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Q02447

- SP3_HUMAN

UniProt

Q02447 - SP3_HUMAN

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Protein

Transcription factor Sp3

Gene

SP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-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.12 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri621 – 64525C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri651 – 67525C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri681 – 70323C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. core promoter proximal region sequence-specific DNA binding Source: Ensembl
  3. double-stranded DNA binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
  6. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  1. B cell differentiation Source: Ensembl
  2. definitive hemopoiesis Source: Ensembl
  3. embryonic camera-type eye morphogenesis Source: Ensembl
  4. embryonic placenta development Source: Ensembl
  5. embryonic process involved in female pregnancy Source: Ensembl
  6. embryonic skeletal system development Source: Ensembl
  7. enucleate erythrocyte differentiation Source: Ensembl
  8. granulocyte differentiation Source: Ensembl
  9. liver development Source: Ensembl
  10. lung development Source: Ensembl
  11. megakaryocyte differentiation Source: Ensembl
  12. monocyte differentiation Source: Ensembl
  13. natural killer cell differentiation Source: Ensembl
  14. negative regulation of transcription, DNA-templated Source: UniProtKB
  15. ossification Source: Ensembl
  16. positive regulation of transcription, DNA-templated Source: UniProtKB
  17. regulation of transcription, DNA-templated Source: UniProtKB
  18. T cell differentiation Source: Ensembl
  19. trophectodermal cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ02447.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Sp3
Alternative name(s):
SPR-2
Gene namesi
Name:SP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11208. SP3.

Subcellular locationi

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

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. transcriptional repressor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201K → R: Some loss of sumoylation. Slight increase in transcriptional activity. Large increase in transcriptional activity; when associated with R-551. 1 Publication
Mutagenesisi551 – 5533KEE → AAA: Increases transcriptional activity. 1 Publication
Mutagenesisi551 – 5533KEE → REA: 200-fold increase in transcriptional activation. 1 Publication
Mutagenesisi551 – 5533KEE → RED: 200-fold increase in transcriptional activation. 1 Publication
Mutagenesisi551 – 5522KE → RA: 200-fold increase in transcriptional activation.
Mutagenesisi551 – 5522KE → RD: 200-fold increase in transcriptional activation.
Mutagenesisi551 – 5511K → 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. 3 Publications
Mutagenesisi551 – 5511K → 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. 3 Publications

Organism-specific databases

PharmGKBiPA36045.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 781781Transcription factor Sp3PRO_0000047141Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731Phosphoserine3 Publications
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei551 – 5511N6-acetyllysine; alternate2 Publications
Cross-linki551 – 551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei563 – 5631Phosphoserine1 Publication
Modified residuei646 – 6461Phosphoserine1 Publication

Post-translational modificationi

Not glycosylated.
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.7 Publications
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.7 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ02447.
PaxDbiQ02447.
PRIDEiQ02447.

PTM databases

PhosphoSiteiQ02447.

Miscellaneous databases

PMAP-CutDBQ02447.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ02447.
CleanExiHS_SP3.
ExpressionAtlasiQ02447. baseline and differential.
GenevestigatoriQ02447.

Organism-specific databases

HPAiCAB004580.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-348158,EBI-78473

Protein-protein interaction databases

BioGridi112553. 37 interactions.
IntActiQ02447. 7 interactions.
MINTiMINT-189716.
STRINGi9606.ENSP00000310301.

