR   ZFIN; ZDB-GENE-041010-138; fip1l1b.
DR   eggNOG; KOG1049; Eukaryota.
DR   InParanoid; Q5XJD3; -.
DR   OrthoDB; 929913at2759; -.
DR   PhylomeDB; Q5XJD3; -.
DR   Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DRE-72187; mRNA 3'-end processing.
DR   Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-DRE-77595; Processing of Intronless Pre-mRNAs.
DR   PRO; PR:Q5XJD3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR   InterPro; IPR007854; Fip1_dom.
DR   Pfam; PF05182; Fip1; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..570
FT                   /note="Pre-mRNA 3'-end-processing factor FIP1"
FT                   /id="PRO_0000215041"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..34
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..105
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         125
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   570 AA;  62966 MW;  9EE1C8C2E28F9B37 CRC64;
     MSAEEADKTT TTDASAGDEE EEWLYGDEGE SKETEEEEAK LTAAISATST TPVAEDAPTT
     TNNSSDSATP PTTTTTTGNG VASQEEAPGE DEDSESDSDD DDDDVRVTIG DIKTGAPQYT
     GYGGTPVNLN IKSAGSRAYG AGAKVKGVDL EAPGSINGVP VLEADMESFE EKPWRKPGAD
     LSDYFNYGFN EDTWKAYCEK QKRLRMGLDV LNIGSTTSKI SVQQGRTGNN EKEITIPAHA
     SKAEFTSPSN LYKAGLNQGR ISPPHWAGPP SQDLSYYTKT PGTIDVIGGQ TATISRVEGR
     RRHNLEGNNI QVISEHSSSE VEPEVQKMPP PFFPPGPLPP NIPPPPFLPP PVSQAPPLIP
     PHRMPITVPP PNFPPPTGGP PPSLIPTLDN SGHPGGYDGR PVAPYPFPTG GFPPPMQGAV
     NPWPGLMENP KQWDYYPRRD KEREKERERE RQRDRGHERD HSPNAGPYNS MAMCSDEERY
     RSYRDYGDRG YERHRERASR EKEERHGGRR HREKEEGRHK SSRSSSRRRH ESEEGDSHRR
     HKHKKSKRSK EGKEPSEERS ADQENQEAME
 
 
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