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Protein

Transcription factor Sp1

Gene

Sp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. Positively regulates the transcription of the core clock component ARNTL/BMAL1 (By similarity). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri627 – 65630C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri657 – 68630C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri687 – 71428C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-RNO-2426168. Activation of gene expression by SREBF (SREBP).
R-RNO-6807505. RNA polymerase II transcribes snRNA genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Sp1
Gene namesi
Name:Sp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3738. Sp1.

Subcellular locationi

  • Nucleus
  • Cytoplasm By similarity

  • Note: Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear chromatin Source: ParkinsonsUK-UCL
  • nucleoplasm Source: Ensembl
  • nucleus Source: UniProtKB
  • protein-DNA complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 786785Transcription factor Sp1PRO_0000047139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei7 – 71PhosphoserineCombined sources
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei60 – 601PhosphoserineBy similarity
Modified residuei102 – 1021Phosphoserine; by ATMBy similarity
Modified residuei279 – 2791Phosphothreonine; by MAPK8By similarity
Modified residuei454 – 4541Phosphothreonine; by MAPK1 AND MAPK3By similarity
Glycosylationi492 – 4921O-linked (GlcNAc)By similarity
Modified residuei613 – 6131Phosphoserine; alternateBy similarity
Glycosylationi613 – 6131O-linked (GlcNAc); alternateBy similarity
Modified residuei641 – 6411Phosphothreonine; alternateBy similarity
Glycosylationi641 – 6411O-linked (GlcNAc); alternateBy similarity
Modified residuei642 – 6421Phosphoserine; by PKC/PRKCZ; alternateBy similarity
Glycosylationi642 – 6421O-linked (GlcNAc); alternateBy similarity
Modified residuei652 – 6521Phosphothreonine; by PKC/PRKCZBy similarity
Modified residuei669 – 6691PhosphothreonineBy similarity
Modified residuei671 – 6711Phosphoserine; by PKC/PRKCZBy similarity
Modified residuei682 – 6821Phosphothreonine; by PKC/PRKCZBy similarity
Glycosylationi699 – 6991O-linked (GlcNAc)By similarity
Glycosylationi703 – 7031O-linked (GlcNAc)By similarity
Modified residuei704 – 7041N6-acetyllysineBy similarity
Modified residuei740 – 7401Phosphothreonine; by MAPK1, MAPK3 AND MAPK8By similarity

Post-translational modificationi

Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-60 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-102 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-454 and Thr-740 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-279 and Thr-740 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-60 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-60 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues (By similarity).By similarity
Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter (By similarity).By similarity
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By similarity).By similarity
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity).By similarity
O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei64 – 652CleavageBy similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ01714.
PRIDEiQ01714.

PTM databases

iPTMnetiQ01714.
PhosphoSiteiQ01714.

Expressioni

Tissue specificityi

Expressed in all tissues tested, including lung, kidney, spleen and thymus.1 Publication

Gene expression databases

BgeeiENSRNOG00000014084.
GenevisibleiQ01714. RN.

Interactioni

Subunit structurei

Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding. Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts (deacetylated form) with EP300; the interaction enhances gene expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1 (By similarity). Interacts with SMARCA4/BRG1. Interacts with ATF7IP and TBP. Interacts with MEIS2 and PBX1. Interacts with EGR1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NfyaP185762EBI-862787,EBI-862695

GO - Molecular functioni

  • histone acetyltransferase binding Source: RGD

Protein-protein interaction databases

BioGridi246914. 7 interactions.
IntActiQ01714. 1 interaction.
STRINGi10116.ENSRNOP00000019403.

Structurei

3D structure databases

ProteinModelPortaliQ01714.
SMRiQ01714. Positions 615-713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 8382Repressor domainBy similarityAdd
BLAST
Regioni147 – 252106Transactivation domain A (Gln-rich)By similarityAdd
BLAST
Regioni262 – 496235Transactivation domain B (Gln-rich)By similarityAdd
BLAST
Regioni497 – 611115Transactivation domain C (highly charged)By similarityAdd
BLAST
Regioni620 – 786167VZV IE62-bindingBy similarityAdd
BLAST
Regioni709 – 78678Domain DBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 144109Ser/Thr-richAdd
BLAST
Compositional biasi36 – 138103Ser-richAdd
BLAST
Compositional biasi157 – 21458Gln-richAdd
BLAST
Compositional biasi272 – 380109Ser/Thr-richAdd
BLAST
Compositional biasi272 – 35281Ser-richAdd
BLAST
Compositional biasi353 – 481129Gln-richAdd
BLAST

