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Q02447 (SP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor Sp3
Alternative name(s):
SPR-2
Gene names
Name:SP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional factor that can act as an activator or repressor depending on isoform and/orpost-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping. Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Subunit structure

Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts with HDAC1; the interaction deacetylates SP3 and regulates its transcriptional activity. Interacts with HDAC2 (preferably the CK2-phosphorylated form); the interaction deacetylates SP3 and regulates its transcriptional activity. Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a Ref.11 Ref.13 Ref.15 Ref.20 Ref.26

Subcellular location

Nucleus. NucleusPML body. Note: Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies. Ref.14 Ref.17 Ref.21

Tissue specificity

Ubiquitously expressed.

Post-translational modification

Not glycosylated. Ref.16

Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-551 also control transcriptional activity. Ceramides can also regulate acetylation/deacetylation events through altering the interaction of HDAC with SP3. In vitro, C(18)-ceramides, but not C(16)-ceramides, increase the interaction of HDAC1 with SP3 and enhance the deacetylation of SP3 and the subsequent repression of the TERT promoter. Ref.12 Ref.15 Ref.18 Ref.20

Sumoylated on all isoforms. Sumoylated on 2 sites in longer isoforms with Lys-551 being the major site. Sumoylation at this site promotes nuclear localization to the nuclear periphery, nuclear dots and PML nuclear bodies. Sumoylation on Lys-551 represses the transactivation activity, except for the largest isoform, L-Sp3, which has little effect on transactivation. Alternate sumoylation and acetylation at Lys-551 also control transcriptional activity. Ref.12 Ref.15 Ref.18 Ref.20

Sequence similarities

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

Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

T cell differentiation

Inferred from electronic annotation. Source: Ensembl

definitive hemopoiesis

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

embryonic process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system development

Inferred from electronic annotation. Source: Ensembl

enucleate erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

granulocyte differentiation

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

megakaryocyte differentiation

Inferred from electronic annotation. Source: Ensembl

monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20091743. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12771217. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12560508. Source: UniProtKB

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred by curator PubMed 12560508. Source: UniProtKB

transcriptional repressor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.11Ref.13PubMed 17130167. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033722EBI-348158,EBI-78473

Alternative products

This entry describes 6 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q02447-1)

Also known as: Large; L-Sp3;

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.
Isoform 2 (identifier: Q02447-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
Note: Produced by alternative initiation at Met-13 of isoform 1. No experimental confirmation available.
Isoform 3 (identifier: Q02447-3)

Also known as: M1-Sp3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-285: Missing.
Note: Produced by alternative initiation at Met-286 of isoform 1. No experimental confirmation available.
Isoform 4 (identifier: Q02447-4)

Also known as: M2-Sp3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.
Note: Produced by alternative initiation at Met-303 of isoform 1. No experimental confirmation available.
Isoform 5 (identifier: Q02447-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MTAPEKPVKQEEMAALDVDSGGGGGGGGGHGEYLQQQQQHGNGAVAAAAAAQDTQPSPLALLAATCSKI → M
Note: Produced by alternative splicing. An AUA codon is translated into Met and used as a translation initiation site (in vitro).
Isoform 6 (identifier: Q02447-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
     53-93: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 781781Transcription factor Sp3
PRO_0000047141

Regions

Zinc finger621 – 64525C2H2-type 1
Zinc finger651 – 67525C2H2-type 2
Zinc finger681 – 70323C2H2-type 3
Region138 – 237100Transactivation domain (Gln-rich)
Region350 – 499150Transactivation domain (Gln-rich)
Region534 – 62087Repressor domain
Compositional bias21 – 3111Poly-Gly
Compositional bias35 – 395Poly-Gln
Compositional bias44 – 10057Ala-rich

Amino acid modifications

Modified residue731Phosphoserine Ref.23 Ref.24 Ref.25
Modified residue5511N6-acetyllysine; alternate Ref.12 Ref.18
Modified residue5631Phosphoserine Ref.23
Modified residue6461Phosphoserine Ref.23
Cross-link120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14
Cross-link551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.14 Ref.17 Ref.19 Ref.22

