ST18_HUMAN
ID ST18_HUMAN Reviewed; 1047 AA.
AC O60284; Q17RY1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Suppression of tumorigenicity 18 protein;
DE AltName: Full=Zinc finger protein 387;
GN Name=ST18; Synonyms=KIAA0535, ZNF387;
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].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15489893; DOI=10.1038/sj.onc.1208131;
RA Jandrig B., Seitz S., Hinzmann B., Arnold W., Micheel B., Koelble K.,
RA Siebert R., Schwartz A., Ruecker K., Schlag P.M., Scherneck S.,
RA Rosenthal A.;
RT "ST18 is a breast cancer tumor suppressor gene at human chromosome
RT 8q11.2.";
RL Oncogene 23:9295-9302(2004).
RN [4]
RP STRUCTURE BY NMR OF 812-906 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of tandem repeat of the fifth and sixth zinc-finger
RT C2HC domains from human ST18.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Repressor that binds to DNA sequences containing a bipartite
CC element consisting of a direct repeat of the sequence 5'-AAAGTTT-3'
CC separated by 2-9 nucleotides. Represses basal transcription activity
CC from target promoters (By similarity). Inhibits colony formation in
CC cultured breast cancer cells. {ECO:0000250,
CC ECO:0000269|PubMed:15489893}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15489893}.
CC -!- TISSUE SPECIFICITY: Detected at low levels in heart, liver, kidney,
CC skeletal muscle, pancreas, testis, ovary and prostate. Detected at even
CC lower levels in mammary epithelial cells and breast cancer cells.
CC {ECO:0000269|PubMed:15489893}.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
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DR EMBL; AB011107; BAA25461.1; -; mRNA.
DR EMBL; BC117147; AAI17148.1; -; mRNA.
DR EMBL; BC117149; AAI17150.1; -; mRNA.
DR CCDS; CCDS6149.1; -.
DR RefSeq; NP_055497.1; NM_014682.2.
DR RefSeq; XP_006716550.1; XM_006716487.1.
DR RefSeq; XP_011515931.1; XM_011517629.1.
DR RefSeq; XP_011515933.1; XM_011517631.1.
DR RefSeq; XP_011515934.1; XM_011517632.1.
DR RefSeq; XP_011515935.1; XM_011517633.1.
DR RefSeq; XP_011515936.1; XM_011517634.1.
DR RefSeq; XP_011515937.1; XM_011517635.1.
DR RefSeq; XP_011515938.1; XM_011517636.2.
DR RefSeq; XP_011515939.1; XM_011517637.1.
DR RefSeq; XP_011515940.1; XM_011517638.2.
DR RefSeq; XP_016869536.1; XM_017014047.1.
DR RefSeq; XP_016869537.1; XM_017014048.1.
DR RefSeq; XP_016869538.1; XM_017014049.1.
DR RefSeq; XP_016869539.1; XM_017014050.1.
DR RefSeq; XP_016869540.1; XM_017014051.1.
DR RefSeq; XP_016869541.1; XM_017014052.1.
DR RefSeq; XP_016869542.1; XM_017014053.1.
DR RefSeq; XP_016869543.1; XM_017014054.1.
DR RefSeq; XP_016869544.1; XM_017014055.1.
DR RefSeq; XP_016869545.1; XM_017014056.1.
DR RefSeq; XP_016869546.1; XM_017014057.1.
DR RefSeq; XP_016869547.1; XM_017014058.1.
DR RefSeq; XP_016869548.1; XM_017014059.1.
DR RefSeq; XP_016869549.1; XM_017014060.1.
DR RefSeq; XP_016869550.1; XM_017014061.1.
DR RefSeq; XP_016869551.1; XM_017014062.1.
DR RefSeq; XP_016869552.1; XM_017014063.1.
DR RefSeq; XP_016869553.1; XM_017014064.1.
DR RefSeq; XP_016869554.1; XM_017014065.1.
DR RefSeq; XP_016869555.1; XM_017014066.1.
DR RefSeq; XP_016869556.1; XM_017014067.1.
DR RefSeq; XP_016869557.1; XM_017014068.1.
DR RefSeq; XP_016869558.1; XM_017014069.1.
DR RefSeq; XP_016869559.1; XM_017014070.1.
DR RefSeq; XP_016869560.1; XM_017014071.1.
DR PDB; 2CS8; NMR; -; A=812-906.
DR PDBsum; 2CS8; -.
DR AlphaFoldDB; O60284; -.
DR SMR; O60284; -.
DR BioGRID; 115057; 1.
DR IntAct; O60284; 2.
DR MINT; O60284; -.
DR STRING; 9606.ENSP00000276480; -.
DR iPTMnet; O60284; -.
DR PhosphoSitePlus; O60284; -.
DR BioMuta; ST18; -.
DR MassIVE; O60284; -.
DR MaxQB; O60284; -.
DR PaxDb; O60284; -.
DR PeptideAtlas; O60284; -.
DR PRIDE; O60284; -.
DR ProteomicsDB; 49313; -.
DR Antibodypedia; 24412; 234 antibodies from 26 providers.
DR DNASU; 9705; -.
DR Ensembl; ENST00000276480.11; ENSP00000276480.7; ENSG00000147488.12.
DR Ensembl; ENST00000689386.1; ENSP00000509475.1; ENSG00000147488.12.
DR Ensembl; ENST00000693301.1; ENSP00000508476.1; ENSG00000147488.12.
