SP2_MOUSE
ID SP2_MOUSE Reviewed; 612 AA.
AC Q9D2H6; Q6A0E1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Transcription factor Sp2;
GN Name=Sp2; Synonyms=Kiaa0048;
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] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, 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).
CC -!- FUNCTION: Binds to GC box promoters elements and selectively activates
CC mRNA synthesis from genes that contain functional recognition sites.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D2H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2H6-2; Sequence=VSP_022022;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In SP2, the motif is
CC inactive. {ECO:0000250|UniProtKB:Q02086}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH86457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32155.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172877; BAD32155.1; ALT_INIT; Transcribed_RNA.
DR EMBL; AK019649; BAB31823.1; -; mRNA.
DR EMBL; BC021759; AAH21759.1; ALT_INIT; mRNA.
DR EMBL; BC086457; AAH86457.1; ALT_INIT; mRNA.
DR RefSeq; NP_001074433.1; NM_001080964.1. [Q9D2H6-1]
DR RefSeq; NP_084496.2; NM_030220.3.
DR AlphaFoldDB; Q9D2H6; -.
DR SMR; Q9D2H6; -.
DR BioGRID; 219700; 5.
DR IntAct; Q9D2H6; 2.
DR STRING; 10090.ENSMUSP00000103252; -.
DR iPTMnet; Q9D2H6; -.
DR PhosphoSitePlus; Q9D2H6; -.
DR EPD; Q9D2H6; -.
DR jPOST; Q9D2H6; -.
DR MaxQB; Q9D2H6; -.
DR PaxDb; Q9D2H6; -.
DR PRIDE; Q9D2H6; -.
DR ProteomicsDB; 257547; -. [Q9D2H6-1]
DR ProteomicsDB; 257548; -. [Q9D2H6-2]
DR DNASU; 78912; -.
DR GeneID; 78912; -.
DR KEGG; mmu:78912; -.
DR UCSC; uc007ldg.1; mouse. [Q9D2H6-1]
DR CTD; 6668; -.
DR MGI; MGI:1926162; Sp2.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9D2H6; -.
DR OrthoDB; 1085860at2759; -.
DR BioGRID-ORCS; 78912; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Sp2; mouse.
DR PRO; PR:Q9D2H6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D2H6; protein.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS: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; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO: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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR030451; SP2_TF.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF1; PTHR23235:SF1; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..612
FT /note="Transcription factor Sp2"
FT /id="PRO_0000269192"
FT ZN_FING 524..548
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 554..578
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 584..606
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 166..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..368
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000250|UniProtKB:Q02086"
FT COMPBIAS 226..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02086"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022022"
FT CONFLICT 6
FT /note="M -> T (in Ref. 3; AAH86457)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="Missing (in Ref. 1; BAD32155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 64908 MW; FF2778DC55B4044F CRC64;
MSDPQMSMAA TAAVSPSDYL QPAAATTQDS QPSPLALLAA TCSKIGPPAV EAAVTPPAPP
QPTPRKLVPI KPAPLPLSPC KNSFSILSSK GNILQIQGSQ LSTSYPGGQF VFAIQNPTLI
NKGSRSNASI QYQVPQIQGN SSQTIQVQPS LTNQIQVIPG TNQAITTPST SGHKPVPIKP
APVQKSSTTT TPVQSGANVV KLTGGGSNMT LTLPLNNLVN TSDIGGPAQL LTESPPTPLS
KTNKKARKKS LPVSQPSVAV AEQVETVLIE TTADNIIQAG NNLLIVQSPG GGQPAVVQQV
QVVPPKAEQQ QVVQIPQQAL RVVQAASATL PTVPQKPSQN FQIQTTEPTP TQVYIRTPSG
EVQTVLVQDS PPATAATTST VTCNSPALRA PHLSGTSKKH SAAILRKERP LPKIAPAGSI
ISLNAAQLAA AAQAMQTINI NGVQVQGVPV TITNTGGQQQ LTVQNVSGNN LTISGLSPTQ
IQLQMEQALA GEAQPGEKRR RMACTCPNCK DGEKRSGEQG KKKHVCHIPD CGKTFRKTSL
LRAHVRLHTG ERPFVCNWFF CGKRFTRSDE LQRHARTHTG DKRFECAQCQ KRFMRSDHLT
KHYKTHLGTK GL