Natural variations

Alternative sequence1 – 302302Missing in isoform 4.
VSP_026698
Alternative sequence1 – 285285Missing in isoform 3.
VSP_026699
Alternative sequence1 – 6969MTAPE…TCSKI → M in isoform 5.
VSP_026700
Alternative sequence1 – 1212Missing in isoform 2 and isoform 6.
VSP_026701
Alternative sequence53 – 9341Missing in isoform 6.
VSP_026702
Natural variant1641T → A. Ref.1 Ref.2 Ref.9
Corresponds to variant rs1047640 [ dbSNP | Ensembl ].
VAR_016123

Experimental info

Mutagenesis1201K → R: Some loss of sumoylation. Slight increase in transcriptional activity. Large increase in transcriptional activity; when associated with R-551. Ref.14
Mutagenesis551 – 5533KEE → AAA: Increases transcriptional activity. Ref.14 Ref.17 Ref.19 Ref.20
Mutagenesis551 – 5533KEE → REA: 200-fold increase in transcriptional activation. Ref.14 Ref.17 Ref.19 Ref.20
Mutagenesis551 – 5533KEE → RED: 200-fold increase in transcriptional activation. Ref.14 Ref.17 Ref.19 Ref.20
Mutagenesis551 – 5522KE → RA: 200-fold increase in transcriptional activation. Ref.14 Ref.19 Ref.20
Mutagenesis551 – 5522KE → RD: 200-fold increase in transcriptional activation. Ref.14 Ref.19 Ref.20
Mutagenesis5511K → Q: A decreased interaction with HDAC1 and deacetylation of SP3. Increase of about 4.5% of activity of the TERT promoter. Decreased recruitment of HDAC1 and increased binding of RNA polymerase II with promoter DNA. Ref.14 Ref.19 Ref.20
Mutagenesis5511K → R: Great loss of sumoylation, 20-fold increase in transcriptional activity and diffuse nuclear localization. Further small increase in transcriptional activity; when associated with R-120. Increased interaction with HDAC1 and deacetylation of SP3. About 50% decrease in activity of the TERT promoter. Enhances recruitment of HDAC1 and inhibits binding of RNA polymerase II with promoter DNA. Ref.14 Ref.19 Ref.20
Sequence conflict691I → M in AAR30505. Ref.2
Sequence conflict711P → G in AAA36630. Ref.7
Sequence conflict7391N → K in AAL58086. Ref.1
Sequence conflict7391N → K in AAR30505. Ref.2
Sequence conflict7391N → K in AAR30506. Ref.2
Sequence conflict7391N → K in CAA48562. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Large) (L-Sp3) [UniParc].

Last modified May 16, 2003. Version 3.
Checksum: DCFD4363509DB49D

FASTA78181,925
        10         20         30         40         50         60 
MTAPEKPVKQ EEMAALDVDS GGGGGGGGGH GEYLQQQQQH GNGAVAAAAA AQDTQPSPLA 

        70         80         90        100        110        120 
LLAATCSKIG PPSPGDDEEE AAAAAGAPAA AGATGDLASA QLGGAPNRWE VLSATPTTIK 

       130        140        150        160        170        180 
DEAGNLVQIP SAATSSGQYV LPLQNLQNQQ IFSVAPGSDS SNGTVSSVQY QVIPQIQSAD 

       190        200        210        220        230        240 
GQQVQIGFTG SSDNGGINQE SSQIQIIPGS NQTLLASGTP SANIQNLIPQ TGQVQVQGVA 

       250        260        270        280        290        300 
IGGSSFPGQT QVVANVPLGL PGNITFVPIN SVDLDSLGLS GSSQTMTAGI NADGHLINTG 

       310        320        330        340        350        360 
QAMDSSDNSE RTGERVSPDI NETNTDTDLF VPTSSSSQLP VTIDSTGILQ QNTNSLTTSS 

       370        380        390        400        410        420 
GQVHSSDLQG NYIQSPVSEE TQAQNIQVST AQPVVQHLQL QESQQPTSQA QIVQGITPQT 

       430        440        450        460        470        480 
IHGVQASGQN ISQQALQNLQ LQLNPGTFLI QAQTVTPSGQ VTWQTFQVQG VQNLQNLQIQ 

       490        500        510        520        530        540 
NTAAQQITLT PVQTLTLGQV AAGGAFTSTP VSLSTGQLPN LQTVTVNSID SAGIQLHPGE 

       550        560        570        580        590        600 
NADSPADIRI KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQQHQ EGKRLRRVAC 

       610        620        630        640        650        660 
TCPNCKEGGG RGTNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP FVCNWMYCGK 

       670        680        690        700        710        720 
RFTRSDELQR HRRTHTGEKK FVCPECSKRF MRSDHLAKHI KTHQNKKGIH SSSTVLASVE 

       730        740        750        760        770        780 
AARDDTLITA GGTTLILANI QQGSVSGIGT VNTSATSNQD ILTNTEIPLQ LVTVSGNETM 


E 

« Hide

Isoform 2 [UniParc].

