SP3_MOUSE
ID SP3_MOUSE Reviewed; 783 AA.
AC O70494; A2AQK9; Q68FF2; Q8CF64; Q8K378;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transcription factor Sp3;
GN Name=Sp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-783 (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RX PubMed=9628590; DOI=10.1089/dna.1998.17.471;
RA Yajima S., Lee S.H., Minowa T., Mouradian M.M.;
RT "Sp family transcription factors regulate expression of rat D2 dopamine
RT receptor gene.";
RL DNA Cell Biol. 17:471-479(1998).
RN [5]
RP ACETYLATION AT LYS-553, AND FUNCTION.
RX PubMed=15554904; DOI=10.1042/bj20041101;
RA Ehlting C., Haussinger D., Bode J.G.;
RT "Sp3 is involved in the regulation of SOCS3 gene expression.";
RL Biochem. J. 387:737-745(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-565 AND SER-568, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcriptional factor that can act as an activator or
CC repressor depending on isoform and/or post-translational modifications.
CC Binds to GT and GC boxes promoter elements. Competes with SP1 for the
CC GC-box promoters. Weak activator of transcription but can activate a
CC number of genes involved in different processes such as cell-cycle
CC regulation, hormone-induction and house-keeping (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15554904}.
CC -!- SUBUNIT: Interacts with HLTF; the interaction may be required for basal
CC transcriptional activity of HLTF. Interacts with HDAC1; the interaction
CC deacetylates SP3 and regulates its transcriptional activity. Interacts
CC with HDAC2 (preferably the CK2-phosphorylated form); the interaction
CC deacetylates SP3 and regulates its transcriptional activity. Ceramides
CC can also regulate acetylation/deacetylation events through altering the
CC interaction of HDAC with SP3. Interacts with MEIS2 isoform Meis2D and
CC PBX1 isoform PBX1a (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O70494; Q9Z2D6: Mecp2; NbExp=2; IntAct=EBI-643514, EBI-1188816;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}.
CC Note=Localizes to the nuclear periphery and in nuclear dots when
CC sumoylated. Some localization in PML nuclear bodies (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O70494-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70494-2; Sequence=VSP_016783;
CC Name=3;
CC IsoId=O70494-3; Sequence=VSP_016782, VSP_016784;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q02447}.
CC -!- PTM: Acetylated by histone acetyltransferase p300, deacetylated by
CC HDACs. Acetylation/deacetylation states regulate transcriptional
CC activity. Acetylation appears to activate transcription. Alternate
CC sumoylation and acetylation at Lys-553 also control transcriptional
CC activity (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated on all isoforms. Sumoylated on 2 sites in longer
CC isoforms with Lys-553 being the major site. Sumoylation at this site
CC promotes nuclear localization to the nuclear periphery, nuclear dots
CC and PML nuclear bodies. Sumoylation on Lys-553 represses the
CC transactivation activity, except for the largest isoform which has
CC little effect on transactivation. Alternate sumoylation and acetylation
CC at Lys-553 also control transcriptional activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27797.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE21310.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK004607; BAC25090.1; -; mRNA.
DR EMBL; AK132702; BAE21310.1; ALT_INIT; mRNA.
DR EMBL; AL844840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027797; AAH27797.2; ALT_INIT; mRNA.
DR EMBL; BC079874; AAH79874.1; -; mRNA.
DR EMBL; AF062567; AAC16322.1; -; mRNA.
DR CCDS; CCDS16122.1; -. [O70494-1]
DR RefSeq; NP_001018052.1; NM_001018042.3. [O70494-1]
DR RefSeq; NP_001091895.1; NM_001098425.1.
DR AlphaFoldDB; O70494; -.
DR SMR; O70494; -.
DR BioGRID; 203418; 9.
DR IntAct; O70494; 2.
DR MINT; O70494; -.
DR STRING; 10090.ENSMUSP00000099750; -.
DR iPTMnet; O70494; -.
DR PhosphoSitePlus; O70494; -.
DR EPD; O70494; -.
DR MaxQB; O70494; -.
DR PaxDb; O70494; -.
DR PeptideAtlas; O70494; -.
DR PRIDE; O70494; -.
DR ProteomicsDB; 263297; -. [O70494-1]
DR ProteomicsDB; 263298; -. [O70494-2]
DR ProteomicsDB; 263299; -. [O70494-3]
DR Antibodypedia; 3887; 412 antibodies from 33 providers.
DR DNASU; 20687; -.
DR Ensembl; ENSMUST00000066003; ENSMUSP00000065807; ENSMUSG00000027109. [O70494-2]
DR Ensembl; ENSMUST00000102689; ENSMUSP00000099750; ENSMUSG00000027109. [O70494-1]
DR GeneID; 20687; -.
DR KEGG; mmu:20687; -.
DR UCSC; uc008kca.2; mouse. [O70494-1]
DR UCSC; uc008kcb.2; mouse. [O70494-2]
DR CTD; 6670; -.
DR MGI; MGI:1277166; Sp3.
DR VEuPathDB; HostDB:ENSMUSG00000027109; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155099; -.
DR HOGENOM; CLU_019688_2_1_1; -.
DR InParanoid; O70494; -.
DR OMA; TCTQVES; -.
DR OrthoDB; 1085860at2759; -.
DR PhylomeDB; O70494; -.
DR TreeFam; TF350150; -.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR BioGRID-ORCS; 20687; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Sp3; mouse.
DR PRO; PR:O70494; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70494; protein.
DR Bgee; ENSMUSG00000027109; Expressed in indifferent gonad and 253 other tissues.
DR Genevisible; O70494; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0060216; P:definitive hemopoiesis; IGI:MGI.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IGI:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IGI:MGI.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0001889; P:liver development; IGI:MGI.
DR GO; GO:0030324; P:lung development; IGI:MGI.
DR GO; GO:0030219; P:megakaryocyte differentiation; IGI:MGI.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IGI:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IGI:MGI.
DR InterPro; IPR030452; SP3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF3; PTHR23235:SF3; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..783
FT /note="Transcription factor Sp3"
FT /id="PRO_0000047142"
FT ZN_FING 623..647
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 653..677
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 683..705
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..239
FT /note="Transactivation domain (Gln-rich)"
FT /evidence="ECO:0000250"
FT REGION 302..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..501
FT /note="Transactivation domain (Gln-rich)"
FT /evidence="ECO:0000250"
FT REGION 536..622
FT /note="Repressor domain"
FT /evidence="ECO:0000250"
FT MOTIF 463..471
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q02447"
FT COMPBIAS 29..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 553
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15554904"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02447"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q02447"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q02447"
FT CROSSLNK 595
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02447"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016782"
FT VAR_SEQ 52..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9628590"
FT /id="VSP_016783"
FT VAR_SEQ 65..94
FT /note="CSKIGPPSPGDDDEEAAVAAAAGVPAAAAG -> MKEDRAAIAGRRRRGRRS
FT CAHDEKTAADKR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016784"
FT CONFLICT 231..233
FT /note="PQT -> TRP (in Ref. 3; AAH27797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 82362 MW; E45A00D566454D61 CRC64;
MTAPEKPVKQ EEMAALDVDG GGGGGGHGEY LQQQQQQQQQ HGNGAAAAAA QDTQPSPLAL
LAATCSKIGP PSPGDDDEEA AVAAAAGVPA AAAGATGDLA SAQLGGAPNR WEVLSATPTT
IKDEAGNLVQ IPGAATSSGQ YVLPLQNLQN QQIFSVAPGS DSSNGTVSNV QYQVIPQIQS
TDAQQVQIGF TGSSDNGGIN QENSQIQIIP GSNQTLLASG TPPANIQNLI PQTGQVQVQG
VAIGGSSFPG QTQVVANVPL GLPGNITFVP INSVDLDSLG LSGSSQTMTA GINADGHLIN
TGQAMDSSDN SERTGERVSP DVNETNADTD LFVPTSSSSQ LPVTIDSTGI LQQNTNSLTT
TSGQVHSSDL QGNYIQSPVS EETQAQNIQV STAQPVVQHL QLQDSQQPTS QAQIVQGITP
QTIHGVQASG QNISQQALQN LQLQLNPGTF LIQAQTVTPS GQITWQTFQV QGVQNLQNLQ
IQNTAAQQIT LTPVQTLTLG QVAAGGALTS TPVSLSTGQL PNLQTVTVNS IDSTGIQLHP
GENADSPADI RIKEEEPDPE EWQLSGDSTL NTNDLTHLRV QVVDEEGDQQ HQEGKRLRRV
ACTCPNCKEG GGRGTNLGKK KQHICHIPGC GKVYGKTSHL RAHLRWHSGE RPFICNWMFC
GKRFTRSDEL QRHRRTHTGE KKFVCPECSK RFMRSDHLAK HIKTHQNKKV IHSSSTVLAS
VEAGRDDALI TAGGTTLILA NIQQGSVSGI GTVNTSATSN QDILTNTEIP LQLVTVSGNE
TME
