Reviewed, UniProtKB/Swiss-Prot P08047 (SP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcription factor Sp1

Gene names

Name:	SP1
Synonyms:	TSFP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	785 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites. Can interact with G/C-rich motifs from serotonin receptor promoter.
Subunit structure	Interacts with ATF7IP, ATF7IP2, POGZ, HCFC1, AATF and PHC2. Interacts with varicella-zoster virus IE62 protein and HIV-1 Vpr. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the two proteins in DNA binding. Ref.8 Ref.11 Ref.13 Ref.14 Ref.16
Subcellular location	Nucleus.
Post-translational modification	O-glycosylated; contains N-acetylglucosamine side chains. Ref.7
Sequence similarities	Belongs to the Sp1 C2H2-type zinc-finger protein family. Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription from RNA polymerase II promoter, global Inferred from direct assay. Source: HGNC transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Ref.7 Inferred by curator. Source: UniProtKB
Molecular function	RNA polymerase II transcription factor activity Ref.7 Non-traceable author statement. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay. Source: HGNC transcription activator activity Inferred from direct assay. Source: MGI transcription factor activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-298336,EBI-298336
ABL1	P00519	1	EBI-298336,EBI-375543
ATF7IP	Q6VMQ6	1	EBI-298336,EBI-928732
CRK	P46108	1	EBI-298336,EBI-886
E2F1	Q01094	2	EBI-298336,EBI-448924
ELF1	P32519	1	EBI-298336,EBI-765526
FYN	P06241	1	EBI-298336,EBI-515315
GRB2	P62993	1	EBI-298336,EBI-401755
HCFC1	P51610	2	EBI-298336,EBI-396176
KLF10	Q13118	1	EBI-298336,EBI-1389509
MYC	P01106	2	EBI-298336,EBI-447544
NCK1	P16333	1	EBI-298336,EBI-389883
Nfya	P18576	1	EBI-298336,EBI-862695	From a different organism.
Nfya	P23708	2	EBI-298336,EBI-862337	From a different organism.
PHC2	Q8IXK0	1	EBI-298336,EBI-713786
POGZ	Q7Z3K3	1	EBI-298336,EBI-1389308
POU2F1	P14859	1	EBI-298336,EBI-624770
RNASEN	Q9NRR4	1	EBI-298336,EBI-528367
RNF19A	Q9NV58	1	EBI-298336,EBI-1390270
SF3A1	Q15459	1	EBI-298336,EBI-1054743
SRC	P12931	1	EBI-298336,EBI-621482
SREBF2	Q12772	1	EBI-298336,EBI-465059

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 785

785

Transcription factor Sp1

PRO_0000047137

Regions

Zinc finger

626 – 650

25

C2H2-type 1

Zinc finger

656 – 680

25

C2H2-type 2

Zinc finger

686 – 708

23

C2H2-type 3

Region

619 – 785

167

VZV IE62-binding

Amino acid modifications

Modified residue

7

1

Phosphoserine By similarity

Modified residue

59

1

Phosphoserine Ref.15 Ref.17

Modified residue

651

1

Phosphothreonine Ref.18

Natural variations

Natural variant

737

1

T → A: dbSNP rs3741665.

VAR_019971

Experimental info

Sequence conflict

366

1

D → G AA sequence Ref.4

Sequence conflict

670

1

S → F AA sequence Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

785

Helix Strand Turn

Details...

