ZSC26_HUMAN
ID ZSC26_HUMAN Reviewed; 478 AA.
AC Q16670; Q5JPG4; Q7Z3Q6; Q96A17;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 26;
DE AltName: Full=Protein SRE-ZBP;
DE AltName: Full=Zinc finger protein 187;
GN Name=ZSCAN26; Synonyms=ZNF187;
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=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-220.
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-478 (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=1569959; DOI=10.1128/mcb.12.5.2432-2443.1992;
RA Attar R.M., Gilman M.Z.;
RT "Expression cloning of a novel zinc finger protein that binds to the c-fos
RT serum response element.";
RL Mol. Cell. Biol. 12:2432-2443(1992).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC -!- INTERACTION:
CC Q16670; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-3920053, EBI-10171416;
CC Q16670; O95273: CCNDBP1; NbExp=3; IntAct=EBI-3920053, EBI-748961;
CC Q16670; Q86X02: CDR2L; NbExp=3; IntAct=EBI-3920053, EBI-11063830;
CC Q16670; A1L4K1: FSD2; NbExp=3; IntAct=EBI-3920053, EBI-5661036;
CC Q16670; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-3920053, EBI-5916454;
CC Q16670; P28799: GRN; NbExp=3; IntAct=EBI-3920053, EBI-747754;
CC Q16670; P04792: HSPB1; NbExp=3; IntAct=EBI-3920053, EBI-352682;
CC Q16670; P60372: KRTAP10-4; NbExp=3; IntAct=EBI-3920053, EBI-10178153;
CC Q16670; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-3920053, EBI-10172150;
CC Q16670; P60409: KRTAP10-7; NbExp=7; IntAct=EBI-3920053, EBI-10172290;
CC Q16670; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-3920053, EBI-10172052;
CC Q16670; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-3920053, EBI-739863;
CC Q16670; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-3920053, EBI-742948;
CC Q16670; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-3920053, EBI-11522433;
CC Q16670; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-3920053, EBI-1105124;
CC Q16670; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-3920053, EBI-725997;
CC Q16670; O76024: WFS1; NbExp=3; IntAct=EBI-3920053, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC ECO:0000269|PubMed:1569959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16670-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16670-2; Sequence=VSP_028702;
CC -!- INDUCTION: By serum stimulation. {ECO:0000269|PubMed:1569959}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97775.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BX537535; CAD97775.1; ALT_FRAME; mRNA.
DR EMBL; AL832741; CAI46119.1; -; mRNA.
DR EMBL; AL021997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013951; AAH13951.1; -; mRNA.
DR EMBL; BC013962; AAH13962.1; -; mRNA.
DR EMBL; Z11773; CAA77818.1; -; mRNA.
DR CCDS; CCDS78119.1; -. [Q16670-1]
DR PIR; A44391; A44391.
DR RefSeq; NP_001018854.2; NM_001023560.3.
DR RefSeq; NP_001104509.1; NM_001111039.2. [Q16670-1]
DR RefSeq; NP_001274350.1; NM_001287421.1.
DR RefSeq; NP_001274351.1; NM_001287422.1.
DR RefSeq; NP_689949.3; NM_152736.5.
DR RefSeq; XP_016866753.1; XM_017011264.1. [Q16670-1]
DR AlphaFoldDB; Q16670; -.
DR SMR; Q16670; -.
DR BioGRID; 113526; 53.
DR IntAct; Q16670; 44.
DR STRING; 9606.ENSP00000484931; -.
DR iPTMnet; Q16670; -.
DR PhosphoSitePlus; Q16670; -.
DR BioMuta; ZSCAN26; -.
DR DMDM; 160221312; -.
DR EPD; Q16670; -.
DR jPOST; Q16670; -.
DR MassIVE; Q16670; -.
DR MaxQB; Q16670; -.
DR PeptideAtlas; Q16670; -.
