ZN436_HUMAN
ID ZN436_HUMAN Reviewed; 470 AA.
AC Q9C0F3; Q658I9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Zinc finger protein 436;
GN Name=ZNF436; Synonyms=KIAA1710;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal heart;
RX PubMed=17089209; DOI=10.1007/s11033-006-9019-5;
RA Li Y., Du X., Li F., Deng Y., Yang Z., Wang Y., Pen Z., Wang Z., Yuan W.,
RA Zhu C., Wu X.;
RT "A novel zinc-finger protein ZNF436 suppresses transcriptional activities
RT of AP-1 and SRE.";
RL Mol. Biol. Rep. 33:287-294(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-66, 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).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-196.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be a transcriptional repressor.
CC {ECO:0000269|PubMed:17089209}.
CC -!- INTERACTION:
CC Q9C0F3; Q13895: BYSL; NbExp=3; IntAct=EBI-8489702, EBI-358049;
CC Q9C0F3; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-8489702, EBI-11977221;
CC Q9C0F3; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-8489702, EBI-10961624;
CC Q9C0F3; P49760: CLK2; NbExp=3; IntAct=EBI-8489702, EBI-750020;
CC Q9C0F3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-8489702, EBI-10976677;
CC Q9C0F3; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-8489702, EBI-21603100;
CC Q9C0F3; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-8489702, EBI-744099;
CC Q9C0F3; P22607: FGFR3; NbExp=3; IntAct=EBI-8489702, EBI-348399;
CC Q9C0F3; P14136: GFAP; NbExp=3; IntAct=EBI-8489702, EBI-744302;
CC Q9C0F3; P06396: GSN; NbExp=3; IntAct=EBI-8489702, EBI-351506;
CC Q9C0F3; P01112: HRAS; NbExp=3; IntAct=EBI-8489702, EBI-350145;
CC Q9C0F3; P42858: HTT; NbExp=15; IntAct=EBI-8489702, EBI-466029;
CC Q9C0F3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-8489702, EBI-1055254;
CC Q9C0F3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-8489702, EBI-10975473;
CC Q9C0F3; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-8489702, EBI-8472129;
CC Q9C0F3; P02545: LMNA; NbExp=3; IntAct=EBI-8489702, EBI-351935;
CC Q9C0F3; P07196: NEFL; NbExp=3; IntAct=EBI-8489702, EBI-475646;
CC Q9C0F3; P35240: NF2; NbExp=3; IntAct=EBI-8489702, EBI-1014472;
CC Q9C0F3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-8489702, EBI-741158;
CC Q9C0F3; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-8489702, EBI-14066006;
CC Q9C0F3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-8489702, EBI-5235340;
CC Q9C0F3; O43463: SUV39H1; NbExp=2; IntAct=EBI-8489702, EBI-349968;
CC Q9C0F3; O76024: WFS1; NbExp=3; IntAct=EBI-8489702, EBI-720609;
CC Q9C0F3; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-8489702, EBI-746277;
CC Q9C0F3; Q9Y649; NbExp=3; IntAct=EBI-8489702, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17089209}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain, heart, liver, spleen,
CC bladder, lung, skin, skeletal muscle, stomach and pancreas.
CC {ECO:0000269|PubMed:17089209}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21801.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB051497; BAB21801.1; ALT_INIT; mRNA.
DR EMBL; AL834485; CAD39143.1; -; mRNA.
DR EMBL; AL109936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056400; AAH56400.1; -; mRNA.
DR CCDS; CCDS233.1; -.
DR RefSeq; NP_001070663.1; NM_001077195.1.
DR RefSeq; NP_085137.1; NM_030634.2.
DR AlphaFoldDB; Q9C0F3; -.
DR SMR; Q9C0F3; -.
DR BioGRID; 123316; 19.
DR IntAct; Q9C0F3; 30.
DR MINT; Q9C0F3; -.
