SP3
entrez
6670
canonical
uniprot
Q02447
canonical
ensembl
ENSG00000172845
resolver
ensp
ENSP00000310301
resolver
ensp
ENSP00000406140
resolver
ensp
ENSP00000413665
resolver
genesymbol
SP3
resolver
hgnc
HGNC:11208
resolver
uniprot
A0AVL9
resolver
uniprot
B4E2B7
resolver
uniprot
B7ZLN9
resolver
uniprot
Q59FX5
resolver
uniprot
Q69B26
resolver
uniprot
Q69B27
resolver
uniprot
Q86TP0
resolver
uniprot
Q8TD56
resolver
uniprot
Q8WWU4
resolver
uniprot
Q9BQR1
resolver
uniprot_entry
B7ZLN9_HUMAN
resolver
uniprot_entry
Q59FX5_HUMAN
resolver
uniprot_entry
Q86TP0_HUMAN
resolver
uniprot_entry
SP3_HUMAN
resolver
uniprot_sec
A0AVL9
resolver
uniprot_sec
B4E2B7
resolver
uniprot_sec
Q69B26
resolver
uniprot_sec
Q69B27
resolver
uniprot_sec
Q8TD56
resolver
uniprot_sec
Q8WWU4
resolver
uniprot_sec
Q9BQR1
resolver
amino_acid_sequence
MTAPEKPVKQEEMAALDVDSGGGGGGGGGHGEYLQQQQQHGNGAVAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDEEEAAAAAGAPAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIPQIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQVTWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFVCNWMYCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKGIHSSSTVLASVEAARDDTLITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME
uniprot
proteins
function
FUNCTION: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping. {ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11812829, ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:15247228, ECO:0000269|PubMed:15494207, ECO:0000269|PubMed:15554904, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:17548428, ECO:0000269|PubMed:18187045, ECO:0000269|PubMed:18617891, ECO:0000269|PubMed:9278495}.
uniprot
proteins
mass_dalton
81925
uniprot
proteins
mutagenesis
MUTAGEN 120; /note="K->R: Some loss of sumoylation. Slight increase in transcriptional activity. Large increase in transcriptional activity; when associated with R-551."; /evidence="ECO:0000269|PubMed:12419227"; MUTAGEN 551..553; /note="KEE->AAA: Increases transcriptional activity."; /evidence="ECO:0000269|PubMed:15494207"; MUTAGEN 551..553; /note="KEE->REA: 200-fold increase in transcriptional activation."; /evidence="ECO:0000269|PubMed:15494207"; MUTAGEN 551..553; /note="KEE->RED: 200-fold increase in transcriptional activation."; /evidence="ECO:0000269|PubMed:15494207"; MUTAGEN 551..552; /note="KE->RA: 200-fold increase in transcriptional activation."; MUTAGEN 551..552; /note="KE->RD: 200-fold increase in transcriptional activation."; MUTAGEN 551; /note="K->Q: A decreased interaction with HDAC1 and deacetylation of SP3. Increase of about 4.5% of activity of the TERT promoter. Decreased recruitment of HDAC1 and increased binding of RNA polymerase II with promoter DNA."; /evidence="ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:17548428"; MUTAGEN 551; /note="K->R: Great loss of sumoylation, 20-fold increase in transcriptional activity and diffuse nuclear localization. Further small increase in transcriptional activity; when associated with R-120. Increased interaction with HDAC1 and deacetylation of SP3. About 50% decrease in activity of the TERT promoter. Enhances recruitment of HDAC1 and inhibits binding of RNA polymerase II with promoter DNA."; /evidence="ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:17548428
uniprot
proteins
post_translational_modification
PTM: Not glycosylated.; 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-551 also control transcriptional activity. Ceramides can also regulate acetylation/deacetylation events through altering the interaction of HDAC with SP3. In vitro, C(18)-ceramides, but not C(16)-ceramides, increase the interaction of HDAC1 with SP3 and enhance the deacetylation of SP3 and the subsequent repression of the TERT promoter. {ECO:0000269|PubMed:11812829, ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:15494207, ECO:0000269|PubMed:15554904, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:18617891}.; PTM: Sumoylated on all isoforms. Sumoylated on 2 sites in longer isoforms with Lys-551 being the major site. Sumoylation at this site promotes nuclear localization to the nuclear periphery, nuclear dots and PML nuclear bodies. Sumoylation on Lys-551 represses the transactivation activity, except for the largest isoform, L-Sp3, which has little effect on transactivation. Alternate sumoylation and acetylation at Lys-551 also control transcriptional activity. {ECO:0000269|PubMed:11812829, ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:15494207, ECO:0000269|PubMed:15554904, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:18617891}.
uniprot
proteins
protein_family
Sp1 C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
10391891
uniprot
proteins
pubmed
11812829
uniprot
proteins
pubmed
12176973
uniprot
proteins
pubmed
12297010
uniprot
proteins
pubmed
12411611
uniprot
proteins
pubmed
12419227
uniprot
proteins
pubmed
12837748
uniprot
proteins
pubmed
1341900
uniprot
proteins
pubmed
1454515
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15247228
uniprot
proteins
pubmed
15474306
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15494207
uniprot
proteins
pubmed
15554904
uniprot
proteins
pubmed
16781829
uniprot
proteins
pubmed
17548428
uniprot
proteins
pubmed
18187045
uniprot
proteins
pubmed
18617891
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21746878
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31375868
uniprot
proteins
pubmed
9278495
uniprot
proteins
sequence_length
781
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies.
uniprot
proteins