SP1

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, PubMed:21046154). 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 similarity17 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 key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	626 – 650	C2H2-type 1PROSITE-ProRule annotationAdd BLAST	25
Zinc fingerⁱ	656 – 680	C2H2-type 2PROSITE-ProRule annotationAdd BLAST	25
Zinc fingerⁱ	686 – 708	C2H2-type 3PROSITE-ProRule annotationAdd BLAST	23

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding, Repressor
Biological process	Biological rhythms, Host-virus interaction, Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

PathwayCommonsⁱ	P08047
Reactomeⁱ	R-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
SignaLinkⁱ	P08047
SIGNORⁱ	P08047

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Transcription factor Sp1
Gene namesⁱ	Name:SP1 Synonyms:TSFP1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11205, SP1
MIMⁱ	189906, gene
neXtProtⁱ	NX_P08047
VEuPathDBⁱ	HostDB:ENSG00000185591.9

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	7	S → A: Increase in protein stability. No change in sumoylation. 1 Publication	1
Mutagenesisⁱ	15	V → R: Enhanced transcriptional activity.	1
Mutagenesisⁱ	16	K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. 1 Publication	1
Mutagenesisⁱ	18	E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. 1 Publication	1
Mutagenesisⁱ	19	K → R: No effect on sumoylation nor on proteolytic cleavage. 1 Publication	1
Mutagenesisⁱ	36	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	56	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	59	S → A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing. 3 Publications	1
Mutagenesisⁱ	59	S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. 3 Publications	1
Mutagenesisⁱ	73	S → A: Little effect on activated MAPK8-mediated phosphorylation. 1 Publication	1
Mutagenesisⁱ	81	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	85	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	98	T → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	101	S → A: Significant reduction of phosphorylation on DNA damage. 2 Publications	1
Mutagenesisⁱ	101	S → D: Increase in phosphorylation on DNA damage. 2 Publications	1
Mutagenesisⁱ	117	T → A: No effect on activated MAPK8-mediated phosphorylation. 1 Publication	1
Mutagenesisⁱ	220	S → A: No effect on dephosphorylation by PP2A. 1 Publication	1
Mutagenesisⁱ	250	T → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	278	T → 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 Publication	1
Mutagenesisⁱ	278	T → D: Increased protein stability during mitosis; when associated with D-739. 1 Publication	1
Mutagenesisⁱ	281	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	291	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	296	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	313	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	351	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	355	T → A: No effect on dephosphorylation by PP2A. 2 Publications	1
Mutagenesisⁱ	394	T → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	427	T → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	431	S → A: No effect on phosphorylation on DNA damage. 1 Publication	1
Mutagenesisⁱ	453	T → 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 Publications	1
Mutagenesisⁱ	491	S → A: Loss of O-glycosylation. Increase in transcriptional activity. 2 Publications	1
Mutagenesisⁱ	612	S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. 1 Publication	1
Mutagenesisⁱ	640	T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. 1 Publication	1
Mutagenesisⁱ	641	S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 2 Publications	1
Mutagenesisⁱ	651	T → A: No effect on dephosphorylation by PP2A. 1 Publication	1
Mutagenesisⁱ	668	T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. 1 Publication	1
Mutagenesisⁱ	670	S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. 1 Publication	1
Mutagenesisⁱ	681	T → 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 Publications	1
Mutagenesisⁱ	698	S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 1 Publication	1
Mutagenesisⁱ	702	S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. 1 Publication	1
Mutagenesisⁱ	703	K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. 1 Publication	1
Mutagenesisⁱ	728	S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. 1 Publication	1
Mutagenesisⁱ	732	S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. 1 Publication	1
Mutagenesisⁱ	739	T → 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 Publications	1
Mutagenesisⁱ	739	T → D: Increased protein stability during mitosis; when associated with D-278. 4 Publications	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6667
Open Targets More...OpenTargetsⁱ	ENSG00000185591
PharmGKBⁱ	PA36042

Miscellaneous databases

Pharosⁱ	P08047, Tbio

Pharosⁱ

P08047, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL6103

ChEMBLⁱ

CHEMBL6103

Genetic variation databases

BioMutaⁱ	SP1
DMDMⁱ	13638437

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000047137	2 – 785	Transcription factor Sp1Add BLAST		784

