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Protein

Transcription factor Sp1

Gene

SP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21798247). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).By similarity16 Publications

Miscellaneous

In the hepatoma cell line Hep-G2, SP1 precursor mRNA may undergo homotype trans-splicing leading to the duplication of exons 2 and 3.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri626 – 650C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri656 – 680C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri686 – 708C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processBiological rhythms, Host-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1989781 PPARA activates gene expression
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP08047
SIGNORiP08047

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Sp1
Gene namesi
Name:SP1
Synonyms:TSFP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000185591.9
HGNCiHGNC:11205 SP1
MIMi189906 gene
neXtProtiNX_P08047

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7S → A: Increase in protein stability. No change in sumoylation. 1 Publication1
Mutagenesisi15V → R: Enhanced transcriptional activity. 1
Mutagenesisi16K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. 1 Publication1
Mutagenesisi18E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. 1 Publication1
Mutagenesisi19K → R: No effect on sumoylation nor on proteolytic cleavage. 1 Publication1
Mutagenesisi36S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi56S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi59S → A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing. 3 Publications1
Mutagenesisi59S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. 3 Publications1
Mutagenesisi73S → A: Little effect on activated MAPK8-mediated phosphorylation. 1 Publication1
Mutagenesisi81S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi85S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi98T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi101S → A: Significant reduction of phosphorylation on DNA damage. 2 Publications1
Mutagenesisi101S → D: Increase in phosphorylation on DNA damage. 2 Publications1
Mutagenesisi117T → A: No effect on activated MAPK8-mediated phosphorylation. 1 Publication1
Mutagenesisi220S → A: No effect on dephosphorylation by PP2A. 1 Publication1
Mutagenesisi250T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi278T → A: Almost complete abolition of activated MAPK8-mediated phosphorylation and 40% reduction in protein levels during mitosis. Protein levels reduced by 70% during mitosis; when associated with A-739. 1 Publication1
Mutagenesisi278T → D: Increased protein stability during mitosis; when associated with D-739. 1 Publication1
Mutagenesisi281S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi291S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi296S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi313S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi351S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi355T → A: No effect on dephosphorylation by PP2A. 2 Publications1
Mutagenesisi394T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi427T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi431S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi453T → A: Abolishes MAPK-mediated phosphorylation, 50% reduction in MAPK1/MAPK3-mediated activity on VEGF promoter and no effect on dephosphorylation by PP2A. Greatly reduced MAPK1-mediated activity on VEGF promoter; when associated with A-739. 3 Publications1
Mutagenesisi491S → A: Loss of O-glycosylation. Increase in transcriptional activity. 2 Publications1
Mutagenesisi612S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. 1 Publication1
Mutagenesisi640T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. 1 Publication1
Mutagenesisi641S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 2 Publications1
Mutagenesisi651T → A: No effect on dephosphorylation by PP2A. 1 Publication1
Mutagenesisi668T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. 1 Publication1
Mutagenesisi670S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. 1 Publication1
Mutagenesisi681T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. Some effect on dephosphorylation by PP2A. No effect on DNA binding; when associated with A-668 and A-681. 2 Publications1
Mutagenesisi698S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 1 Publication1
Mutagenesisi702S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. 1 Publication1
Mutagenesisi703K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. 1 Publication1
Mutagenesisi728S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. 1 Publication1
Mutagenesisi732S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. 1 Publication1
Mutagenesisi739T → A: Abolishes MAPK-mediated phosphorylation. 50% reduction in MAPK1/MAPK3-mediated activity on VEGF promoter, 40% reduction in protein levels during mitosis and no effect on dephosphorylation by PP2A. Greatly reduced MAPK1-mediated activity on VEGF promoter; when associated with A-453. Protein levels during mitosis reduced by 70%; when associated with A-278. 4 Publications1
Mutagenesisi739T → D: Increased protein stability during mitosis; when associated with D-278. 4 Publications1

Organism-specific databases

DisGeNETi6667
OpenTargetsiENSG00000185591
PharmGKBiPA36042

Chemistry databases

ChEMBLiCHEMBL6103

Polymorphism and mutation databases

BioMutaiSP1
DMDMi13638437

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000471372 – 785Transcription factor Sp1Add BLAST784

