SP2_HUMAN
ID SP2_HUMAN Reviewed; 613 AA.
AC Q02086; A6NK74;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transcription factor Sp2;
GN Name=SP2; Synonyms=KIAA0048;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Lymph, and Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 119-613.
RX PubMed=1341900; DOI=10.1128/mcb.12.10.4251-4261.1992;
RA Kingsley C., Winoto A.;
RT "Cloning of GT box-binding proteins: a novel Sp1 multigene family
RT regulating T-cell receptor gene expression.";
RL Mol. Cell. Biol. 12:4251-4261(1992).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP INACTIVATION OF 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
CC -!- FUNCTION: Binds to GC box promoters elements and selectively activates
CC mRNA synthesis from genes that contain functional recognition sites.
CC -!- INTERACTION:
CC Q02086; Q8N9N5: BANP; NbExp=4; IntAct=EBI-8651703, EBI-744695;
CC Q02086; Q14192: FHL2; NbExp=3; IntAct=EBI-8651703, EBI-701903;
CC Q02086; P33993: MCM7; NbExp=3; IntAct=EBI-8651703, EBI-355924;
CC Q02086-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-9088579, EBI-11524452;
CC Q02086-2; Q9BW66: CINP; NbExp=3; IntAct=EBI-9088579, EBI-739784;
CC Q02086-2; P22607: FGFR3; NbExp=3; IntAct=EBI-9088579, EBI-348399;
CC Q02086-2; Q14192: FHL2; NbExp=3; IntAct=EBI-9088579, EBI-701903;
CC Q02086-2; P06396: GSN; NbExp=3; IntAct=EBI-9088579, EBI-351506;
CC Q02086-2; Q13952-2: NFYC; NbExp=3; IntAct=EBI-9088579, EBI-11956831;
CC Q02086-2; Q16656-4: NRF1; NbExp=3; IntAct=EBI-9088579, EBI-11742836;
CC Q02086-2; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-9088579, EBI-2798044;
CC Q02086-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-9088579, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02086-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02086-2; Sequence=VSP_022021;
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:0000269|PubMed:31375868}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH33814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA05923.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D28588; BAA05923.2; ALT_INIT; mRNA.
DR EMBL; AC018521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94785.1; -; Genomic_DNA.
DR EMBL; BC016680; AAH16680.1; ALT_INIT; mRNA.
DR EMBL; BC033814; AAH33814.1; ALT_INIT; mRNA.
DR EMBL; M97190; AAA36629.1; -; mRNA.
DR CCDS; CCDS11521.2; -. [Q02086-1]
DR PIR; A44489; A44489.
DR RefSeq; NP_003101.3; NM_003110.5. [Q02086-1]
DR AlphaFoldDB; Q02086; -.
DR SMR; Q02086; -.
DR BioGRID; 112551; 34.
DR IntAct; Q02086; 19.
DR MINT; Q02086; -.
DR STRING; 9606.ENSP00000365931; -.
DR GlyGen; Q02086; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q02086; -.
DR PhosphoSitePlus; Q02086; -.
DR BioMuta; SP2; -.
DR DMDM; 119370531; -.
DR EPD; Q02086; -.
DR jPOST; Q02086; -.
DR MassIVE; Q02086; -.
DR MaxQB; Q02086; -.
DR PaxDb; Q02086; -.
DR PeptideAtlas; Q02086; -.
DR PRIDE; Q02086; -.
DR ProteomicsDB; 58047; -. [Q02086-1]
DR ProteomicsDB; 58048; -. [Q02086-2]
DR Antibodypedia; 928; 180 antibodies from 30 providers.
DR DNASU; 6668; -.
DR Ensembl; ENST00000376741.5; ENSP00000365931.4; ENSG00000167182.16. [Q02086-1]
DR GeneID; 6668; -.
DR KEGG; hsa:6668; -.
DR MANE-Select; ENST00000376741.5; ENSP00000365931.4; NM_003110.6; NP_003101.3.
DR UCSC; uc002imk.3; human. [Q02086-1]
DR CTD; 6668; -.
DR DisGeNET; 6668; -.
DR GeneCards; SP2; -.
DR HGNC; HGNC:11207; SP2.
DR HPA; ENSG00000167182; Low tissue specificity.
DR MIM; 601801; gene.
DR neXtProt; NX_Q02086; -.
DR OpenTargets; ENSG00000167182; -.
DR PharmGKB; PA36044; -.
DR VEuPathDB; HostDB:ENSG00000167182; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159590; -.
DR HOGENOM; CLU_034267_0_0_1; -.
DR InParanoid; Q02086; -.
DR OMA; IQYQTVP; -.
DR OrthoDB; 1085860at2759; -.
DR PhylomeDB; Q02086; -.
DR TreeFam; TF350150; -.
DR PathwayCommons; Q02086; -.
DR SignaLink; Q02086; -.
DR SIGNOR; Q02086; -.
DR BioGRID-ORCS; 6668; 175 hits in 1107 CRISPR screens.
DR ChiTaRS; SP2; human.
DR GeneWiki; Sp2_transcription_factor; -.
DR GenomeRNAi; 6668; -.
DR Pharos; Q02086; Tbio.
DR PRO; PR:Q02086; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q02086; protein.
DR Bgee; ENSG00000167182; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q02086; baseline and differential.
DR Genevisible; Q02086; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
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:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0035264; P:multicellular organism growth; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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 1: Evidence at protein 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..613
FT /note="Transcription factor Sp2"
FT /id="PRO_0000047140"
FT ZN_FING 525..549
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 555..579
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 585..607
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 361..369
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 225..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7584044"
FT /id="VSP_022021"
SQ SEQUENCE 613 AA; 64900 MW; DEE6BFCAE3405793 CRC64;
MSDPQTSMAA TAAVSPSDYL QPAASTTQDS QPSPLALLAA TCSKIGPPAV EAAVTPPAPP
QPTPRKLVPI KPAPLPLSPG KNSFGILSSK GNILQIQGSQ LSASYPGGQL VFAIQNPTMI
NKGTRSNANI QYQAVPQIQA SNSQTIQVQP NLTNQIQIIP GTNQAIITPS PSSHKPVPIK
PAPIQKSSTT TTPVQSGANV VKLTGGGGNV TLTLPVNNLV NASDTGAPTQ LLTESPPTPL
SKTNKKARKK SLPASQPPVA VAEQVETVLI ETTADNIIQA GNNLLIVQSP GGGQPAVVQQ
VQVVPPKAEQ QQVVQIPQQA LRVVQAASAT LPTVPQKPSQ NFQIQAAEPT PTQVYIRTPS
GEVQTVLVQD SPPATAAATS NTTCSSPASR APHLSGTSKK HSAAILRKER PLPKIAPAGS
IISLNAAQLA AAAQAMQTIN INGVQVQGVP VTITNTGGQQ QLTVQNVSGN NLTISGLSPT
QIQLQMEQAL AGETQPGEKR RRMACTCPNC KDGEKRSGEQ GKKKHVCHIP DCGKTFRKTS
LLRAHVRLHT GERPFVCNWF FCGKRFTRSD ELQRHARTHT GDKRFECAQC QKRFMRSDHL
TKHYKTHLVT KNL