DR STRING; 9606.ENSP00000313582; -.
DR iPTMnet; Q9C0F3; -.
DR PhosphoSitePlus; Q9C0F3; -.
DR BioMuta; ZNF436; -.
DR DMDM; 20141030; -.
DR EPD; Q9C0F3; -.
DR MassIVE; Q9C0F3; -.
DR PaxDb; Q9C0F3; -.
DR PeptideAtlas; Q9C0F3; -.
DR PRIDE; Q9C0F3; -.
DR ProteomicsDB; 80030; -.
DR Antibodypedia; 15569; 139 antibodies from 24 providers.
DR DNASU; 80818; -.
DR Ensembl; ENST00000314011.9; ENSP00000313582.4; ENSG00000125945.15.
DR Ensembl; ENST00000374608.3; ENSP00000363736.3; ENSG00000125945.15.
DR Ensembl; ENST00000635349.1; ENSP00000489127.1; ENSG00000283009.2.
DR Ensembl; ENST00000635400.2; ENSP00000489469.1; ENSG00000283009.2.
DR GeneID; 80818; -.
DR KEGG; hsa:80818; -.
DR MANE-Select; ENST00000314011.9; ENSP00000313582.4; NM_001077195.2; NP_001070663.1.
DR UCSC; uc001bgt.4; human.
DR CTD; 80818; -.
DR DisGeNET; 80818; -.
DR GeneCards; ZNF436; -.
DR HGNC; HGNC:20814; ZNF436.
DR HPA; ENSG00000125945; Low tissue specificity.
DR MIM; 611703; gene.
DR neXtProt; NX_Q9C0F3; -.
DR OpenTargets; ENSG00000125945; -.
DR PharmGKB; PA134911283; -.
DR VEuPathDB; HostDB:ENSG00000125945; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000153587; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q9C0F3; -.
DR OMA; EAHTGIR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9C0F3; -.
DR TreeFam; TF337055; -.
DR PathwayCommons; Q9C0F3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9C0F3; -.
DR BioGRID-ORCS; 80818; 14 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF436; human.
DR GeneWiki; ZNF436; -.
DR GenomeRNAi; 80818; -.
DR Pharos; Q9C0F3; Tbio.
DR PRO; PR:Q9C0F3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9C0F3; protein.
DR Bgee; ENSG00000125945; Expressed in cortical plate and 106 other tissues.
DR Genevisible; Q9C0F3; HS.
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; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..470
FT /note="Zinc finger protein 436"
FT /id="PRO_0000047584"
FT DOMAIN 14..86
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 138..160
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 166..188
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 194..216
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 222..244
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 62..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 196
FT /note="C -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035579"
SQ SEQUENCE 470 AA; 54277 MW; D14EA2026529FCC7 CRC64;
MAATLLMAGS QAPVTFEDMA MYLTREEWRP LDAAQRDLYR DVMQENYGNV VSLDFEIRSE
NEVNPKQEIS EDVQFGTTSE RPAENAEENP ESEEGFESGD RSERQWGDLT AEEWVSYPLQ
PVTDLLVHKE VHTGIRYHIC SHCGKAFSQI SDLNRHQKTH TGDRPYKCYE CGKGFSRSSH
LIQHQRTHTG ERPYDCNECG KSFGRSSHLI QHQTIHTGEK PHKCNECGKS FCRLSHLIQH
QRTHSGEKPY ECEECGKSFS RSSHLAQHQR THTGEKPYEC NECGRGFSER SDLIKHYRVH
TGERPYKCDE CGKNFSQNSD LVRHRRAHTG EKPYHCNECG ENFSRISHLV QHQRTHTGEK
PYECNACGKS FSRSSHLITH QKIHTGEKPY ECNECWRSFG ERSDLIKHQR THTGEKPYEC
VQCGKGFTQS SNLITHQRVH TGEKPYECTE CEKSFSRSSA LIKHKRVHTD
