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Q02447

- SP3_HUMAN

UniProt

Q02447 - SP3_HUMAN

Protein

Transcription factor Sp3

Gene

SP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (16 May 2003)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
    7. 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

    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. PML body Source: UniProtKB-SubCell
    3. transcriptional repressor complex Source: Ensembl

    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. 3 Publications
    Mutagenesisi551 – 5533KEE → REA: 200-fold increase in transcriptional activation. 3 Publications
    Mutagenesisi551 – 5533KEE → RED: 200-fold increase in transcriptional activation. 3 Publications
    Mutagenesisi551 – 5522KE → RA: 200-fold increase in transcriptional activation. 3 Publications
    Mutagenesisi551 – 5522KE → RD: 200-fold increase in transcriptional activation. 3 Publications
    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; alternate3 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

    ArrayExpressiQ02447.
    BgeeiQ02447.
    CleanExiHS_SP3.
    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. 31 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.
    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

    MTAPEKPVKQ EEMAALDVDS GGGGGGGGGH GEYLQQQQQH GNGAVAAAAA    50
    AQDTQPSPLA LLAATCSKIG PPSPGDDEEE AAAAAGAPAA AGATGDLASA 100
    QLGGAPNRWE VLSATPTTIK DEAGNLVQIP SAATSSGQYV LPLQNLQNQQ 150
    IFSVAPGSDS SNGTVSSVQY QVIPQIQSAD GQQVQIGFTG SSDNGGINQE 200
    SSQIQIIPGS NQTLLASGTP SANIQNLIPQ TGQVQVQGVA IGGSSFPGQT 250
    QVVANVPLGL PGNITFVPIN SVDLDSLGLS GSSQTMTAGI NADGHLINTG 300
    QAMDSSDNSE RTGERVSPDI NETNTDTDLF VPTSSSSQLP VTIDSTGILQ 350
    QNTNSLTTSS GQVHSSDLQG NYIQSPVSEE TQAQNIQVST AQPVVQHLQL 400
    QESQQPTSQA QIVQGITPQT IHGVQASGQN ISQQALQNLQ LQLNPGTFLI 450
    QAQTVTPSGQ VTWQTFQVQG VQNLQNLQIQ NTAAQQITLT PVQTLTLGQV 500
    AAGGAFTSTP VSLSTGQLPN LQTVTVNSID SAGIQLHPGE NADSPADIRI 550
    KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQQHQ EGKRLRRVAC 600
    TCPNCKEGGG RGTNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP 650
    FVCNWMYCGK RFTRSDELQR HRRTHTGEKK FVCPECSKRF MRSDHLAKHI 700
    KTHQNKKGIH SSSTVLASVE AARDDTLITA GGTTLILANI QQGSVSGIGT 750
    VNTSATSNQD ILTNTEIPLQ LVTVSGNETM E 781
    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. 31 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.
    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

    ArrayExpressi Q02447.
    Bgeei Q02447.
    CleanExi HS_SP3.
    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

    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 1, 2014
    This is version 143 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