Beta strand

620 – 622

3

Beta strand

636 – 638

3

Helix

640 – 651

12

Helix

670 – 677

8

Turn

678 – 680

3

Turn

689 – 692

4

Helix

699 – 706

8

Helix

707 – 709

3

Sequences

	Sequence		Length	Mass (Da)
	P08047-1 [UniParc]. Last modified April 27, 2001. Version 3. Checksum: 43893DBF6518B9EA	FASTA	785	80,693
	10 20 30 40 50 60 MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG GGGQESQPSP 70 80 90 100 110 120 LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL SQGANGWQII SSSSGATPTS 130 140 150 160 170 180 KEQSGSSTNG SNGSESSKNR TVSGGQYVVA AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ 190 200 210 220 230 240 TVDGQQLQFA ATGAQVQQDG SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG 250 260 270 280 290 300 LANNVLSGQT QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT 310 320 330 340 350 360 SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN SQGQTPQRVS 370 380 390 400 410 420 GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL IQPQLVQGGQ ALQALQAAPL 430 440 450 460 470 480 SGQTFTTQAI SQETLQNLQL QAVPNSGPII IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ 490 500 510 520 530 540 TITLAPMQGV SLGQTSSSNT TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS 550 560 570 580 590 600 GIQVHPIQGL PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR 610 620 630 640 650 660 REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH TGERPFMCTW 670 680 690 700 710 720 SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH LSKHIKTHQN KKGGPGVALS 730 740 750 760 770 780 VGTLPLDSGA GSEGSGTATP SALITTNMVA MEAICPEGIA RLANSGINVM QVADLQSINI SGNGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Testis.
[2]	Haggart M.H., Ladurner A.G. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-785. Tissue: Cervix carcinoma.
[3]	"Heterogeneous Sp1 mRNAs in human HepG2 cells include a product of homotypic trans-splicing." Takahara T., Kanazu S., Yanagisawa S., Akanuma H. J. Biol. Chem. 275:38067-38072(2000) [PubMed: 10973950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-558.
[4]	"Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain." Kadonaga J.T., Carner K.R., Masiarz F.R., Tjian R. Cell 51:1079-1090(1987) [PubMed: 3319186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 90-785, PROTEIN SEQUENCE OF 359-375 AND 670-675.
[5]	"Expression of transcription factor Sp1 mRNA in mammalian cells." Nicolas M., Noe V., Ciudad C.J. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-109.
[6]	"Sequencing of the 5' end of human transcription factor SP1 mRNA." Handschug K., Huebner A. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98.
[7]	"O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation." Jackson S.P., Tjian R. Cell 55:125-133(1988) [PubMed: 3139301] [Abstract] Cited for: GLYCOSYLATION.
[8]	"Interaction of virion protein Vpr of human immunodeficiency virus type 1 with cellular transcription factor Sp1 and trans-activation of viral long terminal repeat." Wang L., Mukherjee S., Jia F., Narayan O., Zhao L.J. J. Biol. Chem. 270:25564-25569(1995) [PubMed: 7592727] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[9]	"The serotonin 1a receptor gene contains a TATA-less promoter that responds to MAZ and Sp1." Parks C.L., Shenk T. J. Biol. Chem. 271:4417-4430(1996) [PubMed: 8626793] [Abstract] Cited for: IDENTIFICATION OF SEROTONIN 1A RECEPTOR PROMOTER BINDING SITES.
[10]	"The SV40 capsid protein VP3 cooperates with the cellular transcription factor Sp1 in DNA-binding and in regulating viral promoter activity." Gordon-Shaag A., Ben-Nun-Shaul O., Kasamatsu H., Oppenheim A.B., Oppenheim A. J. Mol. Biol. 275:187-195(1998) [PubMed: 9466902] [Abstract] Cited for: INTERACTION WITH SV40 VP2/3.
[11]	"A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening." Gunther M., Laithier M., Brison O. Mol. Cell. Biochem. 210:131-142(2000) [PubMed: 10976766] [Abstract] Cited for: INTERACTION WITH ATF7IP; PHC2; POGZ AND HCFC1. Tissue: Colon.
[12]	"Cellular transcription factor Sp1 recruits simian virus 40 capsid proteins to the viral packaging signal, ses." Gordon-Shaag A., Ben-Nun-Shaul O., Roitman V., Yosef Y., Oppenheim A. J. Virol. 76:5915-5924(2002) [PubMed: 12021324] [Abstract] Cited for: INTERACTION WITH SV40 VP1.
[13]	"Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter." Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M. J. Biol. Chem. 278:36496-36504(2003) [PubMed: 12847090] [Abstract] Cited for: INTERACTION WITH AATF.
[14]	"Interaction between the varicella zoster virus IE62 major transactivator and cellular transcription factor Sp1." Peng H., He H., Hay J., Ruyechan W.T. J. Biol. Chem. 278:38068-38075(2003) [PubMed: 12855699] [Abstract] Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN.
[15]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins." Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M. J. Biol. Chem. 280:13928-13935(2005) [PubMed: 15691849] [Abstract] Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
[17]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-651, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition." Narayan V.A., Kriwacki R.W., Caradonna J.P. J. Biol. Chem. 272:7801-7809(1997) [PubMed: 9065444] [Abstract] Cited for: STRUCTURE BY NMR OF 654-684 AND 684-712.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00465152.

PIR

A29635.

RefSeq

NP_003100.1.
NP_612482.2.

UniGene

Hs.620754
Hs.649191

3D structure databases

PDBPDBe

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	[»]

DisProt

DP00378.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:36N.

IntAct

P08047. 28 interactions.

PTM databases

GlycoSuiteDB

P08047.

PhosphoSite

P08047.

Proteomic databases

PeptideAtlas

P08047.

PRIDE

P08047.

Genome annotation databases

Ensembl

ENSG00000185591. Homo sapiens. [Contig view]

GeneID

6667.

KEGG

hsa:6667.

UCSC

uc001scw.1. human.

Organism-specific databases

GeneCards

GC12P052060.

H-InvDB

HIX0010670.

HGNC

HGNC:11205. SP1.

HPA

CAB000330.
HPA001853.
HPA012292.

MIM

189906. gene.

PharmGKB

PA25061.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P08047.

HOVERGEN

P08047.

OMA

P08047. TITLAPM.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.
hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
foxm1pathway. FOXM1 transcription factor network.
hif1_tfpathway. HIF-1-alpha transcription factor network.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il4_2pathway. IL4-mediated signaling events.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

P08047.

Bgee

P08047.

CleanEx

HS_SP1.

GermOnline

ENSG00000185591. Homo sapiens.

Family and domain databases

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 2 hits.

Pfam

PF00096. zf-C2H2. 3 hits.
[Graphical view]

ProDom

PD000003. Znf_C2H2. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00355. ZnF_C2H2. 3 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25995.

PMAP-CutDB

P08047.

SOURCE

Search...

Entry information

Entry name

SP1_HUMAN

Accession

Primary (citable) accession number: P08047
Secondary accession number(s): Q86TN8 , Q9H3Q5, Q9NR51, Q9NY21, Q9NYE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	April 27, 2001
Last modified:	July 7, 2009
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)