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei7PhosphoserineCombined sources1 Publication1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei59PhosphoserineCombined sources3 Publications1
Modified residuei101Phosphoserine; by ATM2 Publications1
Modified residuei278Phosphothreonine; by MAPK81 Publication1
Modified residuei453Phosphothreonine; by MAPK1 and MAPK33 Publications1
Glycosylationi491O-linked (GlcNAc) serine2 Publications1
Modified residuei612Phosphoserine; alternate1 Publication1
Glycosylationi612O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei640Phosphothreonine; alternate1 Publication1
Glycosylationi640O-linked (GlcNAc) threonine; alternate1 Publication1
Modified residuei641Phosphoserine; by PKC/PRKCZ; alternate2 Publications1
Glycosylationi641O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei651Phosphothreonine; by PKC/PRKCZCombined sources1
Modified residuei668Phosphothreonine1 Publication1
Modified residuei670Phosphoserine; by PKC/PRKCZ1 Publication1
Modified residuei681Phosphothreonine; by PKC/PRKCZ2 Publications1
Modified residuei698Phosphoserine; alternate1 Publication1
Glycosylationi698O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei702Phosphoserine; alternate1 Publication1 Publication1
Glycosylationi702O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei703N6-acetyllysine1 Publication1
Modified residuei739Phosphothreonine; by MAPK1, MAPK3 and MAPK83 Publications1

Post-translational modificationi

Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-59 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-101 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-278 and Thr-739 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-641 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-668, Ser-670 and Thr-681 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-59 and Thr-681 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-59 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.11 Publications
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.1 Publication
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation.1 Publication
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation.
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation.
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. Also inhibits interaction with the HIV1 promoter. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei63 – 64CleavageCurated2

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP08047
MaxQBiP08047
PaxDbiP08047
PeptideAtlasiP08047
PRIDEiP08047
ProteomicsDBi52061

PTM databases

GlyConnecti605
iPTMnetiP08047
PhosphoSitePlusiP08047
UniCarbKBiP08047

Miscellaneous databases

PMAP-CutDBiP08047

Expressioni

Tissue specificityi

Up-regulated in adenocarcinomas of the stomach (at protein level). Isoform 3 is ubiquitously expressed at low levels.1 Publication

Inductioni

By insulin.1 Publication

Gene expression databases

BgeeiENSG00000185591 Expressed in 208 organ(s), highest expression level in nipple
CleanExiHS_SP1
ExpressionAtlasiP08047 baseline and differential
GenevisibleiP08047 HS

Organism-specific databases

HPAiCAB000330
HPA001853
HPA012292

Interactioni

Subunit structurei

Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. 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. Interacts with ATF7IP and TBP. Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a. Interacts with EGR1 (PubMed:10391891, PubMed:10976766, PubMed:12021324, PubMed:12847090, PubMed:12855699, PubMed:15691849, PubMed:16478997, PubMed:19106100, PubMed:19285002, PubMed:19302979, PubMed:19666599, PubMed:20121949, PubMed:21746878, PubMed:7592727, PubMed:9466902). Interacts with SMARCA4/BRG1. Interacts with RNF112 in an oxidative stress-regulated manner (By similarity). Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (PubMed:12004059).By similarity12 Publications
(Microbial infection) Interacts with varicella-zoster virus IE62 protein.1 Publication
(Microbial infection) 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.2 Publications
(Microbial infection) Interacts with HIV-1 Vpr; the interaction is inhibited by SP1 O-glycosylation.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi112550, 233 interactors
CORUMiP08047
DIPiDIP-36N
ELMiP08047
IntActiP08047, 72 interactors
MINTiP08047
STRINGi9606.ENSP00000329357

Structurei

Secondary structure

1785
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00378
ProteinModelPortaliP08047
SMRiP08047
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08047

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 82Repressor domainAdd BLAST81
Regioni146 – 251Transactivation domain A (Gln-rich)Add BLAST106
Regioni261 – 495Transactivation domain B (Gln-rich)Add BLAST235
Regioni496 – 610Transactivation domain C (highly charged)Add BLAST115
Regioni619 – 785VZV IE62-bindingAdd BLAST167
Regioni708 – 785Domain DAdd BLAST78

