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Transcription factor Sp3

 SP3_CHICK               Reviewed;         771 AA.
Q90WR8;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 102.
RecName: Full=Transcription factor Sp3;
Name=SP3;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH V-JUN.
PubMed=12821939; DOI=10.1038/sj.onc.1206713;
Chamboredon S., Briggs J., Vial E., Hurault J., Galvagni F.,
Oliviero S., Bos T., Castellazzi M.;
"v-Jun downregulates the SPARC target gene by binding to the proximal
promoter indirectly through Sp1/3.";
Oncogene 22:4047-4061(2003).
-!- FUNCTION: Transcriptional factor that can act as an activator or
repressor depending on post-translational modifications. Binds to
GT and GC boxes promoter elements. Competes with SP1 for the GC-
box promoters. Weak activator of transcription (By similarity).
Required for activation of SPARC transcription. {ECO:0000250,
ECO:0000269|PubMed:12821939}.
-!- SUBUNIT: Interacts with HDAC1 and HDAC2; the interaction
deacetylates SP3 and regulates its transcriptional activity (By
similarity). Interacts with v-Jun. {ECO:0000250,
ECO:0000269|PubMed:12821939}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
{ECO:0000250}. Note=Localizes to the nuclear periphery and in
nuclear dots when sumoylated. Some localization in PML nuclear
bodies (By similarity). {ECO:0000250}.
-!- PTM: Acetylated by histone acetyltransferase p300, deacetylated by
HDACs. Acetylation/deacetylation states regulate transcriptional
activity. Acetylation appears to activate transcription. Alternate
sumoylation and acetylation at Lys-541 also control
transcriptional activity.
-!- PTM: Sumoylation represses transcriptional activity. Lys-541 is
the major site. Sumoylation at this site promotes nuclear
localization to the nuclear periphery, nuclear dots and PML
nuclear bodies. Alternate sumoylation and acetylation at Lys-541
also control transcriptional activity (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; AJ317961; CAC84905.1; -; mRNA.
RefSeq; NP_989934.1; NM_204603.1.
UniGene; Gga.2337; -.
UniGene; Gga.49049; -.
ProteinModelPortal; Q90WR8; -.
SMR; Q90WR8; -.
STRING; 9031.ENSGALP00000015174; -.
PaxDb; Q90WR8; -.
Ensembl; ENSGALT00000068500; ENSGALP00000046340; ENSGALG00000031796.
GeneID; 395302; -.
KEGG; gga:395302; -.
CTD; 6670; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118984; -.
HOGENOM; HOG000234295; -.
HOVERGEN; HBG008933; -.
InParanoid; Q90WR8; -.
KO; K09193; -.
OrthoDB; EOG091G0HX6; -.
PhylomeDB; Q90WR8; -.
Reactome; R-GGA-3232118; SUMOylation of transcription factors.
PRO; PR:Q90WR8; -.
Proteomes; UP000000539; Chromosome 7.
Bgee; ENSGALG00000009327; -.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0030219; P:megakaryocyte differentiation; IEA:Ensembl.
GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR030452; SP3.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR23235:SF3; PTHR23235:SF3; 1.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 771 Transcription factor Sp3.
/FTId=PRO_0000047143.
ZN_FING 611 635 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 641 665 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 671 693 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 129 228 Transactivation domain (Gln-rich).
{ECO:0000250}.
REGION 341 489 Transactivation domain (Gln-rich).
{ECO:0000250}.
REGION 524 610 Repressor domain. {ECO:0000250}.
COMPBIAS 34 106 Ala-rich.
COMPBIAS 325 328 Poly-Ser.
MOD_RES 541 541 N6-acetyllysine; alternate.
{ECO:0000250}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 541 541 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
SEQUENCE 771 AA; 80950 MW; 36E795D490AE79B4 CRC64;
MTAPEQPVKQ EEMAALDVDS SGHGEYLQHG NGNASASAAA AAPQDAQPSP LALLAATCSK
IGPPSPEEDE AAAAAASHSA GATGDLASVQ LAGTPNRWEV LSAAPATIKD EAGNIVQIPG
AATVTSSGQY VLPIQSLQNQ QIFSVAPGSD SSNGTVSNVQ YQVIPQIQTA DGQQVQLGFA
ASSDNSSINQ ETGQIQIIPG SNQTIIASGS PSANIQNILS QSGQVQVQGV AIGGSSFPGQ
AQVVANVPLG LPGNITFVPI NSVDLDSLGL GSGSQTMTAG INADGHLINT GQAMDSSDNS
ERTGEQVSPE ITETATDNDL FVPTSSSSQL PVTIDSSSIL EQNANNLTTT SGQVHSSDLQ
GNYIQTSVSD DTQAQNIQVS TAQPIVQHIQ LQESQQPTSQ AQIVQGIAQQ TIHGVQASQS
ISPQALQNLQ LQLNPGTFLI QAQTVTPSGQ ITWQTFQVQG VQNLQNLQIQ NAPGQQITLT
PVQTLTLGQV AAGGALTSTP VSLSTAQLPN LQTVTVNSID SAGIQLHQGE NAGSPADIRI
KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQPHQ EGKRLRRVAC TCPNCKEGGG
RGSNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP FVCNWMFCGK RFTRSDELQR
HRRTHTGEKK FVCPECSKRF MRSDHLAKHI KTHQNKKGIH SSSTVLASVE ATSDDTLITA
GGTTLILANI QQGSVSGIGT VNTSGTSNQD ILTNTEIPLQ LVTVSGNETM E


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