Checksum: C02D0B852BBF9389
Show »

FASTA76980,557
Isoform 3 (M1-Sp3) [UniParc].

Checksum: 65658E7F04158661
Show »

FASTA49653,715
Isoform 4 (M2-Sp3) [UniParc].

Checksum: DA04C2A90DFA307A
Show »

FASTA47952,050
Isoform 5 [UniParc].

Checksum: B0CF8FC66DA30478
Show »

FASTA71375,330
Isoform 6 [UniParc].

Checksum: E9D95D6717E9F885
Show »

FASTA72876,814

References

« Hide 'large scale' references
[1]"AUA as a translation initiation site in vitro for the human transcription factor Sp3."
Hernandez E.M., Johnson A., Notario V., Chen A., Richert J.R.
J. Biochem. Mol. Biol. 35:273-282(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT ALA-164.
[2]"Human transcription factor Sp3: genomic structure, identification of a processed pseudogene, and transcript analysis."
Moran K.M., Crusio R.H., Chan C.H., Grekova M.C., Richert J.R.
Gene 341:235-247(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), ALTERNATIVE INITIATION (ISOFORMS 2; 3 AND 4), VARIANT ALA-164.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Trachea.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lung.
[5]"5' genomic structure of human Sp3."
Oleksiak M.F., Crawford D.L.
Mol. Biol. Evol. 19:2026-2029(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
[6]"Regulation of hTERT-gene transcription by SP3."
Meyer-Grahle U.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-112.
[7]Kingsley C., Winoto A.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 71-781, SEQUENCE REVISION.
Tissue: T-cell.
[8]"Cloning of GT box-binding proteins: a novel Sp1 multigene family regulating T-cell receptor gene expression."
Kingsley C., Winoto A.
Mol. Cell. Biol. 12:4251-4261(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-781.
[9]"Cloning by recognition site screening of two novel GT box binding proteins: a family of Sp1 related genes."
Hagen G., Mueller S., Beato M., Suske G.
Nucleic Acids Res. 20:5519-5525(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-781, VARIANT ALA-164.
Tissue: Uterus.
[10]"Sp3 is a transcriptional activator of the human alpha2(I) collagen gene."
Ihn H., Trojanowska M.
Nucleic Acids Res. 25:3712-3717(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene."
Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.
J. Biol. Chem. 274:19573-19580(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HLTF.
[12]"Transcription factor Sp3 is regulated by acetylation."
Braun H., Koop R., Ertmer A., Nacht S., Suske G.
Nucleic Acids Res. 29:4994-5000(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-551, FUNCTION, MUTAGENESIS OF 551-LYS--GLU-557.
[13]"The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2."
Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R.
J. Biol. Chem. 277:35783-35786(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1 AND HDAC2.
[14]"SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization."
Ross S., Best J.L., Zon L.I., Gill G.
Mol. Cell 10:831-842(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-120 AND LYS-551, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-120 AND LYS-551.
[15]"Acetylated SP3 is a transcriptional activator."
Ammanamanchi S., Freeman J.W., Brattain M.G.
J. Biol. Chem. 278:35775-35780(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1 AND EP300, ACETYLATION, FUNCTION.
[16]"Complexity of translationally controlled transcription factor Sp3 isoform expression."
Sapetschnig A., Koch F., Rischitor G., Mennenga T., Suske G.
J. Biol. Chem. 279:42095-42105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, ALTERNATIVE PRODUCTS, LACK OF GLYCOSYLATION, FUNCTION.
[17]"Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism."
Spengler M.L., Kennett S.B., Moorefield K.S., Simmons S.O., Brattain M.G., Horowitz J.M.
Cell. Signal. 17:153-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-551, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 551-LYS--GLU-553.
[18]"Sp3 is involved in the regulation of SOCS3 gene expression."
Ehlting C., Haussinger D., Bode J.G.
Biochem. J. 387:737-745(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-551, FUNCTION.
[19]"The modification of Sp3 isoforms by SUMOylation has differential effects on the SRC1A promoter."
Ellis D.J., Dehm S.M., Bonham K.
Gene 379:68-78(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-551, FUNCTION OF ISOFORMS, MUTAGENESIS OF LYS-551.
[20]"Mechanisms of ceramide-mediated repression of the human telomerase reverse transcriptase promoter via deacetylation of Sp3 by histone deacetylase 1."
Wooten-Blanks L.G., Song P., Senkal C.E., Ogretmen B.
FASEB J. 21:3386-3397(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEACETYLATION, INTERACTION WITH HDAC1, MUTAGENESIS OF LYS-551.
[21]"Nuclear organization and chromatin dynamics -- Sp1, Sp3 and histone deacetylases."
Davie J.R., He S., Li L., Sekhavat A., Espino P., Drobic B., Dunn K.L., Sun J.M., Chen H.Y., Yu J., Pritchard S., Wang X.
Adv. Enzyme Regul. 48:189-208(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[22]"SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing."
Stielow B., Sapetschnig A., Wink C., Kraeger I., Suske G.
EMBO Rep. 9:899-906(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-551, FUNCTION OF ISOFORMS.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-563 AND SER-646, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1."
Bjerke G.A., Hyman-Walsh C., Wotton D.
Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEIS2 AND PBX1.
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY070137 mRNA. Translation: AAL58086.1.
AY441957 mRNA. Translation: AAR30505.1.
AY441958 mRNA. Translation: AAR30506.1.
AK304199 mRNA. Translation: BAG65079.1.
BC126414 mRNA. Translation: AAI26415.1.
AF494280 Genomic DNA. Translation: AAM12875.1.
AJ310752 mRNA. Translation: CAC34575.1.
M97191 mRNA. Translation: AAA36630.2.
X68560 mRNA. Translation: CAA48562.1.
CCDSCCDS2254.1. [Q02447-1]
CCDS46452.1. [Q02447-5]
PIRB44489.
RefSeqNP_001017371.3. NM_001017371.4. [Q02447-5]
NP_001166183.1. NM_001172712.1.
NP_003102.1. NM_003111.4. [Q02447-1]
UniGeneHs.531587.