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi36 – 143Ser/Thr-richAdd BLAST108
Compositional biasi271 – 379Ser/Thr-richAdd BLAST109

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri626 – 650C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri656 – 680C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri686 – 708C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00760000118984
HOGENOMiHOG000234295
HOVERGENiHBG008933
InParanoidiP08047
KOiK04684
OMAiQTQYVAN
OrthoDBiEOG091G0HX6
PhylomeDBiP08047
TreeFamiTF350150

Family and domain databases

InterProiView protein in InterPro
IPR030449 SP1
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PANTHERiPTHR23235:SF16 PTHR23235:SF16, 1 hit
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 3 hits
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

Sequences (3+)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P08047-1) [UniParc]FASTAAdd to basket
Also known as: Sp1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG
60 70 80 90 100
GGGQESQPSP LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL
110 120 130 140 150
SQGANGWQII SSSSGATPTS KEQSGSSTNG SNGSESSKNR TVSGGQYVVA
160 170 180 190 200
AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ TVDGQQLQFA ATGAQVQQDG
210 220 230 240 250
SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG LANNVLSGQT
260 270 280 290 300
QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT
310 320 330 340 350
SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN
360 370 380 390 400
SQGQTPQRVS GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL
410 420 430 440 450
IQPQLVQGGQ ALQALQAAPL SGQTFTTQAI SQETLQNLQL QAVPNSGPII
460 470 480 490 500
IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ TITLAPMQGV SLGQTSSSNT
510 520 530 540 550
TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS GIQVHPIQGL
560 570 580 590 600
PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR
610 620 630 640 650
REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH
660 670 680 690 700
TGERPFMCTW SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH
710 720 730 740 750
LSKHIKTHQN KKGGPGVALS VGTLPLDSGA GSEGSGTATP SALITTNMVA
760 770 780
MEAICPEGIA RLANSGINVM QVADLQSINI SGNGF
Length:785
Mass (Da):80,693
Last modified:April 27, 2001 - v3
Checksum:i43893DBF6518B9EA
GO
Isoform 2 (identifier: P08047-2) [UniParc]FASTAAdd to basket
Also known as: Sp1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.

Show »
Length:778
Mass (Da):79,892
Checksum:i74D5DA9A1F8DC8EA
GO
Isoform 3 (identifier: P08047-3) [UniParc]FASTAAdd to basket
Also known as: Sp1c

The sequence of this isoform differs from the canonical sequence as follows:
     54-101: Missing.

Show »
Length:737
Mass (Da):75,824
Checksum:iD830B2947A96C8B9
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BVI2H3BVI2_HUMAN
Transcription factor Sp1
SP1
230Annotation score:
H3BUU5H3BUU5_HUMAN
Transcription factor Sp1
SP1
162Annotation score:

Sequence cautioni

The sequence AAH43224 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti366D → G AA sequence (PubMed:3319186).Curated1
Sequence conflicti670S → F AA sequence (PubMed:3319186).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019971737T → A. Corresponds to variant dbSNP:rs3741665Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0539341 – 7Missing in isoform 2. Curated7
Alternative sequenceiVSP_05393554 – 101Missing in isoform 3. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN908228 mRNA Translation: CBM42955.1
AC068889 Genomic DNA No translation available.
AC073611 Genomic DNA No translation available.
CH471054 Genomic DNA Translation: EAW96699.1
BC043224 mRNA Translation: AAH43224.1 Different initiation.
BC062539 mRNA Translation: AAH62539.1
AF252284 mRNA Translation: AAF67726.1
AB039286 Genomic DNA Translation: BAB13476.1
J03133 mRNA Translation: AAA61154.1
AF255682 mRNA Translation: AAF78781.1
AJ272134 mRNA Translation: CAB75345.1
CCDSiCCDS44898.1 [P08047-2]
CCDS8857.1 [P08047-1]
PIRiA29635
RefSeqiNP_001238754.1, NM_001251825.1 [P08047-3]
NP_003100.1, NM_003109.1 [P08047-2]
NP_612482.2, NM_138473.2 [P08047-1]
XP_011536998.1, XM_011538696.2 [P08047-2]
UniGeneiHs.620754
Hs.649191

Genome annotation databases

EnsembliENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1]
ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2]
GeneIDi6667
KEGGihsa:6667
UCSCiuc001scw.4 human [P08047-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN908228 mRNA Translation: CBM42955.1
AC068889 Genomic DNA No translation available.
AC073611 Genomic DNA No translation available.
CH471054 Genomic DNA Translation: EAW96699.1
BC043224 mRNA Translation: AAH43224.1 Different initiation.
BC062539 mRNA Translation: AAH62539.1
AF252284 mRNA Translation: AAF67726.1
AB039286 Genomic DNA Translation: BAB13476.1
J03133 mRNA Translation: AAA61154.1
AF255682 mRNA Translation: AAF78781.1
AJ272134 mRNA Translation: CAB75345.1
CCDSiCCDS44898.1 [P08047-2]
CCDS8857.1 [P08047-1]
PIRiA29635
RefSeqiNP_001238754.1, NM_001251825.1 [P08047-3]
NP_003100.1, NM_003109.1 [P08047-2]
NP_612482.2, NM_138473.2 [P08047-1]
XP_011536998.1, XM_011538696.2 [P08047-2]
UniGeneiHs.620754
Hs.649191

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SP1NMR-A684-712[»]
1SP2NMR-A654-684[»]
1VA1NMR-A619-654[»]
1VA2NMR-A654-684[»]
1VA3NMR-A684-712[»]
DisProtiDP00378
ProteinModelPortaliP08047
SMRiP08047
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112550, 233 interactors
CORUMiP08047
DIPiDIP-36N
ELMiP08047
IntActiP08047, 72 interactors
MINTiP08047
STRINGi9606.ENSP00000329357

Chemistry databases

ChEMBLiCHEMBL6103

PTM databases

GlyConnecti605
iPTMnetiP08047
PhosphoSitePlusiP08047
UniCarbKBiP08047

Polymorphism and mutation databases

BioMutaiSP1
DMDMi13638437

Proteomic databases

EPDiP08047
MaxQBiP08047
PaxDbiP08047
PeptideAtlasiP08047
PRIDEiP08047
ProteomicsDBi52061

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1]
ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2]
GeneIDi6667
KEGGihsa:6667
UCSCiuc001scw.4 human [P08047-1]

Organism-specific databases

CTDi6667
DisGeNETi6667
EuPathDBiHostDB:ENSG00000185591.9
GeneCardsiSP1
HGNCiHGNC:11205 SP1
HPAiCAB000330
HPA001853
HPA012292
MIMi189906 gene
neXtProtiNX_P08047
OpenTargetsiENSG00000185591
PharmGKBiPA36042
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00760000118984
HOGENOMiHOG000234295
HOVERGENiHBG008933
InParanoidiP08047
KOiK04684
OMAiQTQYVAN
OrthoDBiEOG091G0HX6
PhylomeDBiP08047
TreeFamiTF350150

Enzyme and pathway databases

ReactomeiR-HSA-1989781 PPARA activates gene expression
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP08047
SIGNORiP08047

Miscellaneous databases

ChiTaRSiSP1 human
EvolutionaryTraceiP08047
GeneWikiiSp1_transcription_factor
GenomeRNAii6667
PMAP-CutDBiP08047
PROiPR:P08047
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185591 Expressed in 208 organ(s), highest expression level in nipple
CleanExiHS_SP1
ExpressionAtlasiP08047 baseline and differential
GenevisibleiP08047 HS

Family and domain databases

InterProiView protein in InterPro
IPR030449 SP1
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PANTHERiPTHR23235:SF16 PTHR23235:SF16, 1 hit
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 3 hits
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiSP1_HUMAN
AccessioniPrimary (citable) accession number: P08047
Secondary accession number(s): E4Z9M7
, G5E9M8, Q86TN8, Q9H3Q5, Q9NR51, Q9NY21, Q9NYE7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 27, 2001
Last modified: November 7, 2018
This is version 228 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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