Structurei

3D structure databases

ProteinModelPortaliQ02447.
SMRiQ02447. Positions 573-707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 237100Transactivation domain (Gln-rich)Add
BLAST
Regioni350 – 499150Transactivation domain (Gln-rich)Add
BLAST
Regioni534 – 62087Repressor domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 3111Poly-GlyAdd
BLAST
Compositional biasi35 – 395Poly-Gln
Compositional biasi44 – 10057Ala-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri621 – 64525C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri651 – 67525C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri681 – 70323C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118984.
HOVERGENiHBG008933.
InParanoidiQ02447.
KOiK09193.
OMAiPQIQSTD.
OrthoDBiEOG76HQ15.
PhylomeDBiQ02447.
TreeFamiTF350150.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: Q02447-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTAPEKPVKQ EEMAALDVDS GGGGGGGGGH GEYLQQQQQH GNGAVAAAAA
60 70 80 90 100
AQDTQPSPLA LLAATCSKIG PPSPGDDEEE AAAAAGAPAA AGATGDLASA
110 120 130 140 150
QLGGAPNRWE VLSATPTTIK DEAGNLVQIP SAATSSGQYV LPLQNLQNQQ
160 170 180 190 200
IFSVAPGSDS SNGTVSSVQY QVIPQIQSAD GQQVQIGFTG SSDNGGINQE
210 220 230 240 250
SSQIQIIPGS NQTLLASGTP SANIQNLIPQ TGQVQVQGVA IGGSSFPGQT
260 270 280 290 300
QVVANVPLGL PGNITFVPIN SVDLDSLGLS GSSQTMTAGI NADGHLINTG
310 320 330 340 350
QAMDSSDNSE RTGERVSPDI NETNTDTDLF VPTSSSSQLP VTIDSTGILQ
360 370 380 390 400
QNTNSLTTSS GQVHSSDLQG NYIQSPVSEE TQAQNIQVST AQPVVQHLQL
410 420 430 440 450
QESQQPTSQA QIVQGITPQT IHGVQASGQN ISQQALQNLQ LQLNPGTFLI
460 470 480 490 500
QAQTVTPSGQ VTWQTFQVQG VQNLQNLQIQ NTAAQQITLT PVQTLTLGQV
510 520 530 540 550
AAGGAFTSTP VSLSTGQLPN LQTVTVNSID SAGIQLHPGE NADSPADIRI
560 570 580 590 600
KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQQHQ EGKRLRRVAC
610 620 630 640 650
TCPNCKEGGG RGTNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP
660 670 680 690 700
FVCNWMYCGK RFTRSDELQR HRRTHTGEKK FVCPECSKRF MRSDHLAKHI
710 720 730 740 750
KTHQNKKGIH SSSTVLASVE AARDDTLITA GGTTLILANI QQGSVSGIGT
760 770 780
VNTSATSNQD ILTNTEIPLQ LVTVSGNETM E
Length:781
Mass (Da):81,925
Last modified:May 16, 2003 - v3
Checksum:iDCFD4363509DB49D
GO
Isoform 2 (identifier: Q02447-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:769
Mass (Da):80,557
Checksum:iC02D0B852BBF9389
GO
Isoform 3 (identifier: Q02447-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:496
Mass (Da):53,715
Checksum:i65658E7F04158661
GO
Isoform 4 (identifier: Q02447-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:479
Mass (Da):52,050
Checksum:iDA04C2A90DFA307A
GO
Isoform 5 (identifier: Q02447-5) [UniParc]FASTAAdd to Basket

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).

Show »
Length:713
Mass (Da):75,330
Checksum:iB0CF8FC66DA30478
GO
Isoform 6 (identifier: Q02447-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
     53-93: Missing.

Note: Produced by alternative splicing.

Show »
Length:728
Mass (Da):76,814
Checksum:iE9D95D6717E9F885
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691I → M in AAR30505. (PubMed:15474306)Curated
Sequence conflicti71 – 711P → G in AAA36630. 1 PublicationCurated
Sequence conflicti739 – 7391N → K in AAL58086. (PubMed:12297010)Curated
Sequence conflicti739 – 7391N → K in AAR30505. (PubMed:15474306)Curated
Sequence conflicti739 – 7391N → K in AAR30506. (PubMed:15474306)Curated
Sequence conflicti739 – 7391N → K in CAA48562. (PubMed:1341900)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641T → A.3 Publications
Corresponds to variant rs1047640 [ dbSNP | Ensembl ].
VAR_016123