DR PRIDE; Q16670; -.
DR ProteomicsDB; 61028; -. [Q16670-1]
DR ProteomicsDB; 61029; -. [Q16670-2]
DR ABCD; Q16670; 2 sequenced antibodies.
DR Antibodypedia; 6168; 201 antibodies from 24 providers.
DR DNASU; 7741; -.
DR Ensembl; ENST00000623276.3; ENSP00000485228.1; ENSG00000197062.12. [Q16670-1]
DR GeneID; 7741; -.
DR KEGG; hsa:7741; -.
DR UCSC; uc032wpm.2; human. [Q16670-1]
DR CTD; 7741; -.
DR DisGeNET; 7741; -.
DR GeneCards; ZSCAN26; -.
DR HGNC; HGNC:12978; ZSCAN26.
DR HPA; ENSG00000197062; Low tissue specificity.
DR MIM; 616474; gene.
DR neXtProt; NX_Q16670; -.
DR OpenTargets; ENSG00000197062; -.
DR PharmGKB; PA37559; -.
DR VEuPathDB; HostDB:ENSG00000197062; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162298; -.
DR HOGENOM; CLU_002678_49_2_1; -.
DR InParanoid; Q16670; -.
DR OMA; EKTEYKC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q16670; -.
DR PathwayCommons; Q16670; -.
DR SignaLink; Q16670; -.
DR BioGRID-ORCS; 7741; 4 hits in 165 CRISPR screens.
DR ChiTaRS; ZSCAN26; human.
DR GenomeRNAi; 7741; -.
DR Pharos; Q16670; Tdark.
DR PRO; PR:Q16670; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q16670; protein.
DR Bgee; ENSG00000197062; Expressed in cortical plate and 168 other tissues.
DR ExpressionAtlas; Q16670; baseline and differential.
DR Genevisible; Q16670; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..478
FT /note="Zinc finger and SCAN domain-containing protein 26"
FT /id="PRO_0000307313"
FT DOMAIN 51..133
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 231..253
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..360
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 422..444
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 450..472
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 159..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_028702"
FT VARIANT 59
FT /note="Y -> C (in dbSNP:rs16893892)"
FT /id="VAR_059900"
FT VARIANT 73
FT /note="R -> Q (in dbSNP:rs11965538)"
FT /id="VAR_059901"
FT VARIANT 83
FT /note="E -> K (in dbSNP:rs11965542)"
FT /id="VAR_059902"
FT VARIANT 220
FT /note="R -> S (in dbSNP:rs17851075)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035405"
FT CONFLICT 230
FT /note="E -> G (in Ref. 1; CAI46119)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="L -> S (in Ref. 4; CAA77818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 55254 MW; 91D1230831FC5C77 CRC64;
MATALVSAHS LAPLNLKKEG LRVVREDHYS TWEQGFKLQG NSKGLGQEPL CKQFRQLRYE
ETTGPREALS RLRELCQQWL QPETHTKEQI LELLVLEQFL IILPKELQAR VQEHHPESRE
DVVVVLEDLQ LDLGETGQQD PDQPKKQKIL VEEMAPLKGV QEQQVRHECE VTKPEKEKGE
ETRIENGKLI VVTDSCGRVE SSGKISEPME AHNEGSNLER HQAKPKEKIE YKCSEREQRF
IQHLDLIEHA STHTGKKLCE SDVCQSSSLT GHKKVLSREK GHQCHECGKA FQRSSHLVRH
QKIHLGEKPY QCNECGKVFS QNAGLLEHLR IHTGEKPYLC IHCGKNFRRS SHLNRHQRIH
SQEEPCECKE CGKTFSQALL LTHHQRIHSH SKSHQCNECG KAFSLTSDLI RHHRIHTGEK
PFKCNICQKA FRLNSHLAQH VRIHNEEKPY QCSECGEAFR QRSGLFQHQR YHHKDKLA