DR GeneID; 9705; -.
DR KEGG; hsa:9705; -.
DR MANE-Select; ENST00000689386.1; ENSP00000509475.1; NM_001352837.2; NP_001339766.1.
DR UCSC; uc003xra.3; human.
DR CTD; 9705; -.
DR DisGeNET; 9705; -.
DR GeneCards; ST18; -.
DR HGNC; HGNC:18695; ST18.
DR HPA; ENSG00000147488; Tissue enriched (brain).
DR neXtProt; NX_O60284; -.
DR OpenTargets; ENSG00000147488; -.
DR PharmGKB; PA38642; -.
DR VEuPathDB; HostDB:ENSG00000147488; -.
DR eggNOG; KOG3803; Eukaryota.
DR GeneTree; ENSGT00940000159905; -.
DR HOGENOM; CLU_007226_0_0_1; -.
DR InParanoid; O60284; -.
DR OMA; DECYLIS; -.
DR OrthoDB; 116799at2759; -.
DR PhylomeDB; O60284; -.
DR TreeFam; TF317299; -.
DR PathwayCommons; O60284; -.
DR SignaLink; O60284; -.
DR BioGRID-ORCS; 9705; 7 hits in 1090 CRISPR screens.
DR ChiTaRS; ST18; human.
DR EvolutionaryTrace; O60284; -.
DR GenomeRNAi; 9705; -.
DR Pharos; O60284; Tbio.
DR PRO; PR:O60284; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O60284; protein.
DR Bgee; ENSG00000147488; Expressed in corpus callosum and 141 other tissues.
DR ExpressionAtlas; O60284; baseline and differential.
DR Genevisible; O60284; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR013681; Myelin_TF.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF08474; MYT1; 1.
DR Pfam; PF01530; zf-C2HC; 6.
DR SUPFAM; SSF103637; SSF103637; 6.
DR PROSITE; PS51802; ZF_CCHHC; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1047
FT /note="Suppression of tumorigenicity 18 protein"
FT /id="PRO_0000234030"
FT ZN_FING 359..402
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 403..446
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 715..758
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 759..802
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 807..850
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 860..903
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 41..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 920..992
FT /evidence="ECO:0000255"
FT COMPBIAS 65..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 742
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 748
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 768
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 786
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 792
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 834
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 840
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT VARIANT 515
FT /note="R -> C (in dbSNP:rs2303460)"
FT /id="VAR_052732"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:2CS8"
FT STRAND 827..830
FT /evidence="ECO:0007829|PDB:2CS8"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:2CS8"
FT HELIX 841..847
FT /evidence="ECO:0007829|PDB:2CS8"
FT TURN 890..892
FT /evidence="ECO:0007829|PDB:2CS8"
FT HELIX 894..899
FT /evidence="ECO:0007829|PDB:2CS8"
SQ SEQUENCE 1047 AA; 115155 MW; 4EE28F09AE7C106B CRC64;
MDAEAEDKTL RTRSKGTEVP MDSLIQELSV AYDCSMAKKR TAEDQALGVP VNKRKSLLMK
PRHYSPKADC QEDRSDRTED DGPLETHGHS TAEEIMIKPM DESLLSTAQE NSSRKEDRYS
CYQELMVKSL MHLGKFEKNV SVQTVSENLN DSGIQSLKAE SDEADECFLI HSDDGRDKID
DSQPPFCSSD DNESNSESAE NGWDSGSNFS EETKPPRVPK YVLTDHKKDL LEVPEIKTEG
DKFIPCENRC DSETERKDPQ NALAEPLDGN AQPSFPDVEE EDSESLAVMT EEGSDLEKAK
GNLSLLEQAI ALQAERGCVF HNTYKELDRF LLEHLAGERR QTKVIDMGGR QIFNNKHSPR
PEKRETKCPI PGCDGTGHVT GLYPHHRSLS GCPHKVRVPL EILAMHENVL KCPTPGCTGR
GHVNSNRNTH RSLSGCPIAA AEKLAMSQDK NQLDSPQTGQ CPDQAHRTSL VKQIEFNFPS
QAITSPRATV SKEQEKFGKV PFDYASFDAQ VFGKRPLIQT VQGRKTPPFP ESKHFPNPVK
FPNRLPSAGA HTQSPGRASS YSYGQCSEDT HIAAAAAILN LSTRCREATD ILSNKPQSLH
AKGAEIEVDE NGTLDLSMKK NRILDKSAPL TSSNTSIPTP SSSPFKTSSI LVNAAFYQAL
CDQEGWDTPI NYSKTHGKTE EEKEKDPVSS LENLEEKKFP GEASIPSPKP KLHARDLKKE
LITCPTPGCD GSGHVTGNYA SHRSVSGCPL ADKTLKSLMA ANSQELKCPT PGCDGSGHVT
GNYASHRSLS GCPRARKGGV KMTPTKEEKE DPELKCPVIG CDGQGHISGK YTSHRTASGC
PLAAKRQKEN PLNGASLSWK LNKQELPHCP LPGCNGLGHV NNVFVTHRSL SGCPLNAQVI
KKGKVSEELM TIKLKATGGI ESDEEIRHLD EEIKELNESN LKIEADMMKL QTQITSMESN
LKTIEEENKL IEQNNESLLK ELAGLSQALI SSLADIQLPQ MGPISEQNFE AYVNTLTDMY
SNLERDYSPE CKALLESIKQ AVKGIHV