Sequence similaritiesi

Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri627 – 65630C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri657 – 68630C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri687 – 71428C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118984.
HOGENOMiHOG000234295.
HOVERGENiHBG008933.
InParanoidiQ01714.
KOiK04684.
OMAiGWQIISS.
OrthoDBiEOG091G0HX6.
PhylomeDBiQ01714.
TreeFamiTF350150.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR030450. Sp1_fam.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR23235. PTHR23235. 1 hit.
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01714-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQDHSMDE VTAVKIEKGV GGNNGGSGNG GGAAFSQTRS SSTGSSSSSG
60 70 80 90 100
GGGGQESQPS PLALLAATCS RIESPNENSN NSQGPSQSGG TGELDLTATQ
110 120 130 140 150
LSQGANGWQI ISSSSGATPT SKEQSGNSTN GSNGSESSKN RTVSGGQYVV
160 170 180 190 200
AATPNLQNQQ VLTGLPGVMP NIQYQVIPQF QTVDGQQLQF AATGAQVQQD
210 220 230 240 250
GSGQIQIIPG ANQQIITNRG SGGNIIAAMP NLLQQAVPLQ GLANNVLSGQ
260 270 280 290 300
TQYVTNVPVA LNGNITLLPV NSVSAATLTP SSQAGTISSS GSQESGSQPV
310 320 330 340 350
TSGTAISSAS LVSSQASSSS FFTNANSYST TTTTSNMGIM NFTSSGSSGT
360 370 380 390 400
SSQGQTSQRV GGLQGSDSLN IQQNQTSGGS LQGSQQKEGE QSQQTQQQQI
410 420 430 440 450
LIQPQLVQGG QALQALQAAP LSGQTFTTQA ISQETLQNLQ LQAVQNSGPI
460 470 480 490 500
IIRTPTVGPN GQVSWQTLQL QNLQVQNPQA QTITLAPMQG VSLGQTSSSN
510 520 530 540 550
TTLTPIASAA SIPAGTVTVN AAQLSSMPGL QTINLSALGT SGIQVHQLPG
560 570 580 590 600
LPLAIANTPG DHGAQLGLHG PGGDGIHDET AGGEEGENSP DPQPQAGRRT
610 620 630 640 650
RREACTCPYC KDSEGRGSGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW
660 670 680 690 700
HTGERPFMCN WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD
710 720 730 740 750
HLSKHIKTHQ NKKGGPGVAL SVGTLPLDSG AGSEGSGTAT PSALITTNMV
760 770 780
AMEAICPEGI ARLANSGINV MQVTELQSIN ISGNGF
Length:786
Mass (Da):80,772
Last modified:June 21, 2005 - v2
Checksum:i3DE2AD93F95E7C0B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781N → NEN in BAA02235 (PubMed:1356762).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12768 mRNA. Translation: BAA02235.1.
AB077988 Genomic DNA. Translation: BAC05486.1.
PIRiJS0747.
RefSeqiNP_036787.2. NM_012655.2.
UniGeneiRn.44609.

Genome annotation databases

EnsembliENSRNOT00000019403; ENSRNOP00000019403; ENSRNOG00000014084.
GeneIDi24790.
KEGGirno:24790.
UCSCiRGD:3738. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12768 mRNA. Translation: BAA02235.1.
AB077988 Genomic DNA. Translation: BAC05486.1.
PIRiJS0747.
RefSeqiNP_036787.2. NM_012655.2.
UniGeneiRn.44609.

3D structure databases

ProteinModelPortaliQ01714.
SMRiQ01714. Positions 615-713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246914. 7 interactions.
IntActiQ01714. 1 interaction.
STRINGi10116.ENSRNOP00000019403.

PTM databases

iPTMnetiQ01714.
PhosphoSiteiQ01714.

Proteomic databases

PaxDbiQ01714.
PRIDEiQ01714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019403; ENSRNOP00000019403; ENSRNOG00000014084.
GeneIDi24790.
KEGGirno:24790.
UCSCiRGD:3738. rat.

Organism-specific databases

CTDi6667.
RGDi3738. Sp1.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118984.
HOGENOMiHOG000234295.
HOVERGENiHBG008933.
InParanoidiQ01714.
KOiK04684.
OMAiGWQIISS.
OrthoDBiEOG091G0HX6.
PhylomeDBiQ01714.
TreeFamiTF350150.

Enzyme and pathway databases

ReactomeiR-RNO-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-RNO-2426168. Activation of gene expression by SREBF (SREBP).
R-RNO-6807505. RNA polymerase II transcribes snRNA genes.

Miscellaneous databases

PROiQ01714.

Gene expression databases

BgeeiENSRNOG00000014084.
GenevisibleiQ01714. RN.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR030450. Sp1_fam.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR23235. PTHR23235. 1 hit.
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSP1_RAT
AccessioniPrimary (citable) accession number: Q01714
Secondary accession number(s): Q8K4R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 21, 2005
Last modified: September 7, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.