ID   SP7_HUMAN               Reviewed;         431 AA.
AC   Q8TDD2; B3KY26; Q3MJ72; Q7Z718;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Transcription factor Sp7;
DE   AltName: Full=Zinc finger protein osterix;
GN   Name=SP7; Synonyms=OSX;
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] (ISOFORM 1).
RX   PubMed=11792318; DOI=10.1016/s0092-8674(01)00622-5;
RA   Nakashima K., Zhou X., Kunkel G., Zhang Z., Deng J.M., Behringer R.R.,
RA   de Crombrugghe B.;
RT   "The novel zinc finger-containing transcription factor osterix is required
RT   for osteoblast differentiation and bone formation.";
RL   Cell 108:17-29(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=14604442; DOI=10.1186/1471-2164-4-43;
RA   Milona M.-A., Gough J.E., Edgar A.J.;
RT   "Expression of alternatively spliced isoforms of human Sp7 in osteoblast-
RT   like cells.";
RL   BMC Genomics 4:43-43(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Osteosarcoma;
RX   PubMed=15474293; DOI=10.1016/j.gene.2004.05.026;
RA   Gao Y., Jheon A., Nourkeyhani H., Kobayashi H., Ganss B.;
RT   "Molecular cloning, structure, expression, and chromosomal localization of
RT   the human Osterix (SP7) gene.";
RL   Gene 341:101-110(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Trachea;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [8]
RP   INVOLVEMENT IN OI12.
RX   PubMed=20579626; DOI=10.1016/j.ajhg.2010.05.016;
RA   Lapunzina P., Aglan M., Temtamy S., Caparros-Martin J.A., Valencia M.,
RA   Leton R., Martinez-Glez V., Elhossini R., Amr K., Vilaboa N.,
RA   Ruiz-Perez V.L.;
RT   "Identification of a frameshift mutation in Osterix in a patient with
RT   recessive osteogenesis imperfecta.";
RL   Am. J. Hum. Genet. 87:110-114(2010).
RN   [9]
RP   FUNCTION, UBIQUITINATION AT LYS-58 AND LYS-230, AND MUTAGENESIS OF LYS-58
RP   AND LYS-230.
RX   PubMed=23457570; DOI=10.1371/journal.pone.0056451;
RA   Peng Y., Shi K., Wang L., Lu J., Li H., Pan S., Ma C.;
RT   "Characterization of Osterix protein stability and physiological role in
RT   osteoblast differentiation.";
RL   PLoS ONE 8:E56451-E56451(2013).
RN   [10]
RP   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: Transcriptional activator essential for osteoblast
CC       differentiation (PubMed:23457570). Binds to SP1 and EKLF consensus
CC       sequences and to other G/C-rich sequences (By similarity).
CC       {ECO:0000250|UniProtKB:Q8VI67, ECO:0000269|PubMed:23457570}.
CC   -!- SUBUNIT: Interacts with RIOX1; the interaction is direct and inhibits
CC       transcription activator activity. {ECO:0000250|UniProtKB:Q8VI67}.
CC   -!- INTERACTION:
CC       Q8TDD2; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-10713842, EBI-11986315;
CC       Q8TDD2; O95995: GAS8; NbExp=3; IntAct=EBI-10713842, EBI-1052570;
CC       Q8TDD2; P47897: QARS1; NbExp=5; IntAct=EBI-10713842, EBI-347462;
CC       Q8TDD2; Q9BVG3: TRIM62; NbExp=5; IntAct=EBI-10713842, EBI-6929619;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VI67}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=alpha, long;
CC         IsoId=Q8TDD2-1; Sequence=Displayed;
CC       Name=2; Synonyms=beta, short;
CC         IsoId=Q8TDD2-2; Sequence=VSP_047639;
CC   -!- TISSUE SPECIFICITY: Restricted to bone-derived cell.
CC       {ECO:0000269|PubMed:15474293}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:31375868}.
CC   -!- PTM: Ubiquitination at leads to proteasomal degradation. SP7 is a
CC       short-live protein with an endogenous half-life of approximately 12
CC       hours. {ECO:0000269|PubMed:23457570}.
CC   -!- PTM: Propionylated. Depropionylation at Lys-371 by SIRT7 activates
CC       transcription factor activity and positively regulates bone formation
CC       by osteoblasts. {ECO:0000250|UniProtKB:Q8VI67}.
CC   -!- DISEASE: Osteogenesis imperfecta 12 (OI12) [MIM:613849]: A form of
CC       osteogenesis imperfecta, a connective tissue disorder characterized by
CC       low bone mass, bone fragility and susceptibility to fractures after
CC       minimal trauma. Disease severity ranges from very mild forms without
CC       fractures to intrauterine fractures and perinatal lethality.
CC       Extraskeletal manifestations, which affect a variable number of
CC       patients, are dentinogenesis imperfecta, hearing loss, and blue
CC       sclerae. OI12 is an autosomal recessive form characterized by recurrent
CC       fractures, mild bone deformations, generalized osteoporosis, delayed
CC       teeth eruption, no dentinogenesis imperfecta, normal hearing, and white
CC       sclerae. {ECO:0000269|PubMed:20579626}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 2]: Generally expressed at much higher level
CC       than isoform 1. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=The
CC       SP7 gene homepage;
CC       URL="https://www.LOVD.nl/SP7";
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DR   EMBL; AF466179; AAO33377.1; -; mRNA.
DR   EMBL; AY150673; AAN85556.1; -; mRNA.
DR   EMBL; AY150674; AAN85557.1; -; mRNA.
DR   EMBL; AF477981; AAL84281.1; -; mRNA.
DR   EMBL; AK128520; BAG54688.1; -; mRNA.
DR   EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW96695.1; -; Genomic_DNA.
DR   EMBL; CH471054; EAW96697.1; -; Genomic_DNA.
DR   EMBL; BC101549; AAI01550.1; -; mRNA.
DR   EMBL; BC113613; AAI13614.1; -; mRNA.
DR   CCDS; CCDS44897.1; -. [Q8TDD2-1]
DR   CCDS; CCDS73475.1; -. [Q8TDD2-2]
DR   RefSeq; NP_001166938.1; NM_001173467.2. [Q8TDD2-1]
DR   RefSeq; NP_001287766.1; NM_001300837.1. [Q8TDD2-2]
DR   RefSeq; NP_690599.1; NM_152860.1. [Q8TDD2-1]
DR   RefSeq; XP_011536202.1; XM_011537900.2.
DR   AlphaFoldDB; Q8TDD2; -.
DR   SMR; Q8TDD2; -.
DR   BioGRID; 125723; 299.
DR   IntAct; Q8TDD2; 285.
DR   MINT; Q8TDD2; -.
DR   STRING; 9606.ENSP00000443827; -.
DR   GlyGen; Q8TDD2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TDD2; -.
DR   PhosphoSitePlus; Q8TDD2; -.
DR   BioMuta; SP7; -.
DR   DMDM; 30913318; -.
DR   MassIVE; Q8TDD2; -.
DR   MaxQB; Q8TDD2; -.
DR   PaxDb; 9606-ENSP00000443827; -.
DR   PeptideAtlas; Q8TDD2; -.
DR   ProteomicsDB; 69477; -.
DR   ProteomicsDB; 74269; -. [Q8TDD2-1]
DR   Antibodypedia; 3133; 201 antibodies from 33 providers.
DR   DNASU; 121340; -.
DR   Ensembl; ENST00000303846.3; ENSP00000302812.3; ENSG00000170374.6. [Q8TDD2-1]
DR   Ensembl; ENST00000536324.4; ENSP00000443827.2; ENSG00000170374.6. [Q8TDD2-1]
DR   Ensembl; ENST00000537210.2; ENSP00000441367.2; ENSG00000170374.6. [Q8TDD2-2]
DR   Ensembl; ENST00000708981.1; ENSP00000517441.1; ENSG00000291837.1. [Q8TDD2-1]
DR   Ensembl; ENST00000708982.1; ENSP00000517442.1; ENSG00000291837.1. [Q8TDD2-1]
DR   Ensembl; ENST00000708983.1; ENSP00000517443.1; ENSG00000291837.1. [Q8TDD2-2]
DR   GeneID; 121340; -.
DR   KEGG; hsa:121340; -.
DR   MANE-Select; ENST00000536324.4; ENSP00000443827.2; NM_001173467.3; NP_001166938.1.
DR   UCSC; uc001sct.4; human. [Q8TDD2-1]
DR   AGR; HGNC:17321; -.
DR   CTD; 121340; -.
DR   DisGeNET; 121340; -.
DR   GeneCards; SP7; -.
DR   HGNC; HGNC:17321; SP7.
DR   HPA; ENSG00000170374; Not detected.
DR   MalaCards; SP7; -.
DR   MIM; 606633; gene.
DR   MIM; 613849; phenotype.
DR   neXtProt; NX_Q8TDD2; -.
DR   OpenTargets; ENSG00000170374; -.
DR   Orphanet; 1513; Craniodiaphyseal dysplasia.
DR   Orphanet; 216820; Osteogenesis imperfecta type 4.
DR   PharmGKB; PA134917046; -.
DR   VEuPathDB; HostDB:ENSG00000170374; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161293; -.
DR   HOGENOM; CLU_019484_4_2_1; -.
DR   InParanoid; Q8TDD2; -.
DR   OMA; NTPSPWW; -.
DR   OrthoDB; 5359201at2759; -.
DR   PhylomeDB; Q8TDD2; -.
DR   TreeFam; TF350150; -.
DR   PathwayCommons; Q8TDD2; -.
DR   Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR   SignaLink; Q8TDD2; -.
DR   SIGNOR; Q8TDD2; -.
DR   BioGRID-ORCS; 121340; 18 hits in 1169 CRISPR screens.
DR   GeneWiki; Sp7_transcription_factor; -.
DR   GenomeRNAi; 121340; -.
DR   Pharos; Q8TDD2; Tbio.
DR   PRO; PR:Q8TDD2; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q8TDD2; Protein.
DR   Bgee; ENSG00000170374; Expressed in primordial germ cell in gonad and 31 other cell types or tissues.
DR   ExpressionAtlas; Q8TDD2; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISS:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; ISS:BHF-UCL.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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:0034224; P:cellular response to zinc ion starvation; IEA:Ensembl.
DR   GO; GO:0071529; P:cementum mineralization; IEA:Ensembl.
DR   GO; GO:0071344; P:diphosphate metabolic process; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0001649; P:osteoblast differentiation; IDA:BHF-UCL.
DR   GO; GO:2000738; P:positive regulation of stem cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   CDD; cd22542; SP7_N; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR23235:SF19; TRANSCRIPTION FACTOR SP7; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
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; Q8TDD2; HS.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Osteogenesis imperfecta; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..431
FT                   /note="Transcription factor Sp7"
FT                   /id="PRO_0000047150"
FT   ZN_FING         294..318
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         324..348
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         354..376
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          30..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           156..164
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000269|PubMed:31375868"
FT   COMPBIAS        186..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         41
FT                   /note="N6-propionyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT   MOD_RES         45
FT                   /note="N6-propionyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT   MOD_RES         361
FT                   /note="N6-propionyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT   MOD_RES         371
FT                   /note="N6-propionyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:23457570"
FT   CROSSLNK        230
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:23457570"
FT   VAR_SEQ         1..18
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14604442"
FT                   /id="VSP_047639"
FT   MUTAGEN         58
FT                   /note="K->R: Enhances osteogenic differentiation in C2C12
FT                   cells."
FT                   /evidence="ECO:0000269|PubMed:23457570"
FT   MUTAGEN         230
FT                   /note="K->R: Enhances osteogenic differentiation in C2C12
FT                   cells."
FT                   /evidence="ECO:0000269|PubMed:23457570"
SQ   SEQUENCE   431 AA;  44994 MW;  454A6FEA84309FF9 CRC64;
     MASSLLEEEV HYGSSPLAML TAACSKFGGS SPLRDSTTLG KAGTKKPYSV GSDLSASKTM
     GDAYPAPFTS TNGLLSPAGS PPAPTSGYAN DYPPFSHSFP GPTGTQDPGL LVPKGHSSSD
     CLPSVYTSLD MTHPYGSWYK AGIHAGISPG PGNTPTPWWD MHPGGNWLGG GQGQGDGLQG
     TLPTGPAQPP LNPQLPTYPS DFAPLNPAPY PAPHLLQPGP QHVLPQDVYK PKAVGNSGQL
     EGSGGAKPPR GASTGGSGGY GGSGAGRSSC DCPNCQELER LGAAAAGLRK KPIHSCHIPG
     CGKVYGKASH LKAHLRWHTG ERPFVCNWLF CGKRFTRSDE LERHVRTHTR EKKFTCLLCS
     KRFTRSDHLS KHQRTHGEPG PGPPPSGPKE LGEGRSTGEE EASQTPRPSA SPATPEKAPG
     GSPEQSNLLE I
//