ID   SP4_HUMAN               Reviewed;         784 AA.
AC   Q02446; O60402; Q32M52;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Transcription factor Sp4;
DE   AltName: Full=SPR-1;
GN   Name=SP4;
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 [MRNA], AND VARIANT LYS-197.
RC   TISSUE=Uterus;
RX   PubMed=1454515; DOI=10.1093/nar/20.21.5519;
RA   Hagen G., Mueller S., Beato M., Suske G.;
RT   "Cloning by recognition site screening of two novel GT box binding
RT   proteins: a family of Sp1 related genes.";
RL   Nucleic Acids Res. 20:5519-5525(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [9]
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 GT and GC boxes promoters elements. Probable
CC       transcriptional activator.
CC   -!- INTERACTION:
CC       Q02446; Q13444: ADAM15; NbExp=3; IntAct=EBI-10198587, EBI-77818;
CC       Q02446; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-10198587, EBI-541426;
CC       Q02446; Q9BTQ8: ATXN7L1; NbExp=3; IntAct=EBI-10198587, EBI-10298510;
CC       Q02446; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-10198587, EBI-16429704;
CC       Q02446; B4DE54: BANP; NbExp=3; IntAct=EBI-10198587, EBI-16429313;
CC       Q02446; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-10198587, EBI-11524452;
CC       Q02446; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-10198587, EBI-16429296;
CC       Q02446; Q96Q77: CIB3; NbExp=6; IntAct=EBI-10198587, EBI-10292696;
CC       Q02446; P27658: COL8A1; NbExp=3; IntAct=EBI-10198587, EBI-747133;
CC       Q02446; P41970: ELK3; NbExp=3; IntAct=EBI-10198587, EBI-1758534;
CC       Q02446; Q75MZ5: FOXP2; NbExp=4; IntAct=EBI-10198587, EBI-10255915;
CC       Q02446; P52655: GTF2A1; NbExp=3; IntAct=EBI-10198587, EBI-389518;
CC       Q02446; A0A024R5S0: hCG_2003792; NbExp=6; IntAct=EBI-10198587, EBI-10188461;
CC       Q02446; Q8TAP4: LMO3; NbExp=3; IntAct=EBI-10198587, EBI-742259;
CC       Q02446; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10198587, EBI-739832;
CC       Q02446; Q4G0S1: LOC730441; NbExp=3; IntAct=EBI-10198587, EBI-10241801;
CC       Q02446; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-10198587, EBI-348259;
CC       Q02446; Q13952-2: NFYC; NbExp=3; IntAct=EBI-10198587, EBI-11956831;
CC       Q02446; Q16656: NRF1; NbExp=3; IntAct=EBI-10198587, EBI-2547810;
CC       Q02446; Q16656-4: NRF1; NbExp=3; IntAct=EBI-10198587, EBI-11742836;
CC       Q02446; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-10198587, EBI-448407;
CC       Q02446; Q96T60: PNKP; NbExp=3; IntAct=EBI-10198587, EBI-1045072;
CC       Q02446; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-10198587, EBI-1389308;
CC       Q02446; P14859: POU2F1; NbExp=5; IntAct=EBI-10198587, EBI-624770;
CC       Q02446; P14859-6: POU2F1; NbExp=3; IntAct=EBI-10198587, EBI-11526590;
CC       Q02446; P86479: PRR20C; NbExp=5; IntAct=EBI-10198587, EBI-10172814;
CC       Q02446; P86480: PRR20D; NbExp=3; IntAct=EBI-10198587, EBI-12754095;
CC       Q02446; Q02446: SP4; NbExp=3; IntAct=EBI-10198587, EBI-10198587;
CC       Q02446; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-10198587, EBI-12023934;
CC       Q02446; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-10198587, EBI-12037215;
CC       Q02446; Q14119: VEZF1; NbExp=3; IntAct=EBI-10198587, EBI-11980193;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Abundant in brain.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors. In SP4, the motif is
CC       inactive. {ECO:0000269|PubMed:31375868}.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; X68561; CAA48563.1; -; mRNA.
DR   EMBL; AK289728; BAF82417.1; -; mRNA.
DR   EMBL; AC004595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471073; EAW93733.1; -; Genomic_DNA.
DR   EMBL; BC109300; AAI09301.1; -; mRNA.
DR   CCDS; CCDS5373.1; -.
DR   PIR; S26638; S26638.
DR   RefSeq; NP_001313472.1; NM_001326543.1.
DR   RefSeq; NP_003103.2; NM_003112.4.
DR   AlphaFoldDB; Q02446; -.
DR   SMR; Q02446; -.
DR   BioGRID; 112554; 62.
DR   IntAct; Q02446; 32.
DR   STRING; 9606.ENSP00000222584; -.
DR   GlyCosmos; Q02446; 22 sites, 2 glycans.
DR   GlyGen; Q02446; 22 sites, 2 O-linked glycans (22 sites).
DR   iPTMnet; Q02446; -.
DR   PhosphoSitePlus; Q02446; -.
DR   BioMuta; SP4; -.
DR   DMDM; 218511800; -.
DR   EPD; Q02446; -.
DR   jPOST; Q02446; -.
DR   MassIVE; Q02446; -.
DR   MaxQB; Q02446; -.
DR   PaxDb; 9606-ENSP00000222584; -.
DR   PeptideAtlas; Q02446; -.
DR   ProteomicsDB; 58090; -.
DR   Antibodypedia; 4135; 89 antibodies from 22 providers.
DR   DNASU; 6671; -.
DR   Ensembl; ENST00000222584.8; ENSP00000222584.3; ENSG00000105866.15.
DR   GeneID; 6671; -.
DR   KEGG; hsa:6671; -.
DR   MANE-Select; ENST00000222584.8; ENSP00000222584.3; NM_003112.5; NP_003103.2.
DR   UCSC; uc003sva.4; human.
DR   AGR; HGNC:11209; -.
DR   CTD; 6671; -.
DR   DisGeNET; 6671; -.
DR   GeneCards; SP4; -.
DR   HGNC; HGNC:11209; SP4.
DR   HPA; ENSG00000105866; Low tissue specificity.
DR   MIM; 600540; gene.
DR   neXtProt; NX_Q02446; -.
DR   OpenTargets; ENSG00000105866; -.
DR   PharmGKB; PA36046; -.
DR   VEuPathDB; HostDB:ENSG00000105866; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000157827; -.
DR   HOGENOM; CLU_019688_2_0_1; -.
DR   InParanoid; Q02446; -.
DR   OMA; NQQAILP; -.
DR   OrthoDB; 5396935at2759; -.
DR   PhylomeDB; Q02446; -.
DR   TreeFam; TF350150; -.
DR   PathwayCommons; Q02446; -.
DR   SignaLink; Q02446; -.
DR   SIGNOR; Q02446; -.
DR   BioGRID-ORCS; 6671; 10 hits in 1179 CRISPR screens.
DR   ChiTaRS; SP4; human.
DR   GeneWiki; Sp4_transcription_factor; -.
DR   GenomeRNAi; 6671; -.
DR   Pharos; Q02446; Tbio.
DR   PRO; PR:Q02446; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q02446; Protein.
DR   Bgee; ENSG00000105866; Expressed in cerebellar vermis and 185 other cell types or tissues.
DR   ExpressionAtlas; Q02446; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
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:0042802; F:identical protein binding; IPI:IntAct.
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; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   CDD; cd22536; SP4_N; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   InterPro; IPR039938; Sp4-like.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR14947:SF21; C2H2-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14947; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
DR   Genevisible; Q02446; HS.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..784
FT                   /note="Transcription factor Sp4"
FT                   /id="PRO_0000047144"
FT   ZN_FING         647..671
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         677..701
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         707..729
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           467..475
FT                   /note="9aaTAD; inactive"
FT                   /evidence="ECO:0000269|PubMed:31375868"
FT   COMPBIAS        32..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         197
FT                   /note="Q -> K (in dbSNP:rs1042848)"
FT                   /evidence="ECO:0000269|PubMed:1454515"
FT                   /id="VAR_047975"
FT   CONFLICT        379..380
FT                   /note="QP -> HA (in Ref. 1; CAA48563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="A -> Q (in Ref. 1; CAA48563)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   784 AA;  81985 MW;  5B0B03EC03657993 CRC64;
     MSDQKKEEEE EAAAAAAMAT EGGKTSEPEN NNKKPKTSGS QDSQPSPLAL LAATCSKIGT
     PGENQATGQQ QIIIDPSQGL VQLQNQPQQL ELVTTQLAGN AWQLVASTPP ASKENNVSQP
     ASSSSSSSSS NNGSASPTKT KSGNSSTPGQ FQVIQVQNPS GSVQYQVIPQ LQTVEGQQIQ
     INPTSSSSLQ DLQGQIQLIS AGNNQAILTA ANRTASGNIL AQNLANQTVP VQIRPGVSIP
     LQLQTLPGTQ AQVVTTLPIN IGGVTLALPV INNVAAGGGT GQVGQPAATA DSGTSNGNQL
     VSTPTNTTTS ASTMPESPSS STTCTTTAST SLTSSDTLVS SADTGQYAST SASSSERTIE
     ESQTPAATES EAQSSSQLQP NGMQNAQDQS NSLQQVQIVG QPILQQIQIQ QPQQQIIQAI
     PPQSFQLQSG QTIQTIQQQP LQNVQLQAVN PTQVLIRAPT LTPSGQISWQ TVQVQNIQSL
     SNLQVQNAGL SQQLTITPVS SSGGTTLAQI APVAVAGAPI TLNTAQLASV PNLQTVSVAN
     LGAAGVQVQG VPVTITSVAG QQQGQDGVKV QQATIAPVTV AVGGIANATI GAVSPDQLTQ
     VHLQQGQQTS DQEVQPGKRL RRVACSCPNC REGEGRGSNE PGKKKQHICH IEGCGKVYGK
     TSHLRAHLRW HTGERPFICN WMFCGKRFTR SDELQRHRRT HTGEKRFECP ECSKRFMRSD
     HLSKHVKTHQ NKKGGGTALA IVTSGELDSS VTEVLGSPRI VTVAAISQDS NPATPNVSTN
     MEEF
//