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AP2B_CANLF
ID   AP2B_CANLF              Reviewed;         460 AA.
AC   Q76HI7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Transcription factor AP-2-beta;
DE            Short=AP2-beta;
DE   AltName: Full=Activating enhancer-binding protein 2-beta;
GN   Name=TFAP2B;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Brain;
RA   Hashizume C., Takeuchi Y., Mori Y.;
RT   "Canis familiaris transcription factor AP-2 beta mRNA, complete cds.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sequence-specific DNA-binding protein that interacts with
CC       inducible viral and cellular enhancer elements to regulate
CC       transcription of selected genes. AP-2 factors bind to the consensus
CC       sequence 5'-GCCNNNGGC-3' and activate genes involved in a large
CC       spectrum of important biological functions including proper eye, face,
CC       body wall, limb and neural tube development. They also suppress a
CC       number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-beta
CC       appears to be required for normal face and limb development and for
CC       proper terminal differentiation and function of renal tubular epithelia
CC       (By similarity). {ECO:0000250|UniProtKB:Q92481}.
CC   -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC       other AP-2 family members. Interacts with CITED4. Interacts with UBE2I.
CC       Interacts with KCTD1; this interaction represses transcription
CC       activation. Interacts with CITED2 (via C-terminus); the interaction
CC       stimulates TFAP2B-transcriptional activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q92481}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61313}. Note=In
CC       the brain, localizes to the arcuate hypothalamic nucleus, the
CC       ventromedial hypothalamic nucleus and the accumbens nucleus of the
CC       ventral striatum. {ECO:0000250|UniProtKB:Q61313}.
CC   -!- PTM: Sumoylated on Lys-21; which inhibits transcriptional activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC80223.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB101212; BAC80223.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001002977.1; NM_001002977.1.
DR   AlphaFoldDB; Q76HI7; -.
DR   STRING; 9615.ENSCAFP00000055095; -.
DR   PaxDb; Q76HI7; -.
DR   Ensembl; ENSCAFT00040009886; ENSCAFP00040008572; ENSCAFG00040005270.
DR   GeneID; 403463; -.
DR   KEGG; cfa:403463; -.
DR   CTD; 7021; -.
DR   eggNOG; KOG3811; Eukaryota.
DR   HOGENOM; CLU_035175_4_1_1; -.
DR   InParanoid; Q76HI7; -.
DR   OMA; WALLVTY; -.
DR   OrthoDB; 641707at2759; -.
DR   TreeFam; TF313718; -.
DR   Reactome; R-CFA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR   Reactome; R-CFA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0035909; P:aorta morphogenesis; ISS:UniProtKB.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0097275; P:cellular ammonium homeostasis; ISS:UniProtKB.
DR   GO; GO:0097276; P:cellular creatinine homeostasis; ISS:UniProtKB.
DR   GO; GO:0097277; P:cellular urea homeostasis; ISS:UniProtKB.
DR   GO; GO:0072044; P:collecting duct development; ISS:UniProtKB.
DR   GO; GO:0072017; P:distal tubule development; ISS:UniProtKB.
DR   GO; GO:0097070; P:ductus arteriosus closure; ISS:UniProtKB.
DR   GO; GO:0035136; P:forelimb morphogenesis; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR   GO; GO:0035137; P:hindlimb morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR   GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0055062; P:phosphate ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; 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   GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR   GO; GO:0055075; P:potassium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0003091; P:renal water homeostasis; ISS:UniProtKB.
DR   GO; GO:0055078; P:sodium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
DR   InterPro; IPR004979; TF_AP2.
DR   InterPro; IPR008122; TF_AP2_beta.
DR   InterPro; IPR013854; TF_AP2_C.
DR   PANTHER; PTHR10812; PTHR10812; 1.
DR   PANTHER; PTHR10812:SF14; PTHR10812:SF14; 1.
DR   Pfam; PF03299; TF_AP-2; 1.
DR   PRINTS; PR01750; AP2BTNSCPFCT.
DR   PRINTS; PR01748; AP2TNSCPFCT.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..460
FT                   /note="Transcription factor AP-2-beta"
FT                   /id="PRO_0000184800"
FT   REGION          30..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..79
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         258
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  50474 MW;  A6420EA0C265DDA2 CRC64;
     MHSPPRDQAA IMLWKLVENV KYEDIYEDRH DGVPSHSSRL SQLGSVSQGP YSSAPPLSHT
     PSSDFQPPYF PPPYQPLPYH QSQDPYSHVN DPYSLNPLHQ PQQHPWGQRQ RQEVGSEAGS
     LLPQPRAALP QLSGLDPRRD YHSVRRPDVL LHSAHHGLDA GMGDSLSLHG LGHPGMEDVQ
     SVEDANNSGM NLLDQSVIKK VPVPPKSVTS LMMNKDGFLG GMSVNTGEVF CSVPGRLSLL
     SSTSKYKVTV GEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLRERLEK IGLNLPAGRR
     KAANVTLLTS LVEGEAVHLA RDFGYICETE FPAKAVSEYL NRQHTDPSDL HSRKNMLLAT
     KQLCKEFTDL LAQDRTPIGN SRPSPILEPG IQSCLTHFSL ITHGFGAPAI CAALTALQNY
     LTEALKGMDK MFLNNTTTNR HTSGEGPGSK TGDKEEKHRK
 
 
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