3D structure databases

ProteinModelPortalQ02447.
SMRQ02447. Positions 573-707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112553. 30 interactions.
IntActQ02447. 7 interactions.
MINTMINT-189716.
STRING9606.ENSP00000310301.

PTM databases

PhosphoSiteQ02447.

Polymorphism databases

DMDM30923147.

Proteomic databases

MaxQBQ02447.
PaxDbQ02447.
PRIDEQ02447.

Protocols and materials databases

DNASU6670.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310015; ENSP00000310301; ENSG00000172845. [Q02447-1]
ENST00000455789; ENSP00000388903; ENSG00000172845. [Q02447-6]
GeneID6670.
KEGGhsa:6670.
UCSCuc002uie.3. human. [Q02447-5]
uc002uif.3. human. [Q02447-6]
uc002uig.3. human. [Q02447-1]

Organism-specific databases

CTD6670.
GeneCardsGC02M174771.
HGNCHGNC:11208. SP3.
HPACAB004580.
MIM601804. gene.
neXtProtNX_Q02447.
PharmGKBPA36045.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOVERGENHBG008933.
InParanoidQ02447.
KOK09193.
OMAPQIQSTD.
OrthoDBEOG76HQ15.
PhylomeDBQ02447.
TreeFamTF350150.

Enzyme and pathway databases

SignaLinkQ02447.

Gene expression databases

ArrayExpressQ02447.
BgeeQ02447.
CleanExHS_SP3.
GenevestigatorQ02447.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSP3. human.
GeneWikiSp3_transcription_factor.
GenomeRNAi6670.
NextBio26005.
PMAP-CutDBQ02447.
PROQ02447.
SOURCESearch...

Entry information

Entry nameSP3_HUMAN
AccessionPrimary (citable) accession number: Q02447
Secondary accession number(s): A0AVL9 expand/collapse secondary AC list , B4E2B7, Q69B26, Q69B27, Q8TD56, Q8WWU4, Q9BQR1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 16, 2003
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM