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NFIB_BOVIN
ID   NFIB_BOVIN              Reviewed;         420 AA.
AC   Q0VCL6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Nuclear factor 1 B-type;
DE            Short=NF1-B;
DE            Short=Nuclear factor 1/B;
DE   AltName: Full=Nuclear factor I/B;
DE            Short=NF-I/B;
DE            Short=NFI-B;
GN   Name=NFIB;
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=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional activator of GFAP, essential for proper brain
CC       development. Recognizes and binds the palindromic sequence 5'-
CC       TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the
CC       origin of replication of adenovirus type 2. These proteins are
CC       individually capable of activating transcription and replication.
CC       {ECO:0000250|UniProtKB:P97863}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00436}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:O00712}.
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00436}.
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DR   EMBL; BC120107; AAI20108.1; -; mRNA.
DR   RefSeq; NP_001069572.1; NM_001076104.2.
DR   AlphaFoldDB; Q0VCL6; -.
DR   STRING; 9913.ENSBTAP00000011234; -.
DR   PaxDb; Q0VCL6; -.
DR   PRIDE; Q0VCL6; -.
DR   Ensembl; ENSBTAT00000075331; ENSBTAP00000063855; ENSBTAG00000027442.
DR   GeneID; 538474; -.
DR   KEGG; bta:538474; -.
DR   CTD; 4781; -.
DR   VEuPathDB; HostDB:ENSBTAG00000027442; -.
DR   VGNC; VGNC:32039; NFIB.
DR   eggNOG; KOG3663; Eukaryota.
DR   GeneTree; ENSGT00950000182916; -.
DR   InParanoid; Q0VCL6; -.
DR   OrthoDB; 967862at2759; -.
DR   ChiTaRS; NFIB; cattle.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000027442; Expressed in intramuscular adipose tissue and 108 other tissues.
DR   ExpressionAtlas; Q0VCL6; baseline and differential.
DR   GO; GO:0044300; C:cerebellar mossy fiber; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0021960; P:anterior commissure morphogenesis; ISS:UniProtKB.
DR   GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0060486; P:club cell differentiation; ISS:UniProtKB.
DR   GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0061141; P:lung ciliated cell differentiation; ISS:UniProtKB.
DR   GO; GO:2000795; P:negative regulation of epithelial cell proliferation involved in lung morphogenesis; ISS:UniProtKB.
DR   GO; GO:2000791; P:negative regulation of mesenchymal cell proliferation involved in lung development; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0021740; P:principal sensory nucleus of trigeminal nerve development; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0060509; P:type I pneumocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0060510; P:type II pneumocyte differentiation; ISS:UniProtKB.
DR   InterPro; IPR000647; CTF/NFI.
DR   InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR   InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR   InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   PANTHER; PTHR11492; PTHR11492; 1.
DR   Pfam; PF00859; CTF_NFI; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR   SMART; SM00523; DWA; 1.
DR   PROSITE; PS00349; CTF_NFI_1; 1.
DR   PROSITE; PS51080; CTF_NFI_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA replication; DNA-binding; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..420
FT                   /note="Nuclear factor 1 B-type"
FT                   /id="PRO_0000273723"
FT   DNA_BIND        2..195
FT                   /note="CTF/NF-I"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT   REGION          189..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           397..405
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   COMPBIAS        252..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..374
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   MOD_RES         286
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P97863"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00712"
FT   MOD_RES         335
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P97863"
FT   MOD_RES         388
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P97863"
SQ   SEQUENCE   420 AA;  47499 MW;  685A0EF488320640 CRC64;
     MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
     LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC
     LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL
     AYYVQEQDSG QSGSPSHNDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP
     IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPNSPAAGS
     RTWHERDQDM SSPTTMKKPE KPLFSSTSPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP
     PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQSWYLG
 
 
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