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 302302Missing in isoform 4. CuratedVSP_026698Add
BLAST
Alternative sequencei1 – 285285Missing in isoform 3. CuratedVSP_026699Add
BLAST
Alternative sequencei1 – 6969MTAPE…TCSKI → M in isoform 5. 1 PublicationVSP_026700Add
BLAST
Alternative sequencei1 – 1212Missing in isoform 2 and isoform 6. 2 PublicationsVSP_026701Add
BLAST
Alternative sequencei53 – 9341Missing in isoform 6. 1 PublicationVSP_026702Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2254.1. [Q02447-1]
CCDS46452.1. [Q02447-5]
PIRiB44489.
RefSeqiNP_001017371.3. NM_001017371.4. [Q02447-5]
NP_001166183.1. NM_001172712.1.
NP_003102.1. NM_003111.4. [Q02447-1]
UniGeneiHs.531587.

Genome annotation databases

EnsembliENST00000310015; ENSP00000310301; ENSG00000172845. [Q02447-1]
GeneIDi6670.
KEGGihsa:6670.
UCSCiuc002uie.3. human. [Q02447-5]
uc002uif.3. human. [Q02447-6]
uc002uig.3. human. [Q02447-1]

Polymorphism databases

DMDMi30923147.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2254.1. [Q02447-1 ]
CCDS46452.1. [Q02447-5 ]
PIRi B44489.
RefSeqi NP_001017371.3. NM_001017371.4. [Q02447-5 ]
NP_001166183.1. NM_001172712.1.
NP_003102.1. NM_003111.4. [Q02447-1 ]
UniGenei Hs.531587.

3D structure databases

ProteinModelPortali Q02447.
SMRi Q02447. Positions 573-707.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112553. 37 interactions.
IntActi Q02447. 7 interactions.
MINTi MINT-189716.
STRINGi 9606.ENSP00000310301.

PTM databases

PhosphoSitei Q02447.

Polymorphism databases

DMDMi 30923147.

Proteomic databases

MaxQBi Q02447.
PaxDbi Q02447.
PRIDEi Q02447.

Protocols and materials databases

DNASUi 6670.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310015 ; ENSP00000310301 ; ENSG00000172845 . [Q02447-1 ]
GeneIDi 6670.
KEGGi hsa:6670.
UCSCi uc002uie.3. human. [Q02447-5 ]
uc002uif.3. human. [Q02447-6 ]
uc002uig.3. human. [Q02447-1 ]

Organism-specific databases

CTDi 6670.
GeneCardsi GC02M174771.
HGNCi HGNC:11208. SP3.
HPAi CAB004580.
MIMi 601804. gene.
neXtProti NX_Q02447.
PharmGKBi PA36045.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00760000118984.
HOVERGENi HBG008933.
InParanoidi Q02447.
KOi K09193.
OMAi PQIQSTD.
OrthoDBi EOG76HQ15.
PhylomeDBi Q02447.
TreeFami TF350150.

Enzyme and pathway databases

SignaLinki Q02447.

Miscellaneous databases

ChiTaRSi SP3. human.
GeneWikii Sp3_transcription_factor.
GenomeRNAii 6670.
NextBioi 26005.
PMAP-CutDB Q02447.
PROi Q02447.
SOURCEi Search...

Gene expression databases

Bgeei Q02447.
CleanExi HS_SP3.
ExpressionAtlasi Q02447. baseline and differential.
Genevestigatori Q02447.

Family and domain databases

Gene3Di 3.30.160.60. 3 hits.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 3 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiSP3_HUMAN
AccessioniPrimary (citable) accession number: Q02447
Secondary accession number(s): A0AVL9
, B4E2B7, Q69B26, Q69B27, Q8TD56, Q8WWU4, Q9BQR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 16, 2003
Last modified: October 29, 2014
This is version 144 of the entry and version 3 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3