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineCombined sources	1
Modified residueⁱ	2	PhosphoserineCombined sources	1
Modified residueⁱ	7	PhosphoserineCombined sources1 Publication	1
Cross-linkⁱ	16	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linkⁱ	16	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	59	PhosphoserineCombined sources3 Publications	1
Modified residueⁱ	101	Phosphoserine; by ATM2 Publications	1
Modified residueⁱ	278	Phosphothreonine; by MAPK81 Publication	1
Modified residueⁱ	453	Phosphothreonine; by MAPK1 and MAPK33 Publications	1
Glycosylationⁱ	491	O-linked (GlcNAc) serine2 Publications	1
Modified residueⁱ	612	Phosphoserine; alternate1 Publication	1
Glycosylationⁱ	612	O-linked (GlcNAc) serine; alternate1 Publication	1
Modified residueⁱ	640	Phosphothreonine; alternate1 Publication	1
Glycosylationⁱ	640	O-linked (GlcNAc) threonine; alternate1 Publication	1
Modified residueⁱ	641	Phosphoserine; by PKC/PRKCZ; alternate2 Publications	1
Glycosylationⁱ	641	O-linked (GlcNAc) serine; alternate1 Publication	1
Modified residueⁱ	651	Phosphothreonine; by PKC/PRKCZCombined sources	1
Modified residueⁱ	668	Phosphothreonine1 Publication	1
Modified residueⁱ	670	Phosphoserine; by PKC/PRKCZ1 Publication	1
Modified residueⁱ	681	Phosphothreonine; by PKC/PRKCZ2 Publications	1
Modified residueⁱ	698	Phosphoserine; alternate1 Publication	1
Glycosylationⁱ	698	O-linked (GlcNAc) serine; alternate1 Publication	1
Modified residueⁱ	702	Phosphoserine; alternate1 Publication1 Publication	1
Glycosylationⁱ	702	O-linked (GlcNAc) serine; alternate1 Publication	1
Modified residueⁱ	703	N6-acetyllysine1 Publication	1
Modified residueⁱ	739	Phosphothreonine; by MAPK1, MAPK3 and MAPK83 Publications	1

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 key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	63 – 64	CleavageCurated		2

Keywords - PTMⁱ

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P08047
jPOSTⁱ	P08047
MassIVEⁱ	P08047
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P08047
PaxDbⁱ	P08047
PeptideAtlas More...PeptideAtlasⁱ	P08047
PRIDEⁱ	P08047
ProteomicsDBⁱ	33987 52061 [P08047-1]

PTM databases

GlyConnectⁱ	605, 1 O-Linked glycan
GlyGenⁱ	P08047, 11 sites, 1 O-linked glycan (5 sites)
iPTMnetⁱ	P08047
PhosphoSitePlusⁱ	P08047

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

Bgeeⁱ	ENSG00000185591, Expressed in nipple and 221 other tissues
ExpressionAtlasⁱ	P08047, baseline and differential
Genevisibleⁱ	P08047, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000185591, Low tissue specificity

HPAⁱ

ENSG00000185591, Low tissue specificity

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).

Interacts with DDX3X; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription (PubMed:16818630).

By similarity13 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

Hide details

P08047

With	#Exp.	IntAct
AATF [Q9NY61]	2	EBI-298336,EBI-372428
CDKN2A [Q8N726]	4	EBI-298336,EBI-625922
DLX4 [Q92988]	4	EBI-298336,EBI-1752755
E2F1 [Q01094]	2	EBI-298336,EBI-448924
ELF1 [P32519]	2	EBI-298336,EBI-765526
EPAS1 [Q99814]	2	EBI-298336,EBI-447470
ESR1 [P03372]	2	EBI-298336,EBI-78473
HCFC1 [P51610]	4	EBI-298336,EBI-396176
HDAC1 [Q13547]	2	EBI-298336,EBI-301834
HIF1A [Q16665]	3	EBI-298336,EBI-447269
KLF10 [Q13118]	2	EBI-298336,EBI-1389509
MYC [P01106]	4	EBI-298336,EBI-447544
NCK1 [P16333]	2	EBI-298336,EBI-389883
PHC2 [Q8IXK0]	2	EBI-298336,EBI-713786
POGZ [Q7Z3K3]	2	EBI-298336,EBI-1389308
POU2F1 [P14859]	7	EBI-298336,EBI-624770
RUNX1T1 [Q06455]	2	EBI-298336,EBI-743342
SF3A1 [Q15459]	2	EBI-298336,EBI-1054743
SMAD4 [Q13485]	2	EBI-298336,EBI-347263
SREBF2 [Q12772]	3	EBI-298336,EBI-465059
STAT3 [P40763]	4	EBI-298336,EBI-518675
TBX21 [Q9UL17]	4	EBI-298336,EBI-3922312
TP53 [P04637]	3	EBI-298336,EBI-366083
ZBTB2 [Q8N680]	4	EBI-298336,EBI-2515601
Nfya [P23708] from Mus musculus.	18	EBI-298336,EBI-862337

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	112550, 251 interactors
CORUMⁱ	P08047
Database of interacting proteins More...DIPⁱ	DIP-36N
ELMⁱ	P08047
IntActⁱ	P08047, 74 interactors
Molecular INTeraction database More...MINTⁱ	P08047
STRINGⁱ	9606.ENSP00000329357

Chemistry databases

BindingDBⁱ

P08047

Miscellaneous databases

RNActⁱ	P08047, protein

RNActⁱ

P08047, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	620 – 622	Combined sources	3
Beta strandⁱ	636 – 638	Combined sources	3
Helixⁱ	640 – 651	Combined sources	12
Beta strandⁱ	656 – 658	Combined sources	3
Turnⁱ	661 – 663	Combined sources	3
Beta strandⁱ	666 – 668	Combined sources	3
Helixⁱ	670 – 677	Combined sources	8
Turnⁱ	678 – 680	Combined sources	3
Turnⁱ	681 – 683	Combined sources	3
Turnⁱ	689 – 692	Combined sources	4
Helixⁱ	699 – 706	Combined sources	8
Helixⁱ	707 – 709	Combined sources	3

Show more details

3D structure databases

BMRBⁱ	P08047
SMRⁱ	P08047
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P08047

EvolutionaryTraceⁱ

P08047

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2 – 82	Repressor domainAdd BLAST	81
Regionⁱ	146 – 251	Transactivation domain A (Gln-rich)Add BLAST	106
Regionⁱ	261 – 495	Transactivation domain B (Gln-rich)Add BLAST	235
Regionⁱ	496 – 610	Transactivation domain C (highly charged)Add BLAST	115
Regionⁱ	619 – 785	VZV IE62-bindingAdd BLAST	167
Regionⁱ	708 – 785	Domain DAdd BLAST	78

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	462 – 470	9aaTAD1 Publication		9

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	36 – 143	Ser/Thr-richAdd BLAST		108
Compositional biasⁱ	271 – 379	Ser/Thr-richAdd BLAST		109

Domainⁱ

The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

Sequence similaritiesⁱ

Belongs to the Sp1 C2H2-type zinc-finger protein family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	626 – 650	C2H2-type 1PROSITE-ProRule annotationAdd BLAST	25
Zinc fingerⁱ	656 – 680	C2H2-type 2PROSITE-ProRule annotationAdd BLAST	25
Zinc fingerⁱ	686 – 708	C2H2-type 3PROSITE-ProRule annotationAdd BLAST	23

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG1721, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000157804
HOGENOMⁱ	CLU_019688_2_0_1
InParanoidⁱ	P08047
OMAⁱ	EACTCPM
Database of Orthologous Groups More...OrthoDBⁱ	1085860at2759
PhylomeDBⁱ	P08047
TreeFamⁱ	TF350150

Family and domain databases

Database of protein disorder More...DisProtⁱ	DP00378
IDEALⁱ	IID00266
InterProⁱ	View protein in InterPro IPR036236, Znf_C2H2_sf IPR013087, Znf_C2H2_type
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00096, zf-C2H2, 3 hits
SMARTⁱ	View protein in SMART SM00355, ZnF_C2H2, 3 hits
SUPFAMⁱ	SSF57667, SSF57667, 1 hit
PROSITEⁱ	View 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. Align Add to basket

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

Isoform 1 (identifier: P08047-1) [UniParc]FASTA Add to basket

Also known as: Sp1a

This isoform has been chosen as the canonicalⁱ 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]FASTA Add to basket

Also known as: Sp1b

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

« Hide

        10         20         30         40         50
MDEMTAVVKI EKGVGGNNGG NGNGGGAFSQ ARSSSTGSSS STGGGGQESQ 
        60         70         80         90        100
PSPLALLAAT CSRIESPNEN SNNSQGPSQS GGTGELDLTA TQLSQGANGW 
       110        120        130        140        150
QIISSSSGAT PTSKEQSGSS TNGSNGSESS KNRTVSGGQY VVAAAPNLQN 
       160        170        180        190        200
QQVLTGLPGV MPNIQYQVIP QFQTVDGQQL QFAATGAQVQ QDGSGQIQII 
       210        220        230        240        250
PGANQQIITN RGSGGNIIAA MPNLLQQAVP LQGLANNVLS GQTQYVTNVP 
       260        270        280        290        300
VALNGNITLL PVNSVSAATL TPSSQAVTIS SSGSQESGSQ PVTSGTTISS 
       310        320        330        340        350
ASLVSSQASS SSFFTNANSY STTTTTSNMG IMNFTTSGSS GTNSQGQTPQ 
       360        370        380        390        400
RVSGLQGSDA LNIQQNQTSG GSLQAGQQKE GEQNQQTQQQ QILIQPQLVQ 
       410        420        430        440        450
GGQALQALQA APLSGQTFTT QAISQETLQN LQLQAVPNSG PIIIRTPTVG 
       460        470        480        490        500
PNGQVSWQTL QLQNLQVQNP QAQTITLAPM QGVSLGQTSS SNTTLTPIAS 
       510        520        530        540        550
AASIPAGTVT VNAAQLSSMP GLQTINLSAL GTSGIQVHPI QGLPLAIANA 
       560        570        580        590        600
PGDHGAQLGL HGAGGDGIHD DTAGGEEGEN SPDAQPQAGR RTRREACTCP 
       610        620        630        640        650
YCKDSEGRGS GDPGKKKQHI CHIQGCGKVY GKTSHLRAHL RWHTGERPFM 
       660        670        680        690        700
CTWSYCGKRF TRSDELQRHK RTHTGEKKFA CPECPKRFMR SDHLSKHIKT 
       710        720        730        740        750
HQNKKGGPGV ALSVGTLPLD SGAGSEGSGT ATPSALITTN MVAMEAICPE 
       760        770 
GIARLANSGI NVMQVADLQS INISGNGF

Show »

Length:778

Mass (Da):79,892

Checksum:ⁱ74D5DA9A1F8DC8EA

GO

Isoform 3 (identifier: P08047-3) [UniParc]FASTA Add to basket

Also known as: Sp1c

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

« Hide

        10         20         30         40         50
MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG 
        60         70         80         90        100
GGGQGANGWQ IISSSSGATP TSKEQSGSST NGSNGSESSK NRTVSGGQYV 
       110        120        130        140        150
VAAAPNLQNQ QVLTGLPGVM PNIQYQVIPQ FQTVDGQQLQ FAATGAQVQQ 
       160        170        180        190        200
DGSGQIQIIP GANQQIITNR GSGGNIIAAM PNLLQQAVPL QGLANNVLSG 
       210        220        230        240        250
QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAVTISS SGSQESGSQP 
       260        270        280        290        300
VTSGTTISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTTSGSSG 
       310        320        330        340        350
TNSQGQTPQR VSGLQGSDAL NIQQNQTSGG SLQAGQQKEG EQNQQTQQQQ 
       360        370        380        390        400
ILIQPQLVQG GQALQALQAA PLSGQTFTTQ AISQETLQNL QLQAVPNSGP 
       410        420        430        440        450
IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ AQTITLAPMQ GVSLGQTSSS 
       460        470        480        490        500
NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG TSGIQVHPIQ 
       510        520        530        540        550
GLPLAIANAP GDHGAQLGLH GAGGDGIHDD TAGGEEGENS PDAQPQAGRR 
       560        570        580        590        600
TRREACTCPY CKDSEGRGSG DPGKKKQHIC HIQGCGKVYG KTSHLRAHLR 
       610        620        630        640        650
WHTGERPFMC TWSYCGKRFT RSDELQRHKR THTGEKKFAC PECPKRFMRS 
       660        670        680        690        700
DHLSKHIKTH QNKKGGPGVA LSVGTLPLDS GAGSEGSGTA TPSALITTNM 
       710        720        730 
VAMEAICPEG IARLANSGIN VMQVADLQSI NISGNGF

Show »

Length:737

Mass (Da):75,824

Checksum:ⁱD830B2947A96C8B9

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H3BVI2	H3BVI2_HUMAN	Transcription factor Sp1 Transcription factor Sp1	SP1	230	Annotation score:
H3BUU5	H3BUU5_HUMAN	Transcription factor Sp1 Transcription factor Sp1	SP1	162	Annotation score:

Sequence cautionⁱ

The sequence AAH43224 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	366	D → G AA sequence (PubMed:3319186).Curated		1
Sequence conflictⁱ	670	S → F AA sequence (PubMed:3319186).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_019971	737	T → A. Corresponds to variant dbSNP:rs3741665Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_053934	1 – 7	Missing in isoform 2. Curated		7
Alternative sequenceⁱVSP_053935	54 – 101	Missing in isoform 3. 1 PublicationAdd BLAST		48

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS44898.1 [P08047-2] CCDS8857.1 [P08047-1]
PIRⁱ	A29635
NCBI Reference Sequences More...RefSeqⁱ	NP_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

Genome annotation databases

Ensemblⁱ	ENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1] ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2]
GeneIDⁱ	6667
KEGGⁱ	hsa:6667
UCSC genome browser More...UCSCⁱ	uc001scw.4, human [P08047-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P08047	Isoform 2 of Transcription factor Sp1		HUMAN		778	UniRef100_P08047
Transcription factor Sp1 (Fragment)		HUMAN		230
Transcription factor Sp1 (Fragment)		HUMAN		106
P08047-3	Transcription factor Sp1 (Fragment)		HUMAN		162	UniRef100_P08047-3

Protein	Similar proteins		Species	Score	Length	Source
P08047	Isoform 2 of Transcription factor Sp1		HUMAN		778	UniRef90_P08047
Transcription factor Sp1		HETGA		838
transcription factor Sp1 isoform X1		OCTDE		789
transcription factor Sp1 isoform X1		VULVU		786
Sp1 transcription factor		CAVPO		786
+37
P08047-3	Transcription factor Sp1 (Fragment)		HUMAN		162	UniRef90_P08047-3
Transcription factor Sp1 (Fragment)		TUPCH		661
+7

Protein	Similar proteins		Species	Score	Length	Source
P08047	Isoform 2 of Transcription factor Sp1		HUMAN		778	UniRef50_P08047
Transcription factor Sp1		HETGA		838
transcription factor Sp1 isoform X1		OCTDE		789
Sp1 transcription factor		FELCA		786
Uncharacterized protein		LYNCA		786
+134
P08047-3	Transcription factor Sp1 (Fragment)		HUMAN		162	UniRef50_P08047-3
Transcription factor Sp1 (Fragment)		TUPCH		661
SP1 factor (Fragment)		Prunella himalayana		655
Uncharacterized protein		Hirundo rustica rustica		766
SP1 factor (Fragment)		short-toed tree-creeper		704
+94

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
CCDSⁱ	CCDS44898.1 [P08047-2] CCDS8857.1 [P08047-1]
PIRⁱ	A29635
RefSeqⁱ	NP_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

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1SP1	NMR	-	A	684-712	[»]
	1SP2	NMR	-	A	654-684	[»]
	1VA1	NMR	-	A	619-654	[»]
	1VA2	NMR	-	A	654-684	[»]
	1VA3	NMR	-	A	684-712	[»]
	6PV0	NMR	-	A	654-684	[»]
	6PV1	NMR	-	A	654-684	[»]
	6PV2	NMR	-	A	654-684	[»]
	6PV3	NMR	-	A	655-684	[»]
	6UCO	NMR	-	A	654-684	[»]
	6UCP	NMR	-	A	654-684	[»]
BMRBⁱ	P08047
SMRⁱ	P08047
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	112550, 251 interactors
CORUMⁱ	P08047
DIPⁱ	DIP-36N
ELMⁱ	P08047
IntActⁱ	P08047, 74 interactors
MINTⁱ	P08047
STRINGⁱ	9606.ENSP00000329357

Chemistry databases

BindingDBⁱ	P08047
ChEMBLⁱ	CHEMBL6103

PTM databases

GlyConnectⁱ	605, 1 O-Linked glycan
GlyGenⁱ	P08047, 11 sites, 1 O-linked glycan (5 sites)
iPTMnetⁱ	P08047
PhosphoSitePlusⁱ	P08047

Genetic variation databases

BioMutaⁱ	SP1
DMDMⁱ	13638437

Proteomic databases

EPDⁱ	P08047
jPOSTⁱ	P08047
MassIVEⁱ	P08047
MaxQBⁱ	P08047
PaxDbⁱ	P08047
PeptideAtlasⁱ	P08047
PRIDEⁱ	P08047
ProteomicsDBⁱ	33987 52061 [P08047-1]

Protocols and materials databases

Antibodypediaⁱ	892, 1051 antibodies

Antibodypediaⁱ

892, 1051 antibodies

Genome annotation databases

Ensemblⁱ	ENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1] ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2]
GeneIDⁱ	6667
KEGGⁱ	hsa:6667
UCSCⁱ	uc001scw.4, human [P08047-1]

Organism-specific databases

CTDⁱ	6667
DisGeNETⁱ	6667
GeneCardsⁱ	SP1
HGNCⁱ	HGNC:11205, SP1
HPAⁱ	ENSG00000185591, Low tissue specificity
MIMⁱ	189906, gene
neXtProtⁱ	NX_P08047
OpenTargetsⁱ	ENSG00000185591
PharmGKBⁱ	PA36042
VEuPathDBⁱ	HostDB:ENSG00000185591.9
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1721, Eukaryota
GeneTreeⁱ	ENSGT00940000157804
HOGENOMⁱ	CLU_019688_2_0_1
InParanoidⁱ	P08047
OMAⁱ	EACTCPM
OrthoDBⁱ	1085860at2759
PhylomeDBⁱ	P08047
TreeFamⁱ	TF350150

Enzyme and pathway databases

PathwayCommonsⁱ	P08047
Reactomeⁱ	R-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
SignaLinkⁱ	P08047
SIGNORⁱ	P08047

Miscellaneous databases

BioGRID-ORCSⁱ	6667, 139 hits in 1031 CRISPR screens
ChiTaRSⁱ	SP1, human
EvolutionaryTraceⁱ	P08047
GeneWikiⁱ	Sp1_transcription_factor
GenomeRNAiⁱ	6667
Pharosⁱ	P08047, Tbio
Protein Ontology More...PROⁱ	PR:P08047
RNActⁱ	P08047, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000185591, Expressed in nipple and 221 other tissues
ExpressionAtlasⁱ	P08047, baseline and differential
Genevisibleⁱ	P08047, HS

Family and domain databases

DisProtⁱ	DP00378
IDEALⁱ	IID00266
InterProⁱ	View protein in InterPro IPR036236, Znf_C2H2_sf IPR013087, Znf_C2H2_type
Pfamⁱ	View protein in Pfam PF00096, zf-C2H2, 3 hits
SMARTⁱ	View protein in SMART SM00355, ZnF_C2H2, 3 hits
SUPFAMⁱ	SSF57667, SSF57667, 1 hit
PROSITEⁱ	View protein in PROSITE PS00028, ZINC_FINGER_C2H2_1, 3 hits PS50157, ZINC_FINGER_C2H2_2, 3 hits
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SP1_HUMAN
Accessionⁱ	P08047Primary (citable) accession number: P08047 Secondary accession number(s): E4Z9M7 Q9NYE7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	April 27, 2001
	Last modified:	April 7, 2021
	This is version 247 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Direct protein sequencing, Reference proteome

Documents

Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P08047 (SP1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Transcription factor Sp1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P08047

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