ZN536_HUMAN
ID ZN536_HUMAN Reviewed; 1300 AA.
AC O15090; A2RU18;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc finger protein 536;
GN Name=ZNF536; Synonyms=KIAA0390;
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=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=19398580; DOI=10.1128/mcb.00362-09;
RA Qin Z., Ren F., Xu X., Ren Y., Li H., Wang Y., Zhai Y., Chang Z.;
RT "ZNF536, a novel zinc finger protein specifically expressed in the brain,
RT negatively regulates neuron differentiation by repressing retinoic acid-
RT induced gene transcription.";
RL Mol. Cell. Biol. 29:3633-3643(2009).
RN [5]
RP DNA-BINDING, AND FUNCTION.
RX PubMed=14621294; DOI=10.1093/dnares/10.4.155;
RA Sakai T., Hino K., Wada S., Maeda H.;
RT "Identification of the DNA binding specificity of the human ZNF219 protein
RT and its function as a transcriptional repressor.";
RL DNA Res. 10:155-165(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND SER-827, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Transcriptional repressor that negatively regulates neuron
CC differentiation by repressing retinoic acid-induced gene transcription
CC (PubMed:19398580). Binds and interrupts RARA from binding to retinoic
CC acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites
CC known as DR1-DR5 (PubMed:19398580). Recognizes and binds 2 copies of
CC the core DNA sequence 5'-CCCCCA-3' (PubMed:14621294).
CC {ECO:0000269|PubMed:14621294, ECO:0000269|PubMed:19398580}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19398580}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20844.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002388; BAA20844.2; ALT_INIT; mRNA.
DR EMBL; BC132720; AAI32721.1; -; mRNA.
DR EMBL; BC132722; AAI32723.1; -; mRNA.
DR EMBL; BC146757; AAI46758.1; -; mRNA.
DR CCDS; CCDS32984.1; -.
DR RefSeq; NP_055532.1; NM_014717.2.
DR RefSeq; XP_016883031.1; XM_017027542.1.
DR AlphaFoldDB; O15090; -.
DR SMR; O15090; -.
DR BioGRID; 115093; 48.
DR IntAct; O15090; 28.
DR MINT; O15090; -.
DR STRING; 9606.ENSP00000347730; -.
DR iPTMnet; O15090; -.
DR PhosphoSitePlus; O15090; -.
DR BioMuta; ZNF536; -.
DR jPOST; O15090; -.
DR MassIVE; O15090; -.
DR MaxQB; O15090; -.
DR PaxDb; O15090; -.
DR PeptideAtlas; O15090; -.
DR PRIDE; O15090; -.
DR ProteomicsDB; 48443; -.
DR Antibodypedia; 15575; 87 antibodies from 21 providers.
DR DNASU; 9745; -.
DR Ensembl; ENST00000355537.4; ENSP00000347730.1; ENSG00000198597.9.
DR GeneID; 9745; -.
DR KEGG; hsa:9745; -.
DR MANE-Select; ENST00000355537.4; ENSP00000347730.1; NM_014717.3; NP_055532.1.
DR UCSC; uc002nsu.2; human.
DR CTD; 9745; -.
DR DisGeNET; 9745; -.
DR GeneCards; ZNF536; -.
DR HGNC; HGNC:29025; ZNF536.
DR HPA; ENSG00000198597; Tissue enriched (brain).
DR MIM; 618037; gene.
DR neXtProt; NX_O15090; -.
DR OpenTargets; ENSG00000198597; -.
DR PharmGKB; PA134920047; -.
DR VEuPathDB; HostDB:ENSG00000198597; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156397; -.
DR InParanoid; O15090; -.
DR OMA; SDAPGEC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O15090; -.
DR TreeFam; TF332241; -.
DR PathwayCommons; O15090; -.
DR SignaLink; O15090; -.
DR BioGRID-ORCS; 9745; 13 hits in 1092 CRISPR screens.
DR ChiTaRS; ZNF536; human.
DR GenomeRNAi; 9745; -.
DR Pharos; O15090; Tbio.
DR PRO; PR:O15090; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O15090; protein.
DR Bgee; ENSG00000198597; Expressed in buccal mucosa cell and 138 other tissues.
DR ExpressionAtlas; O15090; baseline and differential.
DR Genevisible; O15090; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1300
FT /note="Zinc finger protein 536"
FT /id="PRO_0000271041"
FT ZN_FING 130..152
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 158..180
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..297
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..323
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 631..653
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 751..773
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 779..801
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
SQ SEQUENCE 1300 AA; 141417 MW; 858B5B7047653664 CRC64;
MEEASLCLGV SSAEPEAEPH LSGPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKP
PASLEEKAHV PMSGQPMGSQ MALLANQLGR EVDTSLNGRV DLQQFLNGQN LGIMSQMSDI
EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
KLGNLGKGRG RVREENRLLH ELEERAILRD KQLKGSLLQP RPDLKPPPHA QQAPLAACTL
ALQANHSVPD VAHPVPSPKP ASVQEDAVAP AAGFRCTFCK GKFKKREELD RHIRILHKPY
KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGPNGGGEQ SANEFRCEVC GQVFSQAWFL
KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKNKSPSDPE VPVPMGGMSQ
EAHANLYSRY LSCLQSGFMT PDKAGLSEPS QLYGKGELPM KEKEALGKLL SPISSMAHGV
PEGDKHSLLG CLNLVPPLKS SCIERLQAAA KAAEMDPVNS YQAWQLMARG MAMEHGFLSK
EHPLQRNHED TLANAGVLFD KEKREYVLVG ADGSKQKMPA DLVHSTKVGS QRDLPSKLDP
LESSRDFLSH GLNQTLEYNL QGPGNMKEKP TECPDCGRVF RTYHQVVVHS RVHKRDRKGE
EDGLHVGLDE RRGSGSDQES QSVSRSTTPG SSNVTEESGV GGGLSQTGSA QEDSPHPSSP
SSSDIGEEAG RSAGVQQPAL LRDRSLGSAM KDCPYCGKTF RTSHHLKVHL RIHTGEKPYK
CPHCDYAGTQ SASLKYHLER HHRERQNGAG PLSGQPPNQD HKDEMSSKAS LFIRPDILRG
AFKGLPGIDF RGGPASQQWT SGVLSSGDHS GQATGMSSEV PSDALKGTDL PSKSTHFSEI
GRAYQSIVSN GVNFQGSLQA FMDSFVLSSL KKEKDMKDKA LADPPSMKVH GVDGGEEKPS
GKSSQRKSEK SQYEPLDLSV RPDAASLPGS SVTVQDSIAW HGCLFCAFTT SSMELMALHL
QANHLGKAKR KDNTIGVTVN CKDQAREASK MALLPSLQSN KDLGLSNMIS SLDSASEKMA
QGQLKETLGE QKSGAWTGHV DPAFCNFPSD FYKQFGVYPG MVGSGASSSC PNKEPDGKAH
SEEDVPILIP ETTSKNTTDD LSDIASSEDM DSSKGENNDE EDVETEPEMM TKPLSALSKD
SSSDGGDSLQ PTGTSQPVQG LVSPLSQAPE KQWHSQGLLQ AQDPLAGLPK PERGPQSLDK
PMNMLSVLRA YSSDGLAAFN GLASSTANSG CIKRPDLCGK
