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ZN432_HUMAN
ID   ZN432_HUMAN             Reviewed;         652 AA.
AC   O94892;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=Zinc finger protein 432;
GN   Name=ZNF432; Synonyms=KIAA0798;
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=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   NITRATION [LARGE SCALE ANALYSIS] AT TYR-41, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary adenoma;
RX   PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
RA   Zhan X., Desiderio D.M.;
RT   "Nitroproteins from a human pituitary adenoma tissue discovered with a
RT   nitrotyrosine affinity column and tandem mass spectrometry.";
RL   Anal. Biochem. 354:279-289(2006).
RN   [4]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-416 AND TYR-490.
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 involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       O94892; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-12121104, EBI-10303987;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34518.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB018341; BAA34518.2; ALT_INIT; mRNA.
DR   EMBL; BC002858; AAH02858.1; -; mRNA.
DR   CCDS; CCDS12848.1; -.
DR   RefSeq; NP_001309213.1; NM_001322284.1.
DR   RefSeq; NP_001309214.1; NM_001322285.1.
DR   RefSeq; NP_055465.1; NM_014650.3.
DR   AlphaFoldDB; O94892; -.
DR   SMR; O94892; -.
DR   BioGRID; 115023; 5.
DR   IntAct; O94892; 4.
DR   STRING; 9606.ENSP00000470488; -.
DR   GlyConnect; 2092; 1 N-Linked glycan (1 site).
DR   GlyGen; O94892; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; O94892; -.
DR   PhosphoSitePlus; O94892; -.
DR   BioMuta; ZNF432; -.
DR   jPOST; O94892; -.
DR   MassIVE; O94892; -.
DR   MaxQB; O94892; -.
DR   PaxDb; O94892; -.
DR   PeptideAtlas; O94892; -.
DR   PRIDE; O94892; -.
DR   ProteomicsDB; 50529; -.
DR   Antibodypedia; 56944; 88 antibodies from 14 providers.
DR   DNASU; 9668; -.
DR   Ensembl; ENST00000221315.10; ENSP00000221315.4; ENSG00000256087.7.
DR   Ensembl; ENST00000594154.5; ENSP00000470488.1; ENSG00000256087.7.
DR   GeneID; 9668; -.
DR   KEGG; hsa:9668; -.
DR   MANE-Select; ENST00000221315.10; ENSP00000221315.4; NM_014650.4; NP_055465.1.
DR   UCSC; uc002pyk.4; human.
DR   CTD; 9668; -.
DR   DisGeNET; 9668; -.
DR   GeneCards; ZNF432; -.
DR   HGNC; HGNC:20810; ZNF432.
DR   HPA; ENSG00000256087; Low tissue specificity.
DR   neXtProt; NX_O94892; -.
DR   OpenTargets; ENSG00000256087; -.
DR   PharmGKB; PA134935907; -.
DR   VEuPathDB; HostDB:ENSG00000256087; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163119; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; O94892; -.
DR   OMA; ICSECFP; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; O94892; -.
DR   TreeFam; TF350804; -.
DR   PathwayCommons; O94892; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; O94892; -.
DR   BioGRID-ORCS; 9668; 10 hits in 1099 CRISPR screens.
DR   ChiTaRS; ZNF432; human.
DR   GenomeRNAi; 9668; -.
DR   Pharos; O94892; Tdark.
DR   PRO; PR:O94892; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O94892; protein.
DR   Bgee; ENSG00000256087; Expressed in endothelial cell and 193 other tissues.
DR   ExpressionAtlas; O94892; baseline and differential.
DR   Genevisible; O94892; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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: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   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; 15.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 16.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 9.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nitration; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..652
FT                   /note="Zinc finger protein 432"
FT                   /id="PRO_0000047580"
FT   DOMAIN          8..79
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         205..227
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         233..255
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         261..283
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         289..311
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         317..339
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         345..367
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         373..395
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         401..423
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         429..451
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         457..479
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         485..507
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         513..535
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         541..563
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         567..591
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         597..619
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         625..647
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   MOD_RES         41
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16777052"
FT   VARIANT         416
FT                   /note="L -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035577"
FT   VARIANT         490
FT                   /note="C -> Y (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs755035378)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035578"
SQ   SEQUENCE   652 AA;  74836 MW;  14B61461EE54A6EB CRC64;
     MINAQELLTL EDVTVEFTWE EWQLLGPFQK DLYRDVMLEI YSNLLSMGYQ VSKPDALSKL
     ERGEEPWTME DERHSRICPE NNEVDDHLQD HLENQRMLKS VEQYHEHNAF GNTASQTKSL
     CLFRENHDTF ELYIKTLKSN LSLVNQNKSC EINNSTKFSG DGKSFLHGNY EELYSAAKFS
     VSTKANSTKS QVSKHQRTHE IEKNHVCSEC GKAFVKKSQL TDHERVHTGE KPYGCTLCAK
     VFSRKSRLNE HQRIHKREKS FICSECGKVF TMKSRLIEHQ RTHTGEKPYI CNECGKGFPG
     KRNLIVHQRN HTGEKSYICS ECGKGFTGKS MLIIHQRTHT GEKPYICSEC GKGFTTKHYV
     IIHQRNHTGE KPYICNECGK GFTMKSRMIE HQRTHTGEKP YICSECGKGF PRKSNLIVHQ
     RNHTVEKSYL CSECGKGFTV KSMLIIHQRT HTGEKPYTCS ECGKGFPLKS RLIVHQRTHT
     GEKPYRCSEC GKGFIVNSGL MLHQRTHTGE KPYICNECGK GFAFKSNLVV HQRTHTGEKP
     FMCSECGKGF TMKRYLIVHQ QIHTEEKSCI CSECGRGFAK ETELALHKQV HTGEKPYGCN
     ECGKGFTMKS RLIVHQRTHT GEKPFVCSEC RKAFSSKRNL IVHQRTHNGN KP
 
 
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