SP9_HUMAN
ID SP9_HUMAN Reviewed; 484 AA.
AC P0CG40;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Transcription factor Sp9;
GN Name=SP9;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
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 [3]
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: Transcription factor which plays a key role in limb
CC development. Positively regulates FGF8 expression in the apical
CC ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In SP9, 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; AC018470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11147.1; -; Genomic_DNA.
DR CCDS; CCDS46453.1; -.
DR RefSeq; NP_001138722.1; NM_001145250.1.
DR AlphaFoldDB; P0CG40; -.
DR SMR; P0CG40; -.
DR BioGRID; 935248; 1.
DR IntAct; P0CG40; 2.
DR STRING; 9606.ENSP00000378418; -.
DR GlyGen; P0CG40; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0CG40; -.
DR PhosphoSitePlus; P0CG40; -.
DR BioMuta; SP9; -.
DR DMDM; 300681123; -.
DR jPOST; P0CG40; -.
DR MassIVE; P0CG40; -.
DR MaxQB; P0CG40; -.
DR PaxDb; P0CG40; -.
DR PeptideAtlas; P0CG40; -.
DR PRIDE; P0CG40; -.
DR ProteomicsDB; 52470; -.
DR Antibodypedia; 57975; 19 antibodies from 7 providers.
DR Ensembl; ENST00000394967.3; ENSP00000378418.2; ENSG00000217236.2.
DR GeneID; 100131390; -.
DR KEGG; hsa:100131390; -.
DR MANE-Select; ENST00000394967.3; ENSP00000378418.2; NM_001145250.2; NP_001138722.1.
DR UCSC; uc010zem.2; human.
DR CTD; 100131390; -.
DR GeneCards; SP9; -.
DR HGNC; HGNC:30690; SP9.
DR HPA; ENSG00000217236; Tissue enhanced (brain).
DR neXtProt; NX_P0CG40; -.
DR OpenTargets; ENSG00000217236; -.
DR PharmGKB; PA164726207; -.
DR VEuPathDB; HostDB:ENSG00000217236; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162304; -.
DR HOGENOM; CLU_019484_4_1_1; -.
DR InParanoid; P0CG40; -.
DR OMA; HHHATSV; -.
DR OrthoDB; 664813at2759; -.
DR PhylomeDB; P0CG40; -.
DR TreeFam; TF350150; -.
DR PathwayCommons; P0CG40; -.
DR SignaLink; P0CG40; -.
DR BioGRID-ORCS; 100131390; 15 hits in 1088 CRISPR screens.
DR GenomeRNAi; 100131390; -.
DR Pharos; P0CG40; Tdark.
DR PRO; PR:P0CG40; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P0CG40; protein.
DR Bgee; ENSG00000217236; Expressed in ganglionic eminence and 29 other tissues.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..484
FT /note="Transcription factor Sp9"
FT /id="PRO_0000395450"
FT ZN_FING 332..356
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..386
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 409..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..186
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000269|PubMed:31375868"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64HY3"
SQ SEQUENCE 484 AA; 48915 MW; 4E6F06F8FE824A60 CRC64;
MATSILGEEP RFGTTPLAML AATCNKIGNT SPLTTLPESS AFAKGGFHPW KRSSSSCNLG
SSLSGFAVAT GGRGSGGLAG GSGAANSAFC LASTSPTSSA FSSDYGGLFS NSAAAAAAAA
GVSPQEAGGQ SAFISKVHTT AADGLYPRVG MAHPYESWYK SGFHSTLAAG EVTNGAASSW
WDVHSSPGSW LEVQNPAGGL QSSLHSGAPQ ASLHSQLGTY NPDFSSLTHS AFSSTGLGSS
AAAASHLLST SQHLLAQDGF KPVLPSYSDS SAAVAAAAAS AMISGAAAAA AGGSSARSAR
RYSGRATCDC PNCQEAERLG PAGASLRRKG LHSCHIPGCG KVYGKTSHLK AHLRWHTGER
PFVCNWLFCG KRFTRSDELQ RHLRTHTGEK RFACPVCNKR FMRSDHLSKH IKTHNGGGGG
KKGSDSDTDA SNLETPRSES PDLILHDSGV SAARAAAAAA AAAAAAAAAA SAGGKEAASG